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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 – 15891CalciumBy similarity
Metal bindingi1591 – 15911CalciumBy similarity
Metal bindingi1592 – 15921Calcium; via carbonyl oxygenBy similarity
Metal bindingi1594 – 15941Calcium; via carbonyl oxygenBy similarity
Metal bindingi1597 – 15971CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent conferring tensile strength Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. 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

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti940 – 9489Missing in STL3. 1 Publication
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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 non-syndromic sensorineural deafness type DFNA.
90636. Autosomal recessive non-syndromic 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 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 17361709Collagen alpha-2(XI) chainPRO_0000005840Add
BLAST
Propeptidei1501 – 1736236C-terminal propeptidePRO_0000005841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi1571 ↔ 1603PROSITE-ProRule annotation
Disulfide bondi1577 – 1577InterchainPROSITE-ProRule annotation
Disulfide bondi1594 – 1594InterchainPROSITE-ProRule annotation
Glycosylationi1604 – 16041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1612 ↔ 1733PROSITE-ProRule annotation
Disulfide bondi1655 ↔ 1689PROSITE-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.
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

BgeeiP13942.
CleanExiHS_COL11A2.
ExpressionAtlasiP13942. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 228172Laminin G-likeAdd
BLAST
Domaini399 – 44749Collagen-like 1Add
BLAST
Domaini487 – 54559Collagen-like 2Add
BLAST
Domaini546 – 59045Collagen-like 3Add
BLAST
Domaini805 – 86258Collagen-like 4Add
BLAST
Domaini863 – 89937Collagen-like 5Add
BLAST
Domaini1099 – 115658Collagen-like 6Add
BLAST
Domaini1157 – 117216Collagen-like 7Add
BLAST
Domaini1441 – 149959Collagen-like 8Add
BLAST
Domaini1541 – 1735195Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

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

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOGENOMiHOG000205337.
HOVERGENiHBG004933.
InParanoidiP13942.
KOiK06236.
OMAiCAYAGAS.

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. 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

