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P13942

- COBA2_HUMAN

UniProt

P13942 - COBA2_HUMAN

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Protein
Collagen alpha-2(XI) chain
Gene
COL11A2
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 bindingi1589 – 15891Calcium By similarity
Metal bindingi1591 – 15911Calcium By similarity
Metal bindingi1592 – 15921Calcium; via carbonyl oxygen By similarity
Metal bindingi1594 – 15941Calcium; via carbonyl oxygen By similarity
Metal bindingi1597 – 15971Calcium By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cartilage development Source: UniProtKB
  2. collagen catabolic process Source: Reactome
  3. collagen fibril organization Source: UniProtKB
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. palate development Source: UniProtKB
  7. sensory perception of sound Source: UniProtKB
  8. skeletal system development Source: UniProtKB
  9. soft palate development 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-2(XI) chain
Gene namesi
Name:COL11A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2187. COL11A2.

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 3 (STL3) [MIM:184840]: An autosomal dominant non-ocular form of Stickler syndrome. Classical Stickler syndrome associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular symptoms are absent. 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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti940 – 9489Missing in STL3.
VAR_013594
Otospondylomegaepiphyseal dysplasia (OSMED) [MIM:215150]: A skeletal dysplasia characterized by enlarged epiphyses, disproportionate shortness of the limbs, abnormalities in vertebral bodies, and sensorineural hearing loss. Patients have typical facial features, including mid-face hypoplasia with a short upturned nose and depressed nasal bridge. Cleft palate and a small mandible are also common findings.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti661 – 6611G → R in OSMED. 1 Publication
VAR_001907
Weissenbacher-Zweymueller syndrome (WZS) [MIM:277610]: An autosomal dominant disorder characterized by neonatal micrognathia and rhizomelic chondrodysplasia with dumbbell-shaped femora and humeri, and regression of bone changes and normal growth in later years. WZS is also referred to as heterozygous OSMED.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1441 – 14411G → E in WZS. 1 Publication
VAR_013595
Deafness, autosomal dominant, 13 (DFNA13) [MIM:601868]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti808 – 8081G → E in DFNA13. 1 Publication
VAR_010655
Natural varianti1034 – 10341R → C in DFNA13. 1 Publication
VAR_010656
Deafness, autosomal recessive, 53 (DFNB53) [MIM:609706]: A form of non-syndromic sensorineural deafness characterized by prelingual, profound, non-progressive hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti621 – 6211P → T in DFNB53. 1 Publication
VAR_025276
Fibrochondrogenesis 2 (FBCG2) [MIM:614524]: A severe skeletal dysplasia characterized by a flat midface, short long bones, short ribs with broad metaphyses, and vertebral bodies that show distinctive hypoplastic posterior ends and rounded anterior ends, giving the vertebral bodies a pinched appearance on lateral radiographic views. The chest is small, causing perinatal respiratory problems which usually, but not always, result in lethality. Affected individuals who survive the neonatal period have high myopia, mild to moderate hearing loss, and severe skeletal dysplasia.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications

Keywords - Diseasei

Deafness, Disease mutation, Dwarfism, Non-syndromic deafness, Stickler syndrome

Organism-specific databases

MIMi184840. phenotype.
215150. phenotype.
277610. phenotype.
601868. phenotype.
609706. phenotype.
614524. phenotype.
Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
2021. Fibrochondrogenesis.
1427. Otospondylomegaepiphyseal dysplasia.
166100. Stickler syndrome type 3.
3450. Weissenbacher- Zweymuller syndrome.
PharmGKBiPA26703.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed prediction
Add
BLAST
Chaini28 – 17361709Collagen alpha-2(XI) chain
PRO_0000005840Add
BLAST
Propeptidei1501 – 1736236C-terminal propeptide
PRO_0000005841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1571 ↔ 1603 By similarity
Disulfide bondi1577 – 1577Interchain By similarity
Disulfide bondi1594 – 1594Interchain By similarity
Glycosylationi1604 – 16041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1612 ↔ 1733 By similarity
Disulfide bondi1655 ↔ 1689 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.
A disulfide-bonded peptide called proline/arginine-rich protein or PARP is released from the N-terminus during extracellular processing and is subsequently retained in the cartilage matrix from which it can be isolated in significant amounts.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP13942.
PRIDEiP13942.

