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P02461

- CO3A1_HUMAN

UniProt

P02461 - CO3A1_HUMAN

Protein

Collagen alpha-1(III) chain

Gene

COL3A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of GPR56 in the developing brain and binding to GPR56 inhibits neuronal migration and activates the RhoA pathway by coupling GPR56 to GNA13 and possibly GNA12.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1280 – 12801Calcium
    Metal bindingi1282 – 12821Calcium
    Metal bindingi1283 – 12831Calcium; via carbonyl oxygen
    Metal bindingi1285 – 12851Calcium; via carbonyl oxygen
    Metal bindingi1288 – 12881Calcium

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: UniProtKB
    2. integrin binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. platelet-derived growth factor binding Source: MGI
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. axon guidance Source: Reactome
    3. blood vessel development Source: Ensembl
    4. cell-matrix adhesion Source: UniProtKB
    5. cellular response to amino acid stimulus Source: Ensembl
    6. cerebral cortex development Source: UniProtKB
    7. collagen catabolic process Source: Reactome
    8. collagen fibril organization Source: UniProtKB
    9. digestive tract development Source: Ensembl
    10. extracellular fibril organization Source: UniProtKB
    11. extracellular matrix disassembly Source: Reactome
    12. extracellular matrix organization Source: Reactome
    13. heart development Source: UniProtKB
    14. integrin-mediated signaling pathway Source: UniProtKB
    15. negative regulation of immune response Source: UniProtKB
    16. negative regulation of neuron migration Source: UniProtKB
    17. peptide cross-linking Source: UniProtKB
    18. platelet activation Source: UniProtKB
    19. positive regulation of Rho protein signal transduction Source: UniProtKB
    20. response to cytokine Source: UniProtKB
    21. response to mechanical stimulus Source: Ensembl
    22. response to radiation Source: UniProtKB
    23. skeletal system development Source: Ensembl
    24. skin development Source: UniProtKB
    25. transforming growth factor beta receptor signaling pathway Source: UniProtKB
    26. wound healing Source: UniProtKB

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_163699. Scavenging by Class A Receptors.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(III) chain
    Gene namesi
    Name:COL3A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2201. COL3A1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

    1. collagen type III trimer Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular matrix Source: UniProtKB
    4. extracellular region Source: Reactome
    5. extracellular space Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ehlers-Danlos syndrome 3 (EDS3) [MIM:130020]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. It is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti804 – 8041G → S in EDS3. 1 Publication
    VAR_001783
    Ehlers-Danlos syndrome 4 (EDS4) [MIM:130050]: The most severe form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Characterized by the joint and dermal manifestations as in other forms of the syndrome, characteristic facial features (acrogeria) in most patients, and by proneness to spontaneous rupture of bowel and large arteries. The vascular complications may affect all anatomical areas.26 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831G → C in EDS4. 2 Publications
    VAR_001768
    Natural varianti183 – 1831G → D in EDS4.
    VAR_011095
    Natural varianti183 – 1831G → S in EDS4.
    VAR_011096
    Natural varianti192 – 1921G → V in EDS4.
    VAR_011097
    Natural varianti201 – 2011G → R in EDS4. 2 Publications
    VAR_001769
    Natural varianti204 – 2041G → D in EDS4. 1 Publication
    VAR_011098
    Natural varianti204 – 2041G → S in EDS4.
    VAR_011099
    Natural varianti210 – 2101G → D in EDS4. 1 Publication
    VAR_011100
    Natural varianti219 – 2191G → C in EDS4.
    VAR_011101
    Natural varianti225 – 2251G → V in EDS4.
    VAR_011102
    Natural varianti228 – 2281G → E in EDS4. 2 Publications
    VAR_001770
    Natural varianti240 – 2401G → R in EDS4.
    VAR_011103
    Natural varianti243 – 2431G → V in EDS4.
    VAR_011104
    Natural varianti249 – 2491G → D in EDS4.
    VAR_011105
    Natural varianti249 – 2491G → V in EDS4.
    VAR_011106
    Natural varianti252 – 2521G → D in EDS4.
    VAR_011107
    Natural varianti252 – 2521G → R in EDS4.
    VAR_011108
    Natural varianti252 – 2521G → V in EDS4.
    VAR_011109
    Natural varianti255 – 2551G → V in EDS4.
    VAR_011110
    Natural varianti264 – 2641G → R in EDS4. 1 Publication
    VAR_011111
    Natural varianti267 – 2671G → V in EDS4.
    VAR_011112
    Natural varianti297 – 2971G → R in EDS4. 1 Publication
    VAR_037007
    Natural varianti321 – 3211G → V in EDS4.
    VAR_011113
    Natural varianti327 – 3271G → D in EDS4. 1 Publication
    VAR_011114
    Natural varianti345 – 3451G → R in EDS4.
    VAR_011115
    Natural varianti417 – 4171G → R in EDS4.
    VAR_011116
    Natural varianti444 – 4441G → R in EDS4.
    VAR_011117
    Natural varianti489 – 4891G → E in EDS4.
    VAR_011118
    Natural varianti501 – 5011G → R in EDS4.
    VAR_011119
    Natural varianti519 – 5191G → V in EDS4.
    VAR_011120
    Natural varianti540 – 5401G → R in EDS4. 2 Publications
    VAR_001772
    Natural varianti549 – 5491G → E in EDS4.
    VAR_011121
    Natural varianti552 – 5521G → E in EDS4.
    VAR_011122
    Natural varianti567 – 5671G → E in EDS4. 1 Publication
    VAR_001773
    Natural varianti582 – 5821G → S in EDS4. 1 Publication
    VAR_001774
    Natural varianti588 – 5881G → D in EDS4.
    VAR_011123
    Natural varianti636 – 6361G → R in EDS4.
    VAR_011124
    Natural varianti657 – 6571G → E in EDS4.
    VAR_011125
    Natural varianti660 – 6601G → D in EDS4.
    VAR_011126
    Natural varianti666 – 6661G → D in EDS4. 1 Publication
    VAR_001777
    Natural varianti699 – 6991G → R in EDS4.
    VAR_011128
    Natural varianti726 – 7261G → R in EDS4. 2 Publications
    VAR_001779
    Natural varianti738 – 7381G → S in EDS4.
    VAR_011129
    Natural varianti738 – 7381G → V in EDS4.
    VAR_011130
    Natural varianti744 – 7441G → V in EDS4.
    VAR_011131
    Natural varianti756 – 7561G → E in EDS4. 1 Publication
    VAR_001780
    Natural varianti762 – 7621G → C in EDS4. 1 Publication
    VAR_001781
    Natural varianti828 – 8281G → R in EDS4. 1 Publication
    VAR_001784
    Natural varianti828 – 8281G → W in EDS4.
    VAR_011132
    Natural varianti830 – 8389Missing in EDS4. 1 Publication
    VAR_037008
    Natural varianti852 – 8521G → C in EDS4.
    VAR_011133
    Natural varianti879 – 8791G → V in EDS4.
    VAR_011134
    Natural varianti882 – 8821G → D in EDS4.
    VAR_011135
    Natural varianti900 – 9001G → D in EDS4.
    VAR_011136
    Natural varianti903 – 9031G → E in EDS4.
    VAR_011137
    Natural varianti909 – 9091G → D in EDS4. 1 Publication
    VAR_001785
    Natural varianti909 – 9091G → V in EDS4.
    VAR_011138
    Natural varianti918 – 9181G → E in EDS4.
    VAR_011139
    Natural varianti924 – 9241G → C in EDS4.
    VAR_011140
    Natural varianti936 – 9361G → R in EDS4. 2 Publications
    VAR_001786
    Natural varianti936 – 9361G → S in EDS4.
    VAR_001787
    Natural varianti939 – 9391G → D in EDS4. 1 Publication
    VAR_001788
    Natural varianti942 – 9421G → E in EDS4.
    VAR_011141
    Natural varianti957 – 9571G → S in EDS4; severe variant. 1 Publication
    VAR_001789
    Natural varianti960 – 9601G → V in EDS4; severe variant. 1 Publication
    VAR_001790
    Natural varianti966 – 9661G → V in EDS4.
    VAR_011142
    Natural varianti972 – 9721G → A in EDS4.
    VAR_011143
    Natural varianti984 – 9841G → T in EDS4; requires 2 nucleotide substitutions.
    VAR_011144
    Natural varianti996 – 9961G → E in EDS4. 1 Publication
    VAR_001791
    Natural varianti999 – 9991G → R in EDS4.
    VAR_011145
    Natural varianti1011 – 10111G → E in EDS4.
    VAR_011146
    Natural varianti1014 – 10141G → E in EDS4. 1 Publication
    VAR_001792
    Natural varianti1032 – 10321G → V in EDS4.
    VAR_011147
    Natural varianti1035 – 10351G → C in EDS4.
    VAR_011148
    Natural varianti1044 – 10441G → D in EDS4. 1 Publication
    VAR_011149
    Natural varianti1050 – 10501G → D in EDS4; mild variant. 1 Publication
    VAR_001793
    Natural varianti1050 – 10501G → V in EDS4. 1 Publication
    VAR_011150
    Natural varianti1071 – 10711G → V in EDS4. 1 Publication
    VAR_001794
    Natural varianti1077 – 10771G → V in EDS4. 1 Publication
    VAR_001795
    Natural varianti1089 – 10891G → D in EDS4.
    VAR_011151
    Natural varianti1098 – 10981G → D in EDS4. 1 Publication
    VAR_011152
    Natural varianti1098 – 10981G → V in EDS4.
    VAR_011153
    Natural varianti1101 – 11011G → E in EDS4. 1 Publication
    VAR_001796
    Natural varianti1104 – 11041G → A in EDS4. 1 Publication
    VAR_001797
    Natural varianti1161 – 11611G → V in EDS4.
    VAR_011154
    Natural varianti1164 – 11641G → E in EDS4.
    VAR_011155
    Natural varianti1164 – 11641G → R in EDS4.
    VAR_011156
    Natural varianti1167 – 11671G → V in EDS4. 1 Publication
    VAR_001799
    Natural varianti1170 – 11701G → D in EDS4. 2 Publications
    VAR_001800
    Natural varianti1170 – 11701G → V in EDS4.
    VAR_011157
    Natural varianti1173 – 11731G → E in EDS4. 3 Publications
    VAR_001801
    Natural varianti1173 – 11731G → R in EDS4; Gottron type acrogeria. 1 Publication
    VAR_011158
    Natural varianti1176 – 11761G → V in EDS4; severe. 1 Publication
    VAR_001802
    Natural varianti1179 – 11791G → R in EDS4.
    VAR_011159
    Natural varianti1182 – 11821G → E in EDS4. 1 Publication
    VAR_001803
    Natural varianti1185 – 11851G → D in EDS4; severe variant. 1 Publication
    VAR_001804
    Natural varianti1185 – 11851G → V in EDS4. 1 Publication
    VAR_001805
    Natural varianti1188 – 11881G → E in EDS4; severe variant. 2 Publications
    VAR_001806
    Natural varianti1188 – 11881G → R in EDS4. 1 Publication
    VAR_001807
    Aortic aneurysm, familial abdominal (AAA) [MIM:100070]: A common multifactorial disorder characterized by permanent dilation of the abdominal aorta, usually due to degenerative changes in the aortic wall. Histologically, AAA is characterized by signs of chronic inflammation, destructive remodeling of the extracellular matrix, and depletion of vascular smooth muscle cells.3 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691L → F in AAA.
    VAR_001767
    Natural varianti786 – 7861G → R in AAA. 2 Publications
    VAR_001782

