MOB2_HUMAN
ID MOB2_HUMAN Reviewed; 237 AA.
AC Q70IA6; B4DKP3; Q96M67;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=MOB kinase activator 2;
DE AltName: Full=HCCA2;
DE AltName: Full=Mob2 homolog;
DE AltName: Full=Mps one binder kinase activator-like 2;
GN Name=MOB2; Synonyms=HCCA2;
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Colon, and Testis;
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].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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 STK3 AND STK38L, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Stimulates the autophosphorylation and kinase activity of
CC STK38 and STK38L. {ECO:0000269|PubMed:15067004}.
CC -!- SUBUNIT: Binds STK38 and STK38L.
CC -!- INTERACTION:
CC Q70IA6; Q9NT62: ATG3; NbExp=3; IntAct=EBI-2558739, EBI-988094;
CC Q70IA6; Q9GZT6: CCDC90B; NbExp=3; IntAct=EBI-2558739, EBI-713148;
CC Q70IA6; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-2558739, EBI-12013806;
CC Q70IA6; Q70Z53: FRA10AC1; NbExp=3; IntAct=EBI-2558739, EBI-710176;
CC Q70IA6; Q5JXC2: MIIP; NbExp=3; IntAct=EBI-2558739, EBI-2801965;
CC Q70IA6; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2558739, EBI-741158;
CC Q70IA6; A6NKK0: OR5H1; NbExp=3; IntAct=EBI-2558739, EBI-23725364;
CC Q70IA6; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-2558739, EBI-10192441;
CC Q70IA6; O95562: SFT2D2; NbExp=3; IntAct=EBI-2558739, EBI-4402330;
CC Q70IA6; Q9Y2H1: STK38L; NbExp=10; IntAct=EBI-2558739, EBI-991501;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15067004}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:15067004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q70IA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70IA6-2; Sequence=VSP_012298, VSP_012299;
CC Name=3;
CC IsoId=Q70IA6-3; Sequence=VSP_044472;
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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DR EMBL; AJ580639; CAE45271.1; -; mRNA.
DR EMBL; AK057350; BAB71443.1; -; mRNA.
DR EMBL; AK296658; BAG59255.1; -; mRNA.
DR EMBL; AC091196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047291; AAH47291.1; -; mRNA.
DR EMBL; BC067785; AAH67785.1; -; mRNA.
DR CCDS; CCDS53591.1; -. [Q70IA6-3]
DR RefSeq; NP_001165694.1; NM_001172223.2. [Q70IA6-3]
DR RefSeq; NP_443731.2; NM_053005.5. [Q70IA6-1]
DR AlphaFoldDB; Q70IA6; -.
DR SMR; Q70IA6; -.
DR BioGRID; 123506; 54.
DR IntAct; Q70IA6; 30.
DR MINT; Q70IA6; -.
DR STRING; 9606.ENSP00000328694; -.
DR iPTMnet; Q70IA6; -.
DR PhosphoSitePlus; Q70IA6; -.
DR BioMuta; MOB2; -.
DR DMDM; 56749258; -.
DR EPD; Q70IA6; -.
DR jPOST; Q70IA6; -.
DR MassIVE; Q70IA6; -.
DR MaxQB; Q70IA6; -.
DR PaxDb; Q70IA6; -.
DR PeptideAtlas; Q70IA6; -.
DR PRIDE; Q70IA6; -.
DR ProteomicsDB; 68555; -. [Q70IA6-1]
DR ProteomicsDB; 68556; -. [Q70IA6-2]
DR Antibodypedia; 22879; 151 antibodies from 28 providers.
DR DNASU; 81532; -.
DR Ensembl; ENST00000329957.7; ENSP00000328694.6; ENSG00000182208.15. [Q70IA6-3]
DR GeneID; 81532; -.
DR KEGG; hsa:81532; -.
DR MANE-Select; ENST00000329957.7; ENSP00000328694.6; NM_001172223.3; NP_001165694.1. [Q70IA6-3]
DR UCSC; uc010qwz.3; human. [Q70IA6-1]
DR CTD; 81532; -.
DR DisGeNET; 81532; -.
DR GeneCards; MOB2; -.
DR HGNC; HGNC:24904; MOB2.
DR HPA; ENSG00000182208; Low tissue specificity.
DR MIM; 611969; gene.
DR neXtProt; NX_Q70IA6; -.
DR OpenTargets; ENSG00000182208; -.
DR VEuPathDB; HostDB:ENSG00000182208; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244956; -.
DR InParanoid; Q70IA6; -.
DR OMA; YHAHYPQ; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q70IA6; -.
DR TreeFam; TF300789; -.
DR PathwayCommons; Q70IA6; -.
DR SignaLink; Q70IA6; -.
DR BioGRID-ORCS; 81532; 16 hits in 1087 CRISPR screens.
DR ChiTaRS; MOB2; human.
DR GenomeRNAi; 81532; -.
DR Pharos; Q70IA6; Tbio.
DR PRO; PR:Q70IA6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q70IA6; protein.
DR Bgee; ENSG00000182208; Expressed in popliteal artery and 181 other tissues.
DR ExpressionAtlas; Q70IA6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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: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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..237
FT /note="MOB kinase activator 2"
FT /id="PRO_0000193568"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..6
FT /note="MDWLMG -> MLGDHCSLPEDQARPGQSLQSGLCCKMVLQAVSKVLR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044472"
FT VAR_SEQ 133..142
FT /note="GREFPSSFES -> ENSPAPLSPW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012298"
FT VAR_SEQ 143..237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012299"
FT CONFLICT 49
FT /note="E -> K (in Ref. 2; BAB71443)"
FT /evidence="ECO:0000305"
FT CONFLICT Q70IA6-3:19
FT /note="L -> P (in Ref. 2; BAG59255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26927 MW; 878A3E6E49294689 CRC64;
MDWLMGKSKA KPNGKKPAAE ERKAYLEPEH TKARITDFQF KELVVLPREI DLNEWLASNT
TTFFHHINLQ YSTISEFCTG ETCQTMAVCN TQYYWYDERG KKVKCTAPQY VDFVMSSVQK
LVTDEDVFPT KYGREFPSSF ESLVRKICRH LFHVLAHIYW AHFKETLALE LHGHLNTLYV
HFILFAREFN LLDPKETAIM DDLTEVLCSG AGGVHSGGSG DGAGSGGPGA QNHVKER
