MBIP1_HUMAN - dbPTM
MBIP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBIP1_HUMAN
UniProt AC Q9NS73
Protein Name MAP3K12-binding inhibitory protein 1
Gene Name MBIP
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Nucleus. Cytoplasm. Shows a cytoplasmic localization when coexpressed with MAP3K12.
Protein Description Inhibits the MAP3K12 activity to induce the activation of the JNK/SAPK pathway. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4..
Protein Sequence MAAATELNRPSSGDRNLERRCRPNLSREVLYEIFRSLHTLVGQLDLRDDVVKITIDWNKLQSLSAFQPALLFSALEQHILYLQPFLAKLQSPIKEENTTAVEEIGRTEMGNKNEVNDKFSIGDLQEEEKHKESDLRDVKKTQIHFDPEVVQIKAGKAEIDRRISAFIERKQAEINENNVREFCNVIDCNQENSCARTDAIFTPYPGFKSHVKVSRVVNTYGPQTRPEGIPGSGHKPNSMLRDCGNQAVEERLQNIEAHLRLQTGGPVPRDIYQRIKKLEDKILELEGISPEYFQSVSFSGKRRKVQPPQQNYSLAELDEKISALKQALLRKSREAESMATHHLP
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
5Phosphorylation---MAAATELNRPSS
---CCCCCCCCCCCC
35.9623186163
11PhosphorylationATELNRPSSGDRNLE
CCCCCCCCCCCCCHH
43.6523663014
12PhosphorylationTELNRPSSGDRNLER
CCCCCCCCCCCCHHH
47.6023663014
91PhosphorylationPFLAKLQSPIKEENT
HHHHHCCCCCCCCCC
38.7429255136
94UbiquitinationAKLQSPIKEENTTAV
HHCCCCCCCCCCCHH
63.4621906983
94SumoylationAKLQSPIKEENTTAV
HHCCCCCCCCCCCHH
63.4628112733
94 (in isoform 1)Ubiquitination-63.4621906983
94 (in isoform 2)Ubiquitination-63.4621906983
94 (in isoform 3)Ubiquitination-63.4621906983
94SumoylationAKLQSPIKEENTTAV
HHCCCCCCCCCCCHH
63.46-
98PhosphorylationSPIKEENTTAVEEIG
CCCCCCCCCHHHHHC
21.2930266825
99PhosphorylationPIKEENTTAVEEIGR
CCCCCCCCHHHHHCC
40.0423403867
107PhosphorylationAVEEIGRTEMGNKNE
HHHHHCCCCCCCCCC
25.72-
118UbiquitinationNKNEVNDKFSIGDLQ
CCCCCCCCCCCCCHH
35.49-
118SumoylationNKNEVNDKFSIGDLQ
CCCCCCCCCCCCCHH
35.4928112733
129SumoylationGDLQEEEKHKESDLR
CCHHHHHHHCCCCHH
64.3628112733
129UbiquitinationGDLQEEEKHKESDLR
CCHHHHHHHCCCCHH
64.36-
139SumoylationESDLRDVKKTQIHFD
CCCHHHHHHHHCCCC
55.1628112733
140UbiquitinationSDLRDVKKTQIHFDP
CCHHHHHHHHCCCCH
45.57-
141O-linked_GlycosylationDLRDVKKTQIHFDPE
CHHHHHHHHCCCCHH
27.3430379171
153 (in isoform 3)Ubiquitination-33.7121906983
153UbiquitinationDPEVVQIKAGKAEID
CHHHHEEECCHHHHH
33.712190698
153 (in isoform 2)Ubiquitination-33.7121906983
153 (in isoform 1)Ubiquitination-33.7121906983
153SumoylationDPEVVQIKAGKAEID
CHHHHEEECCHHHHH
33.7128112733
164PhosphorylationAEIDRRISAFIERKQ
HHHHHHHHHHHHHHH
18.4723312004
170UbiquitinationISAFIERKQAEINEN
HHHHHHHHHHHHCCC
40.86-
208UbiquitinationFTPYPGFKSHVKVSR
ECCCCCCHHHCEEEE
45.63-
232PhosphorylationRPEGIPGSGHKPNSM
CCCCCCCCCCCCCHH
32.1623898821
235SumoylationGIPGSGHKPNSMLRD
CCCCCCCCCCHHHHH
49.7928112733
235UbiquitinationGIPGSGHKPNSMLRD
CCCCCCCCCCHHHHH
49.79-
238PhosphorylationGSGHKPNSMLRDCGN
CCCCCCCHHHHHHCH
27.9328555341
263PhosphorylationEAHLRLQTGGPVPRD
HHHHHHHCCCCCCHH
49.0122985185
301SumoylationQSVSFSGKRRKVQPP
HHCCCCCCCCCCCCC
48.0828112733
301AcetylationQSVSFSGKRRKVQPP
HHCCCCCCCCCCCCC
48.0823954790
304SumoylationSFSGKRRKVQPPQQN
CCCCCCCCCCCCCCC
49.6228112733
304UbiquitinationSFSGKRRKVQPPQQN
CCCCCCCCCCCCCCC
49.62-
320UbiquitinationSLAELDEKISALKQA
CHHHHHHHHHHHHHH
41.44-
325UbiquitinationDEKISALKQALLRKS
HHHHHHHHHHHHHHH
32.99-
325AcetylationDEKISALKQALLRKS
HHHHHHHHHHHHHHH
32.9925953088
325SumoylationDEKISALKQALLRKS
HHHHHHHHHHHHHHH
32.9928112733
332PhosphorylationKQALLRKSREAESMA
HHHHHHHHHHHHHHH
28.9923898821

