Full text data of MOB1A
MOB1A
(C2orf6, MOB4B, MOBK1B, MOBKL1B)
[Confidence: low (only semi-automatic identification from reviews)]
MOB kinase activator 1A (Mob1 alpha; Mob1A; Mob1 homolog 1B; Mps one binder kinase activator-like 1B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
MOB kinase activator 1A (Mob1 alpha; Mob1A; Mob1 homolog 1B; Mps one binder kinase activator-like 1B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H8S9
ID MOB1A_HUMAN Reviewed; 216 AA.
AC Q9H8S9; Q53S34; Q9H3T5; Q9HAI0; Q9NVE2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=MOB kinase activator 1A;
DE AltName: Full=Mob1 alpha;
DE Short=Mob1A;
DE AltName: Full=Mob1 homolog 1B;
DE AltName: Full=Mps one binder kinase activator-like 1B;
GN Name=MOB1A; Synonyms=C2orf6, MOB4B, MOBK1B, MOBKL1B;
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 Kagaya S., Kotani S., Todokoro K.;
RT "Human MOB1.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH STK38 AND STK38L.
RX PubMed=15197186; DOI=10.1074/jbc.M404542200;
RA Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.;
RT "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase
RT by the hMOB1 protein.";
RL J. Biol. Chem. 279:35228-35235(2004).
RN [8]
RP PHOSPHORYLATION BY STK3/MST2 AND STK4/MST1.
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 [9]
RP FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, AND INTERACTION WITH
RP STK38 AND STK3/MST2.
RX PubMed=18362890; DOI=10.1038/onc.2008.66;
RA Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M.,
RA Kawata A., Ohno K., Hata Y.;
RT "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2
RT to form the scaffold to activate nuclear Dbf2-related kinase 1.";
RL Oncogene 27:4281-4292(2008).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-216, PARTIAL PROTEIN
RP SEQUENCE, MASS SPECTROMETRY, AND ZINC-BINDING.
RX PubMed=12962634; DOI=10.1016/S0969-2126(03)00182-5;
RA Stavridi E.S., Harris K.G., Huyen Y., Bothos J., Verwoerd P.-M.,
RA Stayrook S.E., Pavletich N.P., Jeffrey P.D., Luca F.C.;
RT "Crystal structure of a human Mob1 protein: toward understanding Mob-
RT regulated cell cycle pathways.";
RL Structure 11:1163-1170(2003).
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 STK38
CC and STK38L. Acts cooperatively with STK3/MST2 to activate STK38.
CC -!- SUBUNIT: Binds STK38 and STK38L. Interacts with LATS1 and LATS2.
CC Forms a tripartite complex with STK38 and STK3/MST2.
CC -!- INTERACTION:
CC O95835:LATS1; NbExp=9; IntAct=EBI-748229, EBI-444209;
CC Q9NRM7:LATS2; NbExp=4; IntAct=EBI-748229, EBI-3506895;
CC Q15208:STK38; NbExp=2; IntAct=EBI-748229, EBI-458376;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H8S9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8S9-2; Sequence=VSP_012295, VSP_012296;
CC Note=May be due to an intron retention;
CC -!- TISSUE SPECIFICITY: Adrenal gland, bone marrow, brain, placenta,
CC prostate, salivary gland, skeletal muscle, testis, thymus, thyroid
CC gland, heart, spinal cord, fetal brain and 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.
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DR EMBL; AB016839; BAB19058.1; -; mRNA.
DR EMBL; AJ577474; CAE12093.1; -; mRNA.
DR EMBL; AK001650; BAA91810.1; -; mRNA.
DR EMBL; AK021657; BAB13868.1; -; mRNA.
DR EMBL; AK023321; BAB14525.1; -; mRNA.
DR EMBL; AC073263; AAX93060.1; -; Genomic_DNA.
DR EMBL; BC003398; AAH03398.1; -; mRNA.
DR RefSeq; NP_060691.2; NM_018221.3.
DR UniGene; Hs.602092; -.
DR PDB; 1PI1; X-ray; 2.00 A; A=33-216.
DR PDB; 4JIZ; X-ray; 2.10 A; A=40-211.
DR PDBsum; 1PI1; -.
DR PDBsum; 4JIZ; -.
DR ProteinModelPortal; Q9H8S9; -.