        10         20         30         40         50
MERCSRCHRL LLLLPLVLGL SAAPGWAGAP PVDVLRALRF PSLPDGVRRA
60 70 80 90 100
KGICPADVAY RVARPAQLSA PTRQLFPGGF PKDFSLLTVV RTRPGLQAPL
110 120 130 140 150
LTLYSAQGVR QLGLELGRPV RFLYEDQTGR PQPPSQPVFR GLSLADGKWH
160 170 180 190 200
RVAVAVKGQS VTLIVDCKKR VTRPLPRSAR PVLDTHGVII FGARILDEEV
210 220 230 240 250
FEGDVQELAI VPGVQAAYES CEQKELECEG GQRERPQNQQ PHRAQRSPQQ
260 270 280 290 300
QPSRLHRPQN QEPQSQPTES LYYDYEPPYY DVMTTGTTPD YQDPTPGEEE
310 320 330 340 350
EILESSLLPP LEEEQTDLQV PPTADRFQAE EYGEGGTDPP EGPYDYTYGY
360 370 380 390 400
GDDYREETEL GPALSAETAH SGAAAHGPRG LKGEKGEPAV LEPGMLVEGP
410 420 430 440 450
PGPEGPAGLI GPPGIQGNPG PVGDPGERGP PGRAGLPGSD GAPGPPGTSL
460 470 480 490 500
MLPFRFGSGG GDKGPVVAAQ EAQAQAILQQ ARLALRGPPG PMGYTGRPGP
510 520 530 540 550
LGQPGSPGLK GESGDLGPQG PRGPQGLTGP PGKAGRRGRA GADGARGMPG
560 570 580 590 600
DPGVKGDRGF DGLPGLPGEK GHRGDTGAQG LPGPPGEDGE RGDDGEIGPR
610 620 630 640 650
GLPGESGPRG LLGPKGPPGI PGPPGVRGMD GPQGPKGSLG PQGEPGPPGQ
660 670 680 690 700
QGTPGTQGLP GPQGAIGPHG EKGPQGKPGL PGMPGSDGPP GHPGKEGPPG
710 720 730 740 750
TKGNQGPSGP QGPLGYPGPR GVKGVDGIRG LKGHKGEKGE DGFPGFKGDI
760 770 780 790 800
GVKGDRGEVG VPGSRGEDGP EGPKGRTGPT GDPGPPGLMG EKGKLGVPGL
810 820 830 840 850
PGYPGRQGPK GSLGFPGFPG ASGEKGARGL SGKSGPRGER GPTGPRGQRG
860 870 880 890 900
PRGATGKSGA KGTSGGDGPH GPPGERGLPG PQGPNGFPGP KGPLGPPGKD
910 920 930 940 950
GLPGHPGQRG EVGFQGKTGP PGPPGVVGPQ GAAGETGPMG ERGHPGPPGP
960 970 980 990 1000
PGEQGLPGTA GKEGTKGDPG PPGAPGKDGP AGLRGFPGER GLPGTAGGPG
1010 1020 1030 1040 1050
LKGNEGPSGP PGPAGSPGER GAAGSGGPIG PPGRPGPQGP PGAAGEKGVP
1060 1070 1080 1090 1100
GEKGPIGPTG RDGVQGPVGL PGPAGPPGVA GEDGDKGEVG DPGQKGTKGN
1110 1120 1130 1140 1150
KGEHGPPGPP GPIGPVGQPG AAGADGEPGA RGPQGHFGAK GDEGTRGFNG
1160 1170 1180 1190 1200
PPGPIGLQGL PGPSGEKGET GDVGPMGPPG PPGPRGPAGP NGADGPQGPP
1210 1220 1230 1240 1250
GGVGNLGPPG EKGEPGESGS PGIQGEPGVK GPRGERGEKG ESGQPGEPGP
1260 1270 1280 1290 1300
PGPKGPTGDD GPKGNPGPVG FPGDPGPPGE GGPRGQDGAK GDRGEDGEPG
1310 1320 1330 1340 1350
QPGSPGPTGE NGPPGPLGKR GPAGSPGSEG RQGGKGAKGD PGAIGAPGKT
1360 1370 1380 1390 1400
GPVGPAGPAG KPGPDGLRGL PGSVGQQGRP GATGQAGPPG PVGPPGLPGL
1410 1420 1430 1440 1450
RGDAGAKGEK GHPGLIGLIG PPGEQGEKGD RGLPGPQGSP GQKGEMGIPG
1460 1470 1480 1490 1500
ASGPIGPGGP PGLPGPAGPK GAKGATGPGG PKGEKGVQGP PGHPGPPGEV
1510 1520 1530 1540 1550
IQPLPIQMPK KTRRSVDGSR LMQEDEAIPT GGAPGSPGGL EEIFGSLDSL
1560 1570 1580 1590 1600
REEIEQMRRP TGTQDSPART CQDLKLCHPE LPDGEYWVDP NQGCARDAFR
1610 1620 1630 1640 1650
VFCNFTAGGE TCVTPRDDVT QFSYVDSEGS PVGVVQLTFL RLLSVSAHQD
1660 1670 1680 1690 1700
VSYPCSGAAR DGPLRLRGAN EDELSPETSP YVKEFRDGCQ TQQGRTVLEV
1710 1720 1730
RTPVLEQLPV LDASFSDLGA PPRRGGVLLG PVCFMG
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71C → G in AAC50213. (PubMed:7559422)Curated
Sequence conflicti7 – 71C → G in AAC50214. (PubMed:7559422)Curated
Sequence conflicti7 – 71C → G in AAC50215. (PubMed:7559422)Curated
Sequence conflicti85 – 851S → P in AAC17464. (PubMed:8838804)Curated
Sequence conflicti85 – 851S → P in AAA35498. (PubMed:8325374)Curated
Sequence conflicti97 – 971Q → R in AAC17464. (PubMed:8838804)Curated
Sequence conflicti97 – 971Q → R in AAA35498. (PubMed:8325374)Curated
Sequence conflicti530 – 5312PP → SL in AAC50213. (PubMed:7559422)Curated
Sequence conflicti530 – 5312PP → SL in AAC50214. (PubMed:7559422)Curated
Sequence conflicti530 – 5312PP → SL in AAC50215. (PubMed:7559422)Curated
