MOB1B_MOUSE
ID MOB1B_MOUSE Reviewed; 216 AA.
AC Q8BPB0;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=MOB kinase activator 1B;
DE AltName: Full=Mob1 homolog 1A;
DE AltName: Full=Mps one binder kinase activator-like 1A;
GN Name=Mob1b; Synonyms=Mobkl1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Activator of LATS1/2 in the Hippo signaling pathway which
CC plays a pivotal role in organ size control and tumor suppression by
CC restricting proliferation and promoting apoptosis. The core of this
CC pathway is composed of a kinase cascade wherein STK3/MST2 and
CC STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates
CC and activates LATS1/2 in complex with its regulatory protein MOB1,
CC which in turn phosphorylates and inactivates YAP1 oncoprotein and
CC WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its
CC translocation into the nucleus to regulate cellular genes important for
CC cell proliferation, cell death, and cell migration. Stimulates the
CC kinase activity of STK38L (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds STK38L. Interacts with LATS1 and LATS2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1 and this phosphorylation
CC enhances its binding to LATS1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; AK077320; BAC36748.1; -; mRNA.
DR CCDS; CCDS39139.1; -.
DR RefSeq; NP_081011.1; NM_026735.2.
DR PDB; 5B5V; X-ray; 2.19 A; A/B/C/D/E/F=1-216.
DR PDB; 5B5W; X-ray; 2.96 A; A=33-216.
DR PDB; 5B6B; X-ray; 3.54 A; A/B/D/F/H/K/M/O=1-216.
DR PDBsum; 5B5V; -.
DR PDBsum; 5B5W; -.
DR PDBsum; 5B6B; -.
DR AlphaFoldDB; Q8BPB0; -.
DR SMR; Q8BPB0; -.
DR STRING; 10090.ENSMUSP00000006424; -.
DR iPTMnet; Q8BPB0; -.
DR PhosphoSitePlus; Q8BPB0; -.
DR jPOST; Q8BPB0; -.
DR MaxQB; Q8BPB0; -.
DR PaxDb; Q8BPB0; -.
DR PRIDE; Q8BPB0; -.
DR ProteomicsDB; 295575; -.
DR Antibodypedia; 24395; 399 antibodies from 28 providers.
DR DNASU; 68473; -.
DR Ensembl; ENSMUST00000006424; ENSMUSP00000006424; ENSMUSG00000006262.
DR GeneID; 68473; -.
DR KEGG; mmu:68473; -.
DR UCSC; uc008yae.1; mouse.
DR CTD; 92597; -.
DR MGI; MGI:1915723; Mob1b.
DR VEuPathDB; HostDB:ENSMUSG00000006262; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244898; -.
DR HOGENOM; CLU_038321_3_2_1; -.
DR InParanoid; Q8BPB0; -.
DR OMA; HYPVIVH; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q8BPB0; -.
DR TreeFam; TF300789; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 68473; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Mob1b; mouse.
DR PRO; PR:Q8BPB0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BPB0; protein.
DR Bgee; ENSMUSG00000006262; Expressed in superior surface of tongue and 251 other tissues.
DR ExpressionAtlas; Q8BPB0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019209; F:kinase activator activity; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0035329; P:hippo signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031952; P:regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR DisProt; DP02570; -.
DR Gene3D; 1.20.140.30; -; 1.
DR InterPro; IPR005301; MOB_kinase_act_fam.
DR InterPro; IPR036703; MOB_kinase_act_sf.
DR PANTHER; PTHR22599; PTHR22599; 1.
DR Pfam; PF03637; Mob1_phocein; 1.
DR SMART; SM01388; Mob1_phocein; 1.
DR SUPFAM; SSF101152; SSF101152; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7L9L4"
FT CHAIN 2..216
FT /note="MOB kinase activator 1B"
FT /id="PRO_0000193565"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L9L4"
FT MOD_RES 12
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:Q7L9L4"
FT MOD_RES 35
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:Q7L9L4"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 53..74
FT /evidence="ECO:0007829|PDB:5B5V"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:5B5V"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5B5V"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5B5V"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:5B5V"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 144..173
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5B5V"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:5B5V"
SQ SEQUENCE 216 AA; 25091 MW; 29EBA287B0CDAF90 CRC64;
MSFLFGSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRMAVMLPEG EDLNEWVAVN
TVDFFNQINM LYGTITDFCT EESCPVMSAG PKYEYHWADG TNIKKPIKCS APKYIDYLMT
WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDPV IQLQEEAHLN
TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LTSKDR
