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Protein

Collagen alpha-1(XI) chain

Gene

COL11A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1625CalciumBy similarity1
Metal bindingi1627CalciumBy similarity1
Metal bindingi1628Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1630Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1633CalciumBy similarity1

GO - Molecular functioni

  • extracellular matrix binding Source: UniProtKB
  • extracellular matrix structural constituent Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein binding, bridging Source: UniProtKB

GO - Biological processi

  • cartilage condensation Source: Ensembl
  • chondrocyte development Source: Ensembl
  • collagen catabolic process Source: Reactome
  • collagen fibril organization Source: UniProtKB
  • detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
  • embryonic skeletal system morphogenesis Source: Ensembl
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix organization Source: UniProtKB
  • inner ear morphogenesis Source: Ensembl
  • ossification Source: Ensembl
  • proteoglycan metabolic process Source: Ensembl
  • sensory perception of sound Source: UniProtKB
  • tendon development Source: Ensembl
  • ventricular cardiac muscle tissue morphogenesis Source: Ensembl
  • visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000060718-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XI) chain
Gene namesi
Name:COL11A1
Synonyms:COLL6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2186. COL11A1.

Subcellular locationi

GO - Cellular componenti

  • collagen type XI trimer Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Stickler syndrome 2 (STL2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Pierre Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable.
See also OMIM:604841
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063675565G → V in STL2. 1 Publication1
Natural variantiVAR_013583625G → V in STL2. 1 PublicationCorresponds to variant rs121912943dbSNPEnsembl.1
Natural variantiVAR_013584676G → R in STL2; overlapping phenotype with Marshall syndrome. 1 PublicationCorresponds to variant rs749663226dbSNPEnsembl.1
Natural variantiVAR_013585921 – 926Missing in STL2; overlapping phenotype with Marshall syndrome. 1 Publication6
Natural variantiVAR_0636761027G → R in STL2. 1 Publication1
Natural variantiVAR_0636771110 – 1118Missing in STL2. 1 Publication9
Natural variantiVAR_0135861313 – 1315Missing in STL2; overlapping phenotype with Marshall syndrome. 1 Publication3
Natural variantiVAR_0636781513G → D in STL2. 1 Publication1
Natural variantiVAR_0135871516G → V in STL2; overlapping phenotype with Marshall syndrome. 2 Publications1
Marshall syndrome (MRSHS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by ocular abnormalities, deafness, craniofacial anomalies, and anhidrotic ectodermal dysplasia. Clinical features include short stature; flat or retruded midface with short, depressed nose, flat nasal bridge and anteverted nares; cleft palate with or without the Pierre Robin sequence; appearance of large eyes with ocular hypertelorism; cataracts, either congenital or juvenile; esotropia; high myopia; sensorineural hearing loss; spondyloepiphyseal abnormalities; calcification of the falx cerebri; ectodermal abnormalities, including defects in sweating and dental structures.
See also OMIM:154780
Fibrochondrogenesis 1 (FBCG1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe short-limbed skeletal dysplasia characterized by broad long-bone metaphyses, pear-shaped vertebral bodies, and characteristic morphology of the growth plate, in which the chondrocytes have a fibroblastic appearance and there are regions of fibrous cartilage extracellular matrix. Clinical features include a flat midface with a small nose and anteverted nares, significant shortening of all limb segments but relatively normal hands and feet, and a small bell-shaped thorax with a protuberant abdomen.
See also OMIM:228520
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065904796G → R in FBCG1. 1 Publication1
Natural variantiVAR_0659051042G → R in FBCG1. 1 Publication1

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Dwarfism, Ectodermal dysplasia, Stickler syndrome

Organism-specific databases

DisGeNETi1301.
MalaCardsiCOL11A1.
MIMi154780. phenotype.
228520. phenotype.
604841. phenotype.
OpenTargetsiENSG00000060718.
Orphaneti250984. Autosomal recessive Stickler syndrome.
2021. Fibrochondrogenesis.
560. Marshall syndrome.
90654. Stickler syndrome type 2.
PharmGKBiPA26702.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL11A1.
DMDMi215274245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35Sequence analysisAdd BLAST35
PropeptideiPRO_000000577436 – 511N-terminal propeptideSequence analysisAdd BLAST476
ChainiPRO_0000005775512 – 1563Collagen alpha-1(XI) chainAdd BLAST1052
PropeptideiPRO_00000057761564 – 1806C-terminal propeptideAdd BLAST243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi61 ↔ 243PROSITE-ProRule annotation
Disulfide bondi182 ↔ 236PROSITE-ProRule annotation
Modified residuei612Allysine1
Modified residuei1452Allysine1
Disulfide bondi1607 ↔ 1639PROSITE-ProRule annotation
Disulfide bondi1630InterchainPROSITE-ProRule annotation
Glycosylationi1640N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1648 ↔ 1803PROSITE-ProRule annotation
Disulfide bondi1714 ↔ 1757PROSITE-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.
N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP12107.
MaxQBiP12107.
PaxDbiP12107.
PeptideAtlasiP12107.
PRIDEiP12107.

