Full text data of MOB1B
MOB1B
(MOB4A, MOBKL1A)
[Confidence: low (only semi-automatic identification from reviews)]
MOB kinase activator 1B (Mob1 homolog 1A; Mob1A; Mob1B; Mps one binder kinase activator-like 1A)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
MOB kinase activator 1B (Mob1 homolog 1A; Mob1A; Mob1B; Mps one binder kinase activator-like 1A)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q7L9L4
ID MOB1B_HUMAN Reviewed; 216 AA.
AC Q7L9L4; B2R8U6; B4DRY3; Q8IY23;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 94.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH STK38L, MASS SPECTROMETRY, AND SUBCELLULAR
RP 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
RT 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
CC which plays a pivotal role in organ size control and tumor
CC suppression by restricting proliferation and promoting apoptosis.
CC The core of this pathway is composed of a kinase cascade wherein
CC STK3/MST2 and STK4/MST1, in complex with its regulatory protein
CC SAV1, phosphorylates and activates LATS1/2 in complex with its
CC regulatory protein MOB1, which in turn phosphorylates and
CC inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of
CC YAP1 by LATS1/2 inhibits its translocation into the nucleus to
CC regulate cellular genes important for cell proliferation, cell
CC death, and cell migration. Stimulates the kinase activity of
CC STK38L.
CC -!- SUBUNIT: Binds STK38L. Interacts with LATS1 and LATS2.
CC -!- INTERACTION:
CC O95835:LATS1; NbExp=5; IntAct=EBI-2558745, EBI-444209;
CC Q9NRM7:LATS2; NbExp=3; IntAct=EBI-2558745, EBI-3506895;
CC Q13043:STK4; NbExp=4; IntAct=EBI-2558745, EBI-367376;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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,
CC placenta, prostate, salivary gland, skeletal muscle, testis,
CC thymus, thyroid gland, uterus, colon with mucosa, fetal brain and
CC fetal liver.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1 and this
CC phosphorylation enhances its binding to LATS1.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001231695.1; NM_001244766.1.
DR RefSeq; NP_775739.1; NM_173468.3.
DR RefSeq; XP_005265766.1; XM_005265709.1.
DR UniGene; Hs.691454; -.
DR UniGene; Hs.744715; -.
DR ProteinModelPortal; Q7L9L4; -.
DR SMR; Q7L9L4; 33-216.
DR IntAct; Q7L9L4; 30.
DR MINT; MINT-5003307; -.
DR STRING; 9606.ENSP00000310189; -.
DR PhosphoSite; Q7L9L4; -.
DR DMDM; 56749324; -.
DR PaxDb; Q7L9L4; -.
DR PRIDE; Q7L9L4; -.
DR Ensembl; ENST00000309395; ENSP00000310189; ENSG00000173542.
DR Ensembl; ENST00000396051; ENSP00000379366; ENSG00000173542.
DR GeneID; 92597; -.
DR KEGG; hsa:92597; -.
DR UCSC; uc011cba.2; human.
DR CTD; 92597; -.
DR GeneCards; GC04P071769; -.
DR HGNC; HGNC:29801; MOB1B.
DR MIM; 609282; gene.
DR neXtProt; NX_Q7L9L4; -.
DR PharmGKB; PA134871841; -.
DR eggNOG; NOG287143; -.
DR HOGENOM; HOG000164685; -.
DR HOVERGEN; HBG052489; -.
DR InParanoid; Q7L9L4; -.
DR KO; K06685; -.
DR OMA; YHQHFSE; -.
DR PhylomeDB; Q7L9L4; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GeneWiki; MOBKL1A; -.
DR GenomeRNAi; 92597; -.
DR NextBio; 77815; -.
DR PRO; PR:Q7L9L4; -.
DR ArrayExpress; Q7L9L4; -.
DR Bgee; Q7L9L4; -.
DR CleanEx; HS_MOBKL1A; -.
DR Genevestigator; Q7L9L4; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019209; F:kinase activator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035329; P:hippo signaling cascade; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR Gene3D; 1.20.140.30; -; 1.
DR InterPro; IPR005301; Mob1_phocein.
DR PANTHER; PTHR22599; PTHR22599; 1.
