RPAP2_HUMAN - dbPTM
RPAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPAP2_HUMAN
UniProt AC Q8IXW5
Protein Name Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
Gene Name RPAP2
Organism Homo sapiens (Human).
Sequence Length 612
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner.
Protein Description Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes..
Protein Sequence MADFAGPSSAGRKAGAPRCSRKAAGTKQTSTLKQEDASKRKAELEAAVRKKIEFERKALHIVEQLLEENITEEFLMECGRFITPAHYSDVVDERSIVKLCGYPLCQKKLGIVPKQKYKISTKTNKVYDITERKSFCSNFCYQASKFFEAQIPKTPVWVREEERHPDFQLLKEEQSGHSGEEVQLCSKAIKTSDIDNPSHFEKQYESSSSSTHSDSSSDNEQDFVSSILPGNRPNSTNIRPQLHQKSIMKKKAGHKANSKHKDKEQTVVDVTEQLGDCKLDSQEKDATCELPLQKVNTQSSSNSTLPERLKASENSESEYSRSEITLVGISKKSAEHFKRKFAKSNQVSRSVSSSVQVCPEVGKRNLLKVLKETLIEWKTEETLRFLYGQNYASVCLKPEASLVKEELDEDDIISDPDSHFPAWRESQNSLDESLPFRGSGTAIKPLPSYENLKKETEKLNLRIREFYRGRYVLGEETTKSQDSEEHDSTFPLIDSSSQNQIRKRIVLEKLSKVLPGLLVPLQITLGDIYTQLKNLVRTFRLTNRNIIHKPAEWTLIAMVLLSLLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNEDLESLTIIFRTSCLPE
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
2Acetylation------MADFAGPSS
------CCCCCCCCH		22.1922814378
8PhosphorylationMADFAGPSSAGRKAG
CCCCCCCCHHHHCCC		31.7225627689
9PhosphorylationADFAGPSSAGRKAGA
CCCCCCCHHHHCCCC		37.5625159151
20PhosphorylationKAGAPRCSRKAAGTK
CCCCCCCCCCCCCCC		37.7918785766
29O-linked_GlycosylationKAAGTKQTSTLKQED
CCCCCCCCCCCCHHH		25.8231492838
29PhosphorylationKAAGTKQTSTLKQED
CCCCCCCCCCCCHHH		25.8229083192
30PhosphorylationAAGTKQTSTLKQEDA
CCCCCCCCCCCHHHH		29.2829083192
31PhosphorylationAGTKQTSTLKQEDAS
CCCCCCCCCCHHHHH		41.1729083192
38O-linked_GlycosylationTLKQEDASKRKAELE
CCCHHHHHHHHHHHH		45.3631492838
38PhosphorylationTLKQEDASKRKAELE
CCCHHHHHHHHHHHH		45.3629083192
39UbiquitinationLKQEDASKRKAELEA
CCHHHHHHHHHHHHH		60.6924816145
107UbiquitinationCGYPLCQKKLGIVPK
CCCCHHHHHHCCCCC		49.31-
125UbiquitinationKISTKTNKVYDITER
EEECCCCCEEECCCC		47.6129967540
127PhosphorylationSTKTNKVYDITERKS
ECCCCCEEECCCCCH		11.8425159151
134PhosphorylationYDITERKSFCSNFCY
EECCCCCHHHHHHHH		37.3929083192
137PhosphorylationTERKSFCSNFCYQAS
CCCCHHHHHHHHHHH		30.8229083192
141PhosphorylationSFCSNFCYQASKFFE
HHHHHHHHHHHHHHH		11.7229083192
144PhosphorylationSNFCYQASKFFEAQI
HHHHHHHHHHHHCCC		17.9229083192
154PhosphorylationFEAQIPKTPVWVREE
HHCCCCCCCEEEECH		20.0927273156
171UbiquitinationHPDFQLLKEEQSGHS
CCCHHHHCHHHCCCC		68.7329967540
175PhosphorylationQLLKEEQSGHSGEEV
HHHCHHHCCCCHHHH		41.5828450419
178PhosphorylationKEEQSGHSGEEVQLC
CHHHCCCCHHHHHHH		51.9628450419
190UbiquitinationQLCSKAIKTSDIDNP
HHHHHHHHHCCCCCH		47.0029967540
192PhosphorylationCSKAIKTSDIDNPSH
HHHHHHHCCCCCHHH		27.8028555341
216PhosphorylationSSTHSDSSSDNEQDF
CCCCCCCCCCCCHHH		46.86-
259UbiquitinationAGHKANSKHKDKEQT
HCCCCCCCCCCHHHH		55.25-
278UbiquitinationTEQLGDCKLDSQEKD
HHHHCCCCCCCCCCC		61.1332015554
294UbiquitinationTCELPLQKVNTQSSS
CCCCCCCCCCCCCCC		45.1732015554
297PhosphorylationLPLQKVNTQSSSNST
CCCCCCCCCCCCCCC		32.5825159151
299PhosphorylationLQKVNTQSSSNSTLP
CCCCCCCCCCCCCCC		33.4227251275
300PhosphorylationQKVNTQSSSNSTLPE
CCCCCCCCCCCCCCH		24.5827251275
303PhosphorylationNTQSSSNSTLPERLK
CCCCCCCCCCCHHHH		33.0128555341
310UbiquitinationSTLPERLKASENSES
CCCCHHHHCCCCCCC		56.9733845483
315PhosphorylationRLKASENSESEYSRS
HHHCCCCCCCCCCCC		38.1521815630
319PhosphorylationSENSESEYSRSEITL
CCCCCCCCCCCCEEE		20.7527642862
343UbiquitinationHFKRKFAKSNQVSRS
HHHHHHHHCCCCCCC		53.7429967540
350PhosphorylationKSNQVSRSVSSSVQV
HCCCCCCCCCCCCEE		20.8829978859
352PhosphorylationNQVSRSVSSSVQVCP
CCCCCCCCCCCEECC		20.3830576142
353PhosphorylationQVSRSVSSSVQVCPE
