CAPS2_HUMAN - dbPTM
CAPS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAPS2_HUMAN
UniProt AC Q86UW7
Protein Name Calcium-dependent secretion activator 2
Gene Name CADPS2
Organism Homo sapiens (Human).
Sequence Length 1296
Subcellular Localization Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Cell junction, synapse. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Probably localizes to different vesicles compared to CADPS. Enriched on
Protein Description Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles (By similarity)..
Protein Sequence MLDPSSSEEESDEGLEEESRDVLVAAGSSQRAPPAPTREGRRDAPGRAGGGGAARSVSPSPSVLSEGRDEPQRQLDDEQERRIRLQLYVFVVRCIAYPFNAKQPTDMARRQQKLNKQQLQLLKERFQAFLNGETQIVADEAFCNAVRSYYEVFLKSDRVARMVQSGGCSANDFREVFKKNIEKRVRSLPEIDGLSKETVLSSWIAKYDAIYRGEEDLCKQPNRMALSAVSELILSKEQLYEMFQQILGIKKLEHQLLYNACQLDNADEQAAQIRRELDGRLQLADKMAKERKFPKFIAKDMENMYIEELRSSVNLLMANLESLPVSKGGPEFKLQKLKRSQNSAFLDIGDENEIQLSKSDVVLSFTLEIVIMEVQGLKSVAPNRIVYCTMEVEGEKLQTDQAEASRPQWGTQGDFTTTHPRPVVKVKLFTESTGVLALEDKELGRVILYPTSNSSKSAELHRMVVPKNSQDSDLKIKLAVRMDKPAHMKHSGYLYALGQKVWKRWKKRYFVLVQVSQYTFAMCSYREKKSEPQELMQLEGYTVDYTDPHPGLQGGCMFFNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSYKPVPAIQTQKLNPKGGTLHADAQLSGKDADRFQKHGMDEFISANPCKLDHAFLFRILQRQTLDHRLNDSYSCLGWFSPGQVFVLDEYCARYGVRGCHRHLCYLAELMEHSENGAVIDPTLLHYSFAFCASHVHGNRPDGIGTVSVEEKERFEEIKERLSSLLENQISHFRYCFPFGRPEGALKATLSLLERVLMKDIATPIPAEEVKKVVRKCLEKAALINYTRLTEYAKIEETMNQASPARKLEEILHLAELCIEVLQQNEEHHAEGREAFAWWPDLLAEHAEKFWALFTVDMDTALEAQPQDSWDSFPLFQLLNNFLRNDTLLCNGKFHKHLQEIFVPLVVRYVDLMESSIAQSIHRGFEQETWQPVKNIANSLPNVALPKVPSLPLNLPQIPNISTASWMPSLYESTNGSATSEDLFWKLDALQMFVFDLHWPEQEFAHHLEQRLKLMASDMLEACVKRTRTAFELKLQKASKTTDLRIPASVCTMFNVLVDAKKQSTKLCALDGGQEQQYHSKIDDLIDNSVKEIISLLVSKFVSVLEGVLSKLSRYDEGTFFSSILSFTVKAAAKYVDVPKPGMDLADTYIMFVRQNQDILREKVNEEMYIEKLFDQWYSSSMKVICVWLTDRLDLQLHIYQLKTLIKIVKKTYRDFRLQGVLEGTLNSKTYDTVHRRLTVEEATASVSEGGGLQGITMKDSDEEEEG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Phosphorylation--MLDPSSSEEESDE
--CCCCCCCHHHCCC		47.3527251275
7Phosphorylation-MLDPSSSEEESDEG
-CCCCCCCHHHCCCC		54.0527251275
11PhosphorylationPSSSEEESDEGLEEE
CCCCHHHCCCCCHHH		44.2127251275
56PhosphorylationGGGGAARSVSPSPSV
CCCCCCCCCCCCHHH		23.4029255136
58PhosphorylationGGAARSVSPSPSVLS
CCCCCCCCCCHHHHC		22.4019664994
60PhosphorylationAARSVSPSPSVLSEG
CCCCCCCCHHHHCCC		23.4623927012
62PhosphorylationRSVSPSPSVLSEGRD
CCCCCCHHHHCCCCC		39.7720363803
65PhosphorylationSPSPSVLSEGRDEPQ
CCCHHHHCCCCCCCC		35.5323927012
187PhosphorylationNIEKRVRSLPEIDGL
HHHHHHHCCCCCCCC		45.4822985185
240PhosphorylationILSKEQLYEMFQQIL
HCCHHHHHHHHHHHH		12.6824043423
311PhosphorylationMYIEELRSSVNLLMA
HHHHHHHHHHHHHHH		51.7927050516
312PhosphorylationYIEELRSSVNLLMAN
HHHHHHHHHHHHHHC		14.4827050516
322PhosphorylationLLMANLESLPVSKGG
HHHHCHHHCCCCCCC		40.9327050516
326PhosphorylationNLESLPVSKGGPEFK
CHHHCCCCCCCHHHH		24.5227050516
366PhosphorylationSDVVLSFTLEIVIME
CCEEEEEEEEEEEEE		21.80-
430PhosphorylationVVKVKLFTESTGVLA
EEEEEEEECCCCEEE		39.19-
455PhosphorylationLYPTSNSSKSAELHR
EEECCCCCCCCEEEE		34.57-
457PhosphorylationPTSNSSKSAELHRMV
ECCCCCCCCEEEEEE		28.9923532336
491PhosphorylationKPAHMKHSGYLYALG
CCCHHCCCCHHHHHH		24.5024719451
509PhosphorylationWKRWKKRYFVLVQVS
HHHHHHCEEEEEEEE		13.6125332170
516PhosphorylationYFVLVQVSQYTFAMC
EEEEEEEEHHHHHHH		10.6125332170
723PhosphorylationYSFAFCASHVHGNRP
HHHHHHHHHHCCCCC		27.50-
815PhosphorylationEKAALINYTRLTEYA
HHHHHHCHHHHHHHH		6.0423403867
816PhosphorylationKAALINYTRLTEYAK
HHHHHCHHHHHHHHH		18.0823403867
938PhosphorylationFVPLVVRYVDLMESS
HHHHHHHHHHHHHHH		6.16-
1061 (in isoform 2)Phosphorylation-42.4017525332
1061PhosphorylationKRTRTAFELKLQKAS
HHHHHHHHHHCHHCC		42.4017525332
1128PhosphorylationEIISLLVSKFVSVLE
HHHHHHHHHHHHHHH		21.98-
1198PhosphorylationEKVNEEMYIEKLFDQ
HHCCHHHHHHHHHHH		14.8118083107
1273PhosphorylationRLTVEEATASVSEGG
EEEHHHHHEEHHCCC		23.8128102081
1275PhosphorylationTVEEATASVSEGGGL
EHHHHHEEHHCCCCC		23.0928102081
1277PhosphorylationEEATASVSEGGGLQG
HHHHEEHHCCCCCCC		28.2029449344
1286PhosphorylationGGGLQGITMKDSDEE
CCCCCCEECCCCCCC		25.6230624053
1290PhosphorylationQGITMKDSDEEEEG-
CCEECCCCCCCCCC-		41.2130624053
1294PhosphorylationMKDSDEEEEG-----
CCCCCCCCCC-----		67.0027251275
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 CAPS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAPS2_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 CAPS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIMB1_HUMANBZRAP1physical
24722188
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAPS2_HUMAN

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Related Literatures of Post-Translational Modification

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