DR SMR; Q9H8S9; 33-216.
DR IntAct; Q9H8S9; 37.
DR MINT; MINT-197366; -.
DR STRING; 9606.ENSP00000379364; -.
DR PhosphoSite; Q9H8S9; -.
DR DMDM; 56749356; -.
DR OGP; Q9H8S9; -.
DR PaxDb; Q9H8S9; -.
DR PRIDE; Q9H8S9; -.
DR DNASU; 55233; -.
DR Ensembl; ENST00000396049; ENSP00000379364; ENSG00000114978.
DR GeneID; 55233; -.
DR KEGG; hsa:55233; -.
DR UCSC; uc002skh.4; human.
DR CTD; 55233; -.
DR GeneCards; GC02M074382; -.
DR HGNC; HGNC:16015; MOB1A.
DR MIM; 609281; gene.
DR neXtProt; NX_Q9H8S9; -.
DR PharmGKB; PA25894; -.
DR eggNOG; NOG287143; -.
DR HOGENOM; HOG000164685; -.
DR HOVERGEN; HBG052489; -.
DR InParanoid; Q9H8S9; -.
DR KO; K06685; -.
DR OMA; EFCTETS; -.
DR OrthoDB; EOG7N0C5K; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; Q9H8S9; -.
DR GeneWiki; MOBKL1B; -.
DR GenomeRNAi; 55233; -.
DR NextBio; 59245; -.
DR PRO; PR:Q9H8S9; -.
DR ArrayExpress; Q9H8S9; -.
DR Bgee; Q9H8S9; -.
DR CleanEx; HS_MOBKL1B; -.
DR Genevestigator; Q9H8S9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035329; P:hippo signaling cascade; 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 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 216 MOB kinase activator 1A.
FT /FTId=PRO_0000193566.
FT METAL 79 79 Zinc.
FT METAL 84 84 Zinc.
FT METAL 161 161 Zinc.
FT METAL 166 166 Zinc.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 12 12 Phosphothreonine (By similarity).
FT MOD_RES 35 35 Phosphothreonine.
FT MOD_RES 74 74 Phosphothreonine; by STK3/MST2.
FT MOD_RES 181 181 Phosphothreonine.
FT VAR_SEQ 138 148 VPFPKNFMSVA -> ELTLSKYSFFF (in isoform
FT 2).
FT /FTId=VSP_012295.
FT VAR_SEQ 149 216 Missing (in isoform 2).
FT /FTId=VSP_012296.
FT CONFLICT 5 5 F -> L (in Ref. 3; BAB14525).
FT CONFLICT 176 176 E -> G (in Ref. 3; BAA91810).
FT HELIX 41 44
FT HELIX 53 74
FT HELIX 75 78
FT TURN 81 83
FT STRAND 85 90
FT STRAND 93 95
FT STRAND 100 102
FT HELIX 111 126
FT TURN 129 131
FT STRAND 135 137
FT HELIX 144 172
FT HELIX 176 193
FT HELIX 198 204
FT HELIX 205 210
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
//
ID MOB1A_HUMAN Reviewed; 216 AA.
AC Q9H8S9; Q53S34; Q9H3T5; Q9HAI0; Q9NVE2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=MOB kinase activator 1A;
DE AltName: Full=Mob1 alpha;
DE Short=Mob1A;
DE AltName: Full=Mob1 homolog 1B;
DE AltName: Full=Mps one binder kinase activator-like 1B;
GN Name=MOB1A; Synonyms=C2orf6, MOB4B, MOBK1B, MOBKL1B;
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 Kagaya S., Kotani S., Todokoro K.;
RT "Human MOB1.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH STK38 AND STK38L.
RX PubMed=15197186; DOI=10.1074/jbc.M404542200;
RA Bichsel S.J., Tamaskovic R., Stegert M.R., Hemmings B.A.;
RT "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase
RT by the hMOB1 protein.";
RL J. Biol. Chem. 279:35228-35235(2004).
RN [8]
RP PHOSPHORYLATION BY STK3/MST2 AND STK4/MST1.
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 [9]
RP FUNCTION, PHOSPHORYLATION AT THR-74 AND THR-181, AND INTERACTION WITH
RP STK38 AND STK3/MST2.
