Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q99715

- COCA1_HUMAN

UniProt

Q99715 - COCA1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Collagen alpha-1(XII) chain

Gene

COL12A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. extracellular matrix structural constituent conferring tensile strength Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. collagen catabolic process Source: Reactome
  3. collagen fibril organization Source: UniProtKB
  4. endodermal cell differentiation Source: UniProtKB
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150401. Collagen degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XII) chain
Gene namesi
Name:COL12A1
Synonyms:COL12A1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2188. COL12A1.

Subcellular locationi

GO - Cellular componenti

  1. collagen type XII trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProtKB
  7. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

Orphaneti610. Bethlem myopathy.
75840. Congenital muscular dystrophy, Ullrich type.
PharmGKBiPA26704.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 30633040Collagen alpha-1(XII) chainPRO_0000005783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi798 – 7981O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi889 – 8891O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi981 – 9811O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2206 – 22061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2528 – 25281N-linked (GlcNAc...)1 Publication
Glycosylationi2679 – 26791N-linked (GlcNAc...)1 Publication
Modified residuei2944 – 294414-hydroxyprolineBy similarity
Modified residuei2947 – 294714-hydroxyprolineBy similarity
Modified residuei2950 – 295014-hydroxyprolineBy similarity
Modified residuei2959 – 295914-hydroxyprolineBy similarity
Modified residuei2965 – 296514-hydroxyprolineBy similarity
Modified residuei2968 – 296814-hydroxyprolineBy similarity
Modified residuei2971 – 297114-hydroxyprolineBy similarity
Modified residuei2983 – 298314-hydroxyprolineBy similarity
Modified residuei3000 – 300014-hydroxyprolineBy similarity
Modified residuei3003 – 300314-hydroxyprolineBy similarity
Modified residuei3014 – 301414-hydroxyprolineBy similarity
Modified residuei3023 – 302314-hydroxyprolineBy similarity
Modified residuei3026 – 302614-hydroxyprolineBy similarity
Modified residuei3029 – 302914-hydroxyprolineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ99715.
PaxDbiQ99715.
PRIDEiQ99715.

PTM databases

PhosphoSiteiQ99715.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ99715.
CleanExiHS_COL12A1.
ExpressionAtlasiQ99715. baseline and differential.
GenevestigatoriQ99715.

Organism-specific databases

HPAiHPA009143.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107700. 1 interaction.
IntActiQ99715. 6 interactions.
STRINGi9606.ENSP00000325146.

Structurei

3D structure databases

ProteinModelPortaliQ99715.
SMRiQ99715. Positions 25-317, 336-418, 440-616, 633-1179, 1196-1367, 1385-2310, 2323-2485, 2508-2724.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 11791Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 316177VWFA 1PROSITE-ProRule annotationAdd
BLAST
Domaini336 – 42691Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini440 – 616177VWFA 2PROSITE-ProRule annotationAdd
BLAST
Domaini634 – 72289Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini725 – 81692Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini817 – 90589Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini907 – 99892Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini999 – 108789Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1089 – 117991Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1199 – 1371173VWFA 3PROSITE-ProRule annotationAdd
BLAST
Domaini1387 – 147690Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1477 – 156791Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini1568 – 165891Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini1659 – 175496Fibronectin type-III 12PROSITE-ProRule annotationAdd
BLAST
Domaini1755 – 184995Fibronectin type-III 13PROSITE-ProRule annotationAdd
BLAST
Domaini1850 – 193586Fibronectin type-III 14PROSITE-ProRule annotationAdd
BLAST
Domaini1936 – 202691Fibronectin type-III 15PROSITE-ProRule annotationAdd
BLAST
Domaini2027 – 211791Fibronectin type-III 16PROSITE-ProRule annotationAdd
BLAST
Domaini2118 – 220689Fibronectin type-III 17PROSITE-ProRule annotationAdd
BLAST
Domaini2207 – 229488Fibronectin type-III 18PROSITE-ProRule annotationAdd
BLAST
Domaini2323 – 2496174VWFA 4PROSITE-ProRule annotationAdd
BLAST
Domaini2520 – 2712193Laminin G-likeAdd
BLAST
Domaini2747 – 279852Collagen-like 1Add
BLAST
Domaini2802 – 285251Collagen-like 2Add
BLAST
Domaini2853 – 289846Collagen-like 3Add
BLAST
Domaini2941 – 299050Collagen-like 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2451 – 2746296Nonhelical region (NC3)Add
BLAST
Regioni2747 – 2898152Triple-helical region (COL2) with 1 imperfectionAdd
BLAST
Regioni2899 – 294143Nonhelical region (NC2)Add
BLAST
Regioni2942 – 3044103Triple-helical region (COL1) with 2 imperfectionsAdd
BLAST
Regioni3045 – 306319Nonhelical region (NC1)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi862 – 8643Cell attachment siteSequence Analysis
Motifi2779 – 27813Cell attachment siteSequence Analysis
Motifi2895 – 28973Cell attachment siteSequence Analysis