PTM databases

iPTMnetiP12107.
PhosphoSitePlusiP12107.

Miscellaneous databases

PMAP-CutDBB1ASK7.

Expressioni

Tissue specificityi

Cartilage, placenta and some tumor or virally transformed cell lines. Isoforms using exon IIA or IIB are found in the cartilage while isoforms using only exon IIB are found in the tendon.

Gene expression databases

BgeeiENSG00000060718.
CleanExiHS_COL11A1.
ExpressionAtlasiP12107. baseline and differential.
GenevisibleiP12107. HS.

Organism-specific databases

HPAiHPA052246.

Interactioni

Subunit structurei

Trimers composed of three different chains: alpha 1(XI), alpha 2(XI), and alpha 3(XI). Alpha 3(XI) is a post-translational modification of alpha 1(II). Alpha 1(V) can also be found instead of alpha 3(XI)=1(II).

GO - Molecular functioni

  • protein binding, bridging Source: UniProtKB

Protein-protein interaction databases

BioGridi107698. 1 interactor.
STRINGi9606.ENSP00000359114.

Structurei

3D structure databases

ProteinModelPortaliP12107.
SMRiP12107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 243Laminin G-likeAdd BLAST173
Domaini442 – 490Collagen-like 1Add BLAST49
Domaini532 – 586Collagen-like 2Add BLAST55
Domaini583 – 641Collagen-like 3Add BLAST59
Domaini616 – 674Collagen-like 4Add BLAST59
Domaini643 – 699Collagen-like 5Add BLAST57
Domaini1393 – 1450Collagen-like 6Add BLAST58
Domaini1429 – 1487Collagen-like 7Add BLAST59
Domaini1483 – 1541Collagen-like 8Add BLAST59
Domaini1577 – 1805Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni230 – 419Nonhelical regionAdd BLAST190
Regioni420 – 508Triple-helical region (interrupted)Add BLAST89
Regioni509 – 511Short nonhelical segment3
Regioni512 – 528TelopeptideAdd BLAST17
Regioni529 – 1542Triple-helical regionAdd BLAST1014
Regioni1543 – 1563Nonhelical region (C-terminal)Add BLAST21