PTM databases

PhosphoSiteiP13942.

Expressioni

Gene expression databases

ArrayExpressiP13942.
BgeeiP13942.
CleanExiHS_COL11A2.
GenevestigatoriP13942.

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
DDR2Q168322EBI-2515504,EBI-1381484

Protein-protein interaction databases

BioGridi107699. 4 interactions.
IntActiP13942. 5 interactions.
MINTiMINT-5222373.
STRINGi9606.ENSP00000414605.

Structurei

3D structure databases

ProteinModelPortaliP13942.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 228172Laminin G-like
Add
BLAST
Domaini399 – 44749Collagen-like 1
Add
BLAST
Domaini487 – 54559Collagen-like 2
Add
BLAST
Domaini546 – 59045Collagen-like 3
Add
BLAST
Domaini805 – 86258Collagen-like 4
Add
BLAST
Domaini863 – 89937Collagen-like 5
Add
BLAST
Domaini1099 – 115658Collagen-like 6
Add
BLAST
Domaini1157 – 117216Collagen-like 7
Add
BLAST
Domaini1441 – 149959Collagen-like 8
Add
BLAST
Domaini1541 – 1735195Fibrillar collagen NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 486272Nonhelical region
Add
BLAST
Regioni487 – 15001014Triple-helical region
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi298 – 3014Poly-Glu

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.
HOGENOMiHOG000205337.
HOVERGENiHBG004933.
InParanoidiP13942.
KOiK06236.
OMAiCAYAGAS.

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. 2 hits.
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 (9)i

Sequence statusi: Complete.

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

This entry describes 9 isoformsi produced by alternative splicing. Align

Note: Isoforms lack exons 6, 7 or 8 or a combination of these exons. Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P13942-1) [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

MERCSRCHRL LLLLPLVLGL SAAPGWAGAP PVDVLRALRF PSLPDGVRRA     50
KGICPADVAY RVARPAQLSA PTRQLFPGGF PKDFSLLTVV RTRPGLQAPL 100
LTLYSAQGVR QLGLELGRPV RFLYEDQTGR PQPPSQPVFR GLSLADGKWH 150
RVAVAVKGQS VTLIVDCKKR VTRPLPRSAR PVLDTHGVII FGARILDEEV 200
FEGDVQELAI VPGVQAAYES CEQKELECEG GQRERPQNQQ PHRAQRSPQQ 250
QPSRLHRPQN QEPQSQPTES LYYDYEPPYY DVMTTGTTPD YQDPTPGEEE 300
EILESSLLPP LEEEQTDLQV PPTADRFQAE EYGEGGTDPP EGPYDYTYGY 350
GDDYREETEL GPALSAETAH SGAAAHGPRG LKGEKGEPAV LEPGMLVEGP 400
PGPEGPAGLI GPPGIQGNPG PVGDPGERGP PGRAGLPGSD GAPGPPGTSL 450
MLPFRFGSGG GDKGPVVAAQ EAQAQAILQQ ARLALRGPPG PMGYTGRPGP 500
LGQPGSPGLK GESGDLGPQG PRGPQGLTGP PGKAGRRGRA GADGARGMPG 550
DPGVKGDRGF DGLPGLPGEK GHRGDTGAQG LPGPPGEDGE RGDDGEIGPR 600
GLPGESGPRG LLGPKGPPGI PGPPGVRGMD GPQGPKGSLG PQGEPGPPGQ 650
QGTPGTQGLP GPQGAIGPHG EKGPQGKPGL PGMPGSDGPP GHPGKEGPPG 700
TKGNQGPSGP QGPLGYPGPR GVKGVDGIRG LKGHKGEKGE DGFPGFKGDI 750
GVKGDRGEVG VPGSRGEDGP EGPKGRTGPT GDPGPPGLMG EKGKLGVPGL 800
PGYPGRQGPK GSLGFPGFPG ASGEKGARGL SGKSGPRGER GPTGPRGQRG 850
PRGATGKSGA KGTSGGDGPH GPPGERGLPG PQGPNGFPGP KGPLGPPGKD 900
GLPGHPGQRG EVGFQGKTGP PGPPGVVGPQ GAAGETGPMG ERGHPGPPGP 950
PGEQGLPGTA GKEGTKGDPG PPGAPGKDGP AGLRGFPGER GLPGTAGGPG 1000
LKGNEGPSGP PGPAGSPGER GAAGSGGPIG PPGRPGPQGP PGAAGEKGVP 1050
GEKGPIGPTG RDGVQGPVGL PGPAGPPGVA GEDGDKGEVG DPGQKGTKGN 1100
KGEHGPPGPP GPIGPVGQPG AAGADGEPGA RGPQGHFGAK GDEGTRGFNG 1150
PPGPIGLQGL PGPSGEKGET GDVGPMGPPG PPGPRGPAGP NGADGPQGPP 1200
GGVGNLGPPG EKGEPGESGS PGIQGEPGVK GPRGERGEKG ESGQPGEPGP 1250
PGPKGPTGDD GPKGNPGPVG FPGDPGPPGE GGPRGQDGAK GDRGEDGEPG 1300
QPGSPGPTGE NGPPGPLGKR GPAGSPGSEG RQGGKGAKGD PGAIGAPGKT 1350
GPVGPAGPAG KPGPDGLRGL PGSVGQQGRP GATGQAGPPG PVGPPGLPGL 1400
RGDAGAKGEK GHPGLIGLIG PPGEQGEKGD RGLPGPQGSP GQKGEMGIPG 1450
ASGPIGPGGP PGLPGPAGPK GAKGATGPGG PKGEKGVQGP PGHPGPPGEV 1500
IQPLPIQMPK KTRRSVDGSR LMQEDEAIPT GGAPGSPGGL EEIFGSLDSL 1550
REEIEQMRRP TGTQDSPART CQDLKLCHPE LPDGEYWVDP NQGCARDAFR 1600
VFCNFTAGGE TCVTPRDDVT QFSYVDSEGS PVGVVQLTFL RLLSVSAHQD 1650
VSYPCSGAAR DGPLRLRGAN EDELSPETSP YVKEFRDGCQ TQQGRTVLEV 1700
RTPVLEQLPV LDASFSDLGA PPRRGGVLLG PVCFMG 1736
Length:1,736
Mass (Da):171,791
Last modified:January 25, 2012 - v5
Checksum:iD687B7AAD6A7774C
GO
Isoform 2 (identifier: P13942-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-292: Missing.