    Keywords - Diseasei

    Aortic aneurysm, Disease mutation, Ehlers-Danlos syndrome

    Organism-specific databases

    MIMi100070. phenotype.
    130020. phenotype.
    130050. phenotype.
    Orphaneti2500. Acrogeria.
    286. Ehlers-Danlos syndrome, vascular type.
    86. Familial abdominal aortic aneurysm.
    231160. Familial cerebral saccular aneurysm.
    PharmGKBiPA26716.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Propeptidei24 – 153130N-terminal propeptidePRO_0000005740Add
    BLAST
    Chaini154 – 12211068Collagen alpha-1(III) chainPRO_0000005741Add
    BLAST
    Propeptidei1222 – 1466245C-terminal propeptidePRO_0000005742Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei263 – 26315-hydroxylysine; alternate
    Glycosylationi263 – 2631O-linked (Gal...); alternate
    Modified residuei284 – 28415-hydroxylysine
    Modified residuei860 – 86015-hydroxylysine
    Modified residuei977 – 97715-hydroxylysine
    Modified residuei1094 – 109415-hydroxylysine; partial
    Modified residuei1106 – 110615-hydroxylysine
    Disulfide bondi1196 – 1196Interchain1 PublicationPROSITE-ProRule annotation
    Disulfide bondi1197 – 1197Interchain1 PublicationPROSITE-ProRule annotation
    Disulfide bondi1262 ↔ 12941 PublicationPROSITE-ProRule annotation
    Disulfide bondi1268 – 1268Interchain (with C-1285)1 PublicationPROSITE-ProRule annotation
    Disulfide bondi1285 – 1285Interchain (with C-1268)1 PublicationPROSITE-ProRule annotation
    Disulfide bondi1302 ↔ 14641 PublicationPROSITE-ProRule annotation
    Disulfide bondi1372 ↔ 14171 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.2 Publications
    O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP02461.
    PRIDEiP02461.

    PTM databases

    PhosphoSiteiP02461.

    Expressioni

    Gene expression databases

    ArrayExpressiP02461.
    BgeeiP02461.
    GenevestigatoriP02461.

    Organism-specific databases

    HPAiCAB016766.
    HPA007583.

    Interactioni

    Subunit structurei

    Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AAEL010235O019492EBI-2431491,EBI-7685554From a different organism.

    Protein-protein interaction databases

    BioGridi107678. 8 interactions.
    DIPiDIP-57177N.
    IntActiP02461. 19 interactions.
    MINTiMINT-7299332.