Domaini

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

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 8 collagen-like domains.Curated
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG41112UQ. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP12107.
KOiK19721.
OMAiHPGKEGQ.
OrthoDBiEOG091G01AE.
PhylomeDBiP12107.
TreeFamiTF323987.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. There is alternative usage of exon IIA or exon IIB. Transcripts containing exon IIA or IIB are present in cartilage, but exon IIB is preferentially utilized in transcripts from tendon.
Isoform A (identifier: P12107-1) [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
MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS
60 70 80 90 100
PEGISKTTGF CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS
110 120 130 140 150
ILFTVKPKKG IQSFLLSIYN EHGIQQIGVE VGRSPVFLFE DHTGKPAPED
160 170 180 190 200
YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV DCKKKTTKPL DRSERAIVDT
210 220 230 240 250
NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS PDCDSSAPKA
260 270 280 290 300
AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEA
310 320 330 340 350
NIVDDFQEYN YGTMESYQTE APRHVSGTNE PNPVEEIFTE EYLTGEDYDS
360 370 380 390 400
QRKNSEDTLY ENKEIDGRDS DLLVDGDLGE YDFYEYKEYE DKPTSPPNEE
410 420 430 440 450
FGPGVPAETD ITETSINGHG AYGEKGQKGE PAVVEPGMLV EGPPGPAGPA
460 470 480 490 500
GIMGPPGLQG PTGPPGDPGD RGPPGRPGLP GADGLPGPPG TMLMLPFRYG
510 520 530 540 550
GDGSKGPTIS AQEAQAQAIL QQARIALRGP PGPMGLTGRP GPVGGPGSSG
560 570 580 590 600
AKGESGDPGP QGPRGVQGPP GPTGKPGKRG RPGADGGRGM PGEPGAKGDR
610 620 630 640 650
GFDGLPGLPG DKGHRGERGP QGPPGPPGDD GMRGEDGEIG PRGLPGEAGP
660 670 680 690 700
RGLLGPRGTP GAPGQPGMAG VDGPPGPKGN MGPQGEPGPP GQQGNPGPQG
710 720 730 740 750
LPGPQGPIGP PGEKGPQGKP GLAGLPGADG PPGHPGKEGQ SGEKGALGPP
760 770 780 790 800
GPQGPIGYPG PRGVKGADGV RGLKGSKGEK GEDGFPGFKG DMGLKGDRGE
810 820 830 840 850
VGQIGPRGED GPEGPKGRAG PTGDPGPSGQ AGEKGKLGVP GLPGYPGRQG
860 870 880 890 900
PKGSTGFPGF PGANGEKGAR GVAGKPGPRG QRGPTGPRGS RGARGPTGKP
910 920 930 940 950
GPKGTSGGDG PPGPPGERGP QGPQGPVGFP GPKGPPGPPG KDGLPGHPGQ
960 970 980 990 1000
RGETGFQGKT GPPGPGGVVG PQGPTGETGP IGERGHPGPP GPPGEQGLPG
1010 1020 1030 1040 1050
AAGKEGAKGD PGPQGISGKD GPAGLRGFPG ERGLPGAQGA PGLKGGEGPQ
1060 1070 1080 1090 1100
GPPGPVGSPG ERGSAGTAGP IGLPGRPGPQ GPPGPAGEKG APGEKGPQGP
1110 1120 1130 1140 1150
AGRDGVQGPV GLPGPAGPAG SPGEDGDKGE IGEPGQKGSK GDKGENGPPG
1160 1170 1180 1190 1200
PPGLQGPVGA PGIAGGDGEP GPRGQQGMFG QKGDEGARGF PGPPGPIGLQ
1210 1220 1230 1240 1250
GLPGPPGEKG ENGDVGPMGP PGPPGPRGPQ GPNGADGPQG PPGSVGSVGG
1260 1270 1280 1290 1300
VGEKGEPGEA GNPGPPGEAG VGGPKGERGE KGEAGPPGAA GPPGAKGPPG
1310 1320 1330 1340 1350
DDGPKGNPGP VGFPGDPGPP GEPGPAGQDG VGGDKGEDGD PGQPGPPGPS
1360 1370 1380 1390 1400
GEAGPPGPPG KRGPPGAAGA EGRQGEKGAK GEAGAEGPPG KTGPVGPQGP
1410 1420 1430 1440 1450
AGKPGPEGLR GIPGPVGEQG LPGAAGQDGP PGPMGPPGLP GLKGDPGSKG
1460 1470 1480 1490 1500
EKGHPGLIGL IGPPGEQGEK GDRGLPGTQG SPGAKGDGGI PGPAGPLGPP
1510 1520 1530 1540 1550
GPPGLPGPQG PKGNKGSTGP AGQKGDSGLP GPPGSPGPPG EVIQPLPILS
1560 1570 1580 1590 1600
SKKTRRHTEG MQADADDNIL DYSDGMEEIF GSLNSLKQDI EHMKFPMGTQ
1610 1620 1630 1640 1650
TNPARTCKDL QLSHPDFPDG EYWIDPNQGC SGDSFKVYCN FTSGGETCIY
1660 1670 1680 1690 1700
PDKKSEGVRI SSWPKEKPGS WFSEFKRGKL LSYLDVEGNS INMVQMTFLK
1710 1720 1730 1740 1750
LLTASARQNF TYHCHQSAAW YDVSSGSYDK ALRFLGSNDE EMSYDNNPFI
1760 1770 1780 1790 1800
KTLYDGCASR KGYEKTVIEI NTPKIDQVPI VDVMINDFGD QNQKFGFEVG

PVCFLG
Length:1,806
Mass (Da):181,065
Last modified:November 25, 2008 - v4
Checksum:i7CBF744263321B43
GO
Isoform B (identifier: P12107-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     261-299: YAPEDIIEYD...VTEETIAQTE → KKKSNFKKKM...ASAKAKLGVK

Show »
Length:1,818
Mass (Da):182,422
Checksum:iD86BD1303BA45C99
GO
Isoform C (identifier: P12107-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     261-299: Missing.

