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P02461

- CO3A1_HUMAN

UniProt

P02461 - CO3A1_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP02461.
ExpressionAtlasiP02461. baseline and differential.
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. 9 interactions.
DIPiDIP-57177N.
IntActiP02461. 20 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 30-68, 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.
GeneTreeiENSGT00760000118776.
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

        10         20         30         40         50
MMSFVQKGSW LLLALLHPTI ILAQQEAVEG GCSHLGQSYA DRDVWKPEPC
60 70 80 90 100
QICVCDSGSV LCDDIICDDQ ELDCPNPEIP FGECCAVCPQ PPTAPTRPPN
110 120 130 140 150
GQGPQGPKGD PGPPGIPGRN GDPGIPGQPG SPGSPGPPGI CESCPTGPQN
160 170 180 190 200
YSPQYDSYDV KSGVAVGGLA GYPGPAGPPG PPGPPGTSGH PGSPGSPGYQ
210 220 230 240 250
GPPGEPGQAG PSGPPGPPGA IGPSGPAGKD GESGRPGRPG ERGLPGPPGI
260 270 280 290 300
KGPAGIPGFP GMKGHRGFDG RNGEKGETGA PGLKGENGLP GENGAPGPMG
310 320 330 340 350
PRGAPGERGR PGLPGAAGAR GNDGARGSDG QPGPPGPPGT AGFPGSPGAK
360 370 380 390 400
GEVGPAGSPG SNGAPGQRGE PGPQGHAGAQ GPPGPPGING SPGGKGEMGP
410 420 430 440 450
AGIPGAPGLM GARGPPGPAG ANGAPGLRGG AGEPGKNGAK GEPGPRGERG
460 470 480 490 500
EAGIPGVPGA KGEDGKDGSP GEPGANGLPG AAGERGAPGF RGPAGPNGIP
510 520 530 540 550
GEKGPAGERG APGPAGPRGA AGEPGRDGVP GGPGMRGMPG SPGGPGSDGK
560 570 580 590 600
PGPPGSQGES GRPGPPGPSG PRGQPGVMGF PGPKGNDGAP GKNGERGGPG
610 620 630 640 650
GPGPQGPPGK NGETGPQGPP GPTGPGGDKG DTGPPGPQGL QGLPGTGGPP
660 670 680 690 700
GENGKPGEPG PKGDAGAPGA PGGKGDAGAP GERGPPGLAG APGLRGGAGP
710 720 730 740 750
PGPEGGKGAA GPPGPPGAAG TPGLQGMPGE RGGLGSPGPK GDKGEPGGPG
760 770 780 790 800
ADGVPGKDGP RGPTGPIGPP GPAGQPGDKG EGGAPGLPGI AGPRGSPGER
810 820 830 840 850
GETGPPGPAG FPGAPGQNGE PGGKGERGAP GEKGEGGPPG VAGPPGGSGP
860 870 880 890 900
AGPPGPQGVK GERGSPGGPG AAGFPGARGL PGPPGSNGNP GPPGPSGSPG
910 920 930 940 950
KDGPPGPAGN TGAPGSPGVS GPKGDAGQPG EKGSPGAQGP PGAPGPLGIA
960 970 980 990 1000
GITGARGLAG PPGMPGPRGS PGPQGVKGES GKPGANGLSG ERGPPGPQGL
1010 1020 1030 1040 1050
PGLAGTAGEP GRDGNPGSDG LPGRDGSPGG KGDRGENGSP GAPGAPGHPG
1060 1070 1080 1090 1100
PPGPVGPAGK SGDRGESGPA GPAGAPGPAG SRGAPGPQGP RGDKGETGER
1110 1120 1130 1140 1150
GAAGIKGHRG FPGNPGAPGS PGPAGQQGAI GSPGPAGPRG PVGPSGPPGK
1160 1170 1180 1190 1200
DGTSGHPGPI GPPGPRGNRG ERGSEGSPGH PGQPGPPGPP GAPGPCCGGV
1210 1220 1230 1240 1250
GAAAIAGIGG EKAGGFAPYY GDEPMDFKIN TDEIMTSLKS VNGQIESLIS
1260 1270 1280 1290 1300
PDGSRKNPAR NCRDLKFCHP ELKSGEYWVD PNQGCKLDAI KVFCNMETGE
1310 1320 1330 1340 1350
TCISANPLNV PRKHWWTDSS AEKKHVWFGE SMDGGFQFSY GNPELPEDVL
1360 1370 1380 1390 1400
DVHLAFLRLL SSRASQNITY HCKNSIAYMD QASGNVKKAL KLMGSNEGEF
1410 1420 1430 1440 1450
KAEGNSKFTY TVLEDGCTKH TGEWSKTVFE YRTRKAVRLP IVDIAPYDIG
1460
GPDQEFGVDV GPVCFL
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]
ENST00000317840; ENSP00000315243; ENSG00000168542. [P02461-2]
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 30-68, 1249-1466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107678. 9 interactions.
DIPi DIP-57177N.
IntActi P02461. 20 interactions.
MINTi MINT-7299332.

Chemistry

ChEMBLi CHEMBL2364188.
DrugBanki DB00048. Collagenase.

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 ]
ENST00000317840 ; ENSP00000315243 ; ENSG00000168542 . [P02461-2 ]
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.
GeneTreei ENSGT00760000118776.
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

Bgeei P02461.
ExpressionAtlasi P02461. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 171 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

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