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P12111

- CO6A3_HUMAN

UniProt

P12111 - CO6A3_HUMAN

Protein

Collagen alpha-3(VI) chain

Gene

COL6A3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 5 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Collagen VI acts as a cell-binding protein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei3122 – 31232Reactive bond

    GO - Molecular functioni

    1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell adhesion Source: UniProtKB-KW
    3. collagen catabolic process Source: Reactome
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. muscle organ development Source: ProtInc

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_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_163906. ECM proteoglycans.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Protein family/group databases

    MEROPSiI02.968.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-3(VI) chain
    Gene namesi
    Name:COL6A3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2213. COL6A3.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type VI trimer Source: ProtInc
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular matrix Source: MGI
    4. extracellular region Source: Reactome
    5. extracellular space Source: BHF-UCL
    6. extracellular vesicular exosome Source: UniProt
    7. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    8. sarcolemma Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Bethlem myopathy (BM) [MIM:158810]: A benign autosomal dominant proximal myopathy characterized by early childhood onset and joint contractures most frequently affecting the elbows and ankles.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti677 – 6771R → H in BM; unknown pathological significance. 2 Publications
    Corresponds to variant rs35227432 [ dbSNP | Ensembl ].
    VAR_058245
    Natural varianti1014 – 10141K → E in BM. 1 Publication
    VAR_058248
    Natural varianti1386 – 13861E → K in BM. 1 Publication
    Corresponds to variant rs146092501 [ dbSNP | Ensembl ].
    VAR_058250
    Natural varianti1467 – 14671N → D in BM. 1 Publication
    VAR_058252
    Natural varianti1679 – 16791G → E in BM. 2 Publications
    VAR_001910
    Natural varianti1726 – 17261L → R in BM. 1 Publication
    VAR_058257
    Natural varianti1985 – 19851V → M in BM. 1 Publication
    VAR_058258
    Natural varianti2047 – 20471G → D in BM. 1 Publication
    VAR_058259
    Natural varianti2056 – 20561G → R in BM. 1 Publication
    VAR_058260
    Natural varianti2080 – 20801G → D in BM. 1 Publication
    VAR_058261
    Natural varianti2941 – 29411A → V in BM. 1 Publication
    Corresponds to variant rs11903206 [ dbSNP | Ensembl ].
    VAR_058264
    Ullrich congenital muscular dystrophy (UCMD) [MIM:254090]: UCMD is a congenital myopathy characterized by muscle weakness and multiple joint contractures, generally noted at birth or early infancy. The clinical course is more severe than in Bethlem myopathy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1064 – 10641R → Q in UCMD. 1 Publication
    Corresponds to variant rs112638391 [ dbSNP | Ensembl ].
    VAR_058249
    Natural varianti1395 – 13951R → Q in UCMD. 1 Publication
    Corresponds to variant rs80272723 [ dbSNP | Ensembl ].
    VAR_058251
    Natural varianti1674 – 16741D → N in UCMD. 1 Publication
    VAR_058255

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi158810. phenotype.
    254090. phenotype.
    Orphaneti610. Bethlem myopathy.
    75840. Congenital muscular dystrophy, Ullrich type.
    PharmGKBiPA26729.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 31773152Collagen alpha-3(VI) chainPRO_0000005847Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei26 – 261Pyrrolidone carboxylic acidCurated
    Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Modified residuei433 – 4331Phosphothreonine1 Publication
    Glycosylationi2079 – 20791N-linked (GlcNAc...)1 Publication
    Disulfide bondi2087 – 2087InterchainPROSITE-ProRule annotation
    Modified residuei2100 – 210014-hydroxyproline1 Publication
    Modified residuei2103 – 210315-hydroxylysine; alternate1 Publication
    Glycosylationi2103 – 21031O-linked (Gal...); alternate
    Modified residuei2206 – 220614-hydroxyproline1 Publication
    Modified residuei2209 – 220915-hydroxylysine; alternate1 Publication
    Glycosylationi2209 – 22091O-linked (Gal...); alternate
    Modified residuei2212 – 221215-hydroxylysine; alternate1 Publication
    Glycosylationi2212 – 22121O-linked (Gal...); alternate
    Modified residuei2239 – 223914-hydroxyproline1 Publication
    Modified residuei2316 – 231614-hydroxyproline1 Publication
    Modified residuei2319 – 231914-hydroxyproline1 Publication
    Modified residuei2322 – 232215-hydroxylysine; alternate1 Publication
    Glycosylationi2322 – 23221O-linked (Gal...); alternate
    Glycosylationi2331 – 23311N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2337 – 233715-hydroxylysine; alternate1 Publication
    Glycosylationi2337 – 23371O-linked (Gal...); alternate
    Glycosylationi2558 – 25581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2677 – 26771N-linked (GlcNAc...)2 Publications
    Glycosylationi2861 – 28611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3037 – 30371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3112 ↔ 3162PROSITE-ProRule annotation
    Disulfide bondi3121 ↔ 3145PROSITE-ProRule annotation
    Disulfide bondi3137 ↔ 3158PROSITE-ProRule annotation

    Post-translational modificationi

    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication
    The N-terminus is blocked.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP12111.
    PaxDbiP12111.
    PRIDEiP12111.