    Structurei

    Secondary structure

    1
    1466
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1236 – 124914
    Beta strandi1253 – 12575
    Helixi1262 – 12687
    Beta strandi1274 – 12796
    Helixi1286 – 12883
    Beta strandi1290 – 12956
    Turni1296 – 12994
    Beta strandi1300 – 13034
    Beta strandi1305 – 13073
    Beta strandi1309 – 13135
    Beta strandi1320 – 13223
    Helixi1328 – 13314
    Beta strandi1339 – 13413
    Beta strandi1343 – 13453
    Helixi1347 – 136014
    Beta strandi1364 – 137411
    Turni1381 – 13844
    Beta strandi1391 – 13933
    Beta strandi1395 – 13973
    Beta strandi1399 – 14046
    Helixi1406 – 14083
    Beta strandi1411 – 14155
    Beta strandi1422 – 143413
    Helixi1436 – 14383
    Beta strandi1443 – 14453
    Beta strandi1455 – 146511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V53X-ray3.20B/C/D564-584[»]
    3DMWX-ray2.30A/B/C1158-1199[»]
    4AE2X-ray1.68A/B/C1222-1466[»]
    4AEJX-ray2.21A/B/C1222-1466[»]
    4AK3X-ray3.50A1222-1466[»]
    4GYXX-ray1.49A/B/C1158-1200[»]
    ProteinModelPortaliP02461.
    SMRiP02461. Positions 1249-1466.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02461.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 8960VWFCPROSITE-ProRule annotationAdd
    BLAST
    Domaini1232 – 1466235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni149 – 16719Nonhelical region (N-terminal)Add
    BLAST
    Regioni168 – 11961029Triple-helical regionAdd
    BLAST
    Regioni1197 – 12059Nonhelical region (C-terminal)

    Domaini

    The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.

    Sequence similaritiesi

    Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
    Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG004933.
    InParanoidiP02461.
    KOiK06236.
    OMAiPGPSGHQ.
    OrthoDBiEOG7TJ3HH.
    PhylomeDBiP02461.
    TreeFamiTF344135.

