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Q99715 (COCA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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(XII) chain
Gene names
Name:COL12A1
Synonyms:COL12A1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3063 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix By similarity.

Subunit structure

Trimer of identical chains each containing 190 kDa of non-triple-helical sequences.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Found in collagen I-containing tissues: both isoform 1 and isoform 2 appear in amnion, chorion, skeletal muscle, small intestine, and in cell culture of dermal fibroblasts, keratinocytes and endothelial cells. Only isoform 2 is found in lung, placenta, kidney and a squamous cell carcinoma cell line. Isoform 1 is also present in the corneal epithelial Bowman's membrane (BM) and the interfibrillar matrix of the corneal stroma, but it is not detected in the limbal BM. Ref.4

Post-translational modification

The triple-helical tail is stabilized by disulfide bonds at each end By similarity.

Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates By similarity.

Isoform 1 O-glycosylation; glycosaminoglycan of chondroitin-sulfate type By similarity.

Sequence similarities

Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.

Contains 4 collagen-like domains.

Contains 18 fibronectin type-III domains.

Contains 1 laminin G-like domain.

Contains 4 VWFA domains.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: The final tissue form of collagen XII may contain homotrimers of either isoform 1 or isoform 2 or any combination of isoform 1 and isoform 2.
Isoform 1 (identifier: Q99715-1)

Also known as: Long;

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 (identifier: Q99715-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     25-1188: Missing.
Isoform 4 (identifier: Q99715-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2651-2726: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 30633040Collagen alpha-1(XII) chain
PRO_0000005783

Regions

Domain27 – 11791Fibronectin type-III 1
Domain140 – 316177VWFA 1
Domain336 – 42691Fibronectin type-III 2
Domain440 – 616177VWFA 2
Domain634 – 72289Fibronectin type-III 3
Domain725 – 81692Fibronectin type-III 4
Domain817 – 90589Fibronectin type-III 5
Domain907 – 99892Fibronectin type-III 6
Domain999 – 108789Fibronectin type-III 7
Domain1089 – 117991Fibronectin type-III 8
Domain1199 – 1371173VWFA 3
Domain1387 – 147690Fibronectin type-III 9
Domain1477 – 156791Fibronectin type-III 10
Domain1568 – 165891Fibronectin type-III 11
Domain1659 – 175496Fibronectin type-III 12
Domain1755 – 184995Fibronectin type-III 13
Domain1850 – 193586Fibronectin type-III 14
Domain1936 – 202691Fibronectin type-III 15
Domain2027 – 211791Fibronectin type-III 16
Domain2118 – 220689Fibronectin type-III 17
Domain2207 – 229488Fibronectin type-III 18
Domain2323 – 2496174VWFA 4
Domain2520 – 2712193Laminin G-like
Domain2747 – 279852Collagen-like 1
Domain2802 – 285251Collagen-like 2
Domain2853 – 289846Collagen-like 3
Domain2941 – 299050Collagen-like 4
Region2451 – 2746296Nonhelical region (NC3)
Region2747 – 2898152Triple-helical region (COL2) with 1 imperfection
Region2899 – 294143Nonhelical region (NC2)
Region2942 – 3044103Triple-helical region (COL1) with 2 imperfections
Region3045 – 306319Nonhelical region (NC1)
Motif862 – 8643Cell attachment site Potential
Motif2779 – 27813Cell attachment site Potential
Motif2895 – 28973Cell attachment site Potential

Amino acid modifications

Modified residue294414-hydroxyproline By similarity
Modified residue294714-hydroxyproline By similarity
Modified residue295014-hydroxyproline By similarity
Modified residue295914-hydroxyproline By similarity
Modified residue296514-hydroxyproline By similarity
Modified residue296814-hydroxyproline By similarity
Modified residue297114-hydroxyproline By similarity
Modified residue298314-hydroxyproline By similarity
Modified residue300014-hydroxyproline By similarity
Modified residue300314-hydroxyproline By similarity
Modified residue301414-hydroxyproline By similarity
Modified residue302314-hydroxyproline By similarity
Modified residue302614-hydroxyproline By similarity
Modified residue302914-hydroxyproline By similarity
Glycosylation7001N-linked (GlcNAc...) Potential
Glycosylation7981O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation8891O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation9811O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation17631N-linked (GlcNAc...) Potential
Glycosylation22061N-linked (GlcNAc...) Potential
Glycosylation25281N-linked (GlcNAc...) Ref.6
Glycosylation26791N-linked (GlcNAc...) Ref.6

