MOB1A_HUMAN
ID MOB1A_HUMAN Reviewed; 216 AA.
AC Q9H8S9; Q53S34; Q9H3T5; Q9HAI0; Q9NVE2;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 178.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., 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 [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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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 project:
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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 by
RT the hMOB1 protein.";
RL J. Biol. Chem. 279:35228-35235(2004).
RN [8]
RP PHOSPHORYLATION AT THR-12 AND THR-35 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 STK38
RP 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 to
RT 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, 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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-216, PARTIAL PROTEIN SEQUENCE,
RP IDENTIFICATION BY 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 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. {ECO:0000269|PubMed:15197186,
CC ECO:0000269|PubMed:18362890, ECO:0000269|PubMed:19739119}.
CC -!- SUBUNIT: Binds STK38 and STK38L. Interacts with LATS1 and LATS2. Forms
CC a tripartite complex with STK38 and STK3/MST2.
CC {ECO:0000269|PubMed:15197186, ECO:0000269|PubMed:18362890,
CC ECO:0000269|PubMed:19739119}.
CC -!- INTERACTION:
CC Q9H8S9; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-748229, EBI-7247651;
CC Q9H8S9; Q9NWS6: FAM118A; NbExp=3; IntAct=EBI-748229, EBI-8638992;
CC Q9H8S9; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-748229, EBI-10175124;
CC Q9H8S9; Q9UKD1: GMEB2; NbExp=3; IntAct=EBI-748229, EBI-948296;
CC Q9H8S9; Q9H2S9: IKZF4; NbExp=3; IntAct=EBI-748229, EBI-1640423;
CC Q9H8S9; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-748229, EBI-2556193;
CC Q9H8S9; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-748229, EBI-739657;
CC Q9H8S9; O95835: LATS1; NbExp=9; IntAct=EBI-748229, EBI-444209;
CC Q9H8S9; Q9NRM7: LATS2; NbExp=4; IntAct=EBI-748229, EBI-3506895;
CC Q9H8S9; Q9NQ48: LZTFL1; NbExp=3; IntAct=EBI-748229, EBI-2824799;
CC Q9H8S9; P49585: PCYT1A; NbExp=3; IntAct=EBI-748229, EBI-2563309;
CC Q9H8S9; Q9UH03: SEPTIN3; NbExp=6; IntAct=EBI-748229, EBI-727037;
CC Q9H8S9; Q13188: STK3; NbExp=7; IntAct=EBI-748229, EBI-992580;
CC Q9H8S9; Q15208: STK38; NbExp=3; IntAct=EBI-748229, EBI-458376;
CC Q9H8S9; Q9Y2H1: STK38L; NbExp=5; IntAct=EBI-748229, EBI-991501;
CC Q9H8S9; Q13043: STK4; NbExp=9; IntAct=EBI-748229, EBI-367376;
CC Q9H8S9; P48775: TDO2; NbExp=6; IntAct=EBI-748229, EBI-743494;
CC Q9H8S9; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-748229, EBI-10278423;
CC Q9H8S9; Q13049: TRIM32; NbExp=3; IntAct=EBI-748229, EBI-742790;
CC Q9H8S9; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-748229, EBI-712969;
CC Q9H8S9; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-748229, EBI-6863748;
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 -!- 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 {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:15197186,
CC ECO:0000269|PubMed:18328708, ECO:0000269|PubMed:18362890}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
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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 CCDS; CCDS46340.1; -. [Q9H8S9-1]
DR RefSeq; NP_001304039.1; NM_001317110.1.
DR RefSeq; NP_001304040.1; NM_001317111.1.
DR RefSeq; NP_001304041.1; NM_001317112.1.
DR RefSeq; NP_060691.2; NM_018221.4. [Q9H8S9-1]
DR PDB; 1PI1; X-ray; 2.00 A; A=33-216.
DR PDB; 4J1V; X-ray; 1.95 A; A/C=33-216.
DR PDB; 4JIZ; X-ray; 2.10 A; A=40-211.
DR PDB; 5BRK; X-ray; 2.30 A; A=1-216.
DR PDB; 5BRM; X-ray; 2.65 A; A/B/C/D/E/F=41-216.
DR PDB; 5TWF; X-ray; 3.14 A; A/B=1-216.
DR PDB; 5TWG; X-ray; 2.30 A; A=1-216.
DR PDB; 5TWH; X-ray; 2.50 A; A=1-216.