    Family and domain databases

    InterProiIPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF01410. COLFI. 1 hit.
    PF01391. Collagen. 10 hits.
    PF00093. VWC. 1 hit.
    [Graphical view]
    ProDomiPD002078. Fib_collagen_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    PROSITEiPS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P02461-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC     50
    QICVCDSGSV LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN 100
    GQGPQGPKGD PGPPGIPGRN GDPGIPGQPG SPGSPGPPGI CESCPTGPQN 150
    YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG PPGPPGTSGH PGSPGSPGYQ 200
    GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG ERGLPGPPGI 250
    KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG 300
    PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK 350
    GEVGPAGSPG SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP 400
    AGIPGAPGLM GARGPPGPAG ANGAPGLRGG AGEPGKNGAK GEPGPRGERG 450
    EAGIPGVPGA KGEDGKDGSP GEPGANGLPG AAGERGAPGF RGPAGPNGIP 500
    GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG SPGGPGSDGK 550
    PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG 600
    GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP 650
    GENGKPGEPG PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP 700
    PGPEGGKGAA GPPGPPGAAG TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG 750
    ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG EGGAPGLPGI AGPRGSPGER 800
    GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG VAGPPGGSGP 850
    AGPPGPQGVK GERGSPGGPG AAGFPGARGL PGPPGSNGNP GPPGPSGSPG 900
    KDGPPGPAGN TGAPGSPGVS GPKGDAGQPG EKGSPGAQGP PGAPGPLGIA 950
    GITGARGLAG PPGMPGPRGS PGPQGVKGES GKPGANGLSG ERGPPGPQGL 1000
    PGLAGTAGEP GRDGNPGSDG LPGRDGSPGG KGDRGENGSP GAPGAPGHPG 1050
    PPGPVGPAGK SGDRGESGPA GPAGAPGPAG SRGAPGPQGP RGDKGETGER 1100
    GAAGIKGHRG FPGNPGAPGS PGPAGQQGAI GSPGPAGPRG PVGPSGPPGK 1150
    DGTSGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGGV 1200
    GAAAIAGIGG EKAGGFAPYY GDEPMDFKIN TDEIMTSLKS VNGQIESLIS 1250
    PDGSRKNPAR NCRDLKFCHP ELKSGEYWVD PNQGCKLDAI KVFCNMETGE 1300
    TCISANPLNV PRKHWWTDSS AEKKHVWFGE SMDGGFQFSY GNPELPEDVL 1350
    DVHLAFLRLL SSRASQNITY HCKNSIAYMD QASGNVKKAL KLMGSNEGEF 1400
    KAEGNSKFTY TVLEDGCTKH TGEWSKTVFE YRTRKAVRLP IVDIAPYDIG 1450
    GPDQEFGVDV GPVCFL 1466
    Length:1,466
    Mass (Da):138,564
    Last modified:January 23, 2007 - v4
    Checksum:iB904B4E05E17D339
    GO
    Isoform 2 (identifier: P02461-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         847-1149: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,163
    Mass (Da):111,907
    Checksum:iBE06E5CA84FBB829
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti163 – 1631G → GG in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti168 – 1681G → V AA sequence (PubMed:557335)Curated
    Sequence conflicti226 – 2283Missing AA sequence (PubMed:557335)Curated
    Sequence conflicti241 – 2411E → D in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti278 – 2781T → A AA sequence (PubMed:557335)Curated
    Sequence conflicti293 – 2953NGA → DGS AA sequence (PubMed:557335)Curated
    Sequence conflicti401 – 4011A → L AA sequence (PubMed:7864881)Curated
    Sequence conflicti409 – 4091L → P AA sequence (PubMed:7864881)Curated
    Sequence conflicti472 – 4721E → D in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti488 – 4903PGF → LGS in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti589 – 5891A → E AA sequence (PubMed:7864881)Curated
    Sequence conflicti614 – 6141T → Y in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti635 – 6351P → R in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti664 – 6641D → E in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti676 – 6761D → N AA sequence (PubMed:687591)Curated
    Sequence conflicti803 – 8031T → P AA sequence (PubMed:7864881)Curated
    Sequence conflicti896 – 8961S → A AA sequence (PubMed:6246925)Curated
    Sequence conflicti980 – 9801S → A AA sequence (PubMed:7016180)Curated
    Sequence conflicti985 – 9895ANGLS → PSGQN AA sequence (PubMed:7016180)Curated
    Sequence conflicti1019 – 10191D → Y in CAA29886. (PubMed:3357782)Curated
    Sequence conflicti1067 – 10671S → P AA sequence (PubMed:7864881)Curated
    Sequence conflicti1070 – 10701A → P AA sequence (PubMed:7864881)Curated
    Sequence conflicti1097 – 10971T → P AA sequence (PubMed:7016180)Curated
    Sequence conflicti1153 – 11542TS → AT AA sequence (PubMed:7016180)Curated
    Sequence conflicti1156 – 11561H → S AA sequence (PubMed:7016180)Curated
    Sequence conflicti1184 – 11841P → S in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti1203 – 12031A → P in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti1210 – 12101G → A in CAA33387. (PubMed:2780304)Curated
    Sequence conflicti1222 – 12221D → P in AAA52002. (PubMed:2579949)Curated
    Sequence conflicti1235 – 12351M → I in AAA52002. (PubMed:2579949)Curated
    Sequence conflicti1241 – 12411V → A in CAA29886. (PubMed:3357782)Curated
    Sequence conflicti1241 – 12411V → A in CAA25879. (PubMed:6096827)Curated
    Sequence conflicti1274 – 12741S → T in AAA52002. (PubMed:2579949)Curated
    Sequence conflicti1332 – 13321M → I in AAA52002. (PubMed:2579949)Curated
    Sequence conflicti1357 – 13571L → P in AAA52002. (PubMed:2579949)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691L → F in AAA.
    VAR_001767
    Natural varianti183 – 1831G → C in EDS4. 2 Publications
    VAR_001768
    Natural varianti183 – 1831G → D in EDS4.
    VAR_011095
    Natural varianti183 – 1831G → S in EDS4.
    VAR_011096
    Natural varianti192 – 1921G → V in EDS4.
    VAR_011097
    Natural varianti201 – 2011G → R in EDS4. 2 Publications
    VAR_001769
    Natural varianti204 – 2041G → D in EDS4. 1 Publication
    VAR_011098
    Natural varianti204 – 2041G → S in EDS4.
    VAR_011099
    Natural varianti210 – 2101G → D in EDS4. 1 Publication
    VAR_011100
    Natural varianti219 – 2191G → C in EDS4.
    VAR_011101
    Natural varianti225 – 2251G → V in EDS4.
    VAR_011102
    Natural varianti228 – 2281G → E in EDS4. 2 Publications
    VAR_001770
    Natural varianti240 – 2401G → R in EDS4.
    VAR_011103
    Natural varianti243 – 2431G → V in EDS4.
    VAR_011104
    Natural varianti249 – 2491G → D in EDS4.
    VAR_011105
    Natural varianti249 – 2491G → V in EDS4.
    VAR_011106
    Natural varianti252 – 2521G → D in EDS4.
    VAR_011107
    Natural varianti252 – 2521G → R in EDS4.
    VAR_011108
    Natural varianti252 – 2521G → V in EDS4.
    VAR_011109
    Natural varianti255 – 2551G → V in EDS4.
    VAR_011110
    Natural varianti264 – 2641G → R in EDS4. 1 Publication
    VAR_011111
    Natural varianti267 – 2671G → V in EDS4.
    VAR_011112
    Natural varianti297 – 2971G → R in EDS4. 1 Publication
    VAR_037007
    Natural varianti303 – 3031G → R in fibromuscular dysplasia and aortic aneurysm. 1 Publication
    VAR_001771
    Natural varianti321 – 3211G → V in EDS4.
    VAR_011113
    Natural varianti327 – 3271G → D in EDS4. 1 Publication
    VAR_011114
    Natural varianti345 – 3451G → R in EDS4.
    VAR_011115
    Natural varianti417 – 4171G → R in EDS4.
    VAR_011116
    Natural varianti420 – 4201G → S in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035738
    Natural varianti444 – 4441G → R in EDS4.
    VAR_011117
    Natural varianti489 – 4891G → E in EDS4.
    VAR_011118
    Natural varianti501 – 5011G → R in EDS4.
    VAR_011119
    Natural varianti519 – 5191G → V in EDS4.
    VAR_011120
    Natural varianti534 – 5341G → E.
    Corresponds to variant rs41263744 [ dbSNP | Ensembl ].
    VAR_055665
    Natural varianti540 – 5401G → R in EDS4. 2 Publications
    VAR_001772
    Natural varianti549 – 5491G → E in EDS4.
    VAR_011121
    Natural varianti552 – 5521G → E in EDS4.
    VAR_011122
    Natural varianti567 – 5671G → E in EDS4. 1 Publication
    VAR_001773
    Natural varianti582 – 5821G → S in EDS4. 1 Publication
    VAR_001774
    Natural varianti588 – 5881G → D in EDS4.
    VAR_011123
    Natural varianti602 – 6021P → T.1 Publication
    Corresponds to variant rs35795890 [ dbSNP | Ensembl ].
    VAR_001775
    Natural varianti635 – 6351P → L.1 Publication
    VAR_001776
    Natural varianti636 – 6361G → R in EDS4.
    VAR_011124
    Natural varianti657 – 6571G → E in EDS4.
    VAR_011125
    Natural varianti660 – 6601G → D in EDS4.
    VAR_011126
    Natural varianti666 – 6661G → D in EDS4. 1 Publication
    VAR_001777
    Natural varianti668 – 6681P → T.1 Publication
    Corresponds to variant rs1801183 [ dbSNP | Ensembl ].
    VAR_011127
    Natural varianti679 – 6791A → T.1 Publication
    Corresponds to variant rs41263773 [ dbSNP | Ensembl ].
    VAR_055666
    Natural varianti686 – 6861P → A.
    Corresponds to variant rs41263775 [ dbSNP | Ensembl ].
    VAR_055667
    Natural varianti698 – 6981A → T.2 Publications
    Corresponds to variant rs1800255 [ dbSNP | Ensembl ].
    VAR_001778
    Natural varianti699 – 6991G → R in EDS4.
    VAR_011128
    Natural varianti726 – 7261G → R in EDS4. 2 Publications
    VAR_001779
    Natural varianti738 – 7381G → S in EDS4.
    VAR_011129
    Natural varianti738 – 7381G → V in EDS4.
    VAR_011130
    Natural varianti744 – 7441G → V in EDS4.
    VAR_011131
    Natural varianti756 – 7561G → E in EDS4. 1 Publication
    VAR_001780
    Natural varianti762 – 7621G → C in EDS4. 1 Publication
    VAR_001781
    Natural varianti786 – 7861G → R in AAA. 2 Publications
    VAR_001782
    Natural varianti804 – 8041G → S in EDS3. 1 Publication
    VAR_001783
    Natural varianti828 – 8281G → R in EDS4. 1 Publication
    VAR_001784
    Natural varianti828 – 8281G → W in EDS4.
    VAR_011132
    Natural varianti830 – 8389Missing in EDS4. 1 Publication
    VAR_037008
    Natural varianti852 – 8521G → C in EDS4.
    VAR_011133
    Natural varianti879 – 8791G → V in EDS4.
    VAR_011134
    Natural varianti882 – 8821G → D in EDS4.
    VAR_011135
    Natural varianti900 – 9001G → D in EDS4.
    VAR_011136
    Natural varianti903 – 9031G → E in EDS4.
    VAR_011137
    Natural varianti909 – 9091G → D in EDS4. 1 Publication
    VAR_001785
    Natural varianti909 – 9091G → V in EDS4.
    VAR_011138
    Natural varianti918 – 9181G → E in EDS4.
    VAR_011139
    Natural varianti924 – 9241G → C in EDS4.
    VAR_011140
    Natural varianti936 – 9361G → R in EDS4. 2 Publications
    VAR_001786
    Natural varianti936 – 9361G → S in EDS4.
    VAR_001787
    Natural varianti939 – 9391G → D in EDS4. 1 Publication
    VAR_001788
    Natural varianti942 – 9421G → E in EDS4.
    VAR_011141
    Natural varianti957 – 9571G → S in EDS4; severe variant. 1 Publication
    VAR_001789
    Natural varianti960 – 9601G → V in EDS4; severe variant. 1 Publication
    VAR_001790
    Natural varianti966 – 9661G → V in EDS4.
    VAR_011142
    Natural varianti972 – 9721G → A in EDS4.
    VAR_011143
    Natural varianti984 – 9841G → T in EDS4; requires 2 nucleotide substitutions.
    VAR_011144
    Natural varianti996 – 9961G → E in EDS4. 1 Publication
    VAR_001791
    Natural varianti999 – 9991G → R in EDS4.
    VAR_011145
    Natural varianti1011 – 10111G → E in EDS4.
    VAR_011146
    Natural varianti1014 – 10141G → E in EDS4. 1 Publication
    VAR_001792
    Natural varianti1032 – 10321G → V in EDS4.
    VAR_011147
    Natural varianti1035 – 10351G → C in EDS4.
    VAR_011148
    Natural varianti1044 – 10441G → D in EDS4. 1 Publication
    VAR_011149
    Natural varianti1050 – 10501G → D in EDS4; mild variant. 1 Publication
    VAR_001793
    Natural varianti1050 – 10501G → V in EDS4. 1 Publication
    VAR_011150
    Natural varianti1071 – 10711G → V in EDS4. 1 Publication
    VAR_001794
    Natural varianti1077 – 10771G → V in EDS4. 1 Publication
    VAR_001795
    Natural varianti1089 – 10891G → D in EDS4.
    VAR_011151
    Natural varianti1098 – 10981G → D in EDS4. 1 Publication
    VAR_011152
    Natural varianti1098 – 10981G → V in EDS4.
    VAR_011153
    Natural varianti1101 – 11011G → E in EDS4. 1 Publication
    VAR_001796
    Natural varianti1104 – 11041G → A in EDS4. 1 Publication
    VAR_001797
    Natural varianti1161 – 11611G → V in EDS4.
    VAR_011154
    Natural varianti1164 – 11641G → E in EDS4.
    VAR_011155
    Natural varianti1164 – 11641G → R in EDS4.
    VAR_011156
    Natural varianti1164 – 11641G → S in spondyloepiphyseal dysplasia.
    VAR_001798
    Natural varianti1167 – 11671G → V in EDS4. 1 Publication
    VAR_001799
    Natural varianti1170 – 11701G → D in EDS4. 2 Publications
    VAR_001800
    Natural varianti1170 – 11701G → V in EDS4.
    VAR_011157
    Natural varianti1173 – 11731G → E in EDS4. 3 Publications
    VAR_001801
    Natural varianti1173 – 11731G → R in EDS4; Gottron type acrogeria. 1 Publication
    VAR_011158
    Natural varianti1176 – 11761G → V in EDS4; severe. 1 Publication
    VAR_001802
    Natural varianti1179 – 11791G → R in EDS4.
    VAR_011159
    Natural varianti1182 – 11821G → E in EDS4. 1 Publication
    VAR_001803
    Natural varianti1185 – 11851G → D in EDS4; severe variant. 1 Publication
    VAR_001804
    Natural varianti1185 – 11851G → V in EDS4. 1 Publication
    VAR_001805
    Natural varianti1188 – 11881G → E in EDS4; severe variant. 2 Publications
    VAR_001806
    Natural varianti1188 – 11881G → R in EDS4. 1 Publication
    VAR_001807
    Natural varianti1205 – 12051I → V.1 Publication
    Corresponds to variant rs2271683 [ dbSNP | Ensembl ].
    VAR_020012
    Natural varianti1353 – 13531H → Q.7 Publications
    Corresponds to variant rs1516446 [ dbSNP | Ensembl ].
    VAR_030115
    Natural varianti1434 – 14341R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035739