Sequence similaritiesi

Contains 4 collagen-like domains.Curated
Contains 18 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 4 VWFA domains.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119000.
HOVERGENiHBG051060.
InParanoidiQ99715.
KOiK08132.
OMAiNRFNQML.
PhylomeDBiQ99715.
TreeFamiTF329914.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
2.60.40.10. 18 hits.
3.40.50.410. 4 hits.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF00041. fn3. 18 hits.
PF00092. VWA. 4 hits.
[Graphical view]
SMARTiSM00060. FN3. 18 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 4 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 11 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 4 hits.
PROSITEiPS50853. FN3. 18 hits.
PS50234. VWFA. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

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) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD
60 70 80 90 100
PIVGYRITVD PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV
110 120 130 140 150
EESVPVIGQL TIQTGSSTKP VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS
160 170 180 190 200
VGRNNFKYIL DFIAALVSAF DIGEEKTRVG VVQYSSDTRT EFNLNQYYQR
210 220 230 240 250
DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG FPKVAIIITD
260 270 280 290 300
GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA
310 320 330 340 350
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV
360 370 380 390 400
KLNWNPSPSP VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY
410 420 430 440 450
QISVSAMKGM TSSEPISIME KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS
460 470 480 490 500
IGIANFVKVR AFLEVLVKSF EISPNRVQIS LVQYSRDPHT EFTLKKFTKV
510 520 530 540 550
EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN VPKVMILITD
560 570 580 590 600
GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE
610 620 630 640 650
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT
660 670 680 690 700
NWSPAGENVF SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN
710 720 730 740 750
VTAEYEDGFS IPLAGEETTE EVKGAPRNLK VTDETTDSFK ITWTQAPGRV
760 770 780 790 800
LRYRIIYRPV AGGESREVTT PPNQRRRTLE NLIPDTKYEV SVIPEYFSGP
810 820 830 840 850
GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK VKQYLVTYTP
860 870 880 890 900
VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT
910 920 930 940 950
TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE
960 970 980 990 1000
KNLPEDAIHT MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK
1010 1020 1030 1040 1050
TLKVDEETEN TMRVTWKPAP GKVVNYRVVY RPHGRGKQMV AKVPPTVTST
1060 1070 1080 1090 1100
VLKRLQPQTT YDITVLPIYK MGEGKLRQGS GTTASRFKSP RNLKTSDPTM
1110 1120 1130 1140 1150
SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN TVVLEELRAG
1160 1170 1180 1190 1200
TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI
1210 1220 1230 1240 1250
VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE
1260 1270 1280 1290 1300
WQLNAHRDKK SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA
1310 1320 1330 1340 1350
RKIGVLITDG KSQDDVEAPS KKLKDEGVEL FAIGIKNADE VELKMIATDP
1360 1370 1380 1390 1400
DDTHAYNVAD FESLSRIVDD LTINLCNSVK GPGDLEAPSN LVISERTHRS
1410 1420 1430 1440 1450
FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV LKDLKPETEY
1460 1470 1480 1490 1500
VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA
1510 1520 1530 1540 1550
TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH
1560 1570 1580 1590 1600
DLTSEPVTVR EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY
1610 1620 1630 1640 1650
KTPEEDVKEV EVDRSETSTS LKDLFSQTLY TVSVSAVHDE GESPPVTAQE
1660 1670 1680 1690 1700
TTRPVPAPTN LKITEVTSEG FRGTWDHGAS DVSLYRITWA PFGSSDKMET
1710 1720 1730 1740 1750
ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS ERTLPILTTQ
1760 1770 1780 1790 1800
APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT
1810 1820 1830 1840 1850
IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL
1860 1870 1880 1890 1900
RVYDPSTSTL NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL
1910 1920 1930 1940 1950
RNLQPDTSYT VTVVPVYTEG DGGRTSDTGR TLMRGLARNV QVYNPTPNSL
1960 1970 1980 1990 2000
DVRWDPAPGP VLQYRVVYSP VDGTRPSESI VVPGNTRMVH LERLIPDTLY
2010 2020 2030 2040 2050
SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS LSVAWDHADG
2060 2070 2080 2090 2100
PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE
2110 2120 2130 2140 2150
DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY
2160 2170 2180 2190 2200
KPVGSNEPME AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG
2210 2220 2230 2240 2250
TTLYLNVTDL KTYQIGWDTF CVKWSPHRAA TSYRLKLSPA DGTRGQEITV
2260 2270 2280 2290 2300
RGSETSHCFT GLSPDTDYGV TVFVQTPNLE GPGVSVKEHT TVKPTEAPTE
2310 2320 2330 2340 2350
PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN KVVKFIFNTV
2360 2370 2380 2390 2400
GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN
2410 2420 2430 2440 2450
TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ
2460 2470 2480 2490 2500
SGFSVFVVGV ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV
2510 2520 2530 2540 2550
CETATSSCPL IYLDGYTSPG FKMLEAYNLT EKNFASVQGV SLESGSFPSY
2560 2570 2580 2590 2600
SAYRIQKNAF VNQPTADLHP NGLPPSYTII LLFRLLPETP SDPFAIWQIT
2610 2620 2630 2640 2650
DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV KTLFYGSFHK
2660 2670 2680 2690 2700
VHIVVTSKSV KIYIDCYEII EKDIKEAGNI TTDGYEILGK LLKGERKSAA
2710 2720 2730 2740 2750
FQIQSFDIVC SPVWTSRDRC CDIPSRRDEG KCPAFPNSCT CTQDSVGPPG
2760 2770 2780 2790 2800
PPGPAGGPGA KGPRGERGIS GAIGPPGPRG DIGPPGPQGP PGPQGPNGLS
2810 2820 2830 2840 2850
IPGEQGRQGM KGDAGEPGLP GRTGTPGLPG PPGPMGPPGD RGFTGKDGAM
2860 2870 2880 2890 2900
GPRGPPGPPG SPGSPGVTGP SGKPGKPGDH GRPGPSGLKG EKGDRGDIAS
2910 2920 2930 2940 2950
QNMMRAVARQ VCEQLISGQM NRFNQMLNQI PNDYQSSRNQ PGPPGPPGPP
2960 2970 2980 2990 3000
GSAGARGEPG PGGRPGFPGT PGMQGPPGER GLPGEKGERG TGSSGPRGLP
3010 3020 3030 3040 3050
GPPGPQGESR TGPPGSTGSR GPPGPPGRPG NSGIRGPPGP PGYCDSSQCA
3060
SIPYNGQGYP GSG
Length:3,063
Mass (Da):333,147
Last modified:May 1, 2007 - v2
Checksum:iEA38CAFECE8393D2
GO
Isoform 2 (identifier: Q99715-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     25-1188: Missing.

