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P12107

- COBA1_HUMAN

UniProt

P12107 - COBA1_HUMAN

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Protein
Collagen alpha-1(XI) chain
Gene
COL11A1, COLL6
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1625 – 16251Calcium By similarity
Metal bindingi1627 – 16271Calcium By similarity
Metal bindingi1628 – 16281Calcium; via carbonyl oxygen By similarity
Metal bindingi1630 – 16301Calcium; via carbonyl oxygen By similarity
Metal bindingi1633 – 16331Calcium By similarity

GO - Molecular functioni

  1. extracellular matrix binding Source: UniProtKB
  2. extracellular matrix structural constituent Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. protein binding, bridging Source: UniProtKB

GO - Biological processi

  1. cartilage condensation Source: Ensembl
  2. chondrocyte development Source: Ensembl
  3. collagen catabolic process Source: Reactome
  4. collagen fibril organization Source: UniProtKB
  5. detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
  6. embryonic skeletal system morphogenesis Source: Ensembl
  7. extracellular matrix disassembly Source: Reactome
  8. extracellular matrix organization Source: UniProtKB
  9. inner ear morphogenesis Source: Ensembl
  10. proteoglycan metabolic process Source: Ensembl
  11. sensory perception of sound Source: UniProtKB
  12. tendon development Source: Ensembl
  13. ventricular cardiac muscle tissue morphogenesis Source: Ensembl
  14. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2186. COL11A1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Stickler syndrome 2 (STL2) [MIM:604841]: An 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. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti565 – 5651G → V in STL2. 1 Publication
VAR_063675
Natural varianti625 – 6251G → V in STL2. 1 Publication
VAR_013583
Natural varianti676 – 6761G → R in STL2; overlapping phenotype with Marshall syndrome. 1 Publication
VAR_013584
Natural varianti921 – 9266Missing in STL2; overlapping phenotype with Marshall syndrome.
VAR_013585
Natural varianti1027 – 10271G → R in STL2. 1 Publication
VAR_063676
Natural varianti1110 – 11189Missing in STL2.
VAR_063677
Natural varianti1313 – 13153Missing in STL2; overlapping phenotype with Marshall syndrome.
VAR_013586
Natural varianti1513 – 15131G → D in STL2. 1 Publication
VAR_063678
Natural varianti1516 – 15161G → V in STL2; overlapping phenotype with Marshall syndrome. 2 Publications
VAR_013587
Marshall syndrome (MRSHS) [MIM:154780]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Fibrochondrogenesis 1 (FBCG1) [MIM:228520]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti796 – 7961G → R in FBCG1. 1 Publication
VAR_065904
Natural varianti1042 – 10421G → R in FBCG1. 1 Publication
VAR_065905

Keywords - Diseasei

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

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535 Reviewed prediction
Add
BLAST
Propeptidei36 – 511476N-terminal propeptide Reviewed prediction
PRO_0000005774Add
BLAST
Chaini512 – 15631052Collagen alpha-1(XI) chain
PRO_0000005775Add
BLAST
Propeptidei1564 – 1806243C-terminal propeptide
PRO_0000005776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 ↔ 243 By similarity
Disulfide bondi182 ↔ 236 By similarity
Modified residuei612 – 6121Allysine
Modified residuei1452 – 14521Allysine
Disulfide bondi1607 ↔ 1639 By similarity
Disulfide bondi1630 – 1630Interchain By similarity
Glycosylationi1640 – 16401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1648 ↔ 1803 By similarity
Disulfide bondi1714 ↔ 1757 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.
N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP12107.
PaxDbiP12107.
PRIDEiP12107.

PTM databases

PhosphoSiteiP12107.

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

ArrayExpressiP12107.
BgeeiP12107.
CleanExiHS_COL11A1.
GenevestigatoriP12107.

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).

Protein-protein interaction databases

BioGridi107698. 2 interactions.
STRINGi9606.ENSP00000351163.