DR Pfam; PF03637; Mob1_phocein; 1.
DR SUPFAM; SSF101152; SSF101152; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 216 MOB kinase activator 1B.
FT /FTId=PRO_0000193564.
FT METAL 79 79 Zinc (By similarity).
FT METAL 84 84 Zinc (By similarity).
FT METAL 161 161 Zinc (By similarity).
FT METAL 166 166 Zinc (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 12 12 Phosphothreonine; by STK4/MST1.
FT MOD_RES 35 35 Phosphothreonine; by STK4/MST1.
FT MOD_RES 74 74 Phosphothreonine (By similarity).
FT MOD_RES 181 181 Phosphothreonine (By similarity).
FT VAR_SEQ 1 5 MSFLF -> MEGATDVNES (in isoform 2).
FT /FTId=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
//
ID MOB1B_HUMAN Reviewed; 216 AA.
AC Q7L9L4; B2R8U6; B4DRY3; Q8IY23;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 94.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH STK38L, MASS SPECTROMETRY, AND SUBCELLULAR
RP 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
RT 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
CC which plays a pivotal role in organ size control and tumor
CC suppression by restricting proliferation and promoting apoptosis.
CC The core of this pathway is composed of a kinase cascade wherein
CC STK3/MST2 and STK4/MST1, in complex with its regulatory protein
CC SAV1, phosphorylates and activates LATS1/2 in complex with its
CC regulatory protein MOB1, which in turn phosphorylates and
CC inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of
CC YAP1 by LATS1/2 inhibits its translocation into the nucleus to
CC regulate cellular genes important for cell proliferation, cell
CC death, and cell migration. Stimulates the kinase activity of
CC STK38L.
CC -!- SUBUNIT: Binds STK38L. Interacts with LATS1 and LATS2.
CC -!- INTERACTION:
CC O95835:LATS1; NbExp=5; IntAct=EBI-2558745, EBI-444209;
CC Q9NRM7:LATS2; NbExp=3; IntAct=EBI-2558745, EBI-3506895;
CC Q13043:STK4; NbExp=4; IntAct=EBI-2558745, EBI-367376;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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,
CC placenta, prostate, salivary gland, skeletal muscle, testis,
CC thymus, thyroid gland, uterus, colon with mucosa, fetal brain and
CC fetal liver.
CC -!- PTM: Phosphorylated by STK3/MST2 and STK4/MST1 and this
CC phosphorylation enhances its binding to LATS1.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001231695.1; NM_001244766.1.
DR RefSeq; NP_775739.1; NM_173468.3.
DR RefSeq; XP_005265766.1; XM_005265709.1.
DR UniGene; Hs.691454; -.
DR UniGene; Hs.744715; -.
DR ProteinModelPortal; Q7L9L4; -.
DR SMR; Q7L9L4; 33-216.
DR IntAct; Q7L9L4; 30.
DR MINT; MINT-5003307; -.
DR STRING; 9606.ENSP00000310189; -.
DR PhosphoSite; Q7L9L4; -.
DR DMDM; 56749324; -.
DR PaxDb; Q7L9L4; -.
DR PRIDE; Q7L9L4; -.
DR Ensembl; ENST00000309395; ENSP00000310189; ENSG00000173542.
DR Ensembl; ENST00000396051; ENSP00000379366; ENSG00000173542.
DR GeneID; 92597; -.
DR KEGG; hsa:92597; -.
DR UCSC; uc011cba.2; human.
DR CTD; 92597; -.
DR GeneCards; GC04P071769; -.
DR HGNC; HGNC:29801; MOB1B.
DR MIM; 609282; gene.
DR neXtProt; NX_Q7L9L4; -.
DR PharmGKB; PA134871841; -.
DR eggNOG; NOG287143; -.
DR HOGENOM; HOG000164685; -.
DR HOVERGEN; HBG052489; -.
DR InParanoid; Q7L9L4; -.
DR KO; K06685; -.
DR OMA; YHQHFSE; -.
DR PhylomeDB; Q7L9L4; -.
DR Reactome; REACT_111102; Signal Transduction.
DR GeneWiki; MOBKL1A; -.
DR GenomeRNAi; 92597; -.
DR NextBio; 77815; -.
