MOB1B_HUMAN
ID MOB1B_HUMAN Reviewed; 216 AA.
AC Q7L9L4; B2R8U6; B4DRY3; Q8IY23;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=MOB kinase activator 1B;
DE AltName: Full=Mob1 homolog 1A;
DE Short=Mob1A;
DE AltName: Full=Mob1B;
DE AltName: Full=Mps one binder kinase activator-like 1A;
GN Name=MOB1B; Synonyms=MOB4A, MOBKL1A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Florindo C.S., Tavares A.A.;
RT "Characterization of the human Mob-1 like proteins.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, INTERACTION WITH STK38L, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15067004; DOI=10.1074/jbc.m401999200;
RA Devroe E., Erdjument-Bromage H., Tempst P., Silver P.A.;
RT "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases.";
RL J. Biol. Chem. 279:24444-24451(2004).
RN [6]
RP PHOSPHORYLATION AT THR-12 AND THR-35.
RX PubMed=18328708; DOI=10.1016/j.cub.2008.02.006;
RA Praskova M., Xia F., Avruch J.;
RT "MOBKL1A/MOBKL1B phosphorylation by MST1 and MST2 inhibits cell
RT proliferation.";
RL Curr. Biol. 18:311-321(2008).
RN [7]
RP FUNCTION, INTERACTION WITH LATS1 AND LATS2, AND TISSUE SPECIFICITY.
RX PubMed=19739119; DOI=10.1002/ijc.24878;
RA Chow A., Hao Y., Yang X.;
RT "Molecular characterization of human homologs of yeast MOB1.";
RL Int. J. Cancer 126:2079-2089(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. {ECO:0000269|PubMed:15067004,
CC ECO:0000269|PubMed:19739119}.
CC -!- SUBUNIT: Binds STK38L. Interacts with LATS1 and LATS2.
CC {ECO:0000269|PubMed:15067004, ECO:0000269|PubMed:19739119}.
CC -!- INTERACTION:
CC Q7L9L4; O95835: LATS1; NbExp=7; IntAct=EBI-2558745, EBI-444209;
CC Q7L9L4; Q9NRM7: LATS2; NbExp=5; IntAct=EBI-2558745, EBI-3506895;
CC Q7L9L4; P49902: NT5C2; NbExp=3; IntAct=EBI-2558745, EBI-742084;
CC Q7L9L4; Q13188: STK3; NbExp=9; IntAct=EBI-2558745, EBI-992580;
CC Q7L9L4; Q13043: STK4; NbExp=4; IntAct=EBI-2558745, EBI-367376;
CC Q7L9L4; Q15025: TNIP1; NbExp=3; IntAct=EBI-2558745, EBI-357849;
CC Q7L9L4; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-2558745, EBI-712969;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15067004}. Nucleus
CC {ECO:0000269|PubMed:15067004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L9L4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L9L4-2; Sequence=VSP_045097;
CC -!- TISSUE SPECIFICITY: Adrenal gland, bone marrow, brain, lung, placenta,
CC prostate, salivary gland, skeletal muscle, testis, thymus, thyroid
CC gland, uterus, colon with mucosa, fetal brain and fetal liver.
CC {ECO:0000269|PubMed:19739119}.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1 and this phosphorylation
CC enhances its binding to LATS1. {ECO:0000269|PubMed:18328708}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; AJ577473; CAE12091.1; -; mRNA.
DR EMBL; AK299481; BAG61445.1; -; mRNA.
DR EMBL; AK313513; BAG36293.1; -; mRNA.
DR EMBL; AC021989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05636.1; -; Genomic_DNA.
DR EMBL; BC038112; AAH38112.1; -; mRNA.
DR CCDS; CCDS34002.1; -. [Q7L9L4-1]
DR CCDS; CCDS58903.1; -. [Q7L9L4-2]
DR RefSeq; NP_001231695.1; NM_001244766.1. [Q7L9L4-2]
DR RefSeq; NP_775739.1; NM_173468.3. [Q7L9L4-1]
DR RefSeq; XP_005265766.1; XM_005265709.2. [Q7L9L4-2]
DR AlphaFoldDB; Q7L9L4; -.
DR SMR; Q7L9L4; -.
DR BioGRID; 124960; 50.
DR IntAct; Q7L9L4; 41.
DR MINT; Q7L9L4; -.
DR STRING; 9606.ENSP00000379366; -.
DR ChEMBL; CHEMBL4295878; -.
DR GlyGen; Q7L9L4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L9L4; -.
DR PhosphoSitePlus; Q7L9L4; -.
DR BioMuta; MOB1B; -.
DR DMDM; 56749324; -.
DR EPD; Q7L9L4; -.
DR jPOST; Q7L9L4; -.
DR MassIVE; Q7L9L4; -.
DR MaxQB; Q7L9L4; -.
DR PaxDb; Q7L9L4; -.
DR PeptideAtlas; Q7L9L4; -.
DR PRIDE; Q7L9L4; -.
DR ProteomicsDB; 4978; -.
DR ProteomicsDB; 68845; -. [Q7L9L4-1]
DR Antibodypedia; 24395; 399 antibodies from 28 providers.
DR DNASU; 92597; -.
DR Ensembl; ENST00000309395.7; ENSP00000310189.3; ENSG00000173542.9. [Q7L9L4-1]
DR Ensembl; ENST00000396051.2; ENSP00000379366.2; ENSG00000173542.9. [Q7L9L4-2]
DR GeneID; 92597; -.
DR KEGG; hsa:92597; -.
DR MANE-Select; ENST00000309395.7; ENSP00000310189.3; NM_173468.4; NP_775739.1.
DR UCSC; uc003hfw.4; human. [Q7L9L4-1]
DR CTD; 92597; -.
DR DisGeNET; 92597; -.
DR GeneCards; MOB1B; -.
DR HGNC; HGNC:29801; MOB1B.
DR HPA; ENSG00000173542; Low tissue specificity.
DR MIM; 609282; gene.
DR neXtProt; NX_Q7L9L4; -.
DR OpenTargets; ENSG00000173542; -.
DR PharmGKB; PA134871841; -.
DR VEuPathDB; HostDB:ENSG00000173542; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244898; -.
DR HOGENOM; CLU_038321_3_2_1; -.
DR InParanoid; Q7L9L4; -.
DR OMA; HYPVIVH; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q7L9L4; -.
DR TreeFam; TF300789; -.
DR PathwayCommons; Q7L9L4; -.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR SignaLink; Q7L9L4; -.
DR SIGNOR; Q7L9L4; -.
DR BioGRID-ORCS; 92597; 13 hits in 1080 CRISPR screens.
DR ChiTaRS; MOB1B; human.
DR GeneWiki; MOBKL1A; -.
DR GenomeRNAi; 92597; -.
DR Pharos; Q7L9L4; Tbio.
DR PRO; PR:Q7L9L4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q7L9L4; protein.
DR Bgee; ENSG00000173542; Expressed in renal medulla and 192 other tissues.
DR ExpressionAtlas; Q7L9L4; baseline and differential.
DR Genevisible; Q7L9L4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019209; F:kinase activator activity; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI: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; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0031952; P:regulation of protein autophosphorylation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..216
FT /note="MOB kinase activator 1B"
FT /id="PRO_0000193564"
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:0007744|PubMed:22814378"
FT MOD_RES 12
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:18328708"
FT MOD_RES 35
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:18328708"
FT VAR_SEQ 1..5
FT /note="MSFLF -> MEGATDVNES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045097"
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
