UniProt ID | CO1A2_HUMAN | |
---|---|---|
UniProt AC | P08123 | |
Protein Name | Collagen alpha-2(I) chain | |
Gene Name | COL1A2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1366 | |
Subcellular Localization | Secreted, extracellular space, extracellular matrix . | |
Protein Description | Type I collagen is a member of group I collagen (fibrillar forming collagen).. | |
Protein Sequence | MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
23 | Pyrrolidone_carboxylic_acid | TLCLATCQSLQEETV HHHHHHHHHHHHHHH | 42.70 | 2394758 | |
23 | Pyrrolidone_carboxylic_acid | TLCLATCQSLQEETV HHHHHHHHHHHHHHH | 42.70 | 2394758 | |
47 | Hydroxylation | PRGERGPPGPPGRDG CCCCCCCCCCCCCCC | 71.41 | 3680255 | |
50 | Hydroxylation | ERGPPGPPGRDGEDG CCCCCCCCCCCCCCC | 57.26 | 3680255 | |
62 | Hydroxylation | EDGPTGPPGPPGPPG CCCCCCCCCCCCCCC | 70.08 | 3680255 | |
65 | Hydroxylation | PTGPPGPPGPPGPPG CCCCCCCCCCCCCCC | 74.06 | 3680255 | |
68 | Hydroxylation | PPGPPGPPGPPGLGG CCCCCCCCCCCCCCC | 74.06 | 3680255 | |
71 | Hydroxylation | PPGPPGPPGLGGNFA CCCCCCCCCCCCCCE | 57.46 | 3680255 | |
80 | Pyrrolidone_carboxylic_acid | LGGNFAAQYDGKGVG CCCCCEEEECCCCCC | 33.16 | - | |
80 | Pyrrolidone_carboxylic_acid | LGGNFAAQYDGKGVG CCCCCEEEECCCCCC | 33.16 | 5529814 | |
80 | Pyrrolidone_carboxylic_acid | LGGNFAAQYDGKGVG CCCCCEEEECCCCCC | 33.16 | 5529814 | |
84 | Allysine | FAAQYDGKGVGLGPG CEEEECCCCCCCCCC | 47.74 | - | |
84 | Deamination | FAAQYDGKGVGLGPG CEEEECCCCCCCCCC | 47.74 | 5529814 | |
93 | Sulfoxidation | VGLGPGPMGLMGPRG CCCCCCCCCCCCCCC | 8.79 | 30846556 | |
96 | Sulfoxidation | GPGPMGLMGPRGPPG CCCCCCCCCCCCCCC | 6.02 | 30846556 | |
102 | Hydroxylation | LMGPRGPPGAAGAPG CCCCCCCCCCCCCCC | 48.13 | 3680255 | |
108 | Hydroxylation | PPGAAGAPGPQGFQG CCCCCCCCCCCCCCC | 54.82 | 3680255 | |
177 | Hydroxylation | TPGLPGFKGIRGHNG CCCCCCCCCCCCCCC | 60.38 | 4319110 | |
177 | O-linked_Glycosylation | TPGLPGFKGIRGHNG CCCCCCCCCCCCCCC | 60.38 | 4319110 | |
198 | Acetylation | QPGAPGVKGEPGAPG CCCCCCCCCCCCCCC | 64.57 | 20167786 | |
209 | Phosphorylation | GAPGENGTPGQTGAR CCCCCCCCCCCCCCC | 35.51 | 24719451 | |
251 | Phosphorylation | GPAGPIGSAGPPGFP CCCCCCCCCCCCCCC | 30.67 | - | |
353 | Phosphorylation | GEPGPAGSKGESGNK CCCCCCCCCCCCCCC | 39.32 | 28787133 | |
357 | Phosphorylation | PAGSKGESGNKGEPG CCCCCCCCCCCCCCC | 57.23 | 28787133 | |
389 | Phosphorylation | GPNGEAGSAGPPGPP CCCCCCCCCCCCCCC | 36.78 | - | |
401 | Phosphorylation | GPPGLRGSPGSRGLP CCCCCCCCCCCCCCC | 21.47 | - | |
404 | Phosphorylation | GLRGSPGSRGLPGAD CCCCCCCCCCCCCCC | 26.93 | - | |
420 | Hydroxylation | RAGVMGPPGSRGASG CCCCCCCCCCCCCCC | 47.89 | 4412529 | |
426 | Phosphorylation | PPGSRGASGPAGVRG CCCCCCCCCCCCCCC | 48.40 | 28857561 | |
441 | Hydroxylation | PNGDAGRPGEPGLMG CCCCCCCCCCCCCCC | 51.05 | 4412529 | |
444 | Hydroxylation | DAGRPGEPGLMGPRG CCCCCCCCCCCCCCC | 47.32 | 4412529 | |
632 | O-linked_Glycosylation | GVVGAVGTAGPSGPS CCEEEEECCCCCCCC | 23.11 | OGP | |
