IN80B_HUMAN - dbPTM
IN80B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IN80B_HUMAN
UniProt AC Q9C086
Protein Name INO80 complex subunit B
Gene Name INO80B
Organism Homo sapiens (Human).
Sequence Length 356
Subcellular Localization Nucleus . Nucleus, nucleolus .
Protein Description Induces growth and cell cycle arrests at the G1 phase of the cell cycle.; Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair..
Protein Sequence MSKLWRRGSTSGAMEAPEPGEALELSLAGAHGHGVHKKKHKKHKKKHKKKHHQEEDAGPTQPSPAKPQLKLKIKLGGQVLGTKSVPTFTVIPEGPRSPSPLMVVDNEEEPMEGVPLEQYRAWLDEDSNLSPSPLRDLSGGLGGQEEEEEQRWLDALEKGELDDNGDLKKEINERLLTARQRALLQKARSQPSPMLPLPVAEGCPPPALTEEMLLKREERARKRRLQAARRAEEHKNQTIERLTKTAATSGRGGRGGARGERRGGRAAAPAPMVRYCSGAQGSTLSFPPGVPAPTAVSQRPSPSGPPPRCSVPGCPHPRRYACSRTGQALCSLQCYRINLQMRLGGPEGPGSPLLAT
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
2Phosphorylation------MSKLWRRGS
------CCCCCCCCC
36.1326074081
9PhosphorylationSKLWRRGSTSGAMEA
CCCCCCCCCCCCCCC
20.0026074081
10PhosphorylationKLWRRGSTSGAMEAP
CCCCCCCCCCCCCCC
33.7225849741
11PhosphorylationLWRRGSTSGAMEAPE
CCCCCCCCCCCCCCC
26.6729496963
26PhosphorylationPGEALELSLAGAHGH
CCCCEEHHHHHHCCC
13.5423882029
60PhosphorylationQEEDAGPTQPSPAKP
CCCCCCCCCCCCCCC
52.7923927012
63PhosphorylationDAGPTQPSPAKPQLK
CCCCCCCCCCCCCEE
27.8929255136
82O-linked_GlycosylationLGGQVLGTKSVPTFT
ECCEEECCCCCCEEE
18.91OGP
84PhosphorylationGQVLGTKSVPTFTVI
CEEECCCCCCEEEEC
32.9220873877
87PhosphorylationLGTKSVPTFTVIPEG
ECCCCCCEEEECCCC
29.7729116813
89PhosphorylationTKSVPTFTVIPEGPR
CCCCCEEEECCCCCC
21.7228464451
97PhosphorylationVIPEGPRSPSPLMVV
ECCCCCCCCCCEEEE
32.6322617229
99PhosphorylationPEGPRSPSPLMVVDN
CCCCCCCCCEEEECC
31.7322617229
119PhosphorylationEGVPLEQYRAWLDED
CCCCHHHHHHHHCCC
7.9122777824
127PhosphorylationRAWLDEDSNLSPSPL
HHHHCCCCCCCCCCH
37.3130266825
130PhosphorylationLDEDSNLSPSPLRDL
HCCCCCCCCCCHHHC
27.8122167270
132PhosphorylationEDSNLSPSPLRDLSG
CCCCCCCCCHHHCCC
32.9422167270
138PhosphorylationPSPLRDLSGGLGGQE
CCCHHHCCCCCCCCH
34.7925159151
168SumoylationLDDNGDLKKEINERL
CCCCCCHHHHHHHHH
53.7717000644
168SumoylationLDDNGDLKKEINERL
CCCCCCHHHHHHHHH
53.77-
192PhosphorylationQKARSQPSPMLPLPV
HHHHCCCCCCCCCCC
18.4624719451
215SumoylationLTEEMLLKREERARK
CCHHHHHHHHHHHHH
54.5217000644
215SumoylationLTEEMLLKREERARK
CCHHHHHHHHHHHHH
54.52-
243PhosphorylationNQTIERLTKTAATSG
CHHHHHHHHHHHHCC
32.3520068231
245PhosphorylationTIERLTKTAATSGRG
HHHHHHHHHHHCCCC
19.1120068231
248PhosphorylationRLTKTAATSGRGGRG
HHHHHHHHCCCCCCC
29.2920068231
249PhosphorylationLTKTAATSGRGGRGG
HHHHHHHCCCCCCCC
23.0520068231
251MethylationKTAATSGRGGRGGAR
HHHHHCCCCCCCCCC
44.13115920685
254MethylationATSGRGGRGGARGER
HHCCCCCCCCCCCCC
43.10115920689
258MethylationRGGRGGARGERRGGR
CCCCCCCCCCCCCCC
51.27115920693
325PhosphorylationRRYACSRTGQALCSL
CCCCCCHHHHHHHHH
19.8328555341
331PhosphorylationRTGQALCSLQCYRIN
HHHHHHHHHEEEEEE
23.48-
335PhosphorylationALCSLQCYRINLQMR
HHHHHEEEEEEEEEC
11.10-
351PhosphorylationGGPEGPGSPLLAT--
CCCCCCCCCCCCC--
18.6023401153
356PhosphorylationPGSPLLAT-------
CCCCCCCC-------
38.8330266825