Natural variations

Alternative sequence25 – 11881164Missing in isoform 2.
VSP_001149
Alternative sequence2651 – 272676Missing in isoform 4.
VSP_024942
Natural variant4611A → P.
Corresponds to variant rs34730529 [ dbSNP | Ensembl ].
VAR_048768
Natural variant17381I → T.
Corresponds to variant rs240736 [ dbSNP | Ensembl ].
VAR_048769
Natural variant20211R → Q.
Corresponds to variant rs34438461 [ dbSNP | Ensembl ].
VAR_061111
Natural variant21601E → V.
Corresponds to variant rs35523808 [ dbSNP | Ensembl ].
VAR_048770
Natural variant25961I → V.
Corresponds to variant rs35710072 [ dbSNP | Ensembl ].
VAR_048771
Natural variant30481Q → H.
Corresponds to variant rs57396313 [ dbSNP | Ensembl ].
VAR_061112
Natural variant30581G → S. Ref.1
Corresponds to variant rs970547 [ dbSNP | Ensembl ].
VAR_032059

Experimental info

Sequence conflict471K → E in AAC51244. Ref.1
Sequence conflict441 – 4422IV → M in AAC01506. Ref.4
Sequence conflict5811R → D in AAC01506. Ref.4
Sequence conflict6891S → N in AAC01506. Ref.4
Sequence conflict7431W → S in AAC01506. Ref.4
Sequence conflict7491R → K in AAC01506. Ref.4
Sequence conflict7531Y → C in AAC51244. Ref.1
Sequence conflict8131V → G in AAC01506. Ref.4
Sequence conflict13551A → D in AAC51244. Ref.1
Sequence conflict16901A → G in AAC51244. Ref.1
Sequence conflict17291P → A in AAC51244. Ref.1
Sequence conflict1949 – 19513SLD → RLG in AAC51244. Ref.1
Sequence conflict26141P → S in AAB23937. Ref.5
Sequence conflict2647 – 26482SF → RK in AAB23937. Ref.5
Sequence conflict28481G → S in AAC51244. Ref.1
Sequence conflict28581P → R in AAC51244. Ref.1
Sequence conflict30351R → Q in AAC51244. Ref.1

Sequences

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

Last modified May 1, 2007. Version 2.
Checksum: EA38CAFECE8393D2

FASTA3,063333,147
        10         20         30         40         50         60 
MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD PIVGYRITVD 

        70         80         90        100        110        120 
PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV EESVPVIGQL TIQTGSSTKP 

       130        140        150        160        170        180 
VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIAALVSAF DIGEEKTRVG 

       190        200        210        220        230        240 
VVQYSSDTRT EFNLNQYYQR DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG 

       250        260        270        280        290        300 
FPKVAIIITD GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA 

       310        320        330        340        350        360 
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV KLNWNPSPSP 

       370        380        390        400        410        420 
VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY QISVSAMKGM TSSEPISIME 

       430        440        450        460        470        480 
KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLVKSF EISPNRVQIS 

       490        500        510        520        530        540 
LVQYSRDPHT EFTLKKFTKV EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN 

       550        560        570        580        590        600 
VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE 

       610        620        630        640        650        660 
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT NWSPAGENVF 

       670        680        690        700        710        720 
SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN VTAEYEDGFS IPLAGEETTE 

       730        740        750        760        770        780 
EVKGAPRNLK VTDETTDSFK ITWTQAPGRV LRYRIIYRPV AGGESREVTT PPNQRRRTLE 

       790        800        810        820        830        840 
NLIPDTKYEV SVIPEYFSGP GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK 

       850        860        870        880        890        900 
VKQYLVTYTP VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT 

       910        920        930        940        950        960 
TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE KNLPEDAIHT 

       970        980        990       1000       1010       1020 
MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK TLKVDEETEN TMRVTWKPAP 

      1030       1040       1050       1060       1070       1080 
GKVVNYRVVY RPHGRGKQMV AKVPPTVTST VLKRLQPQTT YDITVLPIYK MGEGKLRQGS 

      1090       1100       1110       1120       1130       1140 
GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN 

      1150       1160       1170       1180       1190       1200 
TVVLEELRAG TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI 

      1210       1220       1230       1240       1250       1260 
VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK 

      1270       1280       1290       1300       1310       1320 
SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA RKIGVLITDG KSQDDVEAPS 

