RPB11_HUMAN - dbPTM
RPB11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPB11_HUMAN
UniProt AC P52435
Protein Name DNA-directed RNA polymerase II subunit RPB11-a
Gene Name POLR2J
Organism Homo sapiens (Human).
Sequence Length 117
Subcellular Localization Nucleus .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity)..
Protein Sequence MNAPPAFESFLLFEGEKKITINKDTKVPNACLFTINKEDHTLGNIIKSQLLKDPQVLFAGYKVPHPLEHKIIIRVQTTPDYSPQEAFTNAITDLISELSLLEERFRVAIKDKQEGIE
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-------MNAPPAFE
-------CCCCCCCC		9.71-
9PhosphorylationNAPPAFESFLLFEGE
CCCCCCCEEEEEECC		18.1028348404
22UbiquitinationGEKKITINKDTKVPN
CCEEEEECCCCCCCC		27.7423000965
23UbiquitinationEKKITINKDTKVPNA
CEEEEECCCCCCCCE		64.0223000965
25UbiquitinationKITINKDTKVPNACL
EEEECCCCCCCCEEE		35.2323000965
26UbiquitinationITINKDTKVPNACLF
EEECCCCCCCCEEEE		66.8723000965
32UbiquitinationTKVPNACLFTINKED
CCCCCEEEEEEECCC		3.8432015554
37AcetylationACLFTINKEDHTLGN
EEEEEEECCCCCHHH		61.7526051181
37UbiquitinationACLFTINKEDHTLGN
EEEEEEECCCCCHHH		61.7529967540
41PhosphorylationTINKEDHTLGNIIKS
EEECCCCCHHHHHHH		49.00-
46UbiquitinationDHTLGNIIKSQLLKD
CCCHHHHHHHHHHCC		3.9921890473
47UbiquitinationHTLGNIIKSQLLKDP
CCHHHHHHHHHHCCC		28.4921890473
47UbiquitinationHTLGNIIKSQLLKDP
CCHHHHHHHHHHCCC		28.4933845483
51UbiquitinationNIIKSQLLKDPQVLF
HHHHHHHHCCCCEEE		4.6021890473
52UbiquitinationIIKSQLLKDPQVLFA
HHHHHHHCCCCEEEE		75.7821906983
52UbiquitinationIIKSQLLKDPQVLFA
HHHHHHHCCCCEEEE		75.7821890473
61PhosphorylationPQVLFAGYKVPHPLE
CCEEEECCCCCCCCC		12.84-
61UbiquitinationPQVLFAGYKVPHPLE
CCEEEECCCCCCCCC		12.8421890473
62UbiquitinationQVLFAGYKVPHPLEH
CEEEECCCCCCCCCC		48.6621890473
62UbiquitinationQVLFAGYKVPHPLEH
CEEEECCCCCCCCCC		48.6621906983
62AcetylationQVLFAGYKVPHPLEH
CEEEECCCCCCCCCC		48.6625953088
70UbiquitinationVPHPLEHKIIIRVQT
CCCCCCCEEEEEEEE		26.65-
70AcetylationVPHPLEHKIIIRVQT
CCCCCCCEEEEEEEE		26.6525953088
99PhosphorylationTDLISELSLLEERFR
HHHHHHHHHHHHHHH		27.1926437602
109UbiquitinationEERFRVAIKDKQEGI
HHHHHHHHHHHHCCC		5.6224816145
110UbiquitinationERFRVAIKDKQEGIE
HHHHHHHHHHHCCCC		49.4924816145
112UbiquitinationFRVAIKDKQEGIE--
HHHHHHHHHCCCC--		45.29-
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 RPB11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPB11_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 RPB11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB3_HUMANPOLR2Cphysical
9201987
SATB1_HUMANSATB1physical
12036295
AATF_HUMANAATFphysical
10783144
RPAP2_HUMANRPAP2physical
17643375
RPAP3_HUMANRPAP3physical
17643375
GPN1_HUMANGPN1physical
17643375
CTDP1_HUMANCTDP1physical
17643375
T2FB_HUMANGTF2F2physical
17643375
RPB2_HUMANPOLR2Bphysical
17643375
RPB7_HUMANPOLR2Gphysical
17643375
RPAB3_HUMANPOLR2Hphysical
17643375
RPAP1_HUMANRPAP1physical
17643375
TF2B_HUMANGTF2Bphysical
17643375
T2FA_HUMANGTF2F1physical
17643375
RPAB1_HUMANPOLR2Ephysical
17643375
HNRPU_HUMANHNRNPUphysical
17643375
DDB1_HUMANDDB1physical
17643375
INT3_HUMANINTS3physical
17643375
HCFC1_HUMANHCFC1physical
17643375
ELAV1_HUMANELAVL1physical
17643375
MED29_HUMANMED29physical
17643375
MEIG1_HUMANMEIG1physical
17643375
TCEA2_HUMANTCEA2physical
17643375
RPB4_HUMANPOLR2Dphysical
17643375
RPB1_HUMANPOLR2Aphysical
15282305
RPB2_HUMANPOLR2Bphysical
15282305
RPAP1_HUMANRPAP1physical
15282305
CTDP1_HUMANCTDP1physical
15282305
T2FA_HUMANGTF2F1physical
15282305
T2FB_HUMANGTF2F2physical
15282305
RPB4_HUMANPOLR2Dphysical
15282305
RPAB1_HUMANPOLR2Ephysical
15282305
RPB7_HUMANPOLR2Gphysical
15282305
TF2B_HUMANGTF2Bphysical
15282305
ESR1_HUMANESR1physical
16957778
SRC_HUMANSRCphysical
16957778
PSB9_HUMANPSMB9physical
16957778
ELOA1_HUMANTCEB3physical
16957778
RPAC1_HUMANPOLR1Cphysical
25416956
RPB2_HUMANPOLR2Bphysical
26344197
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 RPB11_HUMAN

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Related Literatures of Post-Translational Modification

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