CCCCCCCCCCEECCC		32.1629978859
354PhosphorylationVSRSVSSSVQVCPEV
CCCCCCCCCEECCCC		14.7329978859
363UbiquitinationQVCPEVGKRNLLKVL
EECCCCCHHHHHHHH		43.2029967540
363AcetylationQVCPEVGKRNLLKVL
EECCCCCHHHHHHHH		43.2026051181
391PhosphorylationRFLYGQNYASVCLKP
HHHCCCCCHHEEECC		7.7420068231
401PhosphorylationVCLKPEASLVKEELD
EEECCCHHHCCHHCC		31.8424719451
414PhosphorylationLDEDDIISDPDSHFP
CCCCCCCCCCCCCCH		43.3430266825
418PhosphorylationDIISDPDSHFPAWRE
CCCCCCCCCCHHHHH		32.2030266825
426PhosphorylationHFPAWRESQNSLDES
CCHHHHHHHCCCCCC		26.5320873877
429PhosphorylationAWRESQNSLDESLPF
HHHHHHCCCCCCCCC		29.5720873877
433PhosphorylationSQNSLDESLPFRGSG
HHCCCCCCCCCCCCC		40.8025159151
439PhosphorylationESLPFRGSGTAIKPL
CCCCCCCCCCCCCCC		28.8128102081
441PhosphorylationLPFRGSGTAIKPLPS
CCCCCCCCCCCCCCC		27.2328102081
444UbiquitinationRGSGTAIKPLPSYEN
CCCCCCCCCCCCHHH		37.7329967540
448PhosphorylationTAIKPLPSYENLKKE
CCCCCCCCHHHHHHH		53.4123312004
449PhosphorylationAIKPLPSYENLKKET
CCCCCCCHHHHHHHH		13.5923312004
453UbiquitinationLPSYENLKKETEKLN
CCCHHHHHHHHHHHH		61.2129967540
471PhosphorylationREFYRGRYVLGEETT
HHHHCCCEECCCCCC		11.6620873877
477PhosphorylationRYVLGEETTKSQDSE
CEECCCCCCCCCCCC		34.9120873877
478PhosphorylationYVLGEETTKSQDSEE
EECCCCCCCCCCCCC		31.7920873877
479UbiquitinationVLGEETTKSQDSEEH
ECCCCCCCCCCCCCC		54.24-
480PhosphorylationLGEETTKSQDSEEHD
CCCCCCCCCCCCCCC		36.8123663014
483PhosphorylationETTKSQDSEEHDSTF
CCCCCCCCCCCCCCC		36.9323663014
488PhosphorylationQDSEEHDSTFPLIDS
CCCCCCCCCCCCCCC		33.5823663014
489PhosphorylationDSEEHDSTFPLIDSS
CCCCCCCCCCCCCCC		35.0223663014
509UbiquitinationRKRIVLEKLSKVLPG
HHHHHHHHHHHHCCC		54.6329967540
509AcetylationRKRIVLEKLSKVLPG
HHHHHHHHHHHHCCC		54.637933673
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 RPAP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPAP2_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 RPAP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RMP_HUMANURI1physical
17643375
RPAP3_HUMANRPAP3physical
17643375
KHDR2_HUMANKHDRBS2physical
17643375
PIHD1_HUMANPIH1D1physical
17643375
RPB1_HUMANPOLR2Aphysical
17643375
RPB2_HUMANPOLR2Bphysical
17643375
RPAB3_HUMANPOLR2Hphysical
17643375
RUVB2_HUMANRUVBL2physical
17643375
GPN1_HUMANGPN1physical
17643375
RPC1_HUMANPOLR3Aphysical
17643375
RPB7_HUMANPOLR2Gphysical
17643375
PDRG1_HUMANPDRG1physical
17643375
MED17_HUMANMED17physical
17643375
INT1_HUMANINTS1physical
17643375
TCPE_HUMANCCT5physical
17643375
PP1A_HUMANPPP1CAphysical
17643375
TCPA_HUMANTCP1physical
17643375
INT7_HUMANINTS7physical
17643375
UXT_HUMANUXTphysical
17643375
RPC2_HUMANPOLR3Bphysical
17643375
KHDR3_HUMANKHDRBS3physical
17643375
INT4_HUMANINTS4physical
17643375
GPN3_HUMANGPN3physical
17643375
INT3_HUMANINTS3physical
17643375
MED4_HUMANMED4physical
17643375
TF3C3_HUMANGTF3C3physical
17643375
YBOX1_HUMANYBX1physical
17643375
IF4A2_HUMANEIF4A2physical
17643375
RPB3_HUMANPOLR2Cphysical
17643375
EHBP1_HUMANEHBP1physical
17643375
RPC5_HUMANPOLR3Ephysical
17643375
HELLS_HUMANHELLSphysical
17643375
LRCH2_HUMANLRCH2physical
17643375
RXRG_HUMANRXRGphysical
17643375
NELFE_HUMANNELFEphysical
17643375
PRP31_HUMANPRPF31physical
17643375
DYN2_HUMANDNM2physical
17643375
MED24_HUMANMED24physical
17643375
TOPB1_HUMANTOPBP1physical
17643375
ARMX3_HUMANARMCX3physical
17643375
RPB4_HUMANPOLR2Dphysical
17643375
RFC4_HUMANRFC4physical
17643375
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 RPAP2_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-433, AND MASSSPECTROMETRY.

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