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Q5TAT6 (CODA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XIII) chain
Alternative name(s):
COLXIIIA1
Gene names
Name:COL13A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin. Ref.10 Ref.11 UniProtKB Q9R1N9

Subunit structure

Homotrimer; disulfide-linked. Nucleation of the type XIII collagen triple helix is likely to occur at the N-terminal region with triple helix formation proceeding from the N- to the C-terminus. Interacts with FN1, perlecan/HSPG2 and NID2. Ref.1 Ref.10 Ref.11

Subcellular location

Cell membrane; Single-pass type II membrane protein Ref.1 UniProtKB Q9R1N9.

Tissue specificity

Widely expressed in both fetal and adult ocular tissues (at protein level). In the eye, expression is accentuated in the ciliary muscle, optic nerve and the neural retina. In early placenta, localized to fibroblastoid stromal cells of the placental villi, to endothelial cells of developing capillaries and to cells of the cytotrophoblastic columns. Also detected in large decidual cells of the decidual membrane and to stromal cells of the gestational endometrium, but not in the epithelial cells in the endometrial glands. Ref.9 Ref.10

Sequence caution

The sequence AAA51685.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
Osteogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCollagen
Signal-anchor
Transmembrane
Transmembrane helix
   LigandHeparin-binding
   Molecular functionDevelopmental protein
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell-cell adhesion

Inferred from expression pattern Ref.10. Source: UniProtKB

cell-matrix adhesion

Inferred from physical interaction Ref.11. Source: UniProtKB

collagen catabolic process

Traceable author statement. Source: Reactome

endochondral ossification

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

morphogenesis of a branching structure

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell-cell junction

Inferred from electronic annotation. Source: Ensembl

collagen type XIII

Traceable author statement Ref.6. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionheparin binding

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 Ref.1 (identifier: Q5TAT6-1)

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.
Isoform 2 Ref.2 (identifier: Q5TAT6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     239-260: Missing.
Note: Gene prediction based on EST data.
Isoform 3 Ref.2 (identifier: Q5TAT6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     239-260: Missing.
     617-628: Missing.
Note: Gene prediction based on EST data.
Isoform 4 Ref.4 (identifier: Q5TAT6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     239-260: Missing.
     551-565: Missing.
     617-628: Missing.
Isoform 5 Ref.5 (identifier: Q5TAT6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     551-565: Missing.
Isoform 6 Ref.6 (identifier: Q5TAT6-6)

The sequence of this isoform differs from the canonical sequence as follows:
     566-579: Missing.
Isoform 7 Ref.6 (identifier: Q5TAT6-7)

The sequence of this isoform differs from the canonical sequence as follows:
     566-579: Missing.
     617-628: Missing.
Isoform 8 Ref.4 (identifier: Q5TAT6-8)

The sequence of this isoform differs from the canonical sequence as follows:
     220-238: Missing.
     617-628: Missing.
Isoform 9 Ref.4 (identifier: Q5TAT6-9)

The sequence of this isoform differs from the canonical sequence as follows:
     239-260: Missing.
     551-565: Missing.
     617-628: Missing.
     676-705: Missing.
Isoform 10 (identifier: Q5TAT6-10)

The sequence of this isoform differs from the canonical sequence as follows:
     122-159: Missing.
     220-238: Missing.
     551-565: Missing.
Note: No experimental confirmation available.
Isoform 11 (identifier: Q5TAT6-11)

The sequence of this isoform differs from the canonical sequence as follows:
     135-163: Missing.
     239-260: Missing.
     551-565: Missing.
     617-628: Missing.
     678-706: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Collagen alpha-1(XIII) chain
PRO_0000284679

Regions

Topological domain1 – 4444Cytoplasmic Potential
Transmembrane45 – 6117Helical; Signal-anchor for type II membrane protein; Potential
Topological domain62 – 717656Extracellular Potential
Region1 – 121121Nonhelical region 1 (NC1)
Region122 – 21695Triple-helical region 1 (COL1)
Region217 – 26953Nonhelical region 2 (NC2)
Region270 – 441172Triple-helical region 2 (COL2)
Region442 – 46322Nonhelical region 3 (NC3)
Region464 – 699236Triple-helical region 3 (COL3)
Region700 – 71718Nonhelical region 4 (NC4)