RX PubMed=18362890; DOI=10.1038/onc.2008.66;
RA Hirabayashi S., Nakagawa K., Sumita K., Hidaka S., Kawai T., Ikeda M.,
RA Kawata A., Ohno K., Hata Y.;
RT "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2
RT to form the scaffold to activate nuclear Dbf2-related kinase 1.";
RL Oncogene 27:4281-4292(2008).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-216, PARTIAL PROTEIN
RP SEQUENCE, MASS SPECTROMETRY, AND ZINC-BINDING.
RX PubMed=12962634; DOI=10.1016/S0969-2126(03)00182-5;
RA Stavridi E.S., Harris K.G., Huyen Y., Bothos J., Verwoerd P.-M.,
RA Stayrook S.E., Pavletich N.P., Jeffrey P.D., Luca F.C.;
RT "Crystal structure of a human Mob1 protein: toward understanding Mob-
RT regulated cell cycle pathways.";
RL Structure 11:1163-1170(2003).
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 STK38
CC and STK38L. Acts cooperatively with STK3/MST2 to activate STK38.
CC -!- SUBUNIT: Binds STK38 and STK38L. Interacts with LATS1 and LATS2.
CC Forms a tripartite complex with STK38 and STK3/MST2.
CC -!- INTERACTION:
CC O95835:LATS1; NbExp=9; IntAct=EBI-748229, EBI-444209;
CC Q9NRM7:LATS2; NbExp=4; IntAct=EBI-748229, EBI-3506895;
CC Q15208:STK38; NbExp=2; IntAct=EBI-748229, EBI-458376;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H8S9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8S9-2; Sequence=VSP_012295, VSP_012296;
CC Note=May be due to an intron retention;
CC -!- TISSUE SPECIFICITY: Adrenal gland, bone marrow, brain, placenta,
CC prostate, salivary gland, skeletal muscle, testis, thymus, thyroid
CC gland, heart, spinal cord, fetal brain and 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.
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DR EMBL; AB016839; BAB19058.1; -; mRNA.
DR EMBL; AJ577474; CAE12093.1; -; mRNA.
DR EMBL; AK001650; BAA91810.1; -; mRNA.
DR EMBL; AK021657; BAB13868.1; -; mRNA.
DR EMBL; AK023321; BAB14525.1; -; mRNA.
DR EMBL; AC073263; AAX93060.1; -; Genomic_DNA.
DR EMBL; BC003398; AAH03398.1; -; mRNA.
DR RefSeq; NP_060691.2; NM_018221.3.
DR UniGene; Hs.602092; -.
DR PDB; 1PI1; X-ray; 2.00 A; A=33-216.
DR PDB; 4JIZ; X-ray; 2.10 A; A=40-211.
DR PDBsum; 1PI1; -.
DR PDBsum; 4JIZ; -.
DR ProteinModelPortal; Q9H8S9; -.
DR SMR; Q9H8S9; 33-216.
DR IntAct; Q9H8S9; 37.
DR MINT; MINT-197366; -.
DR STRING; 9606.ENSP00000379364; -.
DR PhosphoSite; Q9H8S9; -.
DR DMDM; 56749356; -.
DR OGP; Q9H8S9; -.
DR PaxDb; Q9H8S9; -.
DR PRIDE; Q9H8S9; -.
DR DNASU; 55233; -.
DR Ensembl; ENST00000396049; ENSP00000379364; ENSG00000114978.
DR GeneID; 55233; -.
DR KEGG; hsa:55233; -.
DR UCSC; uc002skh.4; human.
DR CTD; 55233; -.
DR GeneCards; GC02M074382; -.
DR HGNC; HGNC:16015; MOB1A.
DR MIM; 609281; gene.
DR neXtProt; NX_Q9H8S9; -.
DR PharmGKB; PA25894; -.
DR eggNOG; NOG287143; -.
DR HOGENOM; HOG000164685; -.
DR HOVERGEN; HBG052489; -.
DR InParanoid; Q9H8S9; -.
DR KO; K06685; -.
DR OMA; EFCTETS; -.
DR OrthoDB; EOG7N0C5K; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; Q9H8S9; -.
DR GeneWiki; MOBKL1B; -.
DR GenomeRNAi; 55233; -.
DR NextBio; 59245; -.
DR PRO; PR:Q9H8S9; -.
DR ArrayExpress; Q9H8S9; -.