    PTM databases

    PhosphoSiteiP12111.

    Expressioni

    Gene expression databases

    ArrayExpressiP12111.
    BgeeiP12111.
    CleanExiHS_COL6A3.
    GenevestigatoriP12111.

    Organism-specific databases

    HPAiHPA010080.

    Interactioni

    Subunit structurei

    Trimers composed of three different chains: alpha-1(VI), alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI).

    Protein-protein interaction databases

    IntActiP12111. 4 interactions.
    MINTiMINT-4053347.
    STRINGi9606.ENSP00000295550.

    Structurei

    Secondary structure

    1
    3177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3110 – 31134
    Beta strandi3120 – 31223
    Beta strandi3125 – 31317
    Turni3132 – 31354
    Beta strandi3136 – 31427
    Beta strandi3144 – 31463
    Beta strandi3152 – 31543
    Helixi3155 – 31628

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KNTX-ray1.60A3108-3165[»]
    1KTHX-ray0.95A3108-3165[»]
    1KUNNMR-A3108-3165[»]
    2KNTX-ray1.20A3108-3165[»]
    ProteinModelPortaliP12111.
    SMRiP12111. Positions 1027-1222, 3108-3165.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12111.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 213175VWFA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini242 – 419178VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini445 – 620176VWFA 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini639 – 816178VWFA 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini837 – 1009173VWFA 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1029 – 1205177VWFA 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1233 – 1404172VWFA 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1436 – 1609174VWFA 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1639 – 1812174VWFA 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1838 – 2024187VWFA 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2038 – 209760Collagen-like 1Add
    BLAST
    Domaini2104 – 216360Collagen-like 2Add
    BLAST
    Domaini2174 – 223360Collagen-like 3Add
    BLAST
    Domaini2249 – 230052Collagen-like 4Add
    BLAST
    Domaini2314 – 237360Collagen-like 5Add
    BLAST
    Domaini2402 – 2581180VWFA 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2619 – 2815197VWFA 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini2991 – 308595Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini3112 – 316251BPTI/Kunitz inhibitorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 20382013Nonhelical regionAdd
    BLAST
    Regioni2039 – 2375337Triple-helical regionAdd
    BLAST
    Regioni2376 – 3177802Nonhelical regionAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2040 – 20423Cell attachment site
    Motifi2136 – 21383Cell attachment site
    Motifi2148 – 21503Cell attachment site
    Motifi2154 – 21563Cell attachment site
    Motifi2370 – 23723Cell attachment site

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2863 – 289836Thr-richAdd
    BLAST
    Compositional biasi2908 – 298376Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the type VI collagen family.Curated
    Contains 1 BPTI/Kunitz inhibitor domain.PROSITE-ProRule annotation
    Contains 5 collagen-like domains.Curated
    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 12 VWFA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG237718.
    HOGENOMiHOG000015249.
    HOVERGENiHBG051052.
    InParanoidiP12111.
    KOiK06238.
    OMAiGRHANTK.
    OrthoDBiEOG7N0C3R.
    PhylomeDBiP12111.
    TreeFamiTF337483.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.40.50.410. 12 hits.
    4.10.410.10. 1 hit.
    InterProiIPR008160. Collagen.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01391. Collagen. 1 hit.
    PF00014. Kunitz_BPTI. 1 hit.
    PF00092. VWA. 11 hits.
    [Graphical view]
    PRINTSiPR00759. BASICPTASE.
    SMARTiSM00060. FN3. 1 hit.
    SM00131. KU. 1 hit.
    SM00327. VWA. 12 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF53300. SSF53300. 12 hits.
    SSF57362. SSF57362. 1 hit.
    PROSITEiPS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS50234. VWFA. 12 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12111-1) [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

    MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI     50
    GEEHFQLVRE FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ 100
    EVLSHISNMS YIGGTNQTGK GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT 150
    DGHSKDGLAL PSAELKSADV NVFAIGVEDA DEGALKEIAS EPLNMHMFNL 200
    ENFTSLHDIV GNLVSCVHSS VSPERAGDTE TLKDITAQDS ADIIFLIDGS 250
    NNTGSVNFAV ILDFLVNLLE KLPIGTQQIR VGVVQFSDEP RTMFSLDTYS 300
    TKAQVLGAVK ALGFAGGELA NIGLALDFVV ENHFTRAGGS RVEEGVPQVL 350
    VLISAGPSSD EIRYGVVALK QASVFSFGLG AQAASRAELQ HIATDDNLVF 400
    TVPEFRSFGD LQEKLLPYIV GVAQRHIVLK PPTIVTQVIE VNKRDIVFLV 450
    DGSSALGLAN FNAIRDFIAK VIQRLEIGQD LIQVAVAQYA DTVRPEFYFN 500
    THPTKREVIT AVRKMKPLDG SALYTGSALD FVRNNLFTSS AGYRAAEGIP 550
    KLLVLITGGK SLDEISQPAQ ELKRSSIMAF AIGNKGADQA ELEEIAFDSS 600
    LVFIPAEFRA APLQGMLPGL LAPLRTLSGT PEVHSNKRDI IFLLDGSANV 650
    GKTNFPYVRD FVMNLVNSLD IGNDNIRVGL VQFSDTPVTE FSLNTYQTKS 700
    DILGHLRQLQ LQGGSGLNTG SALSYVYANH FTEAGGSRIR EHVPQLLLLL 750
    TAGQSEDSYL QAANALTRAG ILTFCVGASQ ANKAELEQIA FNPSLVYLMD 800
    DFSSLPALPQ QLIQPLTTYV SGGVEEVPLA QPESKRDILF LFDGSANLVG 850
    QFPVVRDFLY KIIDELNVKP EGTRIAVAQY SDDVKVESRF DEHQSKPEIL 900
    NLVKRMKIKT GKALNLGYAL DYAQRYIFVK SAGSRIEDGV LQFLVLLVAG 950
    RSSDRVDGPA SNLKQSGVVP FIFQAKNADP AELEQIVLSP AFILAAESLP 1000
    KIGDLHPQIV NLLKSVHNGA PAPVSGEKDV VFLLDGSEGV RSGFPLLKEF 1050
    VQRVVESLDV GQDRVRVAVV QYSDRTRPEF YLNSYMNKQD VVNAVRQLTL 1100
    LGGPTPNTGA ALEFVLRNIL VSSAGSRITE GVPQLLIVLT ADRSGDDVRN 1150
    PSVVVKRGGA VPIGIGIGNA DITEMQTISF IPDFAVAIPT FRQLGTVQQV 1200
    ISERVTQLTR EELSRLQPVL QPLPSPGVGG KRDVVFLIDG SQSAGPEFQY 1250
    VRTLIERLVD YLDVGFDTTR VAVIQFSDDP KVEFLLNAHS SKDEVQNAVQ 1300
    RLRPKGGRQI NVGNALEYVS RNIFKRPLGS RIEEGVPQFL VLISSGKSDD 1350
    EVDDPAVELK QFGVAPFTIA RNADQEELVK ISLSPEYVFS VSTFRELPSL 1400
    EQKLLTPITT LTSEQIQKLL ASTRYPPPAV ESDAADIVFL IDSSEGVRPD 1450
    GFAHIRDFVS RIVRRLNIGP SKVRVGVVQF SNDVFPEFYL KTYRSQAPVL 1500
    DAIRRLRLRG GSPLNTGKAL EFVARNLFVK SAGSRIEDGV PQHLVLVLGG 1550
    KSQDDVSRFA QVIRSSGIVS LGVGDRNIDR TELQTITNDP RLVFTVREFR 1600
    ELPNIEERIM NSFGPSAATP APPGVDTPPP SRPEKKKADI VFLLDGSINF 1650
    RRDSFQEVLR FVSEIVDTVY EDGDSIQVGL VQYNSDPTDE FFLKDFSTKR 1700
    QIIDAINKVV YKGGRHANTK VGLEHLRVNH FVPEAGSRLD QRVPQIAFVI 1750
    TGGKSVEDAQ DVSLALTQRG VKVFAVGVRN IDSEEVGKIA SNSATAFRVG 1800
    NVQELSELSE QVLETLHDAM HETLCPGVTD AAKACNLDVI LGFDGSRDQN 1850
    VFVAQKGFES KVDAILNRIS QMHRVSCSGG RSPTVRVSVV ANTPSGPVEA 1900
    FDFDEYQPEM LEKFRNMRSQ HPYVLTEDTL KVYLNKFRQS SPDSVKVVIH 1950
    FTDGADGDLA DLHRASENLR QEGVRALILV GLERVVNLER LMHLEFGRGF 2000
    MYDRPLRLNL LDLDYELAEQ LDNIAEKACC GVPCKCSGQR GDRGPIGSIG 2050
    PKGIPGEDGY RGYPGDEGGP GERGPPGVNG TQGFQGCPGQ RGVKGSRGFP 2100
    GEKGEVGEIG LDGLDGEDGD KGLPGSSGEK GNPGRRGDKG PRGEKGERGD 2150
    VGIRGDPGNP GQDSQERGPK GETGDLGPMG VPGRDGVPGG PGETGKNGGF 2200
    GRRGPPGAKG NKGGPGQPGF EGEQGTRGAQ GPAGPAGPPG LIGEQGISGP 2250
    RGSGGAAGAP GERGRTGPLG RKGEPGEPGP KGGIGNRGPR GETGDDGRDG 2300
    VGSEGRRGKK GERGFPGYPG PKGNPGEPGL NGTTGPKGIR GRRGNSGPPG 2350
    IVGQKGDPGY PGPAGPKGNR GDSIDQCALI QSIKDKCPCC YGPLECPVFP 2400
    TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY 2450
    NNEVTTEIRF ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK 2500
    RVRNGFLMRK VAVFFSNTPT RASPQLREAV LKLSDAGITP LFLTRQEDRQ 2550
    LINALQINNT AVGHALVLPA GRDLTDFLEN VLTCHVCLDI CNIDPSCGFG 2600
    SWRPSFRDRR AAGSDVDIDM AFILDSAETT TLFQFNEMKK YIAYLVRQLD 2650
    MSPDPKASQH FARVAVVQHA PSESVDNASM PPVKVEFSLT DYGSKEKLVD 2700
    FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGEVPEQ 2750
    QLEEAQRVIL QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK 2800
    STELNEEPLM RFGRLLPSFV SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK 2850
    FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT KPVTTTTKPV TTTTKPVTII 2900
    NQPSVKPAAA KPAPAKPVAA KPVATKMATV RPPVAVKPAT AAKPVAAKPA 2950
    AVRPPAAAAA KPVATKPEVP RPQAAKPAAT KPATTKPMVK MSREVQVFEI 3000
    TENSAKLHWE RAEPPGPYFY DLTVTSAHDQ SLVLKQNLTV TDRVIGGLLA 3050
    GQTYHVAVVC YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS 3100
    TEPLALTETD ICKLPKDEGT CRDFILKWYY DPNTKSCARF WYGGCGGNEN 3150
    KFGSQKECEK VCAPVLAKPG VISVMGT 3177
    Length:3,177
    Mass (Da):343,669
    Last modified:November 2, 2010 - v5
    Checksum:i56D54CAC4FBB30AF
    GO
    Isoform 2 (identifier: P12111-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-236: Missing.