Show »
Length:1,899
Mass (Da):205,491
Checksum:iECFB9F5436FF7B24
GO
Isoform 4 (identifier: Q99715-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,987
Mass (Da):324,570
Checksum:iE5EEB57CBFB556E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471K → E in AAC51244. (PubMed:9143499)Curated
Sequence conflicti441 – 4422IV → M in AAC01506. (PubMed:9344363)Curated
Sequence conflicti581 – 5811R → D in AAC01506. (PubMed:9344363)Curated
Sequence conflicti689 – 6891S → N in AAC01506. (PubMed:9344363)Curated
Sequence conflicti743 – 7431W → S in AAC01506. (PubMed:9344363)Curated
Sequence conflicti749 – 7491R → K in AAC01506. (PubMed:9344363)Curated
Sequence conflicti753 – 7531Y → C in AAC51244. (PubMed:9143499)Curated
Sequence conflicti813 – 8131V → G in AAC01506. (PubMed:9344363)Curated
Sequence conflicti1355 – 13551A → D in AAC51244. (PubMed:9143499)Curated
Sequence conflicti1690 – 16901A → G in AAC51244. (PubMed:9143499)Curated
Sequence conflicti1729 – 17291P → A in AAC51244. (PubMed:9143499)Curated
Sequence conflicti1949 – 19513SLD → RLG in AAC51244. (PubMed:9143499)Curated
Sequence conflicti2614 – 26141P → S in AAB23937. (PubMed:1427837)Curated
Sequence conflicti2647 – 26482SF → RK in AAB23937. (PubMed:1427837)Curated
Sequence conflicti2848 – 28481G → S in AAC51244. (PubMed:9143499)Curated
Sequence conflicti2858 – 28581P → R in AAC51244. (PubMed:9143499)Curated
Sequence conflicti3035 – 30351R → Q in AAC51244. (PubMed:9143499)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611A → P.
Corresponds to variant rs34730529 [ dbSNP | Ensembl ].
VAR_048768
Natural varianti1738 – 17381I → T.
Corresponds to variant rs240736 [ dbSNP | Ensembl ].
VAR_048769
Natural varianti2021 – 20211R → Q.
Corresponds to variant rs34438461 [ dbSNP | Ensembl ].
VAR_061111
Natural varianti2160 – 21601E → V.
Corresponds to variant rs35523808 [ dbSNP | Ensembl ].
VAR_048770
Natural varianti2596 – 25961I → V.
Corresponds to variant rs35710072 [ dbSNP | Ensembl ].
VAR_048771
Natural varianti3048 – 30481Q → H.
Corresponds to variant rs57396313 [ dbSNP | Ensembl ].
VAR_061112
Natural varianti3058 – 30581G → S.1 Publication
Corresponds to variant rs970547 [ dbSNP | Ensembl ].
VAR_032059