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei847 – 1149303Missing in isoform 2. 1 PublicationVSP_022502Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14420 mRNA. Translation: CAA32583.1.
    AY054301, AY016295 Genomic DNA. Translation: AAL13167.1.
    KC567894 Genomic DNA. Translation: AGL34959.1.
    GU143397 Genomic DNA. Translation: ACZ58371.1.
    AC066694 Genomic DNA. Translation: AAY24164.1.
    CH471058 Genomic DNA. Translation: EAX10910.1.
    CH471058 Genomic DNA. Translation: EAX10911.1.
    BC028178 mRNA. Translation: AAH28178.1.
    M26939 Genomic DNA. Translation: AAA52040.1.
    X07240 mRNA. Translation: CAA30229.1.
    X15332 mRNA. Translation: CAA33387.1.
    S62925 Genomic DNA. Translation: AAD13937.1.
    S79877 mRNA. Translation: AAB35615.1.
    M59312 Genomic DNA. Translation: AAA52041.1.
    M59227 mRNA. Translation: AAB59383.1.
    M55603 Genomic DNA. No translation available.
    X06700 mRNA. Translation: CAA29886.1.
    X01655 mRNA. Translation: CAA25821.1.
    X01742 mRNA. Translation: CAA25879.1.
    M13146 mRNA. Translation: AAA52003.1.
    M11134 mRNA. Translation: AAA52004.1.
    M10795
    , M10615, M10793, M10794, M10800, M10801 Genomic DNA. Translation: AAA52002.1.
    CCDSiCCDS2297.1. [P02461-1]
    PIRiS05272. CGHU7L.
    RefSeqiNP_000081.1. NM_000090.3.
    UniGeneiHs.443625.

    Genome annotation databases

    EnsembliENST00000304636; ENSP00000304408; ENSG00000168542. [P02461-1]
    GeneIDi1281.
    KEGGihsa:1281.
    UCSCiuc002uqj.1. human. [P02461-1]

    Polymorphism databases

    DMDMi124056490.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    COL3A1

    Collagen type III alpha-1 chain mutations

    Wikipedia

    Type-III collagen entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14420 mRNA. Translation: CAA32583.1 .
    AY054301 , AY016295 Genomic DNA. Translation: AAL13167.1 .
    KC567894 Genomic DNA. Translation: AGL34959.1 .
    GU143397 Genomic DNA. Translation: ACZ58371.1 .
    AC066694 Genomic DNA. Translation: AAY24164.1 .
    CH471058 Genomic DNA. Translation: EAX10910.1 .
    CH471058 Genomic DNA. Translation: EAX10911.1 .
    BC028178 mRNA. Translation: AAH28178.1 .
    M26939 Genomic DNA. Translation: AAA52040.1 .
    X07240 mRNA. Translation: CAA30229.1 .
    X15332 mRNA. Translation: CAA33387.1 .
    S62925 Genomic DNA. Translation: AAD13937.1 .
    S79877 mRNA. Translation: AAB35615.1 .
    M59312 Genomic DNA. Translation: AAA52041.1 .
    M59227 mRNA. Translation: AAB59383.1 .
    M55603 Genomic DNA. No translation available.
    X06700 mRNA. Translation: CAA29886.1 .
    X01655 mRNA. Translation: CAA25821.1 .
    X01742 mRNA. Translation: CAA25879.1 .
    M13146 mRNA. Translation: AAA52003.1 .
    M11134 mRNA. Translation: AAA52004.1 .
    M10795
    , M10615 , M10793 , M10794 , M10800 , M10801 Genomic DNA. Translation: AAA52002.1 .
    CCDSi CCDS2297.1. [P02461-1 ]
    PIRi S05272. CGHU7L.
    RefSeqi NP_000081.1. NM_000090.3.
    UniGenei Hs.443625.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V53 X-ray 3.20 B/C/D 564-584 [» ]
    3DMW X-ray 2.30 A/B/C 1158-1199 [» ]
    4AE2 X-ray 1.68 A/B/C 1222-1466 [» ]
    4AEJ X-ray 2.21 A/B/C 1222-1466 [» ]
    4AK3 X-ray 3.50 A 1222-1466 [» ]
    4GYX X-ray 1.49 A/B/C 1158-1200 [» ]
    ProteinModelPortali P02461.
    SMRi P02461. Positions 1249-1466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107678. 8 interactions.
    DIPi DIP-57177N.
    IntActi P02461. 19 interactions.
    MINTi MINT-7299332.

