SSU72_HUMAN - dbPTM
SSU72_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSU72_HUMAN
UniProt AC Q9NP77
Protein Name RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Gene Name SSU72
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization Nucleus. Cytoplasm. Predominantly in the cytosol.
Protein Description Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK..
Protein Sequence MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSREQETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRTFLHTVCFY
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
3Phosphorylation-----MPSSPLRVAV
-----CCCCCCEEEE
43.2030266825
4Phosphorylation----MPSSPLRVAVV
----CCCCCCEEEEE
23.2930266825
13PhosphorylationLRVAVVCSSNQNRSM
CEEEEEECCCCCHHH
22.2528102081
14PhosphorylationRVAVVCSSNQNRSME
EEEEEECCCCCHHHH
36.9930631047
19PhosphorylationCSSNQNRSMEAHNIL
ECCCCCHHHHHHHHH
28.6428857561
27PhosphorylationMEAHNILSKRGFSVR
HHHHHHHHHCCCEEE
19.2622210691
28 (in isoform 1)Ubiquitination-53.7621890473
28 (in isoform 2)Ubiquitination-53.7621890473
28UbiquitinationEAHNILSKRGFSVRS
HHHHHHHHCCCEEEE
53.7622817900
35PhosphorylationKRGFSVRSFGTGTHV
HCCCEEEEECCCCEE
26.3520068231
38PhosphorylationFSVRSFGTGTHVKLP
CEEEEECCCCEEECC
36.5820068231
40PhosphorylationVRSFGTGTHVKLPGP
EEEECCCCEEECCCC
24.2720068231
43 (in isoform 2)Ubiquitination-41.1621890473
43UbiquitinationFGTGTHVKLPGPAPD
ECCCCEEECCCCCCC
41.1621890473
43 (in isoform 1)Ubiquitination-41.1621890473
43AcetylationFGTGTHVKLPGPAPD
ECCCCEEECCCCCCC
41.1625953088
51UbiquitinationLPGPAPDKPNVYDFK
CCCCCCCCCCEEEHH
37.1221906983
51AcetylationLPGPAPDKPNVYDFK
CCCCCCCCCCEEEHH
37.1226051181
51 (in isoform 2)Ubiquitination-37.1221890473
51 (in isoform 1)Ubiquitination-37.1221890473
55PhosphorylationAPDKPNVYDFKTTYD
CCCCCCEEEHHHCHH
23.4627642862
58 (in isoform 1)Ubiquitination-36.7421890473
58 (in isoform 2)Ubiquitination-36.7421890473
58UbiquitinationKPNVYDFKTTYDQMY
CCCEEEHHHCHHHHH
36.7421906983
61PhosphorylationVYDFKTTYDQMYNDL
EEEHHHCHHHHHHHH
14.9227642862
65PhosphorylationKTTYDQMYNDLLRKD
HHCHHHHHHHHHHHC
10.4127642862
71UbiquitinationMYNDLLRKDKELYTQ
HHHHHHHHCHHHHHH
73.4623000965
73 (in isoform 1)Ubiquitination-53.2921890473
73UbiquitinationNDLLRKDKELYTQNG
HHHHHHCHHHHHHCC
53.2923000965
102UbiquitinationPERFQNCKDLFDLIL
HHHHHCHHHHHHHHH
66.0833845483
116PhosphorylationLTCEERVYDQVVEDL
HHHHHHHHHHHHHHH
13.5928796482

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
3SPhosphorylationKinaseAURBQ96GD4
PSP
4SPhosphorylationKinaseAURBQ96GD4
PSP
19SPhosphorylationKinaseAURKBQ96GD4
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSU72_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 SSU72_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD21_HUMANRAD21physical
20818333
STAG2_HUMANSTAG2physical
20818333
SMC1A_HUMANSMC1Aphysical
20818333
SMC3_HUMANSMC3physical
20818333
THIC_HUMANACAT2physical
22939629
STXB2_HUMANSTXBP2physical
22939629
VINC_HUMANVCLphysical
22939629
XPO1_HUMANXPO1physical
22939629
TEBP_HUMANPTGES3physical
22939629
THOP1_HUMANTHOP1physical
22939629
UBE2H_HUMANUBE2Hphysical
22939629
TIPRL_HUMANTIPRLphysical
22939629
TPIS_HUMANTPI1physical
22939629
RPB1_YEASTRPO21physical
24413056
RPB1_HUMANPOLR2Aphysical
20861839
CPSF1_HUMANCPSF1physical
27880917
CPSF2_HUMANCPSF2physical
27880917
CPSF3_HUMANCPSF3physical
27880917
CSTF2_HUMANCSTF2physical
27880917
CSTF3_HUMANCSTF3physical
27880917
HNRPL_HUMANHNRNPLphysical
27880917
SYMPK_HUMANSYMPKphysical
27880917
CARF_HUMANCDKN2AIPphysical
27880917
ZN638_HUMANZNF638physical
27880917
NCOA5_HUMANNCOA5physical
27880917
PCF11_HUMANPCF11physical
27880917
ELP5_HUMANELP5physical
27880917

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 SSU72_HUMAN

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Related Literatures of Post-Translational Modification

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