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 IN80B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IN80B_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 IN80B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD81_HUMANCD81physical
16169070
IN80E_HUMANINO80Ephysical
17721549
RUVB1_HUMANRUVBL1physical
17721549
RUVB2_HUMANRUVBL2physical
17721549
ACL6A_HUMANACTL6Aphysical
17721549
IN80C_HUMANINO80Cphysical
17721549
TYY1_HUMANYY1physical
17721549
INO80_HUMANINO80physical
17721549
NFRKB_HUMANNFRKBphysical
17721549
TFPT_HUMANTFPTphysical
17721549
ARP5_HUMANACTR5physical
17721549
ARP8_HUMANACTR8physical
17721549
IN80D_HUMANINO80Dphysical
17721549
MCRS1_HUMANMCRS1physical
17721549
IBP2_HUMANIGFBP2physical
19095771
ADIP_HUMANSSX2IPphysical
25416956
THOC4_HUMANALYREFphysical
28561026
CATIN_HUMANCACTINphysical
28561026
MRCKA_HUMANCDC42BPAphysical
28561026
CHD1_HUMANCHD1physical
28561026
DDX17_HUMANDDX17physical
28561026
DDX21_HUMANDDX21physical
28561026
DDX46_HUMANDDX46physical
28561026
DDX5_HUMANDDX5physical
28561026
DDX50_HUMANDDX50physical
28561026
DHX15_HUMANDHX15physical
28561026
DHX30_HUMANDHX30physical
28561026
DHX9_HUMANDHX9physical
28561026
DICER_HUMANDICER1physical
28561026
FBX3_HUMANFBXO3physical
28561026
SPB1_HUMANFTSJ3physical
28561026
NOG2_HUMANGNL2physical
28561026
GNL3_HUMANGNL3physical
28561026
IN80B_HUMANINO80Bphysical
28561026
KIF1C_HUMANKIF1Cphysical
28561026
KIF23_HUMANKIF23physical
28561026
LUC7L_HUMANLUC7Lphysical
28561026
LC7L2_HUMANLUC7L2physical
28561026
MA7D1_HUMANMAP7D1physical
28561026
NPM_HUMANNPM1physical
28561026
PRP19_HUMANPRPF19physical
28561026
PR38B_HUMANPRPF38Bphysical
28561026
PUF60_HUMANPUF60physical
28561026
RBM14_HUMANRBM14physical
28561026
RBM39_HUMANRBM39physical
28561026
RL11_HUMANRPL11physical
28561026
RL12_HUMANRPL12physical
28561026
RL13_HUMANRPL13physical
28561026
RL17_HUMANRPL17physical
28561026
RL18_HUMANRPL18physical
28561026
RL18A_HUMANRPL18Aphysical
28561026
RL19_HUMANRPL19physical
28561026
RL21_HUMANRPL21physical
28561026
RL23A_HUMANRPL23Aphysical
28561026
RL24_HUMANRPL24physical
28561026
RL27_HUMANRPL27physical
28561026
RL27A_HUMANRPL27Aphysical
28561026
RL28_HUMANRPL28physical
28561026
RL3_HUMANRPL3physical
28561026
RL30_HUMANRPL30physical
28561026
RL31_HUMANRPL31physical
28561026
RL36A_HUMANRPL36Aphysical
28561026
RL4_HUMANRPL4physical
28561026
RL6_HUMANRPL6physical
28561026
RL7_HUMANRPL7physical
28561026
RL7A_HUMANRPL7Aphysical
28561026
RL8_HUMANRPL8physical
28561026
RLA0_HUMANRPLP0physical
28561026
RLA2_HUMANRPLP2physical
28561026
RS16_HUMANRPS16physical
28561026
RS2_HUMANRPS2physical
28561026
RS3_HUMANRPS3physical
28561026
RS3A_HUMANRPS3Aphysical
28561026
RS8_HUMANRPS8physical
28561026
RRP12_HUMANRRP12physical
28561026
RL1D1_HUMANRSL1D1physical
28561026
RUVB1_HUMANRUVBL1physical
28561026
RUVB2_HUMANRUVBL2physical
28561026
MTMR5_HUMANSBF1physical
28561026
SFR19_HUMANSCAF1physical
28561026
SCAF8_HUMANSCAF8physical
28561026
PAIRB_HUMANSERBP1physical
28561026
SQSTM_HUMANSQSTM1physical
28561026
SREK1_HUMANSREK1physical
28561026
SRPK1_HUMANSRPK1physical
28561026
SRPK2_HUMANSRPK2physical
28561026
SRS11_HUMANSRSF11physical
28561026
TSR1_HUMANTSR1physical
28561026
U2AF2_HUMANU2AF2physical
28561026
WDR5_HUMANWDR5physical
28561026
YBOX3_HUMANYBX3physical
28561026
ZN768_HUMANZNF768physical
28561026
ARP5_HUMANACTR5physical
28561026
ARP8_HUMANACTR8physical
28561026
BRD2_HUMANBRD2physical
28561026
BRD3_HUMANBRD3physical
28561026
BRD4_HUMANBRD4physical
28561026
INO80_HUMANINO80physical
28561026
NFRKB_HUMANNFRKBphysical
28561026
RPB1_HUMANPOLR2Aphysical
28561026
RPB2_HUMANPOLR2Bphysical
28561026

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 IN80B_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 SER-127; SER-130 ANDSER-132, AND MASS SPECTROMETRY.
"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-97; SER-99; SER-130 ANDSER-132, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASSSPECTROMETRY.

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