DEP1A_HUMAN - dbPTM
DEP1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DEP1A_HUMAN
UniProt AC Q5TB30
Protein Name DEP domain-containing protein 1A
Gene Name DEPDC1
Organism Homo sapiens (Human).
Sequence Length 811
Subcellular Localization Nucleus . Colocalizes with ZNF224 at the nucleus.
Protein Description May be involved in transcriptional regulation as a transcriptional corepressor. The DEPDC1A-ZNF224 complex may play a critical role in bladder carcinogenesis by repressing the transcription of the A20 gene, leading to transport of NF-KB protein into the nucleus, resulting in suppression of apoptosis of bladder cancer cells..
Protein Sequence MESQGVPPGPYRATKLWNEVTTSFRAGMPLRKHRQHFKKYGNCFTAGEAVDWLYDLLRNNSNFGPEVTRQQTIQLLRKFLKNHVIEDIKGRWGSENVDDNNQLFRFPATSPLKTLPRRYPELRKNNIENFSKDKDSIFKLRNLSRRTPKRHGLHLSQENGEKIKHEIINEDQENAIDNRELSQEDVEEVWRYVILIYLQTILGVPSLEEVINPKQVIPQYIMYNMANTSKRGVVILQNKSDDLPHWVLSAMKCLANWPRSNDMNNPTYVGFERDVFRTIADYFLDLPEPLLTFEYYELFVNILVVCGYITVSDRSSGIHKIQDDPQSSKFLHLNNLNSFKSTECLLLSLLHREKNKEESDSTERLQISNPGFQERCAKKMQLVNLRNRRVSANDIMGGSCHNLIGLSNMHDLSSNSKPRCCSLEGIVDVPGNSSKEASSVFHQSFPNIEGQNNKLFLESKPKQEFLLNLHSEENIQKPFSAGFKRTSTLTVQDQEELCNGKCKSKQLCRSQSLLLRSSTRRNSYINTPVAEIIMKPNVGQGSTSVQTAMESELGESSATINKRLCKSTIELSENSLLPASSMLTGTQSLLQPHLERVAIDALQLCCLLLPPPNRRKLQLLMRMISRMSQNVDMPKLHDAMGTRSLMIHTFSRCVLCCAEEVDLDELLAGRLVSFLMDHHQEILQVPSYLQTAVEKHLDYLKKGHIENPGDGLFAPLPTYSYCKQISAQEFDEQKVSTSQAAIAELLENIIKNRSLPLKEKRKKLKQFQKEYPLIYQKRFPTTESEAALFGDKPTIKQPMLILRKPKFRSLR
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
11PhosphorylationQGVPPGPYRATKLWN
CCCCCCCCCHHHHHH		20.8529759185
89UbiquitinationNHVIEDIKGRWGSEN
HCCHHHHCCCCCCCC		55.5432015554
109PhosphorylationQLFRFPATSPLKTLP
EEECCCCCCCCCCCC		30.9930266825
110PhosphorylationLFRFPATSPLKTLPR
EECCCCCCCCCCCCC		30.2730266825
114PhosphorylationPATSPLKTLPRRYPE
CCCCCCCCCCCCCHH		50.0723312004
124UbiquitinationRRYPELRKNNIENFS
CCCHHHHHCCHHCCC		67.9529967540
131PhosphorylationKNNIENFSKDKDSIF
HCCHHCCCCCHHHHH		52.0724247654
134UbiquitinationIENFSKDKDSIFKLR
HHCCCCCHHHHHHHH		58.0529967540
136PhosphorylationNFSKDKDSIFKLRNL
CCCCCHHHHHHHHCC		35.3524719451
240PhosphorylationVVILQNKSDDLPHWV
EEEECCCCCCCHHHH		43.86-
249PhosphorylationDLPHWVLSAMKCLAN
CCHHHHHHHHHHHHC		19.39-
260PhosphorylationCLANWPRSNDMNNPT
HHHCCCCCCCCCCCC		32.8521945579
267PhosphorylationSNDMNNPTYVGFERD
CCCCCCCCCCCCHHH		32.7221945579
268PhosphorylationNDMNNPTYVGFERDV
CCCCCCCCCCCHHHH		10.3821945579
320 (in isoform 5)Ubiquitination-39.8921906983
320UbiquitinationDRSSGIHKIQDDPQS
CCCCCCCCCCCCCCC		39.892190698
329UbiquitinationQDDPQSSKFLHLNNL
CCCCCCCCEEECCCC		58.1329967540
338PhosphorylationLHLNNLNSFKSTECL
EECCCCCCCCHHHHH		36.9025159151
341PhosphorylationNNLNSFKSTECLLLS
CCCCCCCHHHHHHHH		27.6822199227
342PhosphorylationNLNSFKSTECLLLSL
CCCCCCHHHHHHHHH		31.1622199227
348PhosphorylationSTECLLLSLLHREKN
HHHHHHHHHHHHHHC		28.93-
356AcetylationLLHREKNKEESDSTE
HHHHHHCCCCCCCCC		74.137672353
361PhosphorylationKNKEESDSTERLQIS
HCCCCCCCCCCHHCC		41.2528348404
362PhosphorylationNKEESDSTERLQISN
CCCCCCCCCCHHCCC		30.0724719451
391PhosphorylationNLRNRRVSANDIMGG
HCCCCCCCHHHHCCC		21.3924719451
417UbiquitinationHDLSSNSKPRCCSLE
HHCCCCCCCCEEEEE		40.5129967540
422PhosphorylationNSKPRCCSLEGIVDV
CCCCCEEEEEEEEEC		32.8427050516
439PhosphorylationNSSKEASSVFHQSFP
CCCHHHHHHHHHHCC		35.5327050516
439UbiquitinationNSSKEASSVFHQSFP
CCCHHHHHHHHHHCC		35.5329967540
444PhosphorylationASSVFHQSFPNIEGQ
HHHHHHHHCCCCCCC		33.8227050516
467UbiquitinationKPKQEFLLNLHSEEN
CCCHHHHHHCCCHHC		8.5532015554
471PhosphorylationEFLLNLHSEENIQKP
HHHHHCCCHHCCCCC		50.1724719451
484MethylationKPFSAGFKRTSTLTV
CCCCCCCCCCCEEEE		54.57-
485UbiquitinationPFSAGFKRTSTLTVQ
CCCCCCCCCCEEEEC		31.4829967540
510PhosphorylationKSKQLCRSQSLLLRS
CHHHHHHHHHHHHHC		24.1129978859
512PhosphorylationKQLCRSQSLLLRSST
HHHHHHHHHHHHCCC		23.4121712546
517PhosphorylationSQSLLLRSSTRRNSY
HHHHHHHCCCCCCCC		35.7130622161
518PhosphorylationQSLLLRSSTRRNSYI
HHHHHHCCCCCCCCC		21.3530622161
519PhosphorylationSLLLRSSTRRNSYIN
HHHHHCCCCCCCCCC		34.5930622161
523PhosphorylationRSSTRRNSYINTPVA
HCCCCCCCCCCCCHH		26.1128348404
551PhosphorylationSVQTAMESELGESSA
HHHHHHHHHCCCCHH		25.6630206219
556PhosphorylationMESELGESSATINKR
HHHHCCCCHHHHCHH		24.3930206219
557PhosphorylationESELGESSATINKRL
HHHCCCCHHHHCHHH		25.7330206219
559PhosphorylationELGESSATINKRLCK
HCCCCHHHHCHHHCH		27.3430206219
625PhosphorylationQLLMRMISRMSQNVD
HHHHHHHHHHHCCCC		16.76-
701UbiquitinationEKHLDYLKKGHIENP
HHHHHHHHHCCCCCC		50.9429967540
718PhosphorylationGLFAPLPTYSYCKQI
CCCCCCCCHHHHHHC		32.5521945579
719PhosphorylationLFAPLPTYSYCKQIS
CCCCCCCHHHHHHCC		8.8321945579
720PhosphorylationFAPLPTYSYCKQISA
CCCCCCHHHHHHCCH		26.9121945579
721PhosphorylationAPLPTYSYCKQISAQ
CCCCCHHHHHHCCHH		8.0221945579
723UbiquitinationLPTYSYCKQISAQEF
CCCHHHHHHCCHHHC		42.2929967540
751UbiquitinationELLENIIKNRSLPLK
HHHHHHHHCCCCCHH		42.3832015554
769UbiquitinationKKLKQFQKEYPLIYQ
HHHHHHHHHCCCCEE		61.5829967540
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
110SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DEP1A_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 DEP1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ICK_HUMANICKphysical
28514442
SAPC2_HUMANSAPCD2physical
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 DEP1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-512, AND MASSSPECTROMETRY.

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