Show »
Length:1,710
Mass (Da):168,698
Checksum:iA2EDA1C81EEA9D22
GO
Isoform 3 (identifier: P13942-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-313: Missing.

Show »
Length:1,715
Mass (Da):169,485
Checksum:i2362B2D6508A0C24
GO
Isoform 4 (identifier: P13942-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     314-373: Missing.

Show »
Length:1,676
Mass (Da):165,293
Checksum:iA87540ED78D3E198
GO
Isoform 5 (identifier: P13942-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-292: Missing.
     293-313: Missing.

Show »
Length:1,689
Mass (Da):166,393
Checksum:iD53384E69D99D454
GO
Isoform 6 (identifier: P13942-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-292: Missing.
     314-373: Missing.

Show »
Length:1,650
Mass (Da):162,201
Checksum:i1ECC3F4C92956F3F
GO
Isoform 7 (identifier: P13942-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     293-313: Missing.
     314-373: Missing.

Show »
Length:1,655
Mass (Da):162,988
Checksum:i125F75A575246E2E
GO
Isoform 8 (identifier: P13942-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-292: Missing.
     293-313: Missing.
     314-373: Missing.

Show »
Length:1,629
Mass (Da):159,895
Checksum:i9E095488C4B3C32F
GO
Isoform 9 (identifier: P13942-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     267-290: PTESLYYDYEPPYYDVMTTGTTPD → VRELGEPPSAAHPREGRHPGISPP
     291-1736: Missing.

Note: No experimental confirmation available.