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 11881164Missing in isoform 2. 1 PublicationVSP_001149Add
BLAST
Alternative sequencei2651 – 272676Missing in isoform 4. CuratedVSP_024942Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43481.1. [Q99715-2]
CCDS43482.1. [Q99715-1]
PIRiA44479.
RefSeqiNP_004361.3. NM_004370.5. [Q99715-1]
NP_542376.2. NM_080645.2. [Q99715-2]
UniGeneiHs.101302.

Genome annotation databases

EnsembliENST00000322507; ENSP00000325146; ENSG00000111799. [Q99715-1]
ENST00000345356; ENSP00000305147; ENSG00000111799. [Q99715-2]
ENST00000416123; ENSP00000412864; ENSG00000111799. [Q99715-4]
ENST00000611354; ENSP00000481931; ENSG00000111799. [Q99715-1]
GeneIDi1303.
KEGGihsa:1303.
UCSCiuc003phs.3. human. [Q99715-1]
uc003pht.3. human. [Q99715-2]

Polymorphism databases

DMDMi146345397.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS43481.1. [Q99715-2 ]
CCDS43482.1. [Q99715-1 ]
PIRi A44479.
RefSeqi NP_004361.3. NM_004370.5. [Q99715-1 ]
NP_542376.2. NM_080645.2. [Q99715-2 ]
UniGenei Hs.101302.

3D structure databases

ProteinModelPortali Q99715.
SMRi Q99715. Positions 25-317, 336-418, 440-616, 633-1179, 1196-1367, 1385-2310, 2323-2485, 2508-2724.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107700. 1 interaction.
IntActi Q99715. 6 interactions.
STRINGi 9606.ENSP00000325146.

PTM databases

PhosphoSitei Q99715.

Polymorphism databases

DMDMi 146345397.

Proteomic databases

MaxQBi Q99715.
PaxDbi Q99715.
PRIDEi Q99715.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322507 ; ENSP00000325146 ; ENSG00000111799 . [Q99715-1 ]
ENST00000345356 ; ENSP00000305147 ; ENSG00000111799 . [Q99715-2 ]
ENST00000416123 ; ENSP00000412864 ; ENSG00000111799 . [Q99715-4 ]
ENST00000611354 ; ENSP00000481931 ; ENSG00000111799 . [Q99715-1 ]
GeneIDi 1303.
KEGGi hsa:1303.
UCSCi uc003phs.3. human. [Q99715-1 ]
uc003pht.3. human. [Q99715-2 ]

Organism-specific databases

CTDi 1303.
GeneCardsi GC06M075850.
H-InvDB HIX0006013.
HGNCi HGNC:2188. COL12A1.
HPAi HPA009143.
MIMi 120320. gene.
neXtProti NX_Q99715.
Orphaneti 610. Bethlem myopathy.
75840. Congenital muscular dystrophy, Ullrich type.
PharmGKBi PA26704.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000119000.
HOVERGENi HBG051060.
InParanoidi Q99715.
KOi K08132.
OMAi NRFNQML.
PhylomeDBi Q99715.
TreeFami TF329914.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_150401. Collagen degradation.

Miscellaneous databases

ChiTaRSi COL12A1. human.
GeneWikii Collagen,_type_XII,_alpha_1.
GenomeRNAii 1303.
NextBioi 5299.
PROi Q99715.
SOURCEi Search...

Gene expression databases

Bgeei Q99715.
CleanExi HS_COL12A1.
ExpressionAtlasi Q99715. baseline and differential.
Genevestigatori Q99715.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
2.60.40.10. 18 hits.
3.40.50.410. 4 hits.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view ]
Pfami PF01391. Collagen. 4 hits.
PF00041. fn3. 18 hits.
PF00092. VWA. 4 hits.
[Graphical view ]
SMARTi SM00060. FN3. 18 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 4 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 11 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 4 hits.
PROSITEi PS50853. FN3. 18 hits.
PS50234. VWFA. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOCA1_HUMAN
AccessioniPrimary (citable) accession number: Q99715
Secondary accession number(s): O43853
, Q15955, Q5VYK1, Q5VYK2, Q71UR3, Q99716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 2007
Last modified: November 26, 2014
This is version 145 of the entry and version 2 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, Direct protein sequencing, 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