    Show »
    Length:2,971
    Mass (Da):321,354
    Checksum:iBA575D6B63627175
    GO
    Isoform 3 (identifier: P12111-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-236: Missing.
         237-437: Missing.
         1429-1443: AVESDAADIVFLIDS → GEMGASEVLLGAFSI
         1444-3177: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,036
    Mass (Da):113,224
    Checksum:i9614E1488D7CEE0B
    GO
    Isoform 4 (identifier: P12111-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-437: Missing.
         633-832: Missing.

    Show »
    Length:2,570
    Mass (Da):278,203
    Checksum:i952E61BE4F03322C
    GO
    Isoform 5 (identifier: P12111-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-236: Missing.
         1429-1443: AVESDAADIVFLIDS → GEMGASEVLLGAFSI
         1444-3177: Missing.

    Show »
    Length:1,237
    Mass (Da):134,707
    Checksum:i8B77D527A7B34B6D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1282QS → AK in AAB24261. (PubMed:1339440)Curated
    Sequence conflicti137 – 1371R → L in AAB24261. (PubMed:1339440)Curated
    Sequence conflicti381 – 3811A → V in BAG65607. (PubMed:14702039)Curated
    Sequence conflicti608 – 6081F → S in BAG65607. (PubMed:14702039)Curated
    Sequence conflicti885 – 8851K → E in AAI44596. (PubMed:15489334)Curated
    Sequence conflicti885 – 8851K → E in AAI50626. (PubMed:15489334)Curated
    Sequence conflicti1282 – 12821V → A in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti1353 – 13542DD → VV in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2157 – 21571P → R in CAA29557. (PubMed:3665927)Curated
    Sequence conflicti2257 – 22571A → R in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2257 – 22571A → R in M20778. (PubMed:3198591)Curated
    Sequence conflicti2287 – 22871R → P in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2287 – 22871R → P in M20778. (PubMed:3198591)Curated
    Sequence conflicti2357 – 23571D → R in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2357 – 23571D → R in M20778. (PubMed:3198591)Curated
    Sequence conflicti2367 – 23671K → R in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2367 – 23671K → R in M20778. (PubMed:3198591)Curated
    Sequence conflicti2441 – 24411R → T in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2956 – 29561Missing in CAA36267. (PubMed:1689238)Curated
    Sequence conflicti2992 – 29921S → L in CAA36267. (PubMed:1689238)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti411 – 4111L → V.1 Publication
    Corresponds to variant rs113716915 [ dbSNP | Ensembl ].
    VAR_058242
    Natural varianti491 – 4911D → H.1 Publication
    Corresponds to variant rs112010940 [ dbSNP | Ensembl ].
    VAR_058243
    Natural varianti492 – 4921T → S.1 Publication
    Corresponds to variant rs113897824 [ dbSNP | Ensembl ].
    VAR_058244
    Natural varianti538 – 5381T → M.
    Corresponds to variant rs34741387 [ dbSNP | Ensembl ].
    VAR_047279
    Natural varianti659 – 6591R → H.
    Corresponds to variant rs36092870 [ dbSNP | Ensembl ].
    VAR_047280
    Natural varianti677 – 6771R → H in BM; unknown pathological significance. 2 Publications
    Corresponds to variant rs35227432 [ dbSNP | Ensembl ].
    VAR_058245
    Natural varianti807 – 8071A → T.1 Publication
    VAR_058246
    Natural varianti830 – 8301A → S.1 Publication
    Corresponds to variant rs77181645 [ dbSNP | Ensembl ].
    VAR_058247
    Natural varianti886 – 8861V → E.
    Corresponds to variant rs9630964 [ dbSNP | Ensembl ].
    VAR_047281
    Natural varianti1014 – 10141K → E in BM. 1 Publication
    VAR_058248
    Natural varianti1064 – 10641R → Q in UCMD. 1 Publication
    Corresponds to variant rs112638391 [ dbSNP | Ensembl ].
    VAR_058249
    Natural varianti1088 – 10881K → Q.1 Publication
    Corresponds to variant rs11896521 [ dbSNP | Ensembl ].
    VAR_047282
    Natural varianti1386 – 13861E → K in BM. 1 Publication
    Corresponds to variant rs146092501 [ dbSNP | Ensembl ].
    VAR_058250
    Natural varianti1395 – 13951R → Q in UCMD. 1 Publication
    Corresponds to variant rs80272723 [ dbSNP | Ensembl ].
    VAR_058251
    Natural varianti1467 – 14671N → D in BM. 1 Publication
    VAR_058252
    Natural varianti1576 – 15761R → Q.2 Publications
    Corresponds to variant rs61729839 [ dbSNP | Ensembl ].
    VAR_058253
    Natural varianti1632 – 16321R → Q.1 Publication
    Corresponds to variant rs111231885 [ dbSNP | Ensembl ].
    VAR_058254
    Natural varianti1674 – 16741D → N in UCMD. 1 Publication
    VAR_058255
    Natural varianti1679 – 16791G → E in BM. 2 Publications
    VAR_001910
    Natural varianti1687 – 16871P → S.1 Publication
    Corresponds to variant rs35273032 [ dbSNP | Ensembl ].
    VAR_058256
    Natural varianti1726 – 17261L → R in BM. 1 Publication
    VAR_058257
    Natural varianti1985 – 19851V → M in BM. 1 Publication
    VAR_058258
    Natural varianti2047 – 20471G → D in BM. 1 Publication
    VAR_058259
    Natural varianti2056 – 20561G → R in BM. 1 Publication
    VAR_058260
    Natural varianti2080 – 20801G → D in BM. 1 Publication
    VAR_058261
    Natural varianti2218 – 22181P → L.1 Publication
    Corresponds to variant rs36117715 [ dbSNP | Ensembl ].
    VAR_047283
    Natural varianti2431 – 24311D → V.2 Publications
    VAR_058262
    Natural varianti2453 – 24531E → K.1 Publication
    VAR_058263
    Natural varianti2805 – 28051N → T.
    Corresponds to variant rs35848091 [ dbSNP | Ensembl ].
    VAR_047284
    Natural varianti2831 – 28311D → H.3 Publications
    Corresponds to variant rs36104025 [ dbSNP | Ensembl ].
    VAR_001911
    Natural varianti2927 – 29271M → T.1 Publication
    Corresponds to variant rs6728818 [ dbSNP | Ensembl ].
    VAR_047285
    Natural varianti2941 – 29411A → V in BM. 1 Publication
    Corresponds to variant rs11903206 [ dbSNP | Ensembl ].
    VAR_058264
    Natural varianti2988 – 29881M → V.2 Publications
    Corresponds to variant rs11690358 [ dbSNP | Ensembl ].
    VAR_047286
    Natural varianti3012 – 30121A → P.1 Publication
    Corresponds to variant rs2270669 [ dbSNP | Ensembl ].
    VAR_047287
    Natural varianti3069 – 30691T → I.1 Publication
    Corresponds to variant rs1131296 [ dbSNP | Ensembl ].
    VAR_047288