Show »
Length:290
Mass (Da):31,960
Checksum:i7E59579056D3640F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361P → S.
Corresponds to variant rs35116188 [ dbSNP | Ensembl ].
VAR_048804
Natural varianti276 – 2761E → K.
Corresponds to variant rs9277934 [ dbSNP | Ensembl ].
VAR_048805
Natural varianti593 – 5931D → G.1 Publication
VAR_013591
Natural varianti621 – 6211P → T in DFNB53. 1 Publication
VAR_025276
Natural varianti661 – 6611G → R in OSMED. 1 Publication
VAR_001907
Natural varianti808 – 8081G → E in DFNA13. 1 Publication
VAR_010655
Natural varianti824 – 8241E → K.1 Publication
Corresponds to variant rs1799909 [ dbSNP | Ensembl ].
VAR_013592
Natural varianti879 – 8791P → L.1 Publication
VAR_013593
Natural varianti894 – 8941L → P.
Corresponds to variant rs2855430 [ dbSNP | Ensembl ].
VAR_048806
Natural varianti940 – 9489Missing in STL3.
VAR_013594
Natural varianti1034 – 10341R → C in DFNA13. 1 Publication
VAR_010656
Natural varianti1316 – 13161P → T.1 Publication
Corresponds to variant rs2229784 [ dbSNP | Ensembl ].
VAR_013596
Natural varianti1441 – 14411G → E in WZS. 1 Publication
VAR_013595
Natural varianti1600 – 16001R → Q.1 Publication
Corresponds to variant rs1799912 [ dbSNP | Ensembl ].
VAR_013597
Natural varianti1628 – 16281E → D.
Corresponds to variant rs2229790 [ dbSNP | Ensembl ].
VAR_033797
Natural varianti1722 – 17221P → L.
Corresponds to variant rs2229792 [ dbSNP | Ensembl ].
VAR_048807

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei267 – 29226Missing in isoform 2, isoform 5, isoform 6 and isoform 8.
VSP_001167Add
BLAST
Alternative sequencei267 – 29024PTESL…GTTPD → VRELGEPPSAAHPREGRHPG ISPP in isoform 9.
VSP_043432Add
BLAST
Alternative sequencei291 – 17361446Missing in isoform 9.
VSP_043433Add
BLAST
Alternative sequencei293 – 31321Missing in isoform 3, isoform 5, isoform 7 and isoform 8.
VSP_001168Add
BLAST
Alternative sequencei314 – 37360Missing in isoform 4, isoform 6, isoform 7 and isoform 8.
VSP_001169Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71C → G in AAC50213. 1 Publication
Sequence conflicti7 – 71C → G in AAC50214. 1 Publication
Sequence conflicti7 – 71C → G in AAC50215. 1 Publication
Sequence conflicti85 – 851S → P in AAC17464. 1 Publication
Sequence conflicti85 – 851S → P in AAA35498. 1 Publication
Sequence conflicti97 – 971Q → R in AAC17464. 1 Publication
Sequence conflicti97 – 971Q → R in AAA35498. 1 Publication
Sequence conflicti530 – 5312PP → SL in AAC50213. 1 Publication
Sequence conflicti530 – 5312PP → SL in AAC50214. 1 Publication
Sequence conflicti530 – 5312PP → SL in AAC50215. 1 Publication
Sequence conflicti530 – 5312PP → SL in AAC17464. 1 Publication
Sequence conflicti530 – 5312PP → SL in AAA35498. 1 Publication
Sequence conflicti542 – 5421A → P in AAA35498. 1 Publication
Sequence conflicti548 – 5492MP → TL in AAA35498. 1 Publication
Sequence conflicti578 – 5792AQ → PR in AAA35498. 1 Publication
Sequence conflicti704 – 7052NQ → KP in AAA35498. 1 Publication
Sequence conflicti720 – 7201R → Q in AAA35498. 1 Publication
Sequence conflicti726 – 7261D → N in AAA35498. 1 Publication
Sequence conflicti843 – 8464TGPR → HGST in AAA52034. 1 Publication
Sequence conflicti882 – 8843QGP → SGS in AAA52034. 1 Publication
Sequence conflicti1031 – 10322PP → RQ in AAC50213. 1 Publication
Sequence conflicti1031 – 10322PP → RQ in AAC50214. 1 Publication
Sequence conflicti1031 – 10322PP → RQ in AAC50215. 1 Publication
Sequence conflicti1031 – 10322PP → RQ in AAA52034. 1 Publication
Sequence conflicti1091 – 10911D → V in AAA52034. 1 Publication
Sequence conflicti1124 – 11241A → R in AAA52034. 1 Publication
Sequence conflicti1127 – 11337EPGARGP → GAGGLGT in AAA52034. 1 Publication
Sequence conflicti1253 – 12531P → A in AAC50213. 1 Publication
Sequence conflicti1253 – 12531P → A in AAC50214. 1 Publication
Sequence conflicti1253 – 12531P → A in AAC50215. 1 Publication
Sequence conflicti1253 – 12531P → A in AAA52034. 1 Publication
Sequence conflicti1257 – 12571T → Q in AAC50213. 1 Publication
Sequence conflicti1257 – 12571T → Q in AAC50214. 1 Publication
Sequence conflicti1257 – 12571T → Q in AAC50215. 1 Publication
Sequence conflicti1257 – 12571T → Q in AAA52034. 1 Publication
Sequence conflicti1552 – 15521E → R in AAA52034. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32169 Genomic DNA. Translation: AAC50213.1.
U32169 Genomic DNA. Translation: AAC50214.1.
U32169 Genomic DNA. Translation: AAC50215.1.
AL031228 Genomic DNA. Translation: CAA20240.1.
AL645940 Genomic DNA. Translation: CAI18063.2.
AL662824 Genomic DNA. No translation available.
AL844527 Genomic DNA. Translation: CAM25784.1.
AL844527, AL845446 Genomic DNA. Translation: CAI41834.1.
AL845446, AL844527 Genomic DNA. Translation: CAI95551.1.
CR759733 Genomic DNA. Translation: CAQ10294.1.
CR759733 Genomic DNA. Translation: CAQ10296.1.
CR936877 Genomic DNA. Translation: CAQ09060.1.
CR936877 Genomic DNA. Translation: CAQ09062.1.
CH471081 Genomic DNA. Translation: EAX03676.1.
BC053886 mRNA. Translation: AAH53886.1.
U41069
, U41065, U41066, U41067 Genomic DNA. Translation: AAC17464.1.
L18987 mRNA. Translation: AAA35498.1.
J04974 mRNA. Translation: AAA52034.1.
CCDSiCCDS43452.1. [P13942-6]
CCDS54992.1. [P13942-9]
PIRiS34790. CGHU2E.
RefSeqiNP_001157243.1. NM_001163771.1. [P13942-9]
NP_542411.2. NM_080680.2.
NP_542412.2. NM_080681.2.
UniGeneiHs.390171.

