CWC25_HUMAN - dbPTM
CWC25_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CWC25_HUMAN
UniProt AC Q9NXE8
Protein Name Pre-mRNA-splicing factor CWC25 homolog
Gene Name CWC25
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization
Protein Description
Protein Sequence MGGGDLNLKKSWHPQTLRNVEKVWKAEQKHEAERKKIEELQRELREERAREEMQRYAEDVGAVKKKEEKLDWMYQGPGGMVNRDEYLLGRPIDKYVFEKMEEKEAGCSSETGLLPGSIFAPSGANSLLDMASKIREDPLFIIRKKEEEKKREVLNNPVKMKKIKELLQMSLEKKEKKKKKEKKKKHKKHKHRSSSSDRSSSEDEHSAGRSQKKMANSSPVLSKVPGYGLQVRNSDRNQGLQGPLTAEQKRGHGMKNHSRSRSSSHSPPRHASKKSTREAGSRDRRSRSLGRRSRSPRPSKLHNSKVNRRETGQTRSPSPKKEVYQRRHAPGYTRKLSAEELERKRQEMMENAKWREEERLNILKRHAKDEEREQRLEKLDSRDGKFIHRMKLESASTSSLEDRVKRNIYSLQRTSVALEKNFMKR
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
9AcetylationGGGDLNLKKSWHPQT
CCCCCCCCCCCCHHH		43.6225953088
11PhosphorylationGDLNLKKSWHPQTLR
CCCCCCCCCCHHHHH		29.0923401153
16PhosphorylationKKSWHPQTLRNVEKV
CCCCCHHHHHHHHHH		31.9428555341
22AcetylationQTLRNVEKVWKAEQK
HHHHHHHHHHHHHHH		49.4625953088
74PhosphorylationEEKLDWMYQGPGGMV
HHHCCHHCCCCCCCC		13.1820068231
159AcetylationEVLNNPVKMKKIKEL
HHHHCHHHHHHHHHH		46.3825953088
170PhosphorylationIKELLQMSLEKKEKK
HHHHHHHHHHHHHHH		22.0325159151
195PhosphorylationKHKHRSSSSDRSSSE
HHCCCCCCCCCCCCH		37.1930576142
200PhosphorylationSSSSDRSSSEDEHSA
CCCCCCCCCHHHHHH		38.3430576142
201PhosphorylationSSSDRSSSEDEHSAG
CCCCCCCCHHHHHHH		50.76-
206PhosphorylationSSSEDEHSAGRSQKK
CCCHHHHHHHHHHHH		30.3030576142
217PhosphorylationSQKKMANSSPVLSKV
HHHHHHCCCCCHHHC		26.8729255136
218PhosphorylationQKKMANSSPVLSKVP
HHHHHCCCCCHHHCC		20.8729255136
222PhosphorylationANSSPVLSKVPGYGL
HCCCCCHHHCCCCCE		31.6629255136
227PhosphorylationVLSKVPGYGLQVRNS
CHHHCCCCCEEEECC		14.48-
234PhosphorylationYGLQVRNSDRNQGLQ
CCEEEECCCCCCCCC		27.6428555341
245PhosphorylationQGLQGPLTAEQKRGH
CCCCCCCCHHHHCCC		31.1428555341
260PhosphorylationGMKNHSRSRSSSHSP
CCCCCCCCCCCCCCC		39.2623663014
262PhosphorylationKNHSRSRSSSHSPPR
CCCCCCCCCCCCCCC		37.1223663014
263PhosphorylationNHSRSRSSSHSPPRH
CCCCCCCCCCCCCCC		30.8423663014
264PhosphorylationHSRSRSSSHSPPRHA
CCCCCCCCCCCCCCC		29.2723663014
266PhosphorylationRSRSSSHSPPRHASK
CCCCCCCCCCCCCCH		38.2523663014
272PhosphorylationHSPPRHASKKSTREA
CCCCCCCCHHHHHHH		34.2023663014
286PhosphorylationAGSRDRRSRSLGRRS
HCHHHHHHHHHCCCC		27.41-
288PhosphorylationSRDRRSRSLGRRSRS
HHHHHHHHHCCCCCC		36.10-
293PhosphorylationSRSLGRRSRSPRPSK
HHHHCCCCCCCCCHH		35.4317081983
295PhosphorylationSLGRRSRSPRPSKLH
HHCCCCCCCCCHHHC		26.8930576142
299PhosphorylationRSRSPRPSKLHNSKV
CCCCCCCHHHCCCCC		49.4830576142
305AcetylationPSKLHNSKVNRRETG
CHHHCCCCCCCCCCC		49.1725953088
311PhosphorylationSKVNRRETGQTRSPS
CCCCCCCCCCCCCCC		32.5523663014
314PhosphorylationNRRETGQTRSPSPKK
CCCCCCCCCCCCCCH		34.1623663014
316PhosphorylationRETGQTRSPSPKKEV
CCCCCCCCCCCCHHH		32.8726055452
318PhosphorylationTGQTRSPSPKKEVYQ
CCCCCCCCCCHHHHH		51.0726055452
324PhosphorylationPSPKKEVYQRRHAPG
CCCCHHHHHHHCCCC		9.44-
337PhosphorylationPGYTRKLSAEELERK
CCHHCCCCHHHHHHH		36.3523911959
381PhosphorylationQRLEKLDSRDGKFIH
HHHHHHHHCCCCEEE		42.5819664995
385AcetylationKLDSRDGKFIHRMKL
HHHHCCCCEEEEEEC		45.4925953088
391SumoylationGKFIHRMKLESASTS
CCEEEEEECCCCCCC		49.40-
391SumoylationGKFIHRMKLESASTS
CCEEEEEECCCCCCC		49.4028112733
397PhosphorylationMKLESASTSSLEDRV
EECCCCCCCCHHHHH		23.2730576142
398PhosphorylationKLESASTSSLEDRVK
ECCCCCCCCHHHHHH		30.3630576142
399PhosphorylationLESASTSSLEDRVKR
CCCCCCCCHHHHHHH		35.5530576142
409PhosphorylationDRVKRNIYSLQRTSV
HHHHHHHHHHHHHHH		13.5821945579
410PhosphorylationRVKRNIYSLQRTSVA
HHHHHHHHHHHHHHH		17.7721945579
414PhosphorylationNIYSLQRTSVALEKN
HHHHHHHHHHHHHHH		18.0024719451
415PhosphorylationIYSLQRTSVALEKNF
HHHHHHHHHHHHHHH		13.9527251275
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
337SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CWC25_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 CWC25_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAMC3_HUMANLAMC3physical
21988832
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
CING_HUMANCGNphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
CBY1_HUMANCBY1physical
27173435
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 CWC25_HUMAN

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Related Literatures of Post-Translational Modification
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-218, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASSSPECTROMETRY.

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