MOB1A_MOUSE
ID MOB1A_MOUSE Reviewed; 216 AA.
AC Q921Y0; Q3TJA6; Q8C194; Q8C1C7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=MOB kinase activator 1A;
DE AltName: Full=Mob1 homolog 1B;
DE AltName: Full=Mps one binder kinase activator-like 1B;
GN Name=Mob1a; Synonyms=Mobk1b, Mobkl1b;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Fetal head, Placenta, Skin, and Spleen;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 STK38 and STK38L. Acts cooperatively with STK3/MST2
CC to activate STK38 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds STK38 and STK38L. Interacts with LATS1 and LATS2 (By
CC similarity). Forms a tripartite complex with STK38 and STK3/MST2 (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q921Y0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921Y0-2; Sequence=VSP_012297;
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; AK028416; BAC25938.1; -; mRNA.
DR EMBL; AK028695; BAC26070.1; -; mRNA.
DR EMBL; AK167515; BAE39589.1; -; mRNA.
DR EMBL; AK172205; BAE42880.1; -; mRNA.
DR EMBL; BC009149; AAH09149.1; -; mRNA.
DR EMBL; BC033463; AAH33463.1; -; mRNA.
DR CCDS; CCDS39533.1; -. [Q921Y0-1]
DR RefSeq; NP_663546.1; NM_145571.2. [Q921Y0-1]
DR AlphaFoldDB; Q921Y0; -.
DR SMR; Q921Y0; -.
DR BioGRID; 231222; 4.
DR IntAct; Q921Y0; 1.
DR STRING; 10090.ENSMUSP00000054452; -.
DR iPTMnet; Q921Y0; -.
DR PhosphoSitePlus; Q921Y0; -.
DR EPD; Q921Y0; -.
DR jPOST; Q921Y0; -.
DR MaxQB; Q921Y0; -.
DR PaxDb; Q921Y0; -.
DR PeptideAtlas; Q921Y0; -.
DR PRIDE; Q921Y0; -.
DR ProteomicsDB; 295648; -. [Q921Y0-1]
DR ProteomicsDB; 295649; -. [Q921Y0-2]
DR Antibodypedia; 47474; 189 antibodies from 30 providers.
DR DNASU; 232157; -.
DR Ensembl; ENSMUST00000038658; ENSMUSP00000039115; ENSMUSG00000043131. [Q921Y0-2]
DR Ensembl; ENSMUST00000055261; ENSMUSP00000054452; ENSMUSG00000043131. [Q921Y0-1]
DR Ensembl; ENSMUST00000101245; ENSMUSP00000098802; ENSMUSG00000043131. [Q921Y0-1]
DR GeneID; 232157; -.
DR KEGG; mmu:232157; -.
DR UCSC; uc009cnf.1; mouse. [Q921Y0-1]
DR UCSC; uc012eny.1; mouse. [Q921Y0-2]
DR CTD; 55233; -.
DR MGI; MGI:2442631; Mob1a.
DR VEuPathDB; HostDB:ENSMUSG00000043131; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244898; -.
DR HOGENOM; CLU_038321_3_1_1; -.
DR InParanoid; Q921Y0; -.
DR OMA; TCEVMSA; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q921Y0; -.
DR TreeFam; TF300789; -.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR BioGRID-ORCS; 232157; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Mob1a; mouse.
DR PRO; PR:Q921Y0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q921Y0; protein.
DR Bgee; ENSMUSG00000043131; Expressed in ileal epithelium and 253 other tissues.
DR ExpressionAtlas; Q921Y0; baseline and differential.
DR Genevisible; Q921Y0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0007165; P:signal transduction; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT CHAIN 2..216
FT /note="MOB kinase activator 1A"
FT /id="PRO_0000193567"
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:Q9H8S9"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT MOD_RES 74
FT /note="Phosphothreonine; by STK3/MST2"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8S9"
FT VAR_SEQ 61..137
FT /note="TVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWADGTNIKKPIKCSAP
FT KYIDYLMTWVQDQLDDETLFPSKIG -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012297"
FT CONFLICT 105..106
FT /note="KP -> NA (in Ref. 1; BAC25938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 25080 MW; 58043AECAD1F5987 CRC64;
MSFLFSSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRQAVMLPEG EDLNEWIAVN
TVDFFNQINM LYGTITEFCT EASCPVMSAG PRYEYHWADG TNIKKPIKCS APKYIDYLMT
WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDSV MQLQEEAHLN
TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LGSKDR