    Chemistry

    ChEMBLi CHEMBL2364188.
    DrugBanki DB00048. Collagenase.
    DB00039. Palifermin.

    PTM databases

    PhosphoSitei P02461.

    Polymorphism databases

    DMDMi 124056490.

    Proteomic databases

    PaxDbi P02461.
    PRIDEi P02461.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304636 ; ENSP00000304408 ; ENSG00000168542 . [P02461-1 ]
    GeneIDi 1281.
    KEGGi hsa:1281.
    UCSCi uc002uqj.1. human. [P02461-1 ]

    Organism-specific databases

    CTDi 1281.
    GeneCardsi GC02P189803.
    GeneReviewsi COL3A1.
    HGNCi HGNC:2201. COL3A1.
    HPAi CAB016766.
    HPA007583.
    MIMi 100070. phenotype.
    120180. gene.
    130020. phenotype.
    130050. phenotype.
    neXtProti NX_P02461.
    Orphaneti 2500. Acrogeria.
    286. Ehlers-Danlos syndrome, vascular type.
    86. Familial abdominal aortic aneurysm.
    231160. Familial cerebral saccular aneurysm.
    PharmGKBi PA26716.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.
    InParanoidi P02461.
    KOi K06236.
    OMAi PGPSGHQ.
    OrthoDBi EOG7TJ3HH.
    PhylomeDBi P02461.
    TreeFami TF344135.

    Enzyme and pathway databases

    Reactomei REACT_118779. Extracellular matrix organization.
    REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_163699. Scavenging by Class A Receptors.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Miscellaneous databases

    ChiTaRSi COL3A1. human.
    EvolutionaryTracei P02461.
    GeneWikii Collagen,_type_III,_alpha_1.
    GenomeRNAii 1281.
    NextBioi 35489581.
    PROi P02461.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02461.
    Bgeei P02461.
    Genevestigatori P02461.

