CR025_HUMAN - dbPTM
CR025_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CR025_HUMAN
UniProt AC Q96B23
Protein Name Uncharacterized protein C18orf25
Gene Name C18orf25 {ECO:0000312|HGNC:HGNC:28172}
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization
Protein Description
Protein Sequence MKMEEAVGKVEELIESEAPPKASEQETAKEEDGSVELESQVQKDGVADSTVISSMPCLLMELRRDSSESQLASTESDKPTTGRVYESDSSNHCMLSPSSSGHLADSDTLSSAEENEPSQAETAVEGDPSGVSGATVGRKSRRSRSESETSTMAAKKNRQSSDKQNGRVAKVKGHRSQKHKERIRLLRQKREAAARKKYNLLQDSSTSDSDLTCDSSTSSSDDDEEVSGSSKTITAEIPDGPPVVAHYDMSDTNSDPEVVNVDNLLAAAVVQEHSNSVGGQDTGATWRTSGLLEELNAEAGHLDPGFLASDKTSAGNAPLNEEINIASSDSEVEIVGVQEHARCVHPRGGVIQSVSSWKHGSGTQYVSTRQTQSWTAVTPQQTWASPAEVVDLTLDEDSRRKYLL
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
2Sumoylation------MKMEEAVGK
------CCHHHHHHH		55.83-
2Sumoylation------MKMEEAVGK
------CCHHHHHHH		55.83-
16PhosphorylationKVEELIESEAPPKAS
HHHHHHHCCCCCCCC		31.8725159151
21AcetylationIESEAPPKASEQETA
HHCCCCCCCCHHHHH		64.5811922795
21UbiquitinationIESEAPPKASEQETA
HHCCCCCCCCHHHHH		64.5833845483
23PhosphorylationSEAPPKASEQETAKE
CCCCCCCCHHHHHCC		46.0329978859
27PhosphorylationPKASEQETAKEEDGS
CCCCHHHHHCCCCCC		42.6029978859
29SumoylationASEQETAKEEDGSVE
CCHHHHHCCCCCCEE		69.89-
29SumoylationASEQETAKEEDGSVE
CCHHHHHCCCCCCEE		69.89-
34PhosphorylationTAKEEDGSVELESQV
HHCCCCCCEEEEHHH		25.4129255136
39PhosphorylationDGSVELESQVQKDGV
CCCEEEEHHHCCCCC		48.5617525332
49PhosphorylationQKDGVADSTVISSMP
CCCCCCCHHHHHHHH		18.1630377224
50PhosphorylationKDGVADSTVISSMPC
CCCCCCHHHHHHHHH		23.5430377224
53PhosphorylationVADSTVISSMPCLLM
CCCHHHHHHHHHHHH		19.0930377224
54PhosphorylationADSTVISSMPCLLME
CCHHHHHHHHHHHHH		18.6728348404
57GlutathionylationTVISSMPCLLMELRR
HHHHHHHHHHHHHHC		3.2222555962
66PhosphorylationLMELRRDSSESQLAS
HHHHHCCCCHHHHCC		33.9129255136
67PhosphorylationMELRRDSSESQLAST
HHHHCCCCHHHHCCC		45.6229255136
69PhosphorylationLRRDSSESQLASTES
HHCCCCHHHHCCCCC		32.2329255136
73PhosphorylationSSESQLASTESDKPT
CCHHHHCCCCCCCCC		41.1029255136
74PhosphorylationSESQLASTESDKPTT
CHHHHCCCCCCCCCC		33.6229255136
76PhosphorylationSQLASTESDKPTTGR
HHHCCCCCCCCCCCC		51.5329255136
78UbiquitinationLASTESDKPTTGRVY
HCCCCCCCCCCCCCE		54.2524816145
80PhosphorylationSTESDKPTTGRVYES
CCCCCCCCCCCCEEC		47.8529255136
81PhosphorylationTESDKPTTGRVYESD
CCCCCCCCCCCEECC		31.3629255136
132PhosphorylationEGDPSGVSGATVGRK
CCCCCCCCCCCCCCC		26.66-
135PhosphorylationPSGVSGATVGRKSRR
CCCCCCCCCCCCCCC		27.33-
140PhosphorylationGATVGRKSRRSRSES
CCCCCCCCCCCCCHH		31.4026074081
143PhosphorylationVGRKSRRSRSESETS
CCCCCCCCCCHHHHH		38.7629255136
145PhosphorylationRKSRRSRSESETSTM
CCCCCCCCHHHHHHH		46.8829255136
147PhosphorylationSRRSRSESETSTMAA
CCCCCCHHHHHHHHH		47.6329255136
149PhosphorylationRSRSESETSTMAAKK
CCCCHHHHHHHHHHH		38.4829255136
150PhosphorylationSRSESETSTMAAKKN
CCCHHHHHHHHHHHH		16.4829255136
151PhosphorylationRSESETSTMAAKKNR
CCHHHHHHHHHHHHC		20.4629255136
155UbiquitinationETSTMAAKKNRQSSD
HHHHHHHHHHCCCCC		40.8324816145
155AcetylationETSTMAAKKNRQSSD
HHHHHHHHHHCCCCC		40.8325953088
232 (in isoform 2)Phosphorylation-26.0525159151
248 (in isoform 2)Phosphorylation-21.9028348404
248PhosphorylationPPVVAHYDMSDTNSD
CCEEEEEECCCCCCC		21.9027251275
297UbiquitinationGLLEELNAEAGHLDP
HHHHHHHHHCCCCCC		22.2032015554
309PhosphorylationLDPGFLASDKTSAGN
CCCCCCCCCCCCCCC		41.61-
312PhosphorylationGFLASDKTSAGNAPL
CCCCCCCCCCCCCCC		47.0224144214
313PhosphorylationFLASDKTSAGNAPLN
CCCCCCCCCCCCCCC		35.4724144214
326PhosphorylationLNEEINIASSDSEVE
CCCCCEECCCCCCEE		30.7726657352
327PhosphorylationNEEINIASSDSEVEI
CCCCEECCCCCCEEE		35.8118691976
327PhosphorylationNEEINIASSDSEVEI
CCCCEECCCCCCEEE		35.8117192257
328PhosphorylationEEINIASSDSEVEIV
CCCEECCCCCCEEEE		46.4521406692
328PhosphorylationEEINIASSDSEVEIV
CCCEECCCCCCEEEE		46.4529743597
329PhosphorylationEINIASSDSEVEIVG
CCEECCCCCCEEEEE		45.5529743597
330PhosphorylationINIASSDSEVEIVGV
CEECCCCCCEEEEEE		49.5117192257
330PhosphorylationINIASSDSEVEIVGV
CEECCCCCCEEEEEE		49.5117081983
346MethylationEHARCVHPRGGVIQS
CCCEEECCCCCEEEE		39.3524129315
347MethylationHARCVHPRGGVIQSV
CCEEECCCCCEEEEE		38.8924129315
352PhosphorylationHPRGGVIQSVSSWKH
CCCCCEEEEECCEEC		16.9120068231
354PhosphorylationRGGVIQSVSSWKHGS
CCCEEEEECCEECCC		35.4120068231
355O-linked_GlycosylationGGVIQSVSSWKHGSG
CCEEEEECCEECCCC		37.6823301498
355PhosphorylationGGVIQSVSSWKHGSG
CCEEEEECCEECCCC		37.6823401153
356PhosphorylationGVIQSVSSWKHGSGT
CEEEEECCEECCCCC		6.8024719451
357UbiquitinationVIQSVSSWKHGSGTQ
EEEEECCEECCCCCE		39.78-
357SumoylationVIQSVSSWKHGSGTQ
EEEEECCEECCCCCE		39.78-
357SumoylationVIQSVSSWKHGSGTQ
EEEEECCEECCCCCE		39.78-
358UbiquitinationIQSVSSWKHGSGTQY
EEEECCEECCCCCEE		29.4132015554
358SumoylationIQSVSSWKHGSGTQY
EEEECCEECCCCCEE		29.4128112733
360PhosphorylationSVSSWKHGSGTQYVS
EECCEECCCCCEEEE		38.0823401153
362PhosphorylationSSWKHGSGTQYVSTR
CCEECCCCCEEEECE		20.5828796482
363PhosphorylationSWKHGSGTQYVSTRQ
CEECCCCCEEEECEE		39.9127251275
364PhosphorylationWKHGSGTQYVSTRQT
EECCCCCEEEECEEC		9.0128796482
366PhosphorylationHGSGTQYVSTRQTQS
CCCCCEEEECEECCC		16.9728796482
367PhosphorylationGSGTQYVSTRQTQSW
CCCCEEEECEECCCE		19.4228796482
381PhosphorylationWTAVTPQQTWASPAE
EEEECCCCCCCCCCC		20.1128348404
384PhosphorylationVTPQQTWASPAEVVD
ECCCCCCCCCCCEEE		19.0623917254
392PhosphorylationSPAEVVDLTLDEDSR
CCCCEEEEECCCCHH		27.9223917254
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 CR025_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CR025_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 CR025_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BOP1_HUMANBOP1physical
22863883
GPN1_HUMANGPN1physical
22863883
SC24A_HUMANSEC24Aphysical
22863883
GLYC_HUMANSHMT1physical
22863883
ZRAB2_HUMANZRANB2physical
22863883
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 CR025_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-66; SER-76 AND SER-145,AND MASS SPECTROMETRY.
"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-326; SER-327 ANDSER-329, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-326; SER-327 ANDSER-329, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-66 AND SER-69,AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-326; SER-327 ANDSER-329, AND MASS SPECTROMETRY.

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