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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

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
  7. response to glucose Source: Ensembl
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: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProtKB
  7. proteinaceous extracellular matrix Source: UniProtKB-KW
  8. sarcolemma Source: Ensembl
  9. vesicle Source: UniProtKB
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.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

BgeeiP12111.
CleanExiHS_COL6A3.
ExpressionAtlasiP12111. baseline and differential.
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.
GeneTreeiENSGT00760000119051.
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

        10         20         30         40         50
MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI
60 70 80 90 100
GEEHFQLVRE FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ
110 120 130 140 150
EVLSHISNMS YIGGTNQTGK GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT
160 170 180 190 200
DGHSKDGLAL PSAELKSADV NVFAIGVEDA DEGALKEIAS EPLNMHMFNL
210 220 230 240 250
ENFTSLHDIV GNLVSCVHSS VSPERAGDTE TLKDITAQDS ADIIFLIDGS
260 270 280 290 300
NNTGSVNFAV ILDFLVNLLE KLPIGTQQIR VGVVQFSDEP RTMFSLDTYS
310 320 330 340 350
TKAQVLGAVK ALGFAGGELA NIGLALDFVV ENHFTRAGGS RVEEGVPQVL
360 370 380 390 400
VLISAGPSSD EIRYGVVALK QASVFSFGLG AQAASRAELQ HIATDDNLVF
410 420 430 440 450
TVPEFRSFGD LQEKLLPYIV GVAQRHIVLK PPTIVTQVIE VNKRDIVFLV
460 470 480 490 500
DGSSALGLAN FNAIRDFIAK VIQRLEIGQD LIQVAVAQYA DTVRPEFYFN
510 520 530 540 550
THPTKREVIT AVRKMKPLDG SALYTGSALD FVRNNLFTSS AGYRAAEGIP
560 570 580 590 600
KLLVLITGGK SLDEISQPAQ ELKRSSIMAF AIGNKGADQA ELEEIAFDSS
610 620 630 640 650
LVFIPAEFRA APLQGMLPGL LAPLRTLSGT PEVHSNKRDI IFLLDGSANV
660 670 680 690 700
GKTNFPYVRD FVMNLVNSLD IGNDNIRVGL VQFSDTPVTE FSLNTYQTKS
710 720 730 740 750
DILGHLRQLQ LQGGSGLNTG SALSYVYANH FTEAGGSRIR EHVPQLLLLL
760 770 780 790 800
TAGQSEDSYL QAANALTRAG ILTFCVGASQ ANKAELEQIA FNPSLVYLMD
810 820 830 840 850
DFSSLPALPQ QLIQPLTTYV SGGVEEVPLA QPESKRDILF LFDGSANLVG
860 870 880 890 900
QFPVVRDFLY KIIDELNVKP EGTRIAVAQY SDDVKVESRF DEHQSKPEIL
910 920 930 940 950
NLVKRMKIKT GKALNLGYAL DYAQRYIFVK SAGSRIEDGV LQFLVLLVAG
960 970 980 990 1000
RSSDRVDGPA SNLKQSGVVP FIFQAKNADP AELEQIVLSP AFILAAESLP
1010 1020 1030 1040 1050
KIGDLHPQIV NLLKSVHNGA PAPVSGEKDV VFLLDGSEGV RSGFPLLKEF
1060 1070 1080 1090 1100
VQRVVESLDV GQDRVRVAVV QYSDRTRPEF YLNSYMNKQD VVNAVRQLTL
1110 1120 1130 1140 1150
LGGPTPNTGA ALEFVLRNIL VSSAGSRITE GVPQLLIVLT ADRSGDDVRN
1160 1170 1180 1190 1200
PSVVVKRGGA VPIGIGIGNA DITEMQTISF IPDFAVAIPT FRQLGTVQQV
1210 1220 1230 1240 1250
ISERVTQLTR EELSRLQPVL QPLPSPGVGG KRDVVFLIDG SQSAGPEFQY
1260 1270 1280 1290 1300
VRTLIERLVD YLDVGFDTTR VAVIQFSDDP KVEFLLNAHS SKDEVQNAVQ
1310 1320 1330 1340 1350
RLRPKGGRQI NVGNALEYVS RNIFKRPLGS RIEEGVPQFL VLISSGKSDD
1360 1370 1380 1390 1400
EVDDPAVELK QFGVAPFTIA RNADQEELVK ISLSPEYVFS VSTFRELPSL
1410 1420 1430 1440 1450
EQKLLTPITT LTSEQIQKLL ASTRYPPPAV ESDAADIVFL IDSSEGVRPD
1460 1470 1480 1490 1500
GFAHIRDFVS RIVRRLNIGP SKVRVGVVQF SNDVFPEFYL KTYRSQAPVL
1510 1520 1530 1540 1550