Genome annotation databases

EnsembliENST00000341947; ENSP00000339915; ENSG00000204248.
ENST00000383087; ENSP00000372565; ENSG00000227801. [P13942-6]
ENST00000383088; ENSP00000372566; ENSG00000206290. [P13942-9]
ENST00000395194; ENSP00000378620; ENSG00000204248. [P13942-9]
ENST00000439039; ENSP00000410284; ENSG00000227801. [P13942-9]
ENST00000447741; ENSP00000400813; ENSG00000235708. [P13942-9]
ENST00000452937; ENSP00000406347; ENSG00000230930. [P13942-9]
ENST00000547261; ENSP00000450150; ENSG00000227801. [P13942-7]
ENST00000547999; ENSP00000446903; ENSG00000227801. [P13942-3]
ENST00000549289; ENSP00000448643; ENSG00000227801. [P13942-4]
ENST00000549381; ENSP00000448464; ENSG00000227801. [P13942-5]
ENST00000549811; ENSP00000449275; ENSG00000227801. [P13942-1]
ENST00000550561; ENSP00000449393; ENSG00000227801. [P13942-2]
ENST00000551542; ENSP00000447864; ENSG00000227801. [P13942-8]
ENST00000551758; ENSP00000447062; ENSG00000230930.
GeneIDi1302.
KEGGihsa:1302.
UCSCiuc003ocx.1. human. [P13942-1]
uc003oda.3. human. [P13942-9]

Polymorphism databases

DMDMi374095517.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Hereditary hearing loss homepage