      1330       1340       1350       1360       1370       1380 
KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSRIVDD LTINLCNSVK 

      1390       1400       1410       1420       1430       1440 
GPGDLEAPSN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV 

      1450       1460       1470       1480       1490       1500 
LKDLKPETEY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA 

      1510       1520       1530       1540       1550       1560 
TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH DLTSEPVTVR 

      1570       1580       1590       1600       1610       1620 
EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY KTPEEDVKEV EVDRSETSTS 

      1630       1640       1650       1660       1670       1680 
LKDLFSQTLY TVSVSAVHDE GESPPVTAQE TTRPVPAPTN LKITEVTSEG FRGTWDHGAS 

      1690       1700       1710       1720       1730       1740 
DVSLYRITWA PFGSSDKMET ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS 

      1750       1760       1770       1780       1790       1800 
ERTLPILTTQ APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT 

      1810       1820       1830       1840       1850       1860 
IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL RVYDPSTSTL 

      1870       1880       1890       1900       1910       1920 
NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL RNLQPDTSYT VTVVPVYTEG 

      1930       1940       1950       1960       1970       1980 
DGGRTSDTGR TLMRGLARNV QVYNPTPNSL DVRWDPAPGP VLQYRVVYSP VDGTRPSESI 

      1990       2000       2010       2020       2030       2040 
VVPGNTRMVH LERLIPDTLY SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS 

      2050       2060       2070       2080       2090       2100 
LSVAWDHADG PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE 

      2110       2120       2130       2140       2150       2160 
DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY KPVGSNEPME 

      2170       2180       2190       2200       2210       2220 
AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG TTLYLNVTDL KTYQIGWDTF 

      2230       2240       2250       2260       2270       2280 
CVKWSPHRAA TSYRLKLSPA DGTRGQEITV RGSETSHCFT GLSPDTDYGV TVFVQTPNLE 

      2290       2300       2310       2320       2330       2340 
GPGVSVKEHT TVKPTEAPTE PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN 

      2350       2360       2370       2380       2390       2400 
KVVKFIFNTV GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN 

      2410       2420       2430       2440       2450       2460 
TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ SGFSVFVVGV 

      2470       2480       2490       2500       2510       2520 
ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV CETATSSCPL IYLDGYTSPG 

      2530       2540       2550       2560       2570       2580 
FKMLEAYNLT EKNFASVQGV SLESGSFPSY SAYRIQKNAF VNQPTADLHP NGLPPSYTII 

      2590       2600       2610       2620       2630       2640 
LLFRLLPETP SDPFAIWQIT DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV 

      2650       2660       2670       2680       2690       2700 
KTLFYGSFHK VHIVVTSKSV KIYIDCYEII EKDIKEAGNI TTDGYEILGK LLKGERKSAA 

      2710       2720       2730       2740       2750       2760 
FQIQSFDIVC SPVWTSRDRC CDIPSRRDEG KCPAFPNSCT CTQDSVGPPG PPGPAGGPGA 

      2770       2780       2790       2800       2810       2820 
KGPRGERGIS GAIGPPGPRG DIGPPGPQGP PGPQGPNGLS IPGEQGRQGM KGDAGEPGLP 

      2830       2840       2850       2860       2870       2880 
GRTGTPGLPG PPGPMGPPGD RGFTGKDGAM GPRGPPGPPG SPGSPGVTGP SGKPGKPGDH 

      2890       2900       2910       2920       2930       2940 
GRPGPSGLKG EKGDRGDIAS QNMMRAVARQ VCEQLISGQM NRFNQMLNQI PNDYQSSRNQ 

      2950       2960       2970       2980       2990       3000 
PGPPGPPGPP GSAGARGEPG PGGRPGFPGT PGMQGPPGER GLPGEKGERG TGSSGPRGLP 

      3010       3020       3030       3040       3050       3060 
GPPGPQGESR TGPPGSTGSR GPPGPPGRPG NSGIRGPPGP PGYCDSSQCA SIPYNGQGYP 


GSG 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: ECFB9F5436FF7B24
Show »

FASTA1,899205,491
Isoform 4 [UniParc].

