CPZIP_HUMAN - dbPTM
CPZIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPZIP_HUMAN
UniProt AC Q6JBY9
Protein Name CapZ-interacting protein
Gene Name RCSD1
Organism Homo sapiens (Human).
Sequence Length 416
Subcellular Localization
Protein Description Stress-induced phosphorylation of CAPZIP may regulate the ability of F-actin-capping protein to remodel actin filament assembly..
Protein Sequence MEERPAETNANVDNSASPSVAQLAGRFREQAAAAKETPASKPTRRKPPCSLPLFPPKVDLGQNGEEKSPPNASHPPKFKVKSSPLIEKLQANLTFDPAALLPGASPKSPGLKAMVSPFHSPPSTPSSPGVRSRPSEAEEVPVSFDQPPEGSHLPCYNKVRTRGSIKRRPPSRRFRRSQSDCGELGDFRAVESSQQNGAKEEDGDEVLPSKSKAPGSPLSSEGAAGEGVRTLGPAEKPPLRRSPSRTEKQEEDRATEEAKNGEKARRSSEEVDGQHPAQEEVPESPQTSGPEAENRCGSPREEKPAGEEAEMEKATEVKGERVQNEEVGPEHDSQETKKLEEGAAVKETPHSPPGGVKGGDVPKQEKGKEKQQEGAVLEPGCSPQTGPAQLETSSEVQSEPAVPKPEDDTPVQDTKM
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
8PhosphorylationMEERPAETNANVDNS
CCCCCCCCCCCCCCC		41.5628464451
15PhosphorylationTNANVDNSASPSVAQ
CCCCCCCCCCHHHHH		26.1728450419
17PhosphorylationANVDNSASPSVAQLA
CCCCCCCCHHHHHHH		19.9623401153
19PhosphorylationVDNSASPSVAQLAGR
CCCCCCHHHHHHHHH		27.8228450419
37PhosphorylationQAAAAKETPASKPTR
HHHHHHCCCCCCCCC		24.3728111955
50PhosphorylationTRRKPPCSLPLFPPK
CCCCCCCCCCCCCCC		38.5028634298
68PhosphorylationGQNGEEKSPPNASHP
CCCCCCCCCCCCCCC		49.2023401153
73PhosphorylationEKSPPNASHPPKFKV
CCCCCCCCCCCCCCC		43.0722617229
81AcetylationHPPKFKVKSSPLIEK
CCCCCCCCCCHHHHH		45.8919608861
82PhosphorylationPPKFKVKSSPLIEKL
CCCCCCCCCHHHHHH		39.9323401153
83PhosphorylationPKFKVKSSPLIEKLQ
CCCCCCCCHHHHHHH		20.2923401153
94PhosphorylationEKLQANLTFDPAALL
HHHHHCCEECHHHHC		26.2926552605
105PhosphorylationAALLPGASPKSPGLK
HHHCCCCCCCCCCCC		38.4828674151
108PhosphorylationLPGASPKSPGLKAMV
CCCCCCCCCCCCCCC		27.8123401153
112AcetylationSPKSPGLKAMVSPFH
CCCCCCCCCCCCCCC		40.1125953088
116PhosphorylationPGLKAMVSPFHSPPS
CCCCCCCCCCCCCCC		14.5723401153
120PhosphorylationAMVSPFHSPPSTPSS
CCCCCCCCCCCCCCC		38.6026846344
123PhosphorylationSPFHSPPSTPSSPGV
CCCCCCCCCCCCCCC		57.2323401153
124PhosphorylationPFHSPPSTPSSPGVR
CCCCCCCCCCCCCCC		32.7223401153
126PhosphorylationHSPPSTPSSPGVRSR
CCCCCCCCCCCCCCC		49.6123401153
127PhosphorylationSPPSTPSSPGVRSRP
CCCCCCCCCCCCCCC		27.2026846344
132PhosphorylationPSSPGVRSRPSEAEE
CCCCCCCCCCCCCCC		46.2528450419
135PhosphorylationPGVRSRPSEAEEVPV
CCCCCCCCCCCCCCC		48.6126657352
143PhosphorylationEAEEVPVSFDQPPEG
CCCCCCCCCCCCCCC		19.6228450419
151PhosphorylationFDQPPEGSHLPCYNK
CCCCCCCCCCCCCCC		21.8626552605
156PhosphorylationEGSHLPCYNKVRTRG
CCCCCCCCCCCCCCC		18.9726552605
161PhosphorylationPCYNKVRTRGSIKRR
CCCCCCCCCCCCCCC		42.2326437602
164PhosphorylationNKVRTRGSIKRRPPS
CCCCCCCCCCCCCCC		22.9626437602
171PhosphorylationSIKRRPPSRRFRRSQ
CCCCCCCCHHCCCCH		38.48-
177PhosphorylationPSRRFRRSQSDCGEL
CCHHCCCCHHCCCCC		29.7623401153
179PhosphorylationRRFRRSQSDCGELGD
HHCCCCHHCCCCCCC		35.7923401153
192PhosphorylationGDFRAVESSQQNGAK
CCHHHHHHHHHCCCC		27.1826074081
193PhosphorylationDFRAVESSQQNGAKE
CHHHHHHHHHCCCCC		23.4526074081
209PhosphorylationDGDEVLPSKSKAPGS