DR Bgee; Q9H8S9; -.
DR CleanEx; HS_MOBKL1B; -.
DR Genevestigator; Q9H8S9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035329; P:hippo signaling cascade; 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 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 216 MOB kinase activator 1A.
FT /FTId=PRO_0000193566.
FT METAL 79 79 Zinc.
FT METAL 84 84 Zinc.
FT METAL 161 161 Zinc.
FT METAL 166 166 Zinc.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 12 12 Phosphothreonine (By similarity).
FT MOD_RES 35 35 Phosphothreonine.
FT MOD_RES 74 74 Phosphothreonine; by STK3/MST2.
FT MOD_RES 181 181 Phosphothreonine.
FT VAR_SEQ 138 148 VPFPKNFMSVA -> ELTLSKYSFFF (in isoform
FT 2).
FT /FTId=VSP_012295.
FT VAR_SEQ 149 216 Missing (in isoform 2).
FT /FTId=VSP_012296.
FT CONFLICT 5 5 F -> L (in Ref. 3; BAB14525).
FT CONFLICT 176 176 E -> G (in Ref. 3; BAA91810).
FT HELIX 41 44
FT HELIX 53 74
FT HELIX 75 78
FT TURN 81 83
FT STRAND 85 90
FT STRAND 93 95
FT STRAND 100 102
FT HELIX 111 126
FT TURN 129 131
FT STRAND 135 137
FT HELIX 144 172
FT HELIX 176 193
FT HELIX 198 204
FT HELIX 205 210
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
//
MIM
609281
*RECORD*
*FIELD* NO
609281
*FIELD* TI
*609281 MOB1-LIKE PROTEIN 1B; MOBKL1B
;;MATS, DROSOPHILA, HOMOLOG OF, 1; MATS1
*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 and MOBKL1A
(609282), which they named MATS1 and MATS2, respectively. The MATS1
protein contains 216 amino acids and shares 87% 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, and this function was conserved in
human MATS1. Furthermore, human MATS1 could rescue the lethality
associated with loss of Mats function in Drosophila.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MOBKL1B
gene to chromosome 2 (TMAP RH69565).
MOLECULAR GENETICS
Lai et al. (2005) examined 89 human and 8 mouse tumor-derived MATS1 ESTs
and identified 2 with disruptions in the coding region. These were
subsequently verified by resequencing analysis. In the first case, 3
nucleotides were deleted in a MATS1 cDNA derived from a human skin
melanoma, resulting in deletion of the sixth or seventh codon encoding
serine. No MATS1 protein was detected in human embryonic kidney cells
transfected with MATS1 carrying the mutation. Another Mats1 cDNA derived
from a mouse mammary gland carcinoma had a 38-bp insertion immediately
downstream of the fifth codon, causing premature termination. As
expected, no Mats1 protein product was detected.
*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: 05/11/2005
mgross: 5/11/2005
terry: 5/4/2005
mgross: 3/29/2005
*RECORD*
*FIELD* NO
609281
*FIELD* TI
*609281 MOB1-LIKE PROTEIN 1B; MOBKL1B
;;MATS, DROSOPHILA, HOMOLOG OF, 1; MATS1
*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 and MOBKL1A
(609282), which they named MATS1 and MATS2, respectively. The MATS1
protein contains 216 amino acids and shares 87% 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, and this function was conserved in
human MATS1. Furthermore, human MATS1 could rescue the lethality
associated with loss of Mats function in Drosophila.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MOBKL1B
gene to chromosome 2 (TMAP RH69565).
MOLECULAR GENETICS
Lai et al. (2005) examined 89 human and 8 mouse tumor-derived MATS1 ESTs
and identified 2 with disruptions in the coding region. These were
subsequently verified by resequencing analysis. In the first case, 3
nucleotides were deleted in a MATS1 cDNA derived from a human skin
melanoma, resulting in deletion of the sixth or seventh codon encoding
serine. No MATS1 protein was detected in human embryonic kidney cells
transfected with MATS1 carrying the mutation. Another Mats1 cDNA derived
from a mouse mammary gland carcinoma had a 38-bp insertion immediately
downstream of the fifth codon, causing premature termination. As
expected, no Mats1 protein product was detected.
*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: 05/11/2005
mgross: 5/11/2005
terry: 5/4/2005
mgross: 3/29/2005