Checksum: E5EEB57CBFB556E2
Show »

FASTA2,987324,570

References

« Hide 'large scale' references
[1]"Complete primary structure of two splice variants of collagen XII, and assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX) collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-q13."
Gerecke D.R., Olson P.F., Koch M., Knoll J.H.M., Taylor R., Hudson D.L., Champliaud M.-F., Olsen B.R., Burgeson R.E.
Genomics 41:236-242(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1280-1295; 1782-1801 AND 2906-2916, VARIANT SER-3058.
[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. expand/collapse author list , 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]"The chick and human collagen alpha1(XII) gene promoter -- activity of highly conserved regions around the first exon and in the first intron."
Chiquet M., Mumenthaler U., Wittwer M., Jin W., Koch M.
Eur. J. Biochem. 257:362-371(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[4]"Type XII collagen contributes to diversities in human corneal and limbal extracellular matrices."
Wessel H., Anderson S., Fite D., Halvas E., Hempel J., SundarRaj N.
Invest. Ophthalmol. Vis. Sci. 38:2408-2422(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-816 (ISOFORMS 1/4), TISSUE SPECIFICITY.
Tissue: Cornea.
[5]"The mouse alpha 1(XII) and human alpha 1(XII)-like collagen genes are localized on mouse chromosome 9 and human chromosome 6."
Oh S.P., Taylor R.W., Gerecke D.R., Rochelle J.M., Seldin M.F., Olsen B.R.
Genomics 14:225-231(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2567-2755 (ISOFORM 4).
[6]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2528 AND ASN-2679.
Tissue: Liver.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73778 mRNA. Translation: AAC51244.1.
U73779 mRNA. Translation: AAD40483.1.
AL080250, AL096771, AL354664 Genomic DNA. Translation: CAI19898.1.
AL354664, AL080250, AL096771 Genomic DNA. Translation: CAH71310.1.
AL096771, AL354664, AL080250 Genomic DNA. Translation: CAI19908.1.
AF061871 Genomic DNA. Translation: AAC83578.1.
U68139 mRNA. Translation: AAC01506.1.
AH004088 Genomic DNA. Translation: AAB23937.2.
CCDSCCDS43481.1. [Q99715-2]
CCDS43482.1. [Q99715-1]
PIRA44479.
RefSeqNP_004361.3. NM_004370.5. [Q99715-1]
NP_542376.2. NM_080645.2. [Q99715-2]
UniGeneHs.101302.

3D structure databases

ProteinModelPortalQ99715.
SMRQ99715. Positions 25-1179, 1196-1367, 1385-2310, 2317-2724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107700. 1 interaction.
IntActQ99715. 6 interactions.
STRING9606.ENSP00000325146.

PTM databases

PhosphoSiteQ99715.

Polymorphism databases

DMDM146345397.

Proteomic databases

MaxQBQ99715.
PaxDbQ99715.
PRIDEQ99715.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322507; ENSP00000325146; ENSG00000111799. [Q99715-1]
ENST00000345356; ENSP00000305147; ENSG00000111799. [Q99715-2]
ENST00000416123; ENSP00000412864; ENSG00000111799. [Q99715-4]
GeneID1303.
KEGGhsa:1303.
UCSCuc003phs.3. human. [Q99715-1]
uc003pht.3. human. [Q99715-2]

Organism-specific databases

CTD1303.
GeneCardsGC06M075850.
H-InvDBHIX0006013.
HGNCHGNC:2188. COL12A1.
HPAHPA009143.
MIM120320. gene.
neXtProtNX_Q99715.
PharmGKBPA26704.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG051060.
InParanoidQ99715.
KOK08132.
OMANRFNQML.
PhylomeDBQ99715.
TreeFamTF329914.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ99715.
BgeeQ99715.
CleanExHS_COL12A1.
GenevestigatorQ99715.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
2.60.40.10. 18 hits.
3.40.50.410. 4 hits.
InterProIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view]
PfamPF01391. Collagen. 4 hits.
PF00041. fn3. 18 hits.
PF00092. VWA. 4 hits.
[Graphical view]
SMARTSM00060. FN3. 18 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 4 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 11 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 4 hits.
PROSITEPS50853. FN3. 18 hits.
PS50234. VWFA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL12A1. human.
GeneWikiCollagen,_type_XII,_alpha_1.
GenomeRNAi1303.
NextBio5299.
PROQ99715.
SOURCESearch...

Entry information

Entry nameCOCA1_HUMAN
AccessionPrimary (citable) accession number: Q99715
Secondary accession number(s): O43853 expand/collapse secondary AC list , Q15955, Q5VYK1, Q5VYK2, Q71UR3, Q99716
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

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 6

Human chromosome 6: entries, gene names and cross-references to MIM