CCCCCCCCCCCCCCC		45.4626074081
211PhosphorylationDEVLPSKSKAPGSPL
CCCCCCCCCCCCCCC		38.0923898821
216PhosphorylationSKSKAPGSPLSSEGA
CCCCCCCCCCCCCCC		22.9328674151
219PhosphorylationKAPGSPLSSEGAAGE
CCCCCCCCCCCCCCC		29.7226329039
220PhosphorylationAPGSPLSSEGAAGEG
CCCCCCCCCCCCCCC		47.9726329039
230PhosphorylationAAGEGVRTLGPAEKP
CCCCCCCCCCCCCCC		33.3926074081
242PhosphorylationEKPPLRRSPSRTEKQ
CCCCCCCCCCHHHHH		22.3130576142
244PhosphorylationPPLRRSPSRTEKQEE
CCCCCCCCHHHHHHH		53.7530108239
246PhosphorylationLRRSPSRTEKQEEDR
CCCCCCHHHHHHHHH		52.4530108239
255PhosphorylationKQEEDRATEEAKNGE
HHHHHHHHHHHHHHH		34.9426074081
267PhosphorylationNGEKARRSSEEVDGQ
HHHHHHHCHHCCCCC		36.2323401153
268PhosphorylationGEKARRSSEEVDGQH
HHHHHHCHHCCCCCC		35.6423401153
284PhosphorylationAQEEVPESPQTSGPE
CCCCCCCCCCCCCHH		19.0823401153
287PhosphorylationEVPESPQTSGPEAEN
CCCCCCCCCCHHHHH		38.7522115753
288PhosphorylationVPESPQTSGPEAENR
CCCCCCCCCHHHHHC		47.2922115753
298PhosphorylationEAENRCGSPREEKPA
HHHHCCCCCCCCCCC		25.1423401153
333PhosphorylationEVGPEHDSQETKKLE
CCCCCCCCHHHHHHH		31.6523401153
336PhosphorylationPEHDSQETKKLEEGA
CCCCCHHHHHHHCCC		26.3328450419
348PhosphorylationEGAAVKETPHSPPGG
CCCCCCCCCCCCCCC		22.1526329039
351PhosphorylationAVKETPHSPPGGVKG
CCCCCCCCCCCCCCC		33.7123401153
382PhosphorylationAVLEPGCSPQTGPAQ
CCCCCCCCCCCCCCC		26.4226074081
385PhosphorylationEPGCSPQTGPAQLET
CCCCCCCCCCCCCCC		48.8226074081
392PhosphorylationTGPAQLETSSEVQSE
CCCCCCCCCCCCCCC		46.2628348404
393PhosphorylationGPAQLETSSEVQSEP
CCCCCCCCCCCCCCC		18.3528348404
394PhosphorylationPAQLETSSEVQSEPA
CCCCCCCCCCCCCCC		49.5628348404
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
68SPhosphorylationKinaseMAPK8P45983
Uniprot
83SPhosphorylationKinaseMAPK8P45983
Uniprot
108SPhosphorylationKinaseMAPK12P53778
Uniprot
108SPhosphorylationKinaseMAPK13O15264
Uniprot
179SPhosphorylationKinaseMAPKAPK2P49137
Uniprot
179SPhosphorylationKinaseMAPKAPK3Q16644
Uniprot
216SPhosphorylationKinaseMAPK8P45983
Uniprot
244SPhosphorylationKinaseMAPKAPK2P49137
Uniprot
244SPhosphorylationKinaseMAPKAPK3Q16644
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPZIP_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 CPZIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAZA1_HUMANCAPZA1physical
15850461
CAZA2_HUMANCAPZA2physical
28514442
CAPZB_HUMANCAPZBphysical
28514442
CAZA1_HUMANCAPZA1physical
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 CPZIP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-116;SER-120; SER-123; SER-177; SER-179; SER-216; SER-267; SER-268 ANDSER-284, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASSSPECTROMETRY.
"The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ.";
Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C.,Cuenda A., Cohen P.;
Biochem. J. 389:127-135(2005).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITHCAPZA2 AND CAPZB, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT SER-68;SER-83; SER-108; SER-179; SER-216 AND SER-244.

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