UniProt ID | CAVN2_HUMAN | |
---|---|---|
UniProt AC | O95810 | |
Protein Name | Caveolae-associated protein 2 {ECO:0000312|HGNC:HGNC:10690} | |
Gene Name | CAVIN2 {ECO:0000312|HGNC:HGNC:10690} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 425 | |
Subcellular Localization | Cytoplasm, cytosol . Membrane, caveola . Localizes in the caveolae in a caveolin-dependent manner. | |
Protein Description | Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae. [PubMed: 19525939 Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity] | |
Protein Sequence | MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLTLLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAVEGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRKKVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKATSRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQVHQTS | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MGEDAAQAE ------CCHHHHHHH | - | ||
10 | Ubiquitination | EDAAQAEKFQHPGSD HHHHHHHHHCCCCCH | 23000965 | ||
16 | Phosphorylation | EKFQHPGSDMRQEKP HHHCCCCCHHCCCCC | 28060719 | ||
24 | Phosphorylation | DMRQEKPSSPSPMPS HHCCCCCCCCCCCCC | 23401153 | ||
25 | Phosphorylation | MRQEKPSSPSPMPSS HCCCCCCCCCCCCCC | 23927012 | ||
27 | Phosphorylation | QEKPSSPSPMPSSTP CCCCCCCCCCCCCCC | 23401153 | ||
31 | Phosphorylation | SSPSPMPSSTPSPSL CCCCCCCCCCCCCCC | 23927012 | ||
32 | Phosphorylation | SPSPMPSSTPSPSLN CCCCCCCCCCCCCCC | 23927012 | ||
33 | Phosphorylation | PSPMPSSTPSPSLNL CCCCCCCCCCCCCCC | 23927012 | ||
35 | Phosphorylation | PMPSSTPSPSLNLGN CCCCCCCCCCCCCCC | 23927012 | ||
37 | Phosphorylation | PSSTPSPSLNLGNTE CCCCCCCCCCCCCHH | 23927012 | ||
43 | Phosphorylation | PSLNLGNTEEAIRDN CCCCCCCHHHHHHCC | 23403867 | ||
51 | Phosphorylation | EEAIRDNSQVNAVTV HHHHHCCCCCCHHHH | 28270605 | ||
57 | Phosphorylation | NSQVNAVTVLTLLDK CCCCCHHHHHHHHHH | 28270605 | ||
60 | Phosphorylation | VNAVTVLTLLDKLVN CCHHHHHHHHHHHHH | 28270605 | ||
85 | Phosphorylation | KMEQRQISLEGSVKG HHHHHHHHHHHHHHH | 25072903 | ||
89 | Phosphorylation | RQISLEGSVKGIQND HHHHHHHHHHHHHCC | 25072903 | ||
91 | Ubiquitination | ISLEGSVKGIQNDLT HHHHHHHHHHHCCHH | 23000965 | ||
99 | Ubiquitination | GIQNDLTKLSKYQAS HHHCCHHHHHHHHHH | 23000965 | ||
101 | Phosphorylation | QNDLTKLSKYQASTS HCCHHHHHHHHHHCC | 18491316 | ||
102 | Ubiquitination | NDLTKLSKYQASTSN CCHHHHHHHHHHCCH | 23000965 | ||
103 | Phosphorylation | DLTKLSKYQASTSNT CHHHHHHHHHHCCHH | 29116813 | ||
107 | Phosphorylation | LSKYQASTSNTVSKL HHHHHHHCCHHHHHH | 29116813 | ||
112 | Phosphorylation | ASTSNTVSKLLEKSR HHCCHHHHHHHHHHH | 22817900 | ||
113 | Ubiquitination | STSNTVSKLLEKSRK HCCHHHHHHHHHHHH | 23000965 | ||
117 | Ubiquitination | TVSKLLEKSRKVSAH HHHHHHHHHHHHHHH | 23000965 | ||
156 | Ubiquitination | LLRRNHFKVLIFQEE HHHHCCCEEEEEECC | 33845483 | ||
169 | Phosphorylation | EENEIPASVFVKQPV CCCCCCCEEEEECCC | 28060719 | ||
173 | Ubiquitination | IPASVFVKQPVSGAV CCCEEEEECCCCCCC | 33845483 | ||
177 | Phosphorylation | VFVKQPVSGAVEGKE EEEECCCCCCCCCCC | 24505115 | ||
183 | Ubiquitination | VSGAVEGKEELPDEN CCCCCCCCCCCCCCC | 33845483 | ||
192 | Phosphorylation | ELPDENKSLEETLHT CCCCCCCCHHHHHHH | 20058876 | ||
196 | Phosphorylation | ENKSLEETLHTVDLS CCCCHHHHHHHCCCC | 24972180 | ||
199 | Phosphorylation | SLEETLHTVDLSSDD CHHHHHHHCCCCCCC | 24972180 | ||
203 | Phosphorylation | TLHTVDLSSDDDLPH HHHHCCCCCCCCCCC | 20058876 | ||
204 | Phosphorylation | LHTVDLSSDDDLPHD HHHCCCCCCCCCCCC | 20058876 | ||