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 MBIP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MBIP1_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 MBIP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP63_HUMANCEP63physical
16189514
MBIP1_HUMANMBIPphysical
16189514
NDEL1_HUMANNDEL1physical
16189514
DGC6L_HUMANDGCR6Lphysical
16189514
PKHF2_HUMANPLEKHF2physical
16189514
CSR2B_HUMANCSRP2BPphysical
16189514
LMO3_HUMANLMO3physical
16189514
M3K12_HUMANMAP3K12physical
10801814
KAT2B_HUMANKAT2Bphysical
18838386
YETS2_HUMANYEATS2physical
18838386
KAT2A_HUMANKAT2Aphysical
18838386
TAD2A_HUMANTADA2Aphysical
18838386
TADA3_HUMANTADA3physical
18838386
WDR5_HUMANWDR5physical
18838386
SGF29_HUMANCCDC101physical
18838386
NC2B_HUMANDR1physical
18838386
MBIP1_HUMANMBIPphysical
19060904
RPGF1_HUMANRAPGEF1physical
21988832
MYD88_HUMANMYD88physical
21988832
MS18A_HUMANMIS18Aphysical
25416956
CSR2B_HUMANCSRP2BPphysical
25416956
MOAP1_HUMANMOAP1physical
25416956
PKHF2_HUMANPLEKHF2physical
25416956
NDEL1_HUMANNDEL1physical
25416956
DRC7_HUMANDRC7physical
25416956
ING5_HUMANING5physical
25416956
TF2LY_HUMANTGIF2LYphysical
25416956
KLC3_HUMANKLC3physical
25416956
EXOC8_HUMANEXOC8physical
25416956
TXLNB_HUMANTXLNBphysical
25416956
TXLNA_HUMANTXLNAphysical
25416956
ZN131_HUMANZNF131physical
26186194
CSR2B_HUMANCSRP2BPphysical
26186194
YETS2_HUMANYEATS2physical
26186194
PRPK_HUMANTP53RKphysical
26186194
IQGA3_HUMANIQGAP3physical
26186194
ZZZ3_HUMANZZZ3physical
26186194
CRTAP_HUMANCRTAPphysical
26186194
PHLB3_HUMANPHLDB3physical
26186194
STXB4_HUMANSTXBP4physical
26186194
KAT2B_HUMANKAT2Bphysical
26186194
KAT2A_HUMANKAT2Aphysical
26186194
P3H1_HUMANP3H1physical
26186194
BRE1B_HUMANRNF40physical
26186194
GMCL1_HUMANGMCL1physical
26186194
CTR9_HUMANCTR9physical
26186194
TADA3_HUMANTADA3physical
26186194
CC85C_HUMANCCDC85Cphysical
26186194
NC2B_HUMANDR1physical
26186194
TAD2A_HUMANTADA2Aphysical
26186194
F199X_HUMANFAM199Xphysical
26186194
KLH26_HUMANKLHL26physical
26186194
RFWD3_HUMANRFWD3physical
26186194
TPRKB_HUMANTPRKBphysical
26186194
TADA3_HUMANTADA3physical
28514442
TAD2A_HUMANTADA2Aphysical
28514442
CSR2B_HUMANCSRP2BPphysical
28514442
KAT2B_HUMANKAT2Bphysical
28514442
ZZZ3_HUMANZZZ3physical
28514442
ZN131_HUMANZNF131physical
28514442
YETS2_HUMANYEATS2physical
28514442
KAT2A_HUMANKAT2Aphysical
28514442
GMCL1_HUMANGMCL1physical
28514442
STXB4_HUMANSTXBP4physical
28514442
FA92A_HUMANFAM92A1physical
28514442
F199X_HUMANFAM199Xphysical
28514442
RFWD3_HUMANRFWD3physical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
PHLB3_HUMANPHLDB3physical
28514442
CTR9_HUMANCTR9physical
28514442
TPRKB_HUMANTPRKBphysical
28514442
NC2B_HUMANDR1physical
28514442
PRPK_HUMANTP53RKphysical
28514442
BRMS1_HUMANBRMS1physical
28514442
CRTAP_HUMANCRTAPphysical
28514442
KLH26_HUMANKLHL26physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
OSGEP_HUMANOSGEPphysical
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 MBIP1_HUMAN

loading...

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-91, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-91, AND MASSSPECTROMETRY.

TOP