DR PRO; PR:Q7L9L4; -.
DR ArrayExpress; Q7L9L4; -.
DR Bgee; Q7L9L4; -.
DR CleanEx; HS_MOBKL1A; -.
DR Genevestigator; Q7L9L4; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019209; F:kinase activator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035329; P:hippo signaling cascade; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR Gene3D; 1.20.140.30; -; 1.
DR InterPro; IPR005301; Mob1_phocein.
DR PANTHER; PTHR22599; PTHR22599; 1.
DR Pfam; PF03637; Mob1_phocein; 1.
DR SUPFAM; SSF101152; SSF101152; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 216 MOB kinase activator 1B.
FT /FTId=PRO_0000193564.
FT METAL 79 79 Zinc (By similarity).
FT METAL 84 84 Zinc (By similarity).
FT METAL 161 161 Zinc (By similarity).
FT METAL 166 166 Zinc (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 12 12 Phosphothreonine; by STK4/MST1.
FT MOD_RES 35 35 Phosphothreonine; by STK4/MST1.
FT MOD_RES 74 74 Phosphothreonine (By similarity).
FT MOD_RES 181 181 Phosphothreonine (By similarity).
FT VAR_SEQ 1 5 MSFLF -> MEGATDVNES (in isoform 2).
FT /FTId=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
//
MIM
609282
*RECORD*
*FIELD* NO
609282
*FIELD* TI
*609282 MOB1-LIKE PROTEIN 1A; MOBKL1A
;;MATS, DROSOPHILA, HOMOLOG OF, 2; MATS2
*FIELD* TX
read more
CLONING
Lai et al. (2005) identified a Drosophila protein belonging to the Mob1
superfamily that they termed Mats (Mob as tumor suppressor). By database
analysis, they identified 2 human orthologs, MOBKL1B (609281) and
MOBKL1A, which they named MATS1 and MATS2, respectively. The MATS2
protein contains 216 amino acids and shares 88% identity with Drosophila
Mats.
GENE FUNCTION
Lai et al. (2005) described the growth inhibitory functions of
Drosophila Mats. Loss of Mats function resulted in increased cell
proliferation, defective apoptosis, and induction of tissue overgrowth.
Mats physically associated with Lats/Wts kinase (LATS1; 603473) and
stimulated its catalytic activity.
*FIELD* RF
1. Lai, Z.-C.; Wei, X.; Shimizu, T.; Ramos, E.; Rohrbaugh, M.; Nikolaidis,
N.; Ho, L.-L.; Li, Y.: Control of cell proliferation and apoptosis
by Mob as tumor suppressor, Mats. Cell 120: 675-685, 2005.
*FIELD* CD
Stylianos E. Antonarakis: 3/29/2005
*FIELD* ED
mgross: 03/29/2005
*RECORD*
*FIELD* NO
609282
*FIELD* TI
*609282 MOB1-LIKE PROTEIN 1A; MOBKL1A
;;MATS, DROSOPHILA, HOMOLOG OF, 2; MATS2
*FIELD* TX
read more
CLONING
Lai et al. (2005) identified a Drosophila protein belonging to the Mob1
superfamily that they termed Mats (Mob as tumor suppressor). By database
analysis, they identified 2 human orthologs, MOBKL1B (609281) and
MOBKL1A, which they named MATS1 and MATS2, respectively. The MATS2
protein contains 216 amino acids and shares 88% identity with Drosophila
Mats.
GENE FUNCTION
Lai et al. (2005) described the growth inhibitory functions of
Drosophila Mats. Loss of Mats function resulted in increased cell
proliferation, defective apoptosis, and induction of tissue overgrowth.
Mats physically associated with Lats/Wts kinase (LATS1; 603473) and
stimulated its catalytic activity.
*FIELD* RF
1. Lai, Z.-C.; Wei, X.; Shimizu, T.; Ramos, E.; Rohrbaugh, M.; Nikolaidis,
N.; Ho, L.-L.; Li, Y.: Control of cell proliferation and apoptosis
by Mob as tumor suppressor, Mats. Cell 120: 675-685, 2005.
*FIELD* CD
Stylianos E. Antonarakis: 3/29/2005
*FIELD* ED
mgross: 03/29/2005