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P13942

- COBA2_HUMAN

UniProt

P13942 - COBA2_HUMAN

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
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 5 (25 Jan 2012)
      Previous versions | rss
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    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 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

    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

    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 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 – 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

    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.
    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.
    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

    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 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

    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 1, 2014
    This is version 175 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