CAPS1_HUMAN - dbPTM
CAPS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAPS1_HUMAN
UniProt AC Q9ULU8
Protein Name Calcium-dependent secretion activator 1
Gene Name CADPS
Organism Homo sapiens (Human).
Sequence Length 1353
Subcellular Localization Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Cell junction, synapse. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides, with a
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 catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates in DCVs-membrane fusion. However, it may also participate in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity)..
Protein Sequence MLDPSSSEEESDEIVEEESGKEVLGSAPSGARLSPSRTSEGSAGSAGLGGGGAGAGAGVGAGGGGGSGASSGGGAGGLQPSSRAGGGRPSSPSPSVVSEKEKEELERLQKEEEERKKRLQLYVFVMRCIAYPFNAKQPTDMARRQQKISKQQLQTVKDRFQAFLNGETQIMADEAFMNAVQSYYEVFLKSDRVARMVQSGGCSANDSREVFKKHIEKRVRSLPEIDGLSKETVLSSWMAKFDAIYRGEEDPRKQQARMTASAASELILSKEQLYEMFQNILGIKKFEHQLLYNACQLDNPDEQAAQIRRELDGRLQMADQIARERKFPKFVSKEMENMYIEELKSSVNLLMANLESMPVSKGGEFKLQKLKRSHNASIIDMGEESENQLSKSDVVLSFSLEVVIMEVQGLKSLAPNRIVYCTMEVEGGEKLQTDQAEASKPTWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRVILHPTPNSPKQSEWHKMTVSKNCPDQDLKIKLAVRMDKPQNMKHSGYLWAIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSHKPVPPTQVQKLNAKGGNVPQLDAPISQFYADRAQKHGMDEFISSNPCNFDHASLFEMVQRLTLDHRLNDSYSCLGWFSPGQVFVLDEYCARNGVRGCHRHLCYLRDLLERAENGAMIDPTLLHYSFAFCASHVHGNRPDGIGTVTVEEKERFEEIKERLRVLLENQITHFRYCFPFGRPEGALKATLSLLERVLMKDIVTPVPQEEVKTVIRKCLEQAALVNYSRLSEYAKIEENQKDAENVGRLITPAKKLEDTIRLAELVIEVLQQNEEHHAEPHVDKGEAFAWWSDLMVEHAETFLSLFAVDMDAALEVQPPDTWDSFPLFQLLNDFLRTDYNLCNGKFHKHLQDLFAPLVVRYVDLMESSIAQSIHRGFERESWEPVKSLTSNLPNVNLPNVNLPKVPNLPVNIPLGIPQMPTFSAPSWMAAIYDADNGSGTSEDLFWKLDALQTFIRDLHWPEEEFGKHLEQRLKLMASDMIESCVKRTRIAFEVKLQKTSRSTDFRVPQSICTMFNVMVDAKAQSTKLCSMEMGQEHQYHSKIDELIEETVKEMITLLVAKFVTILEGVLAKLSRYDEGTLFSSFLSFTVKAASKYVDVPKPGMDVADAYVTFVRHSQDVLRDKVNEEMYIERLFDQWYNSSMNVICTWLTDRMDLQLHIYQLKTLIRMVKKTYRDFRLQGVLDSTLNSKTYETIRNRLTVEEATASVSEGGGLQGISMKDSDEEDEEDD
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
5Phosphorylation---MLDPSSSEEESD
---CCCCCCCHHHHH		46.2826503514
6Phosphorylation--MLDPSSSEEESDE
--CCCCCCCHHHHHH		47.3526503514
26PhosphorylationSGKEVLGSAPSGARL
HHCCCCCCCCCCCCC		32.6127251275
29PhosphorylationEVLGSAPSGARLSPS
CCCCCCCCCCCCCCC		44.8127251275
34PhosphorylationAPSGARLSPSRTSEG
CCCCCCCCCCCCCCC		18.44-
36PhosphorylationSGARLSPSRTSEGSA
CCCCCCCCCCCCCCC		44.8322210691
39PhosphorylationRLSPSRTSEGSAGSA
CCCCCCCCCCCCCCC		38.5622210691
70PhosphorylationGGGGSGASSGGGAGG
CCCCCCCCCCCCCCC		32.8022210691
71PhosphorylationGGGSGASSGGGAGGL
CCCCCCCCCCCCCCC		40.7122210691
81PhosphorylationGAGGLQPSSRAGGGR
CCCCCCCCCCCCCCC		21.3522210691
82PhosphorylationAGGLQPSSRAGGGRP
CCCCCCCCCCCCCCC		32.6022210691
90PhosphorylationRAGGGRPSSPSPSVV
CCCCCCCCCCCCCCC		54.2226699800
91PhosphorylationAGGGRPSSPSPSVVS
CCCCCCCCCCCCCCC		31.8926657352
93PhosphorylationGGRPSSPSPSVVSEK
CCCCCCCCCCCCCHH		31.5826657352
95PhosphorylationRPSSPSPSVVSEKEK
CCCCCCCCCCCHHHH		39.2227732954
98PhosphorylationSPSPSVVSEKEKEEL
CCCCCCCCHHHHHHH		40.5726657352
221PhosphorylationHIEKRVRSLPEIDGL