218 | Phosphorylation | DEEALEDSAEEKVEE CHHHHHHHHHHHHHH | 20058876 | ||
226 | Phosphorylation | AEEKVEESRAEKIKR HHHHHHHHHHHHHHH | 28060719 | ||
241 | Phosphorylation | SSLKKVDSLKKAFSR HHHHHHHHHHHHHHH | 26657352 | ||
247 | Phosphorylation | DSLKKAFSRQNIEKK HHHHHHHHHHHHHHH | 23403867 | ||
257 | Ubiquitination | NIEKKMNKLGTKIVS HHHHHHHHHCCCEEH | 23000965 | ||
260 | Phosphorylation | KKMNKLGTKIVSVER HHHHHHCCCEEHHHH | - | ||
261 | Ubiquitination | KMNKLGTKIVSVERR HHHHHCCCEEHHHHH | 23000965 | ||
264 | Phosphorylation | KLGTKIVSVERREKI HHCCCEEHHHHHHHH | 28060719 | ||
274 | Phosphorylation | RREKIKKSLTSNHQK HHHHHHHHHHCCCCC | 29691806 | ||
276 | Phosphorylation | EKIKKSLTSNHQKIS HHHHHHHHCCCCCCC | 22798277 | ||
283 | Phosphorylation | TSNHQKISSGKSSPF HCCCCCCCCCCCCCC | 23403867 | ||
284 | Phosphorylation | SNHQKISSGKSSPFK CCCCCCCCCCCCCCC | 23401153 | ||
286 | Ubiquitination | HQKISSGKSSPFKVS CCCCCCCCCCCCCCC | 23000965 | ||
287 | Phosphorylation | QKISSGKSSPFKVSP CCCCCCCCCCCCCCC | 23401153 | ||
288 | Phosphorylation | KISSGKSSPFKVSPL CCCCCCCCCCCCCCC | 23401153 | ||
291 | Ubiquitination | SGKSSPFKVSPLTFG CCCCCCCCCCCCCCC | 23000965 | ||
293 | Phosphorylation | KSSPFKVSPLTFGRK CCCCCCCCCCCCCCH | 26846344 | ||
296 | Phosphorylation | PFKVSPLTFGRKKVR CCCCCCCCCCCHHCC | 30266825 | ||
307 | Phosphorylation | KKVREGESHAENETK HHCCCCCCCCCCCCC | 27535140 | ||
313 | Phosphorylation | ESHAENETKSEDLPS CCCCCCCCCCCCCCC | 24275569 | ||
320 | Phosphorylation | TKSEDLPSSEQMPND CCCCCCCCCCCCCCH | 20058876 | ||
321 | Phosphorylation | KSEDLPSSEQMPNDQ CCCCCCCCCCCCCHH | 20058876 | ||
332 | Phosphorylation | PNDQEEESFAEGHSE CCHHHHHHHHHCCCH | 27251275 | ||
338 | Phosphorylation | ESFAEGHSEASLASA HHHHHCCCHHHHHHH | 27251275 | ||
341 | Phosphorylation | AEGHSEASLASALVE HHCCCHHHHHHHHHH | 24275569 | ||
344 | Phosphorylation | HSEASLASALVEGEI CCHHHHHHHHHHHHH | 27251275 | ||
360 | Phosphorylation | EEAAEKATSRGSNSG HHHHHHHHHCCCCCC | 22617229 | ||
361 | Phosphorylation | EAAEKATSRGSNSGM HHHHHHHHCCCCCCC | 23403867 | ||
364 | Phosphorylation | EKATSRGSNSGMDSN HHHHHCCCCCCCCCC | 30266825 | ||
366 | Phosphorylation | ATSRGSNSGMDSNID HHHCCCCCCCCCCCC | 30266825 | ||
370 | Phosphorylation | GSNSGMDSNIDLTIV CCCCCCCCCCCEEEE | 22617229 | ||
375 | Phosphorylation | MDSNIDLTIVEDEEE CCCCCCEEEECCCHH | 26657352 | ||
384 | Phosphorylation | VEDEEEESVALEQAQ ECCCHHHHHHHHHHH | 26657352 | ||
395 | Phosphorylation | EQAQKVRYEGSYALT HHHHHHCCCCCEECC | 23927012 | ||
398 | Phosphorylation | QKVRYEGSYALTSEE HHHCCCCCEECCHHH | 23927012 | ||
399 | Phosphorylation | KVRYEGSYALTSEEA HHCCCCCEECCHHHH | 23927012 | ||
402 | Phosphorylation | YEGSYALTSEEAERS CCCCEECCHHHHHHC | 23927012 | ||
403 | Phosphorylation | EGSYALTSEEAERSD CCCEECCHHHHHHCC | 23927012 | ||
409 | Phosphorylation | TSEEAERSDGDPVQP CHHHHHHCCCCCCCC | 28192239 | ||
424 | Phosphorylation | AVLQVHQTS------ CEEEEECCC------ | 28060719 | ||
425 | Phosphorylation | VLQVHQTS------- EEEEECCC------- | 28060719 |
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 CAVN2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAVN2_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 CAVN2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NUD18_HUMAN | NUDT18 | physical | 16189514 | |
PKHF2_HUMAN | PLEKHF2 | physical | 16189514 | |
CAVN2_HUMAN | SDPR | physical | 25416956 | |
A1CF_HUMAN | A1CF | physical | 25416956 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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