Show »
Length:1,767
Mass (Da):176,619
Checksum:iDE451EE638FDBCA9
GO
Isoform 4 (identifier: P12107-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     300-415: Missing.

Note: No experimental confirmation available.
Show »
Length:1,690
Mass (Da):167,752
Checksum:iA612FE4054F2F34E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti941 – 944KDGL → RMGC in AAA51891 (PubMed:1690726).Curated4
Sequence conflicti986H → Y in AAA51891 (PubMed:1690726).Curated1
Sequence conflicti1074P → R in AAA51891 (PubMed:1690726).Curated1
Sequence conflicti1142D → G in AAA51891 (PubMed:1690726).Curated1
Sequence conflicti1218M → W in AAA51891 (PubMed:1690726).Curated1
Sequence conflicti1758A → T in AAA51891 (PubMed:1690726).Curated1
Sequence conflicti1786N → S in AAA51891 (PubMed:1690726).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0477238W → G.Corresponds to variant rs12025888dbSNPEnsembl.1
Natural variantiVAR_04772446D → E.Corresponds to variant rs11164663dbSNPEnsembl.1
Natural variantiVAR_047725559G → S.Corresponds to variant rs12143815dbSNPEnsembl.1
Natural variantiVAR_063675565G → V in STL2. 1 Publication1
Natural variantiVAR_013583625G → V in STL2. 1 PublicationCorresponds to variant rs121912943dbSNPEnsembl.1
Natural variantiVAR_013584676G → R in STL2; overlapping phenotype with Marshall syndrome. 1 PublicationCorresponds to variant rs749663226dbSNPEnsembl.1
Natural variantiVAR_065904796G → R in FBCG1. 1 Publication1
Natural variantiVAR_013585921 – 926Missing in STL2; overlapping phenotype with Marshall syndrome. 1 Publication6
Natural variantiVAR_0636761027G → R in STL2. 1 Publication1
Natural variantiVAR_0659051042G → R in FBCG1. 1 Publication1
Natural variantiVAR_0636771110 – 1118Missing in STL2. 1 Publication9
Natural variantiVAR_0135861313 – 1315Missing in STL2; overlapping phenotype with Marshall syndrome. 1 Publication3
Natural variantiVAR_0477261323P → L.3 PublicationsCorresponds to variant rs3753841dbSNPEnsembl.1
Natural variantiVAR_0357431326A → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0357441328Q → K in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs750014974dbSNPEnsembl.1
Natural variantiVAR_0357451328Q → L in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0636781513G → D in STL2. 1 Publication1
Natural variantiVAR_0135871516G → V in STL2; overlapping phenotype with Marshall syndrome. 2 Publications1
Natural variantiVAR_0477271535S → P.4 PublicationsCorresponds to variant rs1676486dbSNPEnsembl.1
Natural variantiVAR_0477281805L → F.Corresponds to variant rs1975916dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001145261 – 299YAPED…IAQTE → KKKSNFKKKMRTVATKSKEK SKKFTPPKSEKFSSKKKKSY QASAKAKLGVK in isoform B. CuratedAdd BLAST39
Alternative sequenceiVSP_001146261 – 299Missing in isoform C. CuratedAdd BLAST39
Alternative sequenceiVSP_046318300 – 415Missing in isoform 4. 1 PublicationAdd BLAST116

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04177 mRNA. Translation: AAA51891.1.
AF101112
, AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04724.1.
AF101112
, AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04725.1.
AF101112
, AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04726.1.
AL627203, AC093150, AC099567 Genomic DNA. Translation: CAH73908.1.
CH471097 Genomic DNA. Translation: EAW72908.1.
CH471097 Genomic DNA. Translation: EAW72910.1.
BC117697 mRNA. Translation: AAI17698.1.
L38956 Genomic DNA. Translation: AAA79171.1.
CCDSiCCDS53348.1. [P12107-3]
CCDS778.1. [P12107-1]
CCDS780.2. [P12107-4]
PIRiA35239. CGHU1E.
RefSeqiNP_001177638.1. NM_001190709.1. [P12107-3]
NP_001845.3. NM_001854.3. [P12107-1]
NP_542196.2. NM_080629.2. [P12107-2]
NP_542197.3. NM_080630.3. [P12107-4]
UniGeneiHs.523446.

Genome annotation databases

EnsembliENST00000353414; ENSP00000302551; ENSG00000060718. [P12107-3]
ENST00000358392; ENSP00000351163; ENSG00000060718. [P12107-2]
ENST00000370096; ENSP00000359114; ENSG00000060718. [P12107-1]
ENST00000512756; ENSP00000426533; ENSG00000060718. [P12107-4]
GeneIDi1301.
KEGGihsa:1301.
UCSCiuc001dul.4. human. [P12107-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04177 mRNA. Translation: AAA51891.1.
AF101112
, AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04724.1.
AF101112
, AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04725.1.
AF101112
, AF101079, AF101080, AF101081, AF101082, AF101083, AF101084, AF101085, AF101086, AF101087, AF101088, AF101089, AF101090, AF101091, AF101092, AF101093, AF101094, AF101095, AF101096, AF101097, AF101098, AF101099, AF101100, AF101101, AF101102, AF101103, AF101104, AF101105, AF101106, AF101107, AF101108, AF101109, AF101110, AF101111 Genomic DNA. Translation: AAF04726.1.
AL627203, AC093150, AC099567 Genomic DNA. Translation: CAH73908.1.
CH471097 Genomic DNA. Translation: EAW72908.1.
CH471097 Genomic DNA. Translation: EAW72910.1.
BC117697 mRNA. Translation: AAI17698.1.
L38956 Genomic DNA. Translation: AAA79171.1.
CCDSiCCDS53348.1. [P12107-3]
CCDS778.1. [P12107-1]
CCDS780.2. [P12107-4]
PIRiA35239. CGHU1E.
RefSeqiNP_001177638.1. NM_001190709.1. [P12107-3]
NP_001845.3. NM_001854.3. [P12107-1]
NP_542196.2. NM_080629.2. [P12107-2]
NP_542197.3. NM_080630.3. [P12107-4]
UniGeneiHs.523446.

3D structure databases

ProteinModelPortaliP12107.
SMRiP12107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107698. 1 interactor.
STRINGi9606.ENSP00000359114.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP12107.
PhosphoSitePlusiP12107.

Polymorphism and mutation databases

BioMutaiCOL11A1.
DMDMi215274245.

Proteomic databases

EPDiP12107.
MaxQBiP12107.
PaxDbiP12107.
PeptideAtlasiP12107.
PRIDEiP12107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353414; ENSP00000302551; ENSG00000060718. [P12107-3]
ENST00000358392; ENSP00000351163; ENSG00000060718. [P12107-2]
ENST00000370096; ENSP00000359114; ENSG00000060718. [P12107-1]
ENST00000512756; ENSP00000426533; ENSG00000060718. [P12107-4]
GeneIDi1301.
KEGGihsa:1301.
UCSCiuc001dul.4. human. [P12107-1]

Organism-specific databases

CTDi1301.
DisGeNETi1301.
GeneCardsiCOL11A1.
GeneReviewsiCOL11A1.
H-InvDBHIX0028847.
HGNCiHGNC:2186. COL11A1.
HPAiHPA052246.
MalaCardsiCOL11A1.
MIMi120280. gene.
154780. phenotype.
228520. phenotype.
604841. phenotype.
neXtProtiNX_P12107.
OpenTargetsiENSG00000060718.
Orphaneti250984. Autosomal recessive Stickler syndrome.
2021. Fibrochondrogenesis.
560. Marshall syndrome.
90654. Stickler syndrome type 2.
PharmGKBiPA26702.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG41112UQ. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP12107.
KOiK19721.
OMAiHPGKEGQ.
OrthoDBiEOG091G01AE.
PhylomeDBiP12107.
TreeFamiTF323987.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000060718-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-8874081. MET activates PTK2 signaling.

Miscellaneous databases

ChiTaRSiCOL11A1. human.
GeneWikiiCollagen,_type_XI,_alpha_1.
GenomeRNAii1301.
PMAP-CutDBB1ASK7.
PROiP12107.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000060718.
CleanExiHS_COL11A1.
ExpressionAtlasiP12107. baseline and differential.
GenevisibleiP12107. HS.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 7 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOBA1_HUMAN
AccessioniPrimary (citable) accession number: P12107
Secondary accession number(s): B1ASK7
, D3DT73, E9PCU0, Q14034, Q149N0, Q9UIT4, Q9UIT5, Q9UIT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 191 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.