HHHHHHHCCCCCCCC		45.4822985185
253AcetylationRGEEDPRKQQARMTA
CCCCCHHHHHHHHHH		52.757927397
259PhosphorylationRKQQARMTASAASEL
HHHHHHHHHHHHHHH		16.3529691806
261PhosphorylationQQARMTASAASELIL
HHHHHHHHHHHHHHC		18.4029691806
264PhosphorylationRMTASAASELILSKE
HHHHHHHHHHHCCHH		32.4329691806
270AcetylationASELILSKEQLYEMF
HHHHHCCHHHHHHHH		46.147927409
339PhosphorylationSKEMENMYIEELKSS
CHHHHHHHHHHHHHH		19.4322115753
373PhosphorylationKLQKLKRSHNASIID
HHHHHHHHCCCEEEE		21.3623312004
377PhosphorylationLKRSHNASIIDMGEE
HHHHCCCEEEECCHH		25.9523312004
392PhosphorylationSENQLSKSDVVLSFS
HCCCCCCCCEEEEEE		32.0624706070
399PhosphorylationSDVVLSFSLEVVIME
CCEEEEEEEEEEEEE		21.9024706070
442PhosphorylationQAEASKPTWGTQGDF
CCHHCCCCCCCCCCC		40.0228111955
445PhosphorylationASKPTWGTQGDFSTT
HCCCCCCCCCCCCCC		22.4228111955
450PhosphorylationWGTQGDFSTTHALPA
CCCCCCCCCCCCCCE		36.8228111955
451PhosphorylationGTQGDFSTTHALPAV
CCCCCCCCCCCCCEE		23.6928111955
452PhosphorylationTQGDFSTTHALPAVK
CCCCCCCCCCCCEEE		12.1728111955
464PhosphorylationAVKVKLFTESTGVLA
EEEEEEEECCCCEEE		39.1928111955
466PhosphorylationKVKLFTESTGVLALE
EEEEEECCCCEEEEC		27.6628111955
467PhosphorylationVKLFTESTGVLALED
EEEEECCCCEEEECC		25.6928111955
485PhosphorylationGRVILHPTPNSPKQS
CCEEEECCCCCCCCC		25.1025332170
488PhosphorylationILHPTPNSPKQSEWH
EEECCCCCCCCCCCC		34.3827732954
533AcetylationGYLWAIGKNVWKRWK
CEEEHHCCCHHHHHH		42.0612655037
747PhosphorylationNGAMIDPTLLHYSFA
CCCCCCHHHHHHHHH		37.9024719451
758PhosphorylationYSFAFCASHVHGNRP
HHHHHHHHHHCCCCC		27.5024719451
837 (in isoform 2)Phosphorylation-3.10-
839 (in isoform 2)Phosphorylation-21.21-
850PhosphorylationEQAALVNYSRLSEYA
HHHHHCCHHHHHHHH		6.4122461510
851PhosphorylationQAALVNYSRLSEYAK
HHHHCCHHHHHHHHH		22.8822461510
854PhosphorylationLVNYSRLSEYAKIEE
HCCHHHHHHHHHHHH		27.70-
856PhosphorylationNYSRLSEYAKIEENQ
CHHHHHHHHHHHHHH		15.15-
874PhosphorylationENVGRLITPAKKLED
HHHHHHCCCHHHHHH		23.06-
882PhosphorylationPAKKLEDTIRLAELV
CHHHHHHHHHHHHHH		9.9123312004
1284PhosphorylationMDLQLHIYQLKTLIR
CHHHHHHHHHHHHHH		9.3125907765
1328PhosphorylationRLTVEEATASVSEGG
CCCHHHHEEEHHCCC		23.8129691806
1330PhosphorylationTVEEATASVSEGGGL
CHHHHEEEHHCCCCC		23.0929691806
1332PhosphorylationEEATASVSEGGGLQG
HHHEEEHHCCCCCCC		28.2029691806
1341PhosphorylationGGGLQGISMKDSDEE
CCCCCCCCCCCCCCC		26.9729691806
1345PhosphorylationQGISMKDSDEEDEED
CCCCCCCCCCCCCCC		41.2129691806
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 CAPS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAPS1_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 CAPS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RYDEN_HUMANC19orf66physical
25416956
F161A_HUMANFAM161Aphysical
25416956
ZN572_HUMANZNF572physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
TTL10_HUMANTTLL10physical
25416956
CQ067_HUMANC17orf67physical
25416956
CLIP1_HUMANCLIP1physical
26186194
CLIP1_HUMANCLIP1physical
28514442
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 CAPS1_HUMAN

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Related Literatures of Post-Translational Modification

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