    Family and domain databases

    InterProi IPR008160. Collagen.
    IPR000885. Fib_collagen_C.
    IPR001007. VWF_C.
    [Graphical view ]
    Pfami PF01410. COLFI. 1 hit.
    PF01391. Collagen. 10 hits.
    PF00093. VWC. 1 hit.
    [Graphical view ]
    ProDomi PD002078. Fib_collagen_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00038. COLFI. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view ]
    PROSITEi PS51461. NC1_FIB. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences."
      Ala-Kokko L., Kontusaari S., Baldwin C.T., Kuivaniemi H., Prockop D.J.
      Biochem. J. 260:509-516(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-1353.
      Tissue: Skin fibroblast.
    2. "Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes."
      Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., Ala-Kokko L.
      Matrix Biol. 20:357-366(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT GLN-1353.
    3. Fang H.
      Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-726.
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-1353.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-1353.
      Tissue: Liver.
    8. "Cloning and analysis of the 5' portion of the human type-III procollagen gene (COL3A1)."
      Benson-Chanda V., Su M.W., Weil D., Chu M.-L., Ramirez F.
      Gene 78:255-265(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
    9. "Nucleotide sequence of a cDNA coding for the amino-terminal region of human prepro alpha 1(III) collagen."
      Toman D., Ricca G., de Crombrugghe B.
      Nucleic Acids Res. 16:7201-7201(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-170 (ISOFORMS 1/2).
      Tissue: Placenta.
    10. "Nucleotide and amino acid sequences of the entire human alpha 1 (III) collagen."
      Janeczko R.A., Ramirez F.
      Nucleic Acids Res. 17:6742-6742(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-1225 (ISOFORM 1).
    11. "Covalent structure of collagen: amino acid sequence of cyanogen bromide peptides from the amino-terminal segment of type III collagen of human liver."
      Seyer J.M., Kang A.H.
      Biochemistry 16:1158-1164(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 168-398, HYDROXYLATION.
    12. Seyer J.M.
      Submitted (DEC-1977) to the PIR data bank
      Cited for: SEQUENCE REVISION.
    13. "Parental somatic and germ-line mosaicism for a multiexon deletion with unusual endpoints in a type III collagen (COL3A1) allele produces Ehlers-Danlos syndrome type IV in the heterozygous offspring."
      Milewicz D.M., Witz A.M., Smith A.C., Manchester D.K., Waldstein G., Byers P.H.
      Am. J. Hum. Genet. 53:62-70(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-194 (ISOFORMS 1/2).
    14. "Abnormal type III collagen produced by an exon-17-skipping mutation of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the extracellular matrix."
      Chiodo A.A., Sillence D.O., Cole W.G., Bateman J.F.
      Biochem. J. 311:939-943(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 302-423 (ISOFORMS 1/2).
    15. "Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new sequences."
      Minafra I.P., Andriolo M., Basirico L., Aquino A., Minafra S., Boutillon M.-M., van der Rest M.
      Biochem. Biophys. Res. Commun. 207:852-859(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 395-416; 579-595; 800-814 AND 1064-1079.
      Tissue: Colon carcinoma.
    16. "Covalent structure of collagen: amino acid sequence of five consecutive CNBr peptides from type III collagen of human liver."
      Seyer J.M., Kang A.H.
      Biochemistry 17:3404-3411(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 399-727.
    17. "G to T transversion at position +5 of a splice donor site causes skipping of the preceding exon in the type III procollagen transcripts of a patient with Ehlers-Danlos syndrome type IV."
      Lee B., Vitale E., Superti-Furga A., Steinmann B., Ramirez F.
      J. Biol. Chem. 266:5256-5259(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 537-605.
    18. "Covalent structure of collagen: amino acid sequence of alpha 1 (III)-CB5 from type III collagen of human liver."
      Seyer J.M., Mainardi C., Kang A.H.
      Biochemistry 19:1583-1589(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 728-964.
    19. "A base substitution at a splice site in the COL3A1 gene causes exon skipping and generates abnormal type III procollagen in a patient with Ehlers-Danlos syndrome type IV."
      Cole W.G., Chiodo A.A., Lamande S.R., Janeczko R., Ramirez F., Dahl H.-H.M., Chan D., Bateman J.F.
      J. Biol. Chem. 265:17070-17077(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 861-1015 (ISOFORM 1).
    20. "Human pro alpha 1(III) collagen: cDNA sequence for the 3' end."
      Mankoo B.S., Dalgleish R.
      Nucleic Acids Res. 16:2337-2337(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 950-1466 (ISOFORM 1), VARIANT GLN-1353.
    21. "Human type III collagen 'variant' is a cDNA cloning artefact."
      Molyneux K., Dalgleish R.
      Nucleic Acids Res. 16:11833-11833(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 1184.
    22. "Covalent structure of collagen: amino acid sequence of alpha 1(III)-CB9 from type III collagen of human liver."
      Seyer J.M., Kang A.H.
      Biochemistry 20:2621-2627(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 965-1200, HYDROXYLATION.
    23. "Molecular cloning and carboxyl-propeptide analysis of human type III procollagen."
      Loidl H.R., Brinker J.M., May M., Pihlajaniemi T., Morrow S., Rosenbloom J., Myers J.C.
      Nucleic Acids Res. 12:9383-9394(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1065-1466 (ISOFORM 1).
    24. "Human type III collagen gene expression is coordinately modulated with the type I collagen genes during fibroblast growth."
      Miskulin M., Dalgleish R., Kluve-Beckerman B., Rennard S.I., Tolstoshev P., Brantly M., Crystal R.G.
      Biochemistry 25:1408-1413(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1161-1200 (ISOFORMS 1/2).
    25. "Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2."
      Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.
      Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1165-1196 (ISOFORMS 1/2).
    26. "Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III) collagen. Partial characterization of the 3' end region of the gene."
      Chu M.-L., Weil D., de Wet W.J., Bernard M.P., Sippola M., Ramirez F.
      J. Biol. Chem. 260:4357-4363(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1122-1466 (ISOFORMS 1/2), VARIANT GLN-1353.
    27. "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
      Kuivaniemi H., Tromp G., Prockop D.J.
      Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    28. "Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries."
      Boudko S.P., Engel J., Okuyama K., Mizuno K., Bachinger H.P., Schumacher M.A.
      J. Biol. Chem. 283:32580-32589(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1158-1199, INTERCHAIN DISULFIDE BONDS.
    29. "Structural basis of fibrillar collagen trimerization and related genetic disorders."
      Bourhis J.M., Mariano N., Zhao Y., Harlos K., Exposito J.Y., Jones E.Y., Moali C., Aghajari N., Hulmes D.J.
      Nat. Struct. Mol. Biol. 19:1031-1036(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1222-1466, PROPEPTIDE, DISULFIDE BONDS, CALCIUM-BINDING SITES.
    30. "Sequencing of cDNA from 50 unrelated patients reveals that mutations in the triple-helical domain of type III procollagen are an infrequent cause of aortic aneurysms."
      Tromp G., Wu Y., Prockop D.J., Madhatheri S.L., Kleinert C., Earley J.J., Zhuang J., Noerrgaard O., Darling R.C., Abbott W.M., Cole C.W., Jaakkola P., Ryynaenen M., Pearce W.H., Yao J.S.T., Majamaa K., Smullens S.N., Gatalica Z.
      , Ferrell R.E., Jimenez S.A., Jackson C.E., Michels V.V., Kaye M., Kuivaniemi H.
      J. Clin. Invest. 91:2539-2545(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AAA ARG-303, VARIANT THR-668.
    31. Cited for: VARIANT THR-698.
    32. "A mutation in the gene for type III procollagen (COL3A1) in a family with aortic aneurysms."
      Kontusaari S., Tromp G., Kuivaniemi H., Romanic A.M., Prockop D.J.
      J. Clin. Invest. 86:1465-1473(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AAA ARG-786.
    33. "A 27-bp deletion from one allele of the type III collagen gene (COL3A1) in a large family with Ehlers-Danlos syndrome type IV."
      Richards A.J., Lloyd J.C., Narcisi P., Ward P.N., Nicholls A.C., De Paepe A., Pope F.M.
      Hum. Genet. 88:325-330(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 830-PRO--PRO-838 DEL.
    34. "The substitution of glycine 661 by arginine in type III collagen produces mutant molecules with different thermal stabilities and causes Ehlers-Danlos syndrome type IV."
      Richards A.J., Narcisi P., Lloyd J.C., Ferguson C., Pope F.M.
      J. Med. Genet. 30:690-693(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ARG-828.
    35. "A single base mutation that substitutes serine for glycine 790 of the alpha 1 (III) chain of type III procollagen exposes an arginine and causes Ehlers-Danlos syndrome IV."
      Tromp G., Kuivaniemi H., Shikata H., Prockop D.J.
      J. Biol. Chem. 264:1349-1352(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 SER-957.
    36. "Substitution of valine for glycine 793 in type III procollagen in Ehlers-Danlos syndrome type IV."
      Tromp G., de Paepe A., Nuytinck L., Madhatheri S.L., Kuivaniemi H.
      Hum. Mutat. 5:179-181(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 VAL-960.