Natural variations

Alternative sequence122 – 15938Missing in isoform 10.
VSP_043361
Alternative sequence135 – 16329Missing in isoform 11.
VSP_047230
Alternative sequence220 – 23819Missing in isoform 8 and isoform 10. Ref.4
VSP_052382
Alternative sequence239 – 26022Missing in isoform 2, isoform 3, isoform 4, isoform 9 and isoform 11. Ref.2 Ref.4 Ref.5
VSP_052383
Alternative sequence551 – 56515Missing in isoform 4, isoform 5, isoform 9, isoform 10 and isoform 11. Ref.4 Ref.5
VSP_052384
Alternative sequence566 – 57914Missing in isoform 6 and isoform 7. Ref.6
VSP_052385
Alternative sequence617 – 62812Missing in isoform 3, isoform 4, isoform 7, isoform 8, isoform 9 and isoform 11. Ref.2 Ref.4 Ref.6
VSP_052386
Alternative sequence676 – 70530Missing in isoform 9. Ref.4
VSP_052387
Alternative sequence678 – 70629Missing in isoform 11.
VSP_047231
Natural variant5311H → Q.
Corresponds to variant rs1061954 [ dbSNP | Ensembl ].
VAR_055670

Experimental info

Sequence conflict1821K → F in AAA51685. Ref.4
Sequence conflict3941G → A in CAC00688. Ref.1
Sequence conflict3941G → A in AAA51685. Ref.4
Sequence conflict4661P → L in AAA51685. Ref.4
Sequence conflict4661P → L in AAA52047. Ref.5
Sequence conflict4691P → L in AAA51685. Ref.4
Sequence conflict4691P → L in AAA52047. Ref.5
Sequence conflict4751P → L in AAA51685. Ref.4
Sequence conflict4751P → L in AAA52047. Ref.5
Sequence conflict4781P → L in AAA51685. Ref.4
Sequence conflict4781P → L in AAA52047. Ref.5
Sequence conflict480 – 4812IP → ML in AAA51685. Ref.4
Sequence conflict480 – 4812IP → ML in AAA52047. Ref.5
Sequence conflict4901P → L in AAA51685. Ref.4
Sequence conflict4901P → L in AAA52047. Ref.5
Sequence conflict4931P → L in AAA51685. Ref.4
Sequence conflict4931P → L in AAA52047. Ref.5
Sequence conflict4981Missing in AAA51685. Ref.4
Sequence conflict4981Missing in AAA52047. Ref.5
Sequence conflict5051P → L in AAA51685. Ref.4
Sequence conflict5051P → L in AAA52047. Ref.5
Sequence conflict5111P → L in AAA51685. Ref.4
Sequence conflict5111P → L in AAA52047. Ref.5
Sequence conflict5171P → L in AAA51685. Ref.4
Sequence conflict5171P → L in AAA52047. Ref.5
Sequence conflict5701P → L in AAA52047. Ref.5
Sequence conflict5701P → L in AAA51987. Ref.6
Sequence conflict5701P → L in AAA51990. Ref.6
Sequence conflict5701P → L in AAA51991. Ref.6
Sequence conflict7061E → Q in AAA52047. Ref.5
Sequence conflict7061E → Q in AAA52048. Ref.5
Sequence conflict7061E → Q in AAA51987. Ref.6
Sequence conflict7061E → Q in AAA51988. Ref.6
Sequence conflict7061E → Q in AAA51989. Ref.6
Sequence conflict7061E → Q in AAA51990. Ref.6
Sequence conflict7061E → Q in AAA51991. Ref.6
Sequence conflict7091L → Y in AAA51987. Ref.6
Sequence conflict7091L → Y in AAA51988. Ref.6
Sequence conflict7091L → Y in AAA51989. Ref.6
Sequence conflict7091L → Y in AAA51990. Ref.6
Sequence conflict7091L → Y in AAA51991. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: FD12CA80CC93540F

FASTA71769,950
        10         20         30         40         50         60 
MVAERTHKAA ATGARGPGEL GAPGTVALVA ARAERGARLP SPGSCGLLTL ALCSLALSLL 

        70         80         90        100        110        120 
AHFRTAELQA RVLRLEAERG EQQMETAILG RVNQLLDEKW KLHSRRRREA PKTSPGCNCP 

       130        140        150        160        170        180 
PGPPGPTGRP GLPGDKGAIG MPGRVGSPGD AGLSIIGPRG PPGQPGTRGF PGFPGPIGLD 

       190        200        210        220        230        240 
GKPGHPGPKG DMGLTGPPGQ PGPQGQKGEK GQCGEYPHRE CLSSMPAALR SSQIIALKLL 

       250        260        270        280        290        300 
PLLNSVRLAP PPVIKRRTFQ GEQSQASIQG PPGPPGPPGP SGPLGHPGLP GPMGPPGLPG 

       310        320        330        340        350        360 
PPGPKGDPGI QGYHGRKGER GMPGMPGKHG AKGAPGIAVA GMKGEPGIPG TKGEKGAEGS 