DAIRRLRLRG GSPLNTGKAL EFVARNLFVK SAGSRIEDGV PQHLVLVLGG
1560 1570 1580 1590 1600
KSQDDVSRFA QVIRSSGIVS LGVGDRNIDR TELQTITNDP RLVFTVREFR
1610 1620 1630 1640 1650
ELPNIEERIM NSFGPSAATP APPGVDTPPP SRPEKKKADI VFLLDGSINF
1660 1670 1680 1690 1700
RRDSFQEVLR FVSEIVDTVY EDGDSIQVGL VQYNSDPTDE FFLKDFSTKR
1710 1720 1730 1740 1750
QIIDAINKVV YKGGRHANTK VGLEHLRVNH FVPEAGSRLD QRVPQIAFVI
1760 1770 1780 1790 1800
TGGKSVEDAQ DVSLALTQRG VKVFAVGVRN IDSEEVGKIA SNSATAFRVG
1810 1820 1830 1840 1850
NVQELSELSE QVLETLHDAM HETLCPGVTD AAKACNLDVI LGFDGSRDQN
1860 1870 1880 1890 1900
VFVAQKGFES KVDAILNRIS QMHRVSCSGG RSPTVRVSVV ANTPSGPVEA
1910 1920 1930 1940 1950
FDFDEYQPEM LEKFRNMRSQ HPYVLTEDTL KVYLNKFRQS SPDSVKVVIH
1960 1970 1980 1990 2000
FTDGADGDLA DLHRASENLR QEGVRALILV GLERVVNLER LMHLEFGRGF
2010 2020 2030 2040 2050
MYDRPLRLNL LDLDYELAEQ LDNIAEKACC GVPCKCSGQR GDRGPIGSIG
2060 2070 2080 2090 2100
PKGIPGEDGY RGYPGDEGGP GERGPPGVNG TQGFQGCPGQ RGVKGSRGFP
2110 2120 2130 2140 2150
GEKGEVGEIG LDGLDGEDGD KGLPGSSGEK GNPGRRGDKG PRGEKGERGD
2160 2170 2180 2190 2200
VGIRGDPGNP GQDSQERGPK GETGDLGPMG VPGRDGVPGG PGETGKNGGF
2210 2220 2230 2240 2250
GRRGPPGAKG NKGGPGQPGF EGEQGTRGAQ GPAGPAGPPG LIGEQGISGP
2260 2270 2280 2290 2300
RGSGGAAGAP GERGRTGPLG RKGEPGEPGP KGGIGNRGPR GETGDDGRDG
2310 2320 2330 2340 2350
VGSEGRRGKK GERGFPGYPG PKGNPGEPGL NGTTGPKGIR GRRGNSGPPG
2360 2370 2380 2390 2400
IVGQKGDPGY PGPAGPKGNR GDSIDQCALI QSIKDKCPCC YGPLECPVFP
2410 2420 2430 2440 2450
TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY
2460 2470 2480 2490 2500
NNEVTTEIRF ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK
2510 2520 2530 2540 2550
RVRNGFLMRK VAVFFSNTPT RASPQLREAV LKLSDAGITP LFLTRQEDRQ
2560 2570 2580 2590 2600
LINALQINNT AVGHALVLPA GRDLTDFLEN VLTCHVCLDI CNIDPSCGFG
2610 2620 2630 2640 2650
SWRPSFRDRR AAGSDVDIDM AFILDSAETT TLFQFNEMKK YIAYLVRQLD
2660 2670 2680 2690 2700
MSPDPKASQH FARVAVVQHA PSESVDNASM PPVKVEFSLT DYGSKEKLVD
2710 2720 2730 2740 2750
FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGEVPEQ
2760 2770 2780 2790 2800
QLEEAQRVIL QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK
2810 2820 2830 2840 2850
STELNEEPLM RFGRLLPSFV SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK
2860 2870 2880 2890 2900
FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT KPVTTTTKPV TTTTKPVTII
2910 2920 2930 2940 2950
NQPSVKPAAA KPAPAKPVAA KPVATKMATV RPPVAVKPAT AAKPVAAKPA
2960 2970 2980 2990 3000
AVRPPAAAAA KPVATKPEVP RPQAAKPAAT KPATTKPMVK MSREVQVFEI
3010 3020 3030 3040 3050
TENSAKLHWE RAEPPGPYFY DLTVTSAHDQ SLVLKQNLTV TDRVIGGLLA
3060 3070 3080 3090 3100
GQTYHVAVVC YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS
3110 3120 3130 3140 3150
TEPLALTETD ICKLPKDEGT CRDFILKWYY DPNTKSCARF WYGGCGGNEN
3160 3170
KFGSQKECEK VCAPVLAKPG VISVMGT
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 GC02M238233.
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.
GeneTreei ENSGT00760000119051.
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

Bgeei P12111.
CleanExi HS_COL6A3.
ExpressionAtlasi P12111. baseline and differential.
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: October 29, 2014
This is version 178 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