DR PDB; 5XQZ; X-ray; 2.10 A; A/B=33-216.
DR PDB; 6MCP; X-ray; 2.50 A; B/D=33-216.
DR PDB; 6MCQ; X-ray; 2.57 A; B/D=33-216.
DR PDBsum; 1PI1; -.
DR PDBsum; 4J1V; -.
DR PDBsum; 4JIZ; -.
DR PDBsum; 5BRK; -.
DR PDBsum; 5BRM; -.
DR PDBsum; 5TWF; -.
DR PDBsum; 5TWG; -.
DR PDBsum; 5TWH; -.
DR PDBsum; 5XQZ; -.
DR PDBsum; 6MCP; -.
DR PDBsum; 6MCQ; -.
DR AlphaFoldDB; Q9H8S9; -.
DR SMR; Q9H8S9; -.
DR BioGRID; 120527; 66.
DR DIP; DIP-36594N; -.
DR IntAct; Q9H8S9; 57.
DR MINT; Q9H8S9; -.
DR STRING; 9606.ENSP00000379364; -.
DR iPTMnet; Q9H8S9; -.
DR PhosphoSitePlus; Q9H8S9; -.
DR BioMuta; MOB1A; -.
DR DMDM; 56749356; -.
DR OGP; Q9H8S9; -.
DR EPD; Q9H8S9; -.
DR jPOST; Q9H8S9; -.
DR MassIVE; Q9H8S9; -.
DR MaxQB; Q9H8S9; -.
DR PaxDb; Q9H8S9; -.
DR PeptideAtlas; Q9H8S9; -.
DR PRIDE; Q9H8S9; -.
DR ProteomicsDB; 81237; -. [Q9H8S9-1]
DR ProteomicsDB; 81238; -. [Q9H8S9-2]
DR Antibodypedia; 47474; 189 antibodies from 30 providers.
DR DNASU; 55233; -.
DR Ensembl; ENST00000396049.5; ENSP00000379364.3; ENSG00000114978.18. [Q9H8S9-1]
DR GeneID; 55233; -.
DR KEGG; hsa:55233; -.
DR MANE-Select; ENST00000396049.5; ENSP00000379364.3; NM_018221.5; NP_060691.2.
DR UCSC; uc002skh.5; human. [Q9H8S9-1]
DR CTD; 55233; -.
DR DisGeNET; 55233; -.
DR GeneCards; MOB1A; -.
DR HGNC; HGNC:16015; MOB1A.
DR HPA; ENSG00000114978; Low tissue specificity.
DR MIM; 609281; gene.
DR neXtProt; NX_Q9H8S9; -.
DR OpenTargets; ENSG00000114978; -.
DR PharmGKB; PA25894; -.
DR VEuPathDB; HostDB:ENSG00000114978; -.
DR eggNOG; KOG0440; Eukaryota.
DR GeneTree; ENSGT01050000244898; -.
DR HOGENOM; CLU_038321_3_1_1; -.
DR InParanoid; Q9H8S9; -.
DR OMA; TCEVMSA; -.
DR OrthoDB; 1127941at2759; -.
DR PhylomeDB; Q9H8S9; -.
DR TreeFam; TF300789; -.
DR PathwayCommons; Q9H8S9; -.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR SignaLink; Q9H8S9; -.
DR SIGNOR; Q9H8S9; -.
DR BioGRID-ORCS; 55233; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; MOB1A; human.
DR EvolutionaryTrace; Q9H8S9; -.
DR GeneWiki; MOBKL1B; -.
DR GenomeRNAi; 55233; -.
DR Pharos; Q9H8S9; Tbio.
DR PRO; PR:Q9H8S9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H8S9; protein.
DR Bgee; ENSG00000114978; Expressed in monocyte and 212 other tissues.
DR Genevisible; Q9H8S9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 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; IDA:UniProtKB.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..216
FT /note="MOB kinase activator 1A"
FT /id="PRO_0000193566"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12962634"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12962634"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12962634"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12962634"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18328708"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18328708"
FT MOD_RES 74
FT /note="Phosphothreonine; by STK3/MST2"
FT /evidence="ECO:0000269|PubMed:18362890"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18362890"
FT VAR_SEQ 138..148
FT /note="VPFPKNFMSVA -> ELTLSKYSFFF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012295"
FT VAR_SEQ 149..216
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012296"
FT CONFLICT 5
FT /note="F -> L (in Ref. 3; BAB14525)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> G (in Ref. 3; BAA