       370        380        390        400        410        420 
PGLPGLLGQK GEKGDAGNSI GGGRGEPGPP GLPGPPGPKG EAGVDGQVGP PGQPGDKGER 

       430        440        450        460        470        480 
GAAGEQGPDG PKGSKGEPGK GEMVDYNGNI NEALQEIRTL ALMGPPGLPG QIGPPGAPGI 

       490        500        510        520        530        540 
PGQKGEIGLP GPPGHDGEKG PRGKPGDMGP PGPQGPPGKD GPPGVKGENG HPGSPGEKGE 

       550        560        570        580        590        600 
KGETGQAGSP GEKGEAGEKG NPGAEVPGLP GPEGPPGPPG LQGVPGPKGE AGLDGAKGEK 

       610        620        630        640        650        660 
GFQGEKGDRG PLGLPGASGL DGRPGPPGTP GPIGVPGPAG PKGERGSKGD PGMTGPTGAA 

       670        680        690        700        710 
GLPGLHGPPG DKGNRGERGK KGSRGPKGDK GDQGAPGLDA PCPLGEDGLP VQGCWNK 

« Hide

Isoform 2 [UniParc].

Checksum: 9816F7BCDD8C108B
Show »

FASTA69567,439
Isoform 3 [UniParc].

Checksum: 3BB550FD03062C30
Show »

FASTA68366,377
Isoform 4 [UniParc].

Checksum: AAC18C9E4B45DA4E
Show »

FASTA66864,965
Isoform 5 [UniParc].

Checksum: 66FC08083E0D4A91
Show »

FASTA70268,538
Isoform 6 [UniParc].

Checksum: 62947B1FEEBF6268
Show »

FASTA70368,700
Isoform 7 [UniParc].

Checksum: EEC688B6A5364877
Show »

FASTA69167,638
Isoform 8 [UniParc].

Checksum: 0256074DDF33E752
Show »

FASTA68666,887
Isoform 9 [UniParc].

Checksum: E172A8ADA30B84DC
Show »

FASTA63862,077
Isoform 10 [UniParc].

Checksum: 2BD4AF1794648BDA
Show »

FASTA64563,036
Isoform 11 [UniParc].

Checksum: DDDD4D432DD45849
Show »

FASTA61059,465

References

« Hide 'large scale' references
[1]"A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins."
Snellman A., Tu H., Vaisanen T., Kvist A.-P., Huhtala P., Pihlajaniemi T.
EMBO J. 19:5051-5059(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 10).
Tissue: Testis.
[4]"The alpha 1 chain of type XIII collagen consists of three collagenous and four noncollagenous domains, and its primary transcript undergoes complex alternative splicing."
Pihlajaniemi T., Tamminen M.
J. Biol. Chem. 265:16922-16928(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 44-717 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 84-717 (ISOFORMS 8 AND 9).
Tissue: Endothelial cell.
[5]"Partial characterization of a low molecular weight human collagen that undergoes alternative splicing."
Pihlajaniemi T., Myllyla R., Seyer J., Kurkinen M., Prockop D.J.
Proc. Natl. Acad. Sci. U.S.A. 84:940-944(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 457-717 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 573-717 (ISOFORMS 3/4/7/8).
Tissue: Fibrosarcoma.
[6]"Gene structure for the alpha 1 chain of a human short-chain collagen (type XIII) with alternatively spliced transcripts and translation termination codon at the 5' end of the last exon."
Tikka L., Pihlajaniemi T., Henttu P., Prockop D.J., Tryggvason K.
Proc. Natl. Acad. Sci. U.S.A. 85:7491-7495(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 551-717 (ISOFORMS 6 AND 7), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 551-717 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 566-771 (ISOFORMS 3/4/8).
[7]"Characterization of the spectrum of alternative splicing of alpha 1 (XIII) collagen transcripts in HT-1080 cells and calvarial tissue resulted in identification of two previously unidentified alternatively spliced sequences, one previously unidentified exon, and nine new mRNA variants."
Juvonen M., Pihlajaniemi T.
J. Biol. Chem. 267:24693-24699(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[8]"Patterns of expression of the six alternatively spliced exons affecting the structures of the COL1 and NC2 domains of the alpha 1(XIII) collagen chain in human tissues and cell lines."
Juvonen M., Sandberg M., Pihlajaniemi T.
J. Biol. Chem. 267:24700-24707(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[9]"Location and alternative splicing of type XIII collagen RNA in the early human placenta."
Juvonen M., Pihlajaniemi T., Autio-Harmainen H.
Lab. Invest. 69:541-551(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[10]"Type XIII collagen is widely expressed in the adult and developing human eye and accentuated in the ciliary muscle, the optic nerve and the neural retina."
Sandberg-Lall M., Hagg P.O., Wahlstrom I., Pihlajaniemi T.
Exp. Eye Res. 70:401-410(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]"The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin."
Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R., Pihlajaniemi T.
J. Biol. Chem. 277:23092-23099(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FN1; HSPG2 AND NID2, HEPARIN-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ293624 mRNA. Translation: CAC00688.1.
AC024601 Genomic DNA. No translation available.
AC025426 Genomic DNA. No translation available.
AL138925 Genomic DNA. No translation available.
BC136385 mRNA. Translation: AAI36386.1.
M59217 mRNA. Translation: AAA51685.1. Different initiation.
M33653 mRNA. Translation: AAA52047.1.
M15524 mRNA. Translation: AAA52048.1.
M20803 expand/collapse EMBL AC list , M20795, M20796, M20797, M20798, M20799, M20800, M20801, M20802, M20804, M20805 Genomic DNA. Translation: AAA51987.1.
M20803 expand/collapse EMBL AC list , M20795, M20796, M20797, M20798, M20799, M20800, M20801, M20802, M20804 Genomic DNA. Translation: AAA51988.1.
M20803 expand/collapse EMBL AC list , M20795, M20796, M20797, M20798, M20799, M20801, M20802, M20804 Genomic DNA. Translation: AAA51989.1.
M20803 expand/collapse EMBL AC list , M20796, M20797, M20798, M20799, M20800, M20801, M20802, M20804, M20805 Genomic DNA. Translation: AAA51990.1.
M20803 expand/collapse EMBL AC list , M20796, M20797, M20798, M20799, M20801, M20802, M20804, M20805 Genomic DNA. Translation: AAA51991.1.
PIRB40983.
RefSeqNP_001123575.1. NM_001130103.1.
NP_542988.3. NM_080798.3.
NP_542990.3. NM_080800.3.
NP_542991.3. NM_080801.3.
NP_542992.3. NM_080802.3.
NP_542995.3. NM_080805.3.
UniGeneHs.695934.