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei31 – 437407Missing in isoform 4. 1 PublicationVSP_045718Add
    BLAST
    Alternative sequencei31 – 236206Missing in isoform 2, isoform 3 and isoform 5. 1 PublicationVSP_001172Add
    BLAST
    Alternative sequencei237 – 437201Missing in isoform 3. 1 PublicationVSP_043434Add
    BLAST
    Alternative sequencei633 – 832200Missing in isoform 4. 1 PublicationVSP_045719Add
    BLAST
    Alternative sequencei1429 – 144315AVESD…FLIDS → GEMGASEVLLGAFSI in isoform 3 and isoform 5. 1 PublicationVSP_043435Add
    BLAST
    Alternative sequencei1444 – 31771734Missing in isoform 3 and isoform 5. 1 PublicationVSP_043436Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52022 mRNA. Translation: CAA36267.1.
    AK092021 mRNA. Translation: BAG52467.1.
    AK304870 mRNA. Translation: BAG65607.1.
    AC112715 Genomic DNA. Translation: AAY14906.1.
    AC112721 Genomic DNA. Translation: AAY24135.1.
    BC144595 mRNA. Translation: AAI44596.1.
    BC150625 mRNA. Translation: AAI50626.1.
    S49432 mRNA. Translation: AAB24261.1.
    M20778 mRNA. No translation available.
    X06196 mRNA. Translation: CAA29557.1.
    M27449 mRNA. Translation: AAA52057.1.
    CCDSiCCDS33409.1. [P12111-2]
    CCDS33410.2. [P12111-4]
    CCDS33411.2. [P12111-5]
    CCDS33412.1. [P12111-1]
    CCDS54439.1. [P12111-3]
    PIRiA59140. CGHU3A.
    RefSeqiNP_004360.2. NM_004369.3. [P12111-1]
    NP_476505.3. NM_057164.4. [P12111-3]
    NP_476506.3. NM_057165.4. [P12111-5]
    NP_476507.3. NM_057166.4. [P12111-4]
    NP_476508.2. NM_057167.3. [P12111-2]
    UniGeneiHs.233240.

    Genome annotation databases

    EnsembliENST00000295550; ENSP00000295550; ENSG00000163359. [P12111-1]
    ENST00000353578; ENSP00000315873; ENSG00000163359. [P12111-2]
    ENST00000392003; ENSP00000375860; ENSG00000163359. [P12111-3]
    ENST00000392004; ENSP00000375861; ENSG00000163359. [P12111-5]
    ENST00000409809; ENSP00000386844; ENSG00000163359. [P12111-2]
    ENST00000472056; ENSP00000418285; ENSG00000163359. [P12111-4]
    GeneIDi1293.
    KEGGihsa:1293.
    UCSCiuc002vwl.2. human. [P12111-1]
    uc002vwo.2. human. [P12111-2]
    uc002vwr.3. human. [P12111-3]
    uc010znj.1. human.

    Polymorphism databases

    DMDMi311033499.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52022 mRNA. Translation: CAA36267.1 .
    AK092021 mRNA. Translation: BAG52467.1 .
    AK304870 mRNA. Translation: BAG65607.1 .
    AC112715 Genomic DNA. Translation: AAY14906.1 .
    AC112721 Genomic DNA. Translation: AAY24135.1 .
    BC144595 mRNA. Translation: AAI44596.1 .
    BC150625 mRNA. Translation: AAI50626.1 .
    S49432 mRNA. Translation: AAB24261.1 .
    M20778 mRNA. No translation available.
    X06196 mRNA. Translation: CAA29557.1 .
    M27449 mRNA. Translation: AAA52057.1 .
    CCDSi CCDS33409.1. [P12111-2 ]
    CCDS33410.2. [P12111-4 ]
    CCDS33411.2. [P12111-5 ]
    CCDS33412.1. [P12111-1 ]
    CCDS54439.1. [P12111-3 ]
    PIRi A59140. CGHU3A.
    RefSeqi NP_004360.2. NM_004369.3. [P12111-1 ]
    NP_476505.3. NM_057164.4. [P12111-3 ]
    NP_476506.3. NM_057165.4. [P12111-5 ]
    NP_476507.3. NM_057166.4. [P12111-4 ]
    NP_476508.2. NM_057167.3. [P12111-2 ]
    UniGenei Hs.233240.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KNT X-ray 1.60 A 3108-3165 [» ]
    1KTH X-ray 0.95 A 3108-3165 [» ]
    1KUN NMR - A 3108-3165 [» ]
    2KNT X-ray 1.20 A 3108-3165 [» ]
    ProteinModelPortali P12111.
    SMRi P12111. Positions 1027-1222, 3108-3165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P12111. 4 interactions.
    MINTi MINT-4053347.
    STRINGi 9606.ENSP00000295550.