Sequence conflicti530 – 5312PP → SL in AAC17464. (PubMed:8838804)Curated
Sequence conflicti530 – 5312PP → SL in AAA35498. (PubMed:8325374)Curated
Sequence conflicti542 – 5421A → P in AAA35498. (PubMed:8325374)Curated
Sequence conflicti548 – 5492MP → TL in AAA35498. (PubMed:8325374)Curated
Sequence conflicti578 – 5792AQ → PR in AAA35498. (PubMed:8325374)Curated
Sequence conflicti704 – 7052NQ → KP in AAA35498. (PubMed:8325374)Curated
Sequence conflicti720 – 7201R → Q in AAA35498. (PubMed:8325374)Curated
Sequence conflicti726 – 7261D → N in AAA35498. (PubMed:8325374)Curated
Sequence conflicti843 – 8464TGPR → HGST in AAA52034. (PubMed:2760050)Curated
Sequence conflicti882 – 8843QGP → SGS in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1031 – 10322PP → RQ in AAC50213. (PubMed:7559422)Curated
Sequence conflicti1031 – 10322PP → RQ in AAC50214. (PubMed:7559422)Curated
Sequence conflicti1031 – 10322PP → RQ in AAC50215. (PubMed:7559422)Curated
Sequence conflicti1031 – 10322PP → RQ in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1091 – 10911D → V in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1124 – 11241A → R in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1127 – 11337EPGARGP → GAGGLGT in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1253 – 12531P → A in AAC50213. (PubMed:7559422)Curated
Sequence conflicti1253 – 12531P → A in AAC50214. (PubMed:7559422)Curated
Sequence conflicti1253 – 12531P → A in AAC50215. (PubMed:7559422)Curated
Sequence conflicti1253 – 12531P → A in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1257 – 12571T → Q in AAC50213. (PubMed:7559422)Curated
Sequence conflicti1257 – 12571T → Q in AAC50214. (PubMed:7559422)Curated
Sequence conflicti1257 – 12571T → Q in AAC50215. (PubMed:7559422)Curated
Sequence conflicti1257 – 12571T → Q in AAA52034. (PubMed:2760050)Curated
Sequence conflicti1552 – 15521E → R in AAA52034. (PubMed:2760050)Curated

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. 1 Publication
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. CuratedVSP_001167Add
BLAST
Alternative sequencei267 – 29024PTESL…GTTPD → VRELGEPPSAAHPREGRHPG ISPP in isoform 9. 1 PublicationVSP_043432Add
BLAST
Alternative sequencei291 – 17361446Missing in isoform 9. 1 PublicationVSP_043433Add
BLAST
Alternative sequencei293 – 31321Missing in isoform 3, isoform 5, isoform 7 and isoform 8. CuratedVSP_001168Add
BLAST
Alternative sequencei314 – 37360Missing in isoform 4, isoform 6, isoform 7 and isoform 8. CuratedVSP_001169Add
BLAST

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]
ENST00000549811; ENSP00000449275; ENSG00000227801. [P13942-1]
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 ]
ENST00000549811 ; ENSP00000449275 ; ENSG00000227801 . [P13942-1 ]
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 non-syndromic sensorineural deafness type DFNA.
90636. Autosomal recessive non-syndromic 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.
GeneTreei ENSGT00760000118776.
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

Bgeei P13942.
CleanExi HS_COL11A2.
ExpressionAtlasi P13942. baseline and differential.
Genevestigatori P13942.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
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: October 29, 2014
This is version 176 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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