Structurei

3D structure databases

ProteinModelPortaliP12107.
SMRiP12107. Positions 73-229, 1596-1805.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 243173Laminin G-like
Add
BLAST
Domaini442 – 49049Collagen-like 1
Add
BLAST
Domaini532 – 58655Collagen-like 2
Add
BLAST
Domaini583 – 64159Collagen-like 3
Add
BLAST
Domaini616 – 67459Collagen-like 4
Add
BLAST
Domaini643 – 69957Collagen-like 5
Add
BLAST
Domaini1393 – 145058Collagen-like 6
Add
BLAST
Domaini1429 – 148759Collagen-like 7
Add
BLAST
Domaini1483 – 154159Collagen-like 8
Add
BLAST
Domaini1577 – 1805229Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 419190Nonhelical region
Add
BLAST
Regioni420 – 50889Triple-helical region (interrupted)
Add
BLAST
Regioni509 – 5113Short nonhelical segment
Regioni512 – 52817Telopeptide
Add
BLAST
Regioni529 – 15421014Triple-helical region
Add
BLAST
Regioni1543 – 156321Nonhelical region (C-terminal)
Add
BLAST

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.

Sequence similaritiesi

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG004933.
KOiK06236.
OMAiHPGKEGQ.
OrthoDBiEOG7XPZ4W.
PhylomeDBiP12107.
TreeFamiTF323987.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 8 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. Align

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

MEPWSSRWKT KRWLWDFTVT TLALTFLFQA REVRGAAPVD VLKALDFHNS     50
PEGISKTTGF CTNRKNSKGS DTAYRVSKQA QLSAPTKQLF PGGTFPEDFS 100
ILFTVKPKKG IQSFLLSIYN EHGIQQIGVE VGRSPVFLFE DHTGKPAPED 150
YPLFRTVNIA DGKWHRVAIS VEKKTVTMIV DCKKKTTKPL DRSERAIVDT 200
NGITVFGTRI LDEEVFEGDI QQFLITGDPK AAYDYCEHYS PDCDSSAPKA 250
AQAQEPQIDE YAPEDIIEYD YEYGEAEYKE AESVTEGPTV TEETIAQTEA 300
NIVDDFQEYN YGTMESYQTE APRHVSGTNE PNPVEEIFTE EYLTGEDYDS 350
QRKNSEDTLY ENKEIDGRDS DLLVDGDLGE YDFYEYKEYE DKPTSPPNEE 400
FGPGVPAETD ITETSINGHG AYGEKGQKGE PAVVEPGMLV EGPPGPAGPA 450
GIMGPPGLQG PTGPPGDPGD RGPPGRPGLP GADGLPGPPG TMLMLPFRYG 500
GDGSKGPTIS AQEAQAQAIL QQARIALRGP PGPMGLTGRP GPVGGPGSSG 550
AKGESGDPGP QGPRGVQGPP GPTGKPGKRG RPGADGGRGM PGEPGAKGDR 600
GFDGLPGLPG DKGHRGERGP QGPPGPPGDD GMRGEDGEIG PRGLPGEAGP 650
RGLLGPRGTP GAPGQPGMAG VDGPPGPKGN MGPQGEPGPP GQQGNPGPQG 700
LPGPQGPIGP PGEKGPQGKP GLAGLPGADG PPGHPGKEGQ SGEKGALGPP 750
GPQGPIGYPG PRGVKGADGV RGLKGSKGEK GEDGFPGFKG DMGLKGDRGE 800
VGQIGPRGED GPEGPKGRAG PTGDPGPSGQ AGEKGKLGVP GLPGYPGRQG 850
PKGSTGFPGF PGANGEKGAR GVAGKPGPRG QRGPTGPRGS RGARGPTGKP 900
GPKGTSGGDG PPGPPGERGP QGPQGPVGFP GPKGPPGPPG KDGLPGHPGQ 950
RGETGFQGKT GPPGPGGVVG PQGPTGETGP IGERGHPGPP GPPGEQGLPG 1000
AAGKEGAKGD PGPQGISGKD GPAGLRGFPG ERGLPGAQGA PGLKGGEGPQ 1050
GPPGPVGSPG ERGSAGTAGP IGLPGRPGPQ GPPGPAGEKG APGEKGPQGP 1100
AGRDGVQGPV GLPGPAGPAG SPGEDGDKGE IGEPGQKGSK GDKGENGPPG 1150
PPGLQGPVGA PGIAGGDGEP GPRGQQGMFG QKGDEGARGF PGPPGPIGLQ 1200
GLPGPPGEKG ENGDVGPMGP PGPPGPRGPQ GPNGADGPQG PPGSVGSVGG 1250
VGEKGEPGEA GNPGPPGEAG VGGPKGERGE KGEAGPPGAA GPPGAKGPPG 1300
DDGPKGNPGP VGFPGDPGPP GEPGPAGQDG VGGDKGEDGD PGQPGPPGPS 1350
GEAGPPGPPG KRGPPGAAGA EGRQGEKGAK GEAGAEGPPG KTGPVGPQGP 1400
AGKPGPEGLR GIPGPVGEQG LPGAAGQDGP PGPMGPPGLP GLKGDPGSKG 1450
EKGHPGLIGL IGPPGEQGEK GDRGLPGTQG SPGAKGDGGI PGPAGPLGPP 1500
GPPGLPGPQG PKGNKGSTGP AGQKGDSGLP GPPGSPGPPG EVIQPLPILS 1550
SKKTRRHTEG MQADADDNIL DYSDGMEEIF GSLNSLKQDI EHMKFPMGTQ 1600
TNPARTCKDL QLSHPDFPDG EYWIDPNQGC SGDSFKVYCN FTSGGETCIY 1650
PDKKSEGVRI SSWPKEKPGS WFSEFKRGKL LSYLDVEGNS INMVQMTFLK 1700
LLTASARQNF TYHCHQSAAW YDVSSGSYDK ALRFLGSNDE EMSYDNNPFI 1750
KTLYDGCASR KGYEKTVIEI NTPKIDQVPI VDVMINDFGD QNQKFGFEVG 1800
PVCFLG 1806
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81W → G.
Corresponds to variant rs12025888 [ dbSNP | Ensembl ].
VAR_047723
Natural varianti46 – 461D → E.
Corresponds to variant rs11164663 [ dbSNP | Ensembl ].
VAR_047724
Natural varianti559 – 5591G → S.
Corresponds to variant rs12143815 [ dbSNP | Ensembl ].
VAR_047725
Natural varianti565 – 5651G → V in STL2. 1 Publication
VAR_063675
Natural varianti625 – 6251G → V in STL2. 1 Publication
VAR_013583
Natural varianti676 – 6761G → R in STL2; overlapping phenotype with Marshall syndrome. 1 Publication
VAR_013584
Natural varianti796 – 7961G → R in FBCG1. 1 Publication
VAR_065904
Natural varianti921 – 9266Missing in STL2; overlapping phenotype with Marshall syndrome.
VAR_013585
Natural varianti1027 – 10271G → R in STL2. 1 Publication
VAR_063676
Natural varianti1042 – 10421G → R in FBCG1. 1 Publication
VAR_065905
Natural varianti1110 – 11189Missing in STL2.
VAR_063677
Natural varianti1313 – 13153Missing in STL2; overlapping phenotype with Marshall syndrome.
VAR_013586
Natural varianti1323 – 13231P → L.3 Publications
Corresponds to variant rs3753841 [ dbSNP | Ensembl ].
VAR_047726
Natural varianti1326 – 13261A → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035743
Natural varianti1328 – 13281Q → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035744
Natural varianti1328 – 13281Q → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_035745
Natural varianti1513 – 15131G → D in STL2. 1 Publication
VAR_063678
Natural varianti1516 – 15161G → V in STL2; overlapping phenotype with Marshall syndrome. 2 Publications
VAR_013587
Natural varianti1535 – 15351S → P.4 Publications
Corresponds to variant rs1676486 [ dbSNP | Ensembl ].
VAR_047727
Natural varianti1805 – 18051L → F.
Corresponds to variant rs1975916 [ dbSNP | Ensembl ].
VAR_047728