Gene page

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32169 Genomic DNA. Translation: AAC50213.1 .
U32169 Genomic DNA. Translation: AAC50214.1 .
U32169 Genomic DNA. Translation: AAC50215.1 .
AL031228 Genomic DNA. Translation: CAA20240.1 .
AL645940 Genomic DNA. Translation: CAI18063.2 .
AL662824 Genomic DNA. No translation available.
AL844527 Genomic DNA. Translation: CAM25784.1 .
AL844527 , AL845446 Genomic DNA. Translation: CAI41834.1 .
AL845446 , AL844527 Genomic DNA. Translation: CAI95551.1 .
CR759733 Genomic DNA. Translation: CAQ10294.1 .
CR759733 Genomic DNA. Translation: CAQ10296.1 .
CR936877 Genomic DNA. Translation: CAQ09060.1 .
CR936877 Genomic DNA. Translation: CAQ09062.1 .
CH471081 Genomic DNA. Translation: EAX03676.1 .
BC053886 mRNA. Translation: AAH53886.1 .
U41069
, U41065 , U41066 , U41067 Genomic DNA. Translation: AAC17464.1 .
L18987 mRNA. Translation: AAA35498.1 .
J04974 mRNA. Translation: AAA52034.1 .
CCDSi CCDS43452.1. [P13942-6 ]
CCDS54992.1. [P13942-9 ]
PIRi S34790. CGHU2E.
RefSeqi NP_001157243.1. NM_001163771.1. [P13942-9 ]
NP_542411.2. NM_080680.2.
NP_542412.2. NM_080681.2.
UniGenei Hs.390171.

3D structure databases

ProteinModelPortali P13942.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107699. 4 interactions.
IntActi P13942. 5 interactions.
MINTi MINT-5222373.
STRINGi 9606.ENSP00000414605.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P13942.

Polymorphism databases

DMDMi 374095517.

Proteomic databases

PaxDbi P13942.
PRIDEi P13942.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341947 ; ENSP00000339915 ; ENSG00000204248 .
ENST00000383087 ; ENSP00000372565 ; ENSG00000227801 . [P13942-6 ]
ENST00000383088 ; ENSP00000372566 ; ENSG00000206290 . [P13942-9 ]
ENST00000395194 ; ENSP00000378620 ; ENSG00000204248 . [P13942-9 ]
ENST00000439039 ; ENSP00000410284 ; ENSG00000227801 . [P13942-9 ]
ENST00000447741 ; ENSP00000400813 ; ENSG00000235708 . [P13942-9 ]
ENST00000452937 ; ENSP00000406347 ; ENSG00000230930 . [P13942-9 ]
ENST00000547261 ; ENSP00000450150 ; ENSG00000227801 . [P13942-7 ]
ENST00000547999 ; ENSP00000446903 ; ENSG00000227801 . [P13942-3 ]
ENST00000549289 ; ENSP00000448643 ; ENSG00000227801 . [P13942-4 ]
ENST00000549381 ; ENSP00000448464 ; ENSG00000227801 . [P13942-5 ]
ENST00000549811 ; ENSP00000449275 ; ENSG00000227801 . [P13942-1 ]
ENST00000550561 ; ENSP00000449393 ; ENSG00000227801 . [P13942-2 ]
ENST00000551542 ; ENSP00000447864 ; ENSG00000227801 . [P13942-8 ]
ENST00000551758 ; ENSP00000447062 ; ENSG00000230930 .
GeneIDi 1302.
KEGGi hsa:1302.
UCSCi uc003ocx.1. human. [P13942-1 ]
uc003oda.3. human. [P13942-9 ]

Organism-specific databases

CTDi 1302.
GeneCardsi GC06M033130.
GC06Mj33052.
GC06Mk33108.
GC06Mm33300.
GC06Mn33059.
GeneReviewsi COL11A2.
H-InvDB HIX0033301.
HIX0166403.
HIX0166658.
HIX0166919.
HIX0167181.
HIX0167416.
HIX0184201.
HIX0207630.
HGNCi HGNC:2187. COL11A2.
MIMi 120290. gene.
184840. phenotype.
215150. phenotype.
277610. phenotype.
601868. phenotype.
609706. phenotype.
614524. phenotype.
neXtProti NX_P13942.
Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
90636. Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
2021. Fibrochondrogenesis.
1427. Otospondylomegaepiphyseal dysplasia.
166100. Stickler syndrome type 3.
3450. Weissenbacher- Zweymuller syndrome.
PharmGKBi PA26703.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000205337.
HOVERGENi HBG004933.
InParanoidi P13942.
KOi K06236.
OMAi CAYAGAS.

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 COL11A2_(gene).
GenomeRNAii 1302.
NextBioi 5291.
PROi P13942.
SOURCEi Search...

Gene expression databases

ArrayExpressi P13942.
Bgeei P13942.
CleanExi HS_COL11A2.
Genevestigatori P13942.