    37. "A single base mutation in the gene for type III collagen (COL3A1) converts glycine 847 to glutamic acid in a family with Ehlers-Danlos syndrome type IV. An unaffected family member is mosaic for the mutation."
      Richards A.J., Ward P.N., Narcisi P., Nicholls A.C., Lloyd J.C., Pope F.M.
      Hum. Genet. 89:414-418(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 GLU-1014.
    38. "Single base mutation in the type III procollagen gene that converts the codon for glycine 883 to aspartate in a mild variant of Ehlers-Danlos syndrome IV."
      Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., Prockop D.J.
      J. Biol. Chem. 264:19313-19317(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ASP-1050.
    39. "Inheritance of an RNA splicing mutation (G+ 1 IVS20) in the type III procollagen gene (COL3A1) in a family having aortic aneurysms and easy bruisability: phenotypic overlap between familial arterial aneurysms and Ehlers-Danlos syndrome type IV."
      Kontusaari S., Tromp G., Kuivaniemi H., Ladda R.L., Prockop D.J.
      Am. J. Hum. Genet. 47:112-120(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AAA ARG-786.
    40. "Characterisation of a glycine to valine substitution at amino acid position 910 of the triple helical region of type III collagen in a patient with Ehlers-Danlos syndrome type IV."
      Richards A.J., Lloyd J.C., Ward P.N., de Paepe A., Narcisi P., Pope F.M.
      J. Med. Genet. 28:458-463(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 VAL-1077.
    41. "A COL3A1 glycine 1006 to glutamic acid substitution in a patient with Ehlers-Danlos syndrome type IV detected by denaturing gradient gel electrophoresis."
      Johnson P.H., Richards A.J., Pope F.M., Hopkinson D.A.
      J. Inherit. Metab. Dis. 15:426-430(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 GLU-1173.
    42. "Substitution of aspartate for glycine 1018 in the type III procollagen (COL3A1) gene causes type IV Ehlers-Danlos syndrome: the mutated allele is present in most blood leukocytes of the asymptomatic and mosaic mother."
      Kontusaari S., Tromp G., Kuivaniemi H., Stolle C.A., Pope F.M., Prockop D.J.
      Am. J. Hum. Genet. 51:497-507(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ASP-1185.
    43. "Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV."
      Narcisi P., Wu Y., Tromp G., Earley J.J., Richards A.J., Pope F.M., Kuivaniemi H.
      Am. J. Med. Genet. 46:278-283(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 GLU-1188.
    44. "Substitution of glycines 1000, 1003 and 1006 in type III collagen all cause the acrogeric form of EDS-IV, and destabilise the collagen triple helix."
      Richards A.J., Narcisi P., Lloyd J.C., Johnson P.H., Hopkinson D.A., Pope F.M.
      Matrix 13:47-47(1993)
      Cited for: VARIANTS EDS4 VAL-1167; ASP-1170 AND GLU-1173.
    45. "Exclusion of mutations in the gene for type III collagen (COL3A1) as a common cause of intracranial aneurysms or cervical artery dissections: results from sequence analysis of the coding sequences of type III collagen from 55 unrelated patients."
      Kuivaniemi H., Prockop D.J., Wu Y., Madhatheri S.L., Kleinert C., Earley J.J., Jokinen A., Stolle C.A., Majamaa K., Mylllylae V.V., Noerrgaard O., Schievink W.I., Mokri B., Fukawa O., Ter Berg J.W.M., de Paepe A., Lozano A.M., Leblanc R.
      , Ryynaenen M., Baxter B.T., Shikata H., Ferrell R.E., Tromp G.
      Neurology 43:2652-2658(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-602 AND LEU-635.
    46. "Substitution of glutamic acid for glycine 589 in the triple-helical domain of type III procollagen (COL3A1) in a family with variable phenotype of the Ehlers-Danlos syndrome type IV."
      Madhatheri S.L., Tromp G., Gustavson K.H., Kuivaniemi H.
      Hum. Mol. Genet. 3:511-512(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 GLU-756.
    47. "A family with Ehlers-Danlos syndrome type III/articular hypermobility syndrome has a glycine 637-to-serine substitution in type III collagen."
      Narcisi P., Richards A.J., Ferguson S.D., Pope F.M.
      Hum. Mol. Genet. 3:1617-1620(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS3 SER-804.
    48. "Single-strand conformation polymorphism (SSCP) analysis of the COL3A1 gene detects a mutation that results in the substitution of glycine 1009 to valine and causes severe Ehlers-Danlos syndrome type IV."
      Nuytinck L., De Paepe A., Renard J.P., Adriaens F., Leroy J.
      Hum. Mutat. 3:268-274(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 VAL-1176.
    49. "Marked heterogeneity in COL3A1 mutations that produce the EDS type IV phenotype."
      Goldstein J.A., Schwarze U., Witz A., Byers P.H.
      Matrix Biol. 14:392-393(1994)
      Cited for: VARIANTS EDS4 CYS-183; ARG-201; GLU-228; ARG-540; ARG-936; GLU-996; VAL-1071; ALA-1104; GLU-1182; VAL-1185; GLU-1188 AND ARG-1188.
    50. "Efficient strategy for the detection of mutations in acrogeric Ehlers-Danlos syndrome type IV."
      Johnson P.H., Richards A.J., Lloyd J.C., Pope F.M., Hopkinson D.A.
      Hum. Mutat. 6:336-342(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS4 ASP-909 AND ASP-939.
    51. "Ehlers-Danlos syndrome type IV caused by Gly400Glu, Gly595Cys and Gly1003Asp substitutions in collagen III: clinical features, biochemical screening, and molecular confirmation."
      Mackay K., Raghunath M., Superti-Furga A., Steinmann B., Dalgleish R.
      Clin. Genet. 49:286-295(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS4 GLU-567; CYS-762 AND ASP-1170.
    52. "Abnormal extracellular matrix in Ehlers-Danlos syndrome type IV due to the substitution of glycine 934 by glutamic acid in the triple helical domain of type III collagen."
      McGrory J., Weksberg R., Thorner P., Cole W.G.
      Clin. Genet. 50:442-445(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 GLU-1101.
    53. "A novel G499D substitution in the alpha 1(III) chain of type III collagen produces variable forms of Ehlers-Danlos syndrome type IV."
      McGrory J., Costa T., Cole W.G.
      Hum. Mutat. 7:59-60(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ASP-666.
    54. "A glycine (415)-to-serine substitution results in impaired secretion and decreased thermal stability of type III procollagen in a patient with Ehlers-Danlos syndrome type IV."
      Anderson D.W., Thakker-Varia S., Tromp G., Kuivaniemi H., Stolle C.A.
      Hum. Mutat. 9:62-63(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 SER-582.
    55. "Mutations in the COL3A1 gene result in the Ehlers-Danlos syndrome type IV and alterations in the size and distribution of the major collagen fibrils of the dermis."
      Smith L.T., Schwarze U., Goldstein J., Byers P.H.
      J. Invest. Dermatol. 108:241-247(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS4 CYS-183; ARG-201; GLU-228; ARG-540 AND ARG-936.
    56. "A type III collagen Gly559 to Arg helix mutation in Ehler's-Danlos syndrome type IV."
      Bateman J.F., Chiodo A.A., Weng Y.M., Chan D., Haan E.
      Hum. Mutat. Suppl. 1:S257-S259(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ARG-726.
    57. "COL3A1 mutation leading to acrogeria (Gottron Type)."
      Jansen T., de Paepe A., Luytinck N., Plewig G.
      Br. J. Dermatol. 142:178-180(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS-IV ARG-1173.
    58. "Characterization of 11 new mutations in COL3A1 of individuals with Ehlers-Danlos syndrome type IV: preliminary comparison of RNase cleavage, EMC and DHPLC assays."
      Giunta C., Steinmann B.
      Hum. Mutat. 16:176-177(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS4 ASP-204; ASP-210; ARG-264; ASP-327; ASP-1098 AND GLU-1173.
    59. "Clinical and genetic features of Ehlers-Danlos syndrome type IV, the vascular type."
      Pepin M., Schwarze U., Superti-Furga A., Byers P.H.
      N. Engl. J. Med. 342:673-680(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS4.
    60. "Ehlers-Danlos syndrome type IV with a unique point mutation in COL3A1 and familial phenotype of myocardial infarction without organic coronary stenosis."
      Nishiyama Y., Nejima J., Watanabe A., Kotani E., Sakai N., Hatamochi A., Shinkai H., Kiuchi K., Tamura K., Shimada T., Takano T., Katayama Y.
      J. Intern. Med. 249:103-108(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ASP-1044.
    61. "Ehlers-Danlos syndrome type IV: unusual congenital anomalies in a mother and son with a COL3A1 mutation and a normal collagen III protein profile."
      Kroes H.Y., Pals G., van Essen A.J.
      Clin. Genet. 63:224-227(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 ARG-297.
    62. Erratum
      Kroes H.Y., Pals G., van Essen A.J.
      Clin. Genet. 64:375-375(2003)
    63. "Neurological presentation of Ehlers-Danlos syndrome type IV in a family with parental mosaicism."
      Palmeri S., Mari F., Meloni I., Malandrini A., Ariani F., Villanova M., Pompilio A., Schwarze U., Byers P.H., Renieri A.
      Clin. Genet. 63:510-515(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS4 VAL-1050.
    64. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-420 AND CYS-1434.
    65. "Natural variation in four human collagen genes across an ethnically diverse population."
      Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., Klein T.E., Kwok P.Y.
      Genomics 91:307-314(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-679; THR-698; VAL-1205 AND GLN-1353.

    Entry informationi

    Entry nameiCO3A1_HUMAN
    AccessioniPrimary (citable) accession number: P02461
    Secondary accession number(s): D2JYH5
    , D3DPH4, P78429, Q15112, Q16403, Q53S91, Q541P8, Q6LDB3, Q6LDJ2, Q6LDJ3, Q7KZ56, Q8N6U4, Q9UC88, Q9UC89, Q9UC90, Q9UC91, R4N3C5, V9GZI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 170 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3