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei261 – 29939YAPED…IAQTE → KKKSNFKKKMRTVATKSKEK SKKFTPPKSEKFSSKKKKSY QASAKAKLGVK in isoform B.
VSP_001145Add
BLAST
Alternative sequencei261 – 29939Missing in isoform C.
VSP_001146Add
BLAST
Alternative sequencei300 – 415116Missing in isoform 4.
VSP_046318Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti941 – 9444KDGL → RMGC in AAA51891. 1 Publication
Sequence conflicti986 – 9861H → Y in AAA51891. 1 Publication
Sequence conflicti1074 – 10741P → R in AAA51891. 1 Publication
Sequence conflicti1142 – 11421D → G in AAA51891. 1 Publication
Sequence conflicti1218 – 12181M → W in AAA51891. 1 Publication
Sequence conflicti1758 – 17581A → T in AAA51891. 1 Publication
Sequence conflicti1786 – 17861N → S in AAA51891. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [P12107-1]
uc001dum.3. human. [P12107-2]
uc001dun.3. human. [P12107-3]

Polymorphism databases

DMDMi215274245.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53348.1. [P12107-3 ]
CCDS778.1. [P12107-1 ]
CCDS780.2. [P12107-4 ]
PIRi A35239. CGHU1E.
RefSeqi NP_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 ]
UniGenei Hs.523446.

