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P12111

- CO6A3_HUMAN

UniProt

P12111 - CO6A3_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 31773152Collagen alpha-3(VI) chain
PRO_0000005847Add
BLAST

Amino acid modifications

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

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.
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

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.

Miscellaneous databases

EvolutionaryTraceiP12111.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 20382013Nonhelical region
Add
BLAST
Regioni2039 – 2375337Triple-helical region
Add
BLAST
Regioni2376 – 3177802Nonhelical region
Add
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-rich
Add
BLAST
Compositional biasi2908 – 298376Ala-rich
Add
BLAST

Sequence similaritiesi

Belongs to the type VI collagen family.
Contains 12 VWFA domains.

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

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.
VSP_045718Add
BLAST
Alternative sequencei31 – 236206Missing in isoform 2, isoform 3 and isoform 5.
VSP_001172Add
BLAST
Alternative sequencei237 – 437201Missing in isoform 3.
VSP_043434Add
BLAST
Alternative sequencei633 – 832200Missing in isoform 4.
VSP_045719Add
BLAST
Alternative sequencei1429 – 144315AVESD…FLIDS → GEMGASEVLLGAFSI in isoform 3 and isoform 5.
VSP_043435Add
BLAST
Alternative sequencei1444 – 31771734Missing in isoform 3 and isoform 5.
VSP_043436Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1282QS → AK in AAB24261. 1 Publication
Sequence conflicti137 – 1371R → L in AAB24261. 1 Publication
Sequence conflicti381 – 3811A → V in BAG65607. 1 Publication
Sequence conflicti608 – 6081F → S in BAG65607. 1 Publication
Sequence conflicti885 – 8851K → E in AAI44596. 1 Publication
Sequence conflicti885 – 8851K → E in AAI50626. 1 Publication
Sequence conflicti1282 – 12821V → A in CAA36267. 1 Publication
Sequence conflicti1353 – 13542DD → VV in CAA36267. 1 Publication
Sequence conflicti2157 – 21571P → R in CAA29557. 1 Publication
Sequence conflicti2257 – 22571A → R in CAA36267. 1 Publication
Sequence conflicti2257 – 22571A → R in M20778. 1 Publication
Sequence conflicti2287 – 22871R → P in CAA36267. 1 Publication
Sequence conflicti2287 – 22871R → P in M20778. 1 Publication
Sequence conflicti2357 – 23571D → R in CAA36267. 1 Publication
Sequence conflicti2357 – 23571D → R in M20778. 1 Publication
Sequence conflicti2367 – 23671K → R in CAA36267. 1 Publication
Sequence conflicti2367 – 23671K → R in M20778. 1 Publication
Sequence conflicti2441 – 24411R → T in CAA36267. 1 Publication
Sequence conflicti2956 – 29561Missing in CAA36267. 1 Publication
Sequence conflicti2992 – 29921S → L in CAA36267. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 176 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

Similar proteinsi