632 | Phosphorylation | GVVGAVGTAGPSGPS CCEEEEECCCCCCCC | 23.11 | 28857561 | |
636 | Phosphorylation | AVGTAGPSGPSGLPG EEECCCCCCCCCCCC | 63.52 | 28857561 | |
639 | Phosphorylation | TAGPSGPSGLPGERG CCCCCCCCCCCCCCC | 57.39 | 28857561 | |
710 | Phosphorylation | GPAGPRGSPGERGEV CCCCCCCCCCCCCCC | 30.89 | - | |
756 | Phosphorylation | ENGVVGPTGPVGAAG CCCCCCCCCCCCCCC | 48.46 | 27690223 | |
776 | Phosphorylation | GPPGPAGSRGDGGPP CCCCCCCCCCCCCCC | 34.89 | 27690223 | |
786 | Phosphorylation | DGGPPGMTGFPGAAG CCCCCCCCCCCCCCC | 41.40 | 27690223 | |
801 | Phosphorylation | RTGPPGPSGISGPPG CCCCCCCCCCCCCCC | 55.46 | 28857561 | |
860 | O-linked_Glycosylation | GTAGPPGTPGPQGLL CCCCCCCCCCCCCCC | 30.74 | OGP | |
981 | Phosphorylation | KHGNRGETGPSGPVG CCCCCCCCCCCCCCC | 58.16 | 30087585 | |
984 | Phosphorylation | NRGETGPSGPVGPAG CCCCCCCCCCCCCCC | 58.01 | 30087585 | |
999 | Phosphorylation | AVGPRGPSGPQGIRG CCCCCCCCCCCCCCC | 66.96 | 30087585 | |
1059 | Phosphorylation | PRGPAGPSGPAGKDG CCCCCCCCCCCCCCC | 57.39 | 26437602 | |
1064 | Acetylation | GPSGPAGKDGRTGHP CCCCCCCCCCCCCCC | 60.15 | 19815447 | |
1073 | Phosphorylation | GRTGHPGTVGPAGIR CCCCCCCCCCCCCCC | 27.09 | - | |
1104 | Phosphorylation | PPGPPGVSGGGYDFG CCCCCCCCCCCCCCC | 37.32 | - | |
1124 | Phosphorylation | YRADQPRSAPSLRPK EECCCCCCCCCCCCC | 51.74 | 27251275 | |
1138 | O-linked_Glycosylation | KDYEVDATLKSLNNQ CCHHHHHHHHHHHHH | 30.20 | 68709277 | |
1138 | Phosphorylation | KDYEVDATLKSLNNQ CCHHHHHHHHHHHHH | 30.20 | - | |
1141 | Phosphorylation | EVDATLKSLNNQIET HHHHHHHHHHHHHHH | 39.17 | 24719451 | |
1148 | Phosphorylation | SLNNQIETLLTPEGS HHHHHHHHHCCCCCC | 28.79 | - | |
1155 | Phosphorylation | TLLTPEGSRKNPART HHCCCCCCCCCCCCC | 38.12 | - | |
1267 | N-linked_Glycosylation | LANYASQNITYHCKN HHHHHHCCCEEEECC | 26.52 | UniProtKB CARBOHYD | |
1295 | Phosphorylation | KAVILQGSNDVELVA EEEEEECCCCEEEEE | 19.52 | - | |
1309 | Phosphorylation | AEGNSRFTYTVLVDG EECCCCEEEEEEEEC | 19.71 | 22798277 | |
1318 | Phosphorylation | TVLVDGCSKKTNEWG EEEEECCCCCCCCCC | 42.59 | 22798277 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CO1A2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CO1A2_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CO1A2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PDGFA_HUMAN | PDGFA | physical | 8900172 | |
PDGFB_HUMAN | PDGFB | physical | 8900172 | |
SGTA_HUMAN | SGTA | physical | 25416956 | |
UBQL1_HUMAN | UBQLN1 | physical | 25416956 | |
SPB5_HUMAN | SERPINB5 | physical | 11788595 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
130060 | Ehlers-Danlos syndrome 7B (EDS7B) | |||||
166200 | Osteogenesis imperfecta 1 (OI1) | |||||
166210 | Osteogenesis imperfecta 2 (OI2) | |||||
225320 | Ehlers-Danlos syndrome, autosomal recessive, cardiac valvular form (EDSCV) | |||||
259420 | Osteogenesis imperfecta 3 (OI3) | |||||
166220 | Osteogenesis imperfecta 4 (OI4) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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