    Chemistry

    ChEMBLi CHEMBL2364188.

    Protein family/group databases

    MEROPSi I02.968.

    PTM databases

    PhosphoSitei P12111.

    Polymorphism databases

    DMDMi 311033499.

    Proteomic databases

    MaxQBi P12111.
    PaxDbi P12111.
    PRIDEi P12111.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295550 ; ENSP00000295550 ; ENSG00000163359 . [P12111-1 ]
    ENST00000353578 ; ENSP00000315873 ; ENSG00000163359 . [P12111-2 ]
    ENST00000392003 ; ENSP00000375860 ; ENSG00000163359 . [P12111-3 ]
    ENST00000392004 ; ENSP00000375861 ; ENSG00000163359 . [P12111-5 ]
    ENST00000409809 ; ENSP00000386844 ; ENSG00000163359 . [P12111-2 ]
    ENST00000472056 ; ENSP00000418285 ; ENSG00000163359 . [P12111-4 ]
    GeneIDi 1293.
    KEGGi hsa:1293.
    UCSCi uc002vwl.2. human. [P12111-1 ]
    uc002vwo.2. human. [P12111-2 ]
    uc002vwr.3. human. [P12111-3 ]
    uc010znj.1. human.

    Organism-specific databases

    CTDi 1293.
    GeneCardsi GC02M238248.
    GeneReviewsi COL6A3.
    H-InvDB HIX0002952.
    HGNCi HGNC:2213. COL6A3.
    HPAi HPA010080.
    MIMi 120250. gene.
    158810. phenotype.
    254090. phenotype.
    neXtProti NX_P12111.
    Orphaneti 610. Bethlem myopathy.
    75840. Congenital muscular dystrophy, Ullrich type.
    PharmGKBi PA26729.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237718.
    HOGENOMi HOG000015249.
    HOVERGENi HBG051052.
    InParanoidi P12111.
    KOi K06238.
    OMAi GRHANTK.
    OrthoDBi EOG7N0C3R.
    PhylomeDBi P12111.
    TreeFami TF337483.

    Enzyme and pathway databases

    Reactomei 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_163906. ECM proteoglycans.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Miscellaneous databases