3D structure databases

ProteinModelPortalQ5TAT6.
ModBaseSearch...
MobiDBSearch...

Chemistry

DrugBankDB01076. Atorvastatin.
DB00641. Simvastatin.

PTM databases

PhosphoSiteQ5TAT6.

Polymorphism databases

DMDM74745860.

Proteomic databases

PaxDbQ5TAT6.
PRIDEQ5TAT6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354547; ENSP00000346553; ENSG00000197467. [Q5TAT6-2]
ENST00000357811; ENSP00000350463; ENSG00000197467. [Q5TAT6-3]
ENST00000398978; ENSP00000381949; ENSG00000197467. [Q5TAT6-1]
ENST00000517713; ENSP00000430061; ENSG00000197467. [Q5TAT6-4]
ENST00000520133; ENSP00000430173; ENSG00000197467. [Q5TAT6-11]
ENST00000520267; ENSP00000428057; ENSG00000197467. [Q5TAT6-10]
ENST00000522165; ENSP00000428342; ENSG00000197467. [Q5TAT6-8]
GeneID1305.
KEGGhsa:1305.
UCSCuc001jqk.2. human. [Q5TAT6-2]
uc001jql.3. human. [Q5TAT6-1]
uc010qjf.2. human. [Q5TAT6-10]
uc021prz.1. human. [Q5TAT6-4]
uc021psc.1. human. [Q5TAT6-8]

Organism-specific databases

CTD1305.
GeneCardsGC10P071561.
H-InvDBHIX0025928.
HGNCHGNC:2190. COL13A1.
HPAHPA050392.
MIM120350. gene.
neXtProtNX_Q5TAT6.
PharmGKBPA26706.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254293.
HOGENOMHOG000085653.
HOVERGENHBG004933.
KOK16617.
PhylomeDBQ5TAT6.
TreeFamTF338175.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ5TAT6.
BgeeQ5TAT6.
GenevestigatorQ5TAT6.

Family and domain databases

InterProIPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCollagen,_type_XIII,_alpha_1.
GenomeRNAi1305.
NextBio5305.
PROQ5TAT6.
SOURCESearch...

Entry information

Entry nameCODA1_HUMAN
AccessionPrimary (citable) accession number: Q5TAT6
Secondary accession number(s): A6NFR5 expand/collapse secondary AC list , B9EGD2, E7EWL8, Q13992, Q13993, Q13994, Q13995, Q13996, Q5TAT4, Q5TAT5, Q7KZ33, Q7KZ49, Q99228, Q9NQ52
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM