CTDP1_HUMAN - dbPTM
CTDP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTDP1_HUMAN
UniProt AC Q9Y5B0
Protein Name RNA polymerase II subunit A C-terminal domain phosphatase
Gene Name CTDP1
Organism Homo sapiens (Human).
Sequence Length 961
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole . Midbody . Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in ana
Protein Description Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation..
Protein Sequence MEVPAAGRVPAEGAPTAAVAEVRCPGPAPLRLLEWRVAAGAAVRIGSVLAVFEAAASAQSSGASQSRVASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVRDPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELAGAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMDKEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRERTLGAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM
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
1Acetylation-------MEVPAAGR
-------CCCCCCCC		12.0622814378
132PhosphorylationAECGQDLTQLQSKNG
HHHCCCHHHHHHCCC		35.2129052541
136PhosphorylationQDLTQLQSKNGKQQV
CCHHHHHHCCCCCCC		36.3629052541
137UbiquitinationDLTQLQSKNGKQQVP
CHHHHHHCCCCCCCC		57.68-
162PhosphorylationSVPELMVSSEQAEQL
CCCHHHCCHHHHHHH		17.75-
163PhosphorylationVPELMVSSEQAEQLG
CCHHHCCHHHHHHHC		23.47-
235AcetylationHCKDFLEKIAKLYEL
HHHHHHHHHHHHHHH		50.5425953088
235UbiquitinationHCKDFLEKIAKLYEL
HHHHHHHHHHHHHHH		50.54-
240PhosphorylationLEKIAKLYELHVFTF
HHHHHHHHHHEEEEC		18.75-
273PhosphorylationLFSHRILSRDECIDP
HHHHHCCCCCHHCCC		35.0024247654
283UbiquitinationECIDPFSKTGNLRNL
HHCCCCCCCCCCCCC		61.912190698
283 (in isoform 1)Ubiquitination-61.9121906983
318UbiquitinationAPNLITVKKYVYFQG
CCCEEEEEEEEEECC		29.72-
319UbiquitinationPNLITVKKYVYFQGT
CCEEEEEEEEEECCC		35.30-
338PhosphorylationAPPGSRESQTRKKVN
CCCCCCHHHHHCCCC		35.42-
340PhosphorylationPGSRESQTRKKVNHS
CCCCHHHHHCCCCCC		54.45-
387PhosphorylationPARELNGSEAATPRD
CHHHCCCCCCCCCCC		24.0023403867
391PhosphorylationLNGSEAATPRDSPRP
CCCCCCCCCCCCCCC		26.3821815630
395PhosphorylationEAATPRDSPRPGKPD
CCCCCCCCCCCCCCC		24.8823401153
414PhosphorylationWPPAQAPTSSQELAG
CCCCCCCCCHHHHCC		43.9826074081
415PhosphorylationPPAQAPTSSQELAGA
CCCCCCCCHHHHCCC		29.0330576142
416PhosphorylationPAQAPTSSQELAGAP
CCCCCCCHHHHCCCC		30.1028985074
446PhosphorylationQRPAQGATGTDLDFD
CCCCCCCCCCCCEEC		47.6527251275
448PhosphorylationPAQGATGTDLDFDLS
CCCCCCCCCCEECCC		29.0927251275
455PhosphorylationTDLDFDLSSDSESSS
CCCEECCCCCCCCCC		33.6630576142
456PhosphorylationDLDFDLSSDSESSSE
CCEECCCCCCCCCCC		53.0730576142
458PhosphorylationDFDLSSDSESSSESE
EECCCCCCCCCCCCC		41.1330576142
460PhosphorylationDLSSDSESSSESEGT
CCCCCCCCCCCCCCC		43.0225921289
461PhosphorylationLSSDSESSSESEGTK
CCCCCCCCCCCCCCC		33.7927690223
462PhosphorylationSSDSESSSESEGTKS
CCCCCCCCCCCCCCC		55.1927251275
464PhosphorylationDSESSSESEGTKSSS
CCCCCCCCCCCCCCC		43.1827251275
467PhosphorylationSSSESEGTKSSSSAS
CCCCCCCCCCCCCCC		24.5727251275
469PhosphorylationSESEGTKSSSSASDG
CCCCCCCCCCCCCCC		34.9829052541
470PhosphorylationESEGTKSSSSASDGE
CCCCCCCCCCCCCCC		29.8423401153
471PhosphorylationSEGTKSSSSASDGES
CCCCCCCCCCCCCCC		36.6923401153
472PhosphorylationEGTKSSSSASDGESE
CCCCCCCCCCCCCCC		33.4723401153
474PhosphorylationTKSSSSASDGESEGK
CCCCCCCCCCCCCCC		48.3623401153
478PhosphorylationSSASDGESEGKRGRQ
CCCCCCCCCCCCCCC		58.1223401153
575PhosphorylationAGESLDQSMEEEEEE
CCCCCCHHHHHHHCC		28.0322817900
584PhosphorylationEEEEEEDTDEDDHLI
HHHHCCCCCCCCCEE		44.5622817900
607UbiquitinationVHTDYYAKYDRYLNK
HHHHHHHHHHHHHCH		31.40-
614AcetylationKYDRYLNKEIEEAPD
HHHHHHCHHHHHCCC		58.4311795043
614UbiquitinationKYDRYLNKEIEEAPD
HHHHHHCHHHHHCCC		58.43-
624UbiquitinationEEAPDIRKIVPELKS
HHCCCHHHHHHHHHH		48.68-
630UbiquitinationRKIVPELKSKVLADV
HHHHHHHHHHHHHHH		46.71-
631PhosphorylationKIVPELKSKVLADVA
HHHHHHHHHHHHHHH		40.3918452278
653UbiquitinationPTNFPIEKTREHYHA
CCCCCCHHHHHHHHH		54.31-
666UbiquitinationHATALGAKILTRLVL
HHHHHHHHHHHHHHC		36.13-
674PhosphorylationILTRLVLSPDAPDRA
HHHHHHCCCCCCCHH		17.1630266825
720UbiquitinationSCLERWDKVEEQLFP
HHHHHHHHHHHHHCC		44.58-
734UbiquitinationPLRDDHTKAQRENSP
CCCCCCHHHHHHCCC		38.82-
740PhosphorylationTKAQRENSPAAFPDR
HHHHHHCCCCCCCCC		15.9119664994
753PhosphorylationDREGVPPTALFHPMP
CCCCCCCCCCCCCCC		29.8930576142
774PhosphorylationPGPEVRIYDSNTGKL
CCCEEEEEECCCCCE		11.62-
780UbiquitinationIYDSNTGKLIRTGAR
EEECCCCCEEECCCC		38.4119608861
780AcetylationIYDSNTGKLIRTGAR
EEECCCCCEEECCCC		38.4119608861
793PhosphorylationARGPPAPSSSLPIRQ
CCCCCCCCCCCCCCC		34.3623312004
794PhosphorylationRGPPAPSSSLPIRQE
CCCCCCCCCCCCCCC		34.5323312004
795PhosphorylationGPPAPSSSLPIRQEP
CCCCCCCCCCCCCCC		42.3724719451
831 (in isoform 4)Phosphorylation-31.2022496350
833 (in isoform 4)Phosphorylation-51.8021815630
836 (in isoform 4)Phosphorylation-52.40-
839PhosphorylationSRRKRQPSMSETMPL
CCCCCCCCHHHCCHH		26.9725159151
841PhosphorylationRKRQPSMSETMPLYT
CCCCCCHHHCCHHHH		33.9622617229
842 (in isoform 4)Phosphorylation-40.25-
843PhosphorylationRQPSMSETMPLYTLC
CCCCHHHCCHHHHHC		19.4422617229
847PhosphorylationMSETMPLYTLCKEDL
HHHCCHHHHHCHHHH		7.5623663014
848PhosphorylationSETMPLYTLCKEDLE
HHCCHHHHHCHHHHH		33.1023663014
856PhosphorylationLCKEDLESMDKEVDD
HCHHHHHHCCHHHHH		39.3125159151
869PhosphorylationDDILGEGSDDSDSEK
HHHHCCCCCCCHHHH		33.6629255136
872PhosphorylationLGEGSDDSDSEKRRP
HCCCCCCCHHHHCCH		48.2929255136
874PhosphorylationEGSDDSDSEKRRPEE
CCCCCCHHHHCCHHH		49.3126503892
904PhosphorylationRTLGAPASSERSAAG
CCCCCCCCCCCHHCC		31.5028985074
905PhosphorylationTLGAPASSERSAAGG
CCCCCCCCCCHHCCC		38.8529496963
913DimethylationERSAAGGRGPRGHKR
CCHHCCCCCCCCHHC		51.53-
913MethylationERSAAGGRGPRGHKR
CCHHCCCCCCCCHHC		51.5315670829
916MethylationAAGGRGPRGHKRKLN
HCCCCCCCCHHCCCC		63.7715670829
916DimethylationAAGGRGPRGHKRKLN
HCCCCCCCCHHCCCC		63.77-
935PhosphorylationASESSRESSNEDEGS
HCHHHHHHCCCCCCC		37.04-
936PhosphorylationSESSRESSNEDEGSS
CHHHHHHCCCCCCCH		39.21-
942PhosphorylationSSNEDEGSSSEADEM
HCCCCCCCHHHHHHH		28.7422817900
943PhosphorylationSNEDEGSSSEADEMA
CCCCCCCHHHHHHHH		42.95-
944PhosphorylationNEDEGSSSEADEMAK
CCCCCCHHHHHHHHH		38.2022817900
961SulfoxidationEAELNDLM-------
HHHHHHHC-------		6.0230846556
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
575SPhosphorylationKinaseCSNK2A1P68400
GPS
575SPhosphorylationKinaseCK2-FAMILY-GPS
575SPhosphorylationKinaseCK2_GROUP-PhosphoELM
584TPhosphorylationKinaseCSNK2A1P68400
GPS
584TPhosphorylationKinaseCK2-FAMILY-GPS
740SPhosphorylationKinaseCSNK2A1P68400
GPS
740SPhosphorylationKinaseCK2-FAMILY-GPS
740SPhosphorylationKinaseCK2_GROUP-PhosphoELM
942SPhosphorylationKinaseCSNK2A1P68400
GPS
942SPhosphorylationKinaseCK2-FAMILY-GPS
943SPhosphorylationKinaseCK2-FAMILY-GPS
944SPhosphorylationKinaseCSNK2A1P68400
GPS
944SPhosphorylationKinaseCK2-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTDP1_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 CTDP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEP50_HUMANWDR77physical
12560496
ANM5_HUMANPRMT5physical
15670829
INT1_HUMANINTS1physical
16239144
INT3_HUMANINTS3physical
16239144
INT6_HUMANINTS6physical
16239144
INT7_HUMANINTS7physical
16239144
INT8_HUMANINTS8physical
16239144
MED1_HUMANMED1physical
16239144
MED14_HUMANMED14physical
16239144
MED23_HUMANMED23physical
16239144
MED15_HUMANMED15physical
16239144
MED24_HUMANMED24physical
16239144
MED16_HUMANMED16physical
16239144
MED25_HUMANMED25physical
16239144
MED17_HUMANMED17physical
16239144
MED26_HUMANMED26physical
16239144
MED4_HUMANMED4physical
16239144
MED7_HUMANMED7physical
16239144
MED6_HUMANMED6physical
16239144
MED8_HUMANMED8physical
16239144
UPP1_HUMANUPP1physical
12036313
PP1A_HUMANPPP1CAphysical
12036313
PP2AA_HUMANPPP2CAphysical
12036313
RPB1_HUMANPOLR2Aphysical
12036313
CSK21_HUMANCSNK2A1physical
12591939
CSK22_HUMANCSNK2A2physical
12591939
HMGB1_HUMANHMGB1physical
12591939
CSK2B_HUMANCSNK2Bphysical
12591939
T2FA_HUMANGTF2F1physical
12591939
RPB1_HUMANPOLR2Aphysical
12591939
RPB1_HUMANPOLR2Aphysical
14576433
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604168Congenital cataracts, facial dysmorphism, and neuropathy (CCFDN)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CTDP1_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-780, AND MASS SPECTROMETRY.
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-674 AND SER-740, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-740, ANDMASS 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-869 AND SER-872, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740, AND MASSSPECTROMETRY.

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