    ChiTaRSi COL6A3. human.
    EvolutionaryTracei P12111.
    GeneWikii COL6A3.
    GenomeRNAii 1293.
    NextBioi 5239.
    PROi P12111.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12111.
    Bgeei P12111.
    CleanExi HS_COL6A3.
    Genevestigatori P12111.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.40.50.410. 12 hits.
    4.10.410.10. 1 hit.
    InterProi IPR008160. Collagen.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR002223. Prot_inh_Kunz-m.
    IPR020901. Prtase_inh_Kunz-CS.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01391. Collagen. 1 hit.
    PF00014. Kunitz_BPTI. 1 hit.
    PF00092. VWA. 11 hits.
    [Graphical view ]
    PRINTSi PR00759. BASICPTASE.
    SMARTi SM00060. FN3. 1 hit.
    SM00131. KU. 1 hit.
    SM00327. VWA. 12 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF53300. SSF53300. 12 hits.
    SSF57362. SSF57362. 1 hit.
    PROSITEi PS00280. BPTI_KUNITZ_1. 1 hit.
    PS50279. BPTI_KUNITZ_2. 1 hit.
    PS50853. FN3. 1 hit.
    PS50234. VWFA. 12 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mosaic structure of globular domains in the human type VI collagen alpha 3 chain: similarity to von Willebrand factor, fibronectin, actin, salivary proteins and aprotinin type protease inhibitors."
      Chu M.-L., Zhang R.-Z., Pan T.-C., Stokes D., Conway D., Kuo H.-J., Glanville R., Mayer U., Mann K., Deutzmann R., Timpl R.
      EMBO J. 9:385-393(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, HYDROXYLATION, VARIANTS VAL-2431; THR-2927; VAL-2988 AND PRO-3012.
      Tissue: Fibroblast.
    2. Chu M.-L.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
      Tissue: Uterus.
    4. "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].
    5. "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 4).
    6. "The human type VI collagen gene. mRNA and protein variants of the alpha 3 chain generated by alternative splicing of an additional 5-end exon."
      Zanussi S., Doliana R., Segat D., Bonaldo P., Colombatti A.
      J. Biol. Chem. 267:24082-24089(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-236, ALTERNATIVE SPLICING.
    7. "Amino acid sequence of the triple-helical domain of human collagen type VI."
      Chu M.-L., Conway D., Pan T.-C., Baldwin C., Mann K., Deutzmann R., Timpl R.
      J. Biol. Chem. 263:18601-18606(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2038-2373.
    8. "Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones."
      Chu M.-L., Mann K., Deutzmann R., Pribula-Conway D., Hsu-Chen C.-C., Bernard M.P., Timpl R.
      Eur. J. Biochem. 168:309-317(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2157.
    9. "Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen."
      Weil D., Mattei M.-G., Passage E., N'Guyen V.C., Pribula-Conway D., Mann K., Deutzmann R., Timpl R., Chu M.-L.
      Am. J. Hum. Genet. 42:435-445(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2151.
      Tissue: Placenta.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2677.
      Tissue: Plasma.
    11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2079 AND ASN-2677.
      Tissue: Liver.
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen."
      Arnoux B., Merigeau K., Saludjian P., Norris F., Norris K., Bjoern S., Olsen O., Petersen L., Ducruix A.
      J. Mol. Biol. 246:609-617(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3108-3165.
    14. "Structure and multiple conformations of the Kunitz-type domain from human type VI collagen alpha3(VI) chain in solution."
      Zweckstetter M., Czisch M., Mayer U., Chu M.-L., Zinth W., Timpl R., Holak T.A.
      Structure 4:195-209(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 3103-3165.
    15. "Solution structure and backbone dynamics of the human alpha3-chain type VI collagen C-terminal Kunitz domain."
      Soerensen M.D., Bjoern S., Norris K., Olsen O., Petersen L., James T.L., Led J.J.
      Biochemistry 36:10439-10450(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 3108-3165.
    16. "Mutations in COL6A3 cause severe and mild phenotypes of Ullrich congenital muscular dystrophy."
      Demir E., Sabatelli P., Allamand V., Ferreiro A., Moghadaszadeh B., Makrelouf M., Topaloglu H., Echenne B., Merlini L., Guicheney P.
      Am. J. Hum. Genet. 70:1446-1458(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE.
    17. "Missense mutation in a von Willebrand factor type A domain of the alpha 3(VI) collagen gene (COL6A3) in a family with Bethlem myopathy."
      Pan T.-C., Zhang R.-Z., Pericak-Vance M.A., Tandan R., Fries T., Stajich J.M., Viles K., Vance J.M., Chu M.-L., Speer M.C.
      Hum. Mol. Genet. 7:807-812(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BM GLU-1679, VARIANT HIS-2831.
    18. "A novel de novo mutation in the triple helix of the COL6A3 gene in a two-generation Italian family affected by Bethlem myopathy. A diagnostic approach in the mutations' screening of type VI collagen."
      Pepe G., Bertini E., Giusti B., Brunelli T., Comeglio P., Saitta B., Merlini L., Chu M.L., Federici G., Abbate R.
      Neuromuscul. Disord. 9:264-271(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BM ARG-2056.
    19. "Automated genomic sequence analysis of the three collagen VI genes: applications to Ullrich congenital muscular dystrophy and Bethlem myopathy."
      Lampe A.K., Dunn D.M., von Niederhausern A.C., Hamil C., Aoyagi A., Laval S.H., Marie S.K., Chu M.-L., Swoboda K., Muntoni F., Bonnemann C.G., Flanigan K.M., Bushby K.M.D., Weiss R.B.
      J. Med. Genet. 42:108-120(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BM HIS-677; GLU-1014; LYS-1386; ASP-1467; GLU-1679; MET-1985; ASP-2047; ASP-2080 AND VAL-2941, VARIANTS UCMD GLN-1064; GLN-1395 AND ASN-1674, VARIANTS VAL-411; HIS-491; SER-492; THR-807; SER-830; GLN-1088; GLN-1576; GLN-1632; SER-1687; LEU-2218 AND HIS-2831.
    20. Cited for: VARIANT BM ARG-1726, VARIANTS HIS-677; GLN-1576; VAL-2431; LYS-2453; HIS-2831; VAL-2988 AND ILE-3069.

    Entry informationi

    Entry nameiCO6A3_HUMAN
    AccessioniPrimary (citable) accession number: P12111
    Secondary accession number(s): A8MT30
    , B4E3U5, B7ZMJ7, E9PFQ6, E9PGQ9, Q16501, Q53QF4, Q53QF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 177 of the entry and version 5 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