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. 2 hits.
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. "The human COL11A2 gene structure indicates that the gene has not evolved with the genes for the major fibrillar collagens."
    Vuoristo M.M., Pihlajamaa T., Vandenberg P., Prockop D.J., Ala-Kokko L.
    J. Biol. Chem. 270:22873-22881(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 9).
    Tissue: Skin.
  5. "The human alpha 2(XI) collagen gene (COL11A2): completion of coding information, identification of the promoter sequence, and precise localization within the major histocompatibility complex reveal overlap with the KE5 gene."
    Lui V.C., Ng L.J., Sat E.W., Cheah K.S.
    Genomics 32:401-412(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-537.
  6. "Molecular cloning of PARP (proline/arginine-rich protein) from human cartilage and subsequent demonstration that PARP is a fragment of the NH2-terminal domain of the collagen alpha 2(XI) chain."
    Zhidkova N.I., Brewton R.G., Mayne R.
    FEBS Lett. 326:25-28(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-807.
    Tissue: Cartilage.
  7. "The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning of cDNA and genomic DNA reveals characteristics of a fibrillar collagen with differences in genomic organization."
    Kimura T., Cheah K.S.E., Chan S.D.H., Lui V.C.H., Mattei M.-G., van der Rest M., Ono K., Solomon E., Ninomiya Y., Olsen B.R.
    J. Biol. Chem. 264:13910-13916(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 730-1690.
  8. "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.
  9. "Autosomal recessive disorder otospondylomegaepiphyseal dysplasia is associated with loss-of-function mutations in the COL11A2 gene."
    Melkoniemi M., Brunner H.G., Manouvrier S., Hennekam R.C.M., Superti-Furga A., Kaeaeriaeinen H., Pauli R.M., van Essen T., Warman M.L., Bonaventure J., Miny P., Ala-Kokko L.
    Am. J. Hum. Genet. 66:368-377(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  10. "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
    Kuivaniemi H., Tromp G., Prockop D.J.
    Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  11. "Dominant and recessive forms of fibrochondrogenesis resulting from mutations at a second locus, COL11A2."
    Tompson S.W., Faqeih E.A., Ala-Kokko L., Hecht J.T., Miki R., Funari T., Funari V.A., Nevarez L., Krakow D., Cohn D.H.
    Am. J. Med. Genet. A 158:309-314(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN FBCG2.
  12. Cited for: VARIANT OSMED ARG-661.
  13. "Genetic mapping of ossification of the posterior longitudinal ligament of the spine."
    Koga H., Sakou T., Taketomi E., Hayashi K., Numasawa T., Harata S., Yone K., Matsunaga S., Otterud B., Inoue I., Leppert M.
    Am. J. Hum. Genet. 62:1460-1467(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLY-593; LYS-824; LEU-879; THR-1316 AND GLN-1600.
  14. "Heterozygous glycine substitution in the COL11A2 gene in the original patient with the Weissenbacher-Zweymueller syndrome demonstrates its identity with heterozygous OSMED (nonocular Stickler syndrome)."
    Pihlajamaa T., Prockop D.J., Faber J., Winterpacht A., Zabel B., Giedion A., Wiesbauer P., Spranger J., Ala-Kokko L.
    Am. J. Med. Genet. 80:115-120(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT WZS GLU-1441.
  15. "Stickler syndrome without eye involvement is caused by mutations in COL11A2, the gene encoding the alpha-2(XI) chain of type XI collagen."
    Sirko-Osadsa D.A., Murray M.A., Scott J.A., Lavery M.A., Warman M.L., Robin N.H.
    J. Pediatr. 132:368-371(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT STL3 940-GLY--PRO-948 DEL.
  16. Cited for: SEQUENCE REVISION TO 1031-1032, VARIANTS DFNA13 GLU-808 AND CYS-1034.
  17. "Mutation of COL11A2 causes autosomal recessive non-syndromic hearing loss at the DFNB53 locus."
    Chen W., Kahrizi K., Meyer N.C., Riazalhosseini Y., Van Camp G., Najmabadi H., Smith R.J.H.
    J. Med. Genet. 42:E61-E61(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DFNB53 THR-621.

Entry informationi

Entry nameiCOBA2_HUMAN
AccessioniPrimary (citable) accession number: P13942
Secondary accession number(s): A6NLX2
, E7ER90, Q07751, Q13271, Q13272, Q13273, Q5JP94, Q5SUI8, Q7Z6C3, Q99866, Q9UIP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 25, 2012
Last modified: September 3, 2014
This is version 174 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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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