MOB1B_HUMAN - dbPTM
MOB1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOB1B_HUMAN
UniProt AC Q7L9L4
Protein Name MOB kinase activator 1B
Gene Name MOB1B
Organism Homo sapiens (Human).
Sequence Length 216
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Activator of LATS1/2 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Stimulates the kinase activity of STK38L..
Protein Sequence MSFLFGSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRMAVMLPEGEDLNEWVAVNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDPVIQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLTSKDR
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
2Acetylation------MSFLFGSRS
------CCCCCCCCC
30.5622814378
2Phosphorylation------MSFLFGSRS
------CCCCCCCCC
30.5620068231
7Phosphorylation-MSFLFGSRSSKTFK
-CCCCCCCCCCCCCC
22.9628450419
9PhosphorylationSFLFGSRSSKTFKPK
CCCCCCCCCCCCCCC
37.5728450419
10PhosphorylationFLFGSRSSKTFKPKK
CCCCCCCCCCCCCCC
34.3128450419
11AcetylationLFGSRSSKTFKPKKN
CCCCCCCCCCCCCCC
60.2619822991
12PhosphorylationFGSRSSKTFKPKKNI
CCCCCCCCCCCCCCC
38.5529116813
16AcetylationSSKTFKPKKNIPEGS
CCCCCCCCCCCCCCC
60.0719823001
17AcetylationSKTFKPKKNIPEGSH
CCCCCCCCCCCCCCH
69.5019823011
17UbiquitinationSKTFKPKKNIPEGSH
CCCCCCCCCCCCCCH
69.50-
23PhosphorylationKKNIPEGSHQYELLK
CCCCCCCCHHHHHHH
13.0217287340
26PhosphorylationIPEGSHQYELLKHAE
CCCCCHHHHHHHHHH
11.7928796482
28 (in isoform 2)Phosphorylation-7.0327642862
30UbiquitinationSHQYELLKHAEATLG
CHHHHHHHHHHHHCC
54.09-
31 (in isoform 2)Phosphorylation-28.8627642862
35PhosphorylationLLKHAEATLGSGNLR
HHHHHHHHCCCCCEE
24.1329255136
38PhosphorylationHAEATLGSGNLRMAV
HHHHHCCCCCEEEEE
27.8525159151
40 (in isoform 2)Phosphorylation-26.6027251275
43 (in isoform 2)Phosphorylation-3.5727251275
74PhosphorylationQINMLYGTITDFCTE
HHHHHHHHHHHHCCC
13.72-
95PhosphorylationSAGPKYEYHWADGTN
CCCCCEEEECCCCCC
10.28-
98 (in isoform 2)Phosphorylation-7.6427642862
104UbiquitinationWADGTNIKKPIKCSA
CCCCCCCCCCCCCCC
55.3421890473
105UbiquitinationADGTNIKKPIKCSAP
CCCCCCCCCCCCCCC
48.45-
109UbiquitinationNIKKPIKCSAPKYID
CCCCCCCCCCCHHHH
4.3121890473
142UbiquitinationKIGVPFPKNFMSVAK
HCCCCCCHHHHHHHH
64.3021890473
147UbiquitinationFPKNFMSVAKTILKR
CCHHHHHHHHHHHHH
4.2121890473
149AcetylationKNFMSVAKTILKRLF
HHHHHHHHHHHHHHH
33.6619608861
181PhosphorylationQEEAHLNTSFKHFIF
CHHHHCCCCHHHHHH
41.7318362890

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
12TPhosphorylationKinaseMST1P26927
Uniprot
12TPhosphorylationKinaseSTK3Q13188
GPS
12TPhosphorylationKinaseSTK4Q13043
GPS
35TPhosphorylationKinaseMST1P26927
Uniprot
35TPhosphorylationKinaseSTK3Q13188
GPS
35TPhosphorylationKinaseSTK4Q13043
GPS
74TPhosphorylationKinaseSTK3Q13188
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOB1B_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 MOB1B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LATS1_HUMANLATS1physical
19739119
LATS2_HUMANLATS2physical
19739119
STK38_HUMANSTK38physical
19919647
LATS2_HUMANLATS2physical
19919647
A4_HUMANAPPphysical
21832049
ST38L_HUMANSTK38Lphysical
15067004
STK38_HUMANSTK38physical
15067004
LATS1_HUMANLATS1physical
18328708
ANR28_HUMANANKRD28physical
24255178
ANR52_HUMANANKRD52physical
24255178
CRLF3_HUMANCRLF3physical
24255178
DOCK6_HUMANDOCK6physical
24255178
DOCK7_HUMANDOCK7physical
24255178
DOCK8_HUMANDOCK8physical
24255178
DYST_HUMANDSTphysical
24255178
IPO11_HUMANIPO11physical
24255178
LATS1_HUMANLATS1physical
24255178
LATS2_HUMANLATS2physical
24255178
LRCH1_HUMANLRCH1physical
24255178
LRCH2_HUMANLRCH2physical
24255178
LRCH3_HUMANLRCH3physical
24255178
M4K4_HUMANMAP4K4physical
24255178
MOB2_HUMANMOB2physical
24255178
PPP6_HUMANPPP6Cphysical
24255178
PP6R1_HUMANPPP6R1physical
24255178
PP6R2_HUMANPPP6R2physical
24255178
PP6R3_HUMANPPP6R3physical
24255178
PTN14_HUMANPTPN14physical
24255178
RASF2_HUMANRASSF2physical
24255178
RASF5_HUMANRASSF5physical
24255178
SAV1_HUMANSAV1physical
24255178
STK3_HUMANSTK3physical
24255178
ST38L_HUMANSTK38Lphysical
24255178
STK4_HUMANSTK4physical
24255178
LATS1_HUMANLATS1physical
24366813
MOB1A_HUMANMOB1Aphysical
24366813
ST38L_HUMANSTK38Lphysical
24366813
ST38L_HUMANSTK38Lphysical
28514442
MOB1A_HUMANMOB1Aphysical
28514442
LATS1_HUMANLATS1physical
28514442
LATS2_HUMANLATS2physical
28514442
STK38_HUMANSTK38physical
28514442
LRCH2_HUMANLRCH2physical
28514442
DOCK7_HUMANDOCK7physical
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 MOB1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cellproliferation.";
Praskova M., Xia F., Avruch J.;
Curr. Biol. 18:311-321(2008).
Cited for: PHOSPHORYLATION AT THR-12 AND THR-35.

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