TOB1_HUMAN - dbPTM
TOB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOB1_HUMAN
UniProt AC P50616
Protein Name Protein Tob1
Gene Name TOB1
Organism Homo sapiens (Human).
Sequence Length 345
Subcellular Localization Cytoplasm. Nucleus. Only a small fraction localizes to the cytoplasm except in late S-phase where more than half of proteins become cytoplasmic..
Protein Description Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. [PubMed: 8632892]
Protein Sequence MQLEIQVALNFIISYLYNKLPRRRVNIFGEELERLLKKKYEGHWYPEKPYKGSGFRCIHIGEKVDPVIEQASKESGLDIDDVRGNLPQDLSVWIDPFEVSYQIGEKGPVKVLYVDDNNENGCELDKEIKNSFNPEAQVFMPISDPASSVSSSPSPPFGHSAAVSPTFMPRSTQPLTFTTATFAATKFGSTKMKNSGRSNKVARTSPINLGLNVNDLLKQKAISSSMHSLYGLGLGSQQQPQQQQQPAQPPPPPPPPQQQQQQKTSALSPNAKEFIFPNMQGQGSSTNGMFPGDSPLNLSPLQYSNAFDVFAAYGGLNEKSFVDGLNFSLNNMQYSNQQFQPVMAN
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
14PhosphorylationVALNFIISYLYNKLP
HHHHHHHHHHHHHCC
12.3124043423
15PhosphorylationALNFIISYLYNKLPR
HHHHHHHHHHHHCCC
11.6424043423
17PhosphorylationNFIISYLYNKLPRRR
HHHHHHHHHHCCCHH
11.3024043423
40PhosphorylationERLLKKKYEGHWYPE
HHHHHHHHCCCCCCC
35.7020090780
66PhosphorylationHIGEKVDPVIEQASK
ECCCCCCHHHHHHHH
31.7932142685
73UbiquitinationPVIEQASKESGLDID
HHHHHHHHHHCCCHH
59.9429967540
110UbiquitinationIGEKGPVKVLYVDDN
CCCCCCEEEEEECCC
29.6529967540
126UbiquitinationENGCELDKEIKNSFN
CCCCCCCHHHHHCCC
74.1629967540
143PhosphorylationAQVFMPISDPASSVS
CEEEEECCCCCHHCC
31.5028348404
147PhosphorylationMPISDPASSVSSSPS
EECCCCCHHCCCCCC
36.3425841592
148PhosphorylationPISDPASSVSSSPSP
ECCCCCHHCCCCCCC
28.2925841592
150PhosphorylationSDPASSVSSSPSPPF
CCCCHHCCCCCCCCC
27.3525841592
151PhosphorylationDPASSVSSSPSPPFG
CCCHHCCCCCCCCCC
44.0825841592
152PhosphorylationPASSVSSSPSPPFGH
CCHHCCCCCCCCCCC
23.1420068231
154PhosphorylationSSVSSSPSPPFGHSA
HHCCCCCCCCCCCCC
47.3420068231
160PhosphorylationPSPPFGHSAAVSPTF
CCCCCCCCCCCCCCC
20.5022210691
164PhosphorylationFGHSAAVSPTFMPRS
CCCCCCCCCCCCCCC
17.3120068231
166PhosphorylationHSAAVSPTFMPRSTQ
CCCCCCCCCCCCCCC
25.6725841592
172PhosphorylationPTFMPRSTQPLTFTT
CCCCCCCCCCCEEEE
35.17-
190PhosphorylationAATKFGSTKMKNSGR
EHHHHCCCCCCCCCC
35.2229759185
204PhosphorylationRSNKVARTSPINLGL
CCCCCCCCCCCCCCC
29.1730278072
205PhosphorylationSNKVARTSPINLGLN
CCCCCCCCCCCCCCC
20.4525159151
268PhosphorylationQQKTSALSPNAKEFI
HHHHCCCCCCHHHHC
18.8025849741
320PhosphorylationYGGLNEKSFVDGLNF
CCCCCHHHHHCCCCE
25.07-

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
152SPhosphorylationKinaseMAPK1P28482
GPS
152SPhosphorylationKinaseMAPK3P27361
GPS
152SPhosphorylationKinaseMAPK9P45984
GPS
154SPhosphorylationKinaseMAPK1P28482
GPS
154SPhosphorylationKinaseMAPK3P27361
GPS
154SPhosphorylationKinaseMAPK9P45984
GPS
164SPhosphorylationKinaseMAPK1P28482
GPS
164SPhosphorylationKinaseMAPK3P27361
GPS
164SPhosphorylationKinaseMAPK9P45984
GPS
-KUbiquitinationE3 ubiquitin ligaseSKP2Q13309
PMID:16951159

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOB1_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 TOB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP1_HUMANPABPC1physical
18056425
CNOT7_HUMANCNOT7physical
18056425
SCMH1_HUMANSCMH1physical
16169070
SETB1_HUMANSETDB1physical
16169070
SMAD4_HUMANSMAD4physical
11163184
SMAD5_HUMANSMAD5physical
11163184
SMAD1_HUMANSMAD1physical
11163184
SMAD9_HUMANSMAD9physical
11163184
CNOT7_HUMANCNOT7physical
10602502
MK01_HUMANMAPK1physical
12151396
MK09_HUMANMAPK9physical
12151396
KS6A1_HUMANRPS6KA1physical
11260258
SKP2_HUMANSKP2physical
16951159
CTNB1_HUMANCTNNB1physical
16890162
SMAD3_HUMANSMAD3physical
16890162
PABP1_HUMANPABPC1physical
17785442
CAF1A_HUMANCHAF1Aphysical
17785442
PAN2_HUMANPAN2physical
17785442
CDC7_HUMANCDC7physical
23066029
A4_HUMANAPPphysical
21832049
CORO7_HUMANCORO7physical
21130766
CNOT6_HUMANCNOT6physical
28514442
CNO6L_HUMANCNOT6Lphysical
28514442
CNOT2_HUMANCNOT2physical
28514442
TB182_HUMANTNKS1BP1physical
28514442
CNOT3_HUMANCNOT3physical
28514442
CNOT9_HUMANRQCD1physical
28514442
CNO11_HUMANCNOT11physical
28514442
CNOT8_HUMANCNOT8physical
28514442
CNOT1_HUMANCNOT1physical
28514442
CNO10_HUMANCNOT10physical
28514442
RAVR1_HUMANRAVER1physical
28514442
FHL2_HUMANFHL2physical
28514442
RN219_HUMANRNF219physical
28514442
ATE1_HUMANATE1physical
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 TOB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204, AND MASSSPECTROMETRY.

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