3D structure databases

ProteinModelPortali P12107.
SMRi P12107. Positions 73-229, 1596-1805.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107698. 2 interactions.
STRINGi 9606.ENSP00000351163.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P12107.

Polymorphism databases

DMDMi 215274245.

Proteomic databases

MaxQBi P12107.
PaxDbi P12107.
PRIDEi P12107.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000353414 ; ENSP00000302551 ; ENSG00000060718 . [P12107-3 ]
ENST00000358392 ; ENSP00000351163 ; ENSG00000060718 . [P12107-2 ]
ENST00000370096 ; ENSP00000359114 ; ENSG00000060718 . [P12107-1 ]
ENST00000512756 ; ENSP00000426533 ; ENSG00000060718 . [P12107-4 ]
GeneIDi 1301.
KEGGi hsa:1301.
UCSCi uc001dul.3. human. [P12107-1 ]
uc001dum.3. human. [P12107-2 ]
uc001dun.3. human. [P12107-3 ]

Organism-specific databases

CTDi 1301.
GeneCardsi GC01M103342.
GeneReviewsi COL11A1.
H-InvDB HIX0028847.
HGNCi HGNC:2186. COL11A1.
HPAi HPA052246.
MIMi 120280. gene.
154780. phenotype.
228520. phenotype.
604841. phenotype.
neXtProti NX_P12107.
Orphaneti 250984. Autosomal recessive Stickler syndrome.
2021. Fibrochondrogenesis.
560. Marshall syndrome.
90654. Stickler syndrome type 2.
PharmGKBi PA26702.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG004933.
KOi K06236.
OMAi HPGKEGQ.
OrthoDBi EOG7XPZ4W.
PhylomeDBi P12107.
TreeFami TF323987.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.

Miscellaneous databases

GeneWikii Collagen,_type_XI,_alpha_1.
GenomeRNAii 1301.
NextBioi 5283.
PMAP-CutDB B1ASK7.
PROi P12107.
SOURCEi Search...

Gene expression databases

ArrayExpressi P12107.
Bgeei P12107.
CleanExi HS_COL11A1.
Genevestigatori P12107.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 8 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Pro-alpha 1(XI) collagen. Structure of the amino-terminal propeptide and expression of the gene in tumor cell lines."
    Yoshioka H., Ramirez F.
    J. Biol. Chem. 265:6423-6426(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANTS LEU-1323 AND PRO-1535.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A; B AND C), VARIANTS STL2/MARSHALL SYNDROME ARG-676; 921-GLN--PRO-926 DEL; 1313-PHE--GLY-1315 DEL; LEU-1323; VAL-1516 AND PRO-1535.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-1535.
  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), VARIANTS LEU-1323 AND PRO-1535.
  6. "Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA demonstrates that type XI belongs to the fibrillar class of collagens and reveals that the expression of the gene is not restricted to cartilagenous tissue."
    Bernard M., Yoshioka H., Rodriguez E., van der Rest M., Kimura T., Ninomiya Y., Olsen B.R., Ramirez F.
    J. Biol. Chem. 263:17159-17166(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 538-1806, PARTIAL PROTEIN SEQUENCE.
  7. "Alternative mRNA processing occurs in the variable region of the pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains."
    Zhidkova N.I., Justice S.K., Mayne R.
    J. Biol. Chem. 270:9486-9493(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
    Tissue: Blood.
  8. "A family with Stickler syndrome type 2 has a mutation in the COL11A1 gene resulting in the substitution of glycine 97 by valine in alpha-1(XI) collagen."
    Richards A.J., Yates J.R.W., Williams R., Payne S.J., Pope F.M., Scott J.D., Snead M.P.
    Hum. Mol. Genet. 5:1339-1343(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT STL2 VAL-625.
  9. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-1326; LYS-1328 AND LEU-1328.
  10. Cited for: VARIANTS FBCG1 ARG-796 AND ARG-1042.
  11. Cited for: VARIANTS STL2 VAL-565; ARG-1027; 1110-VAL--PRO-1118 DEL; ASP-1513 AND VAL-1516.

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: September 3, 2014
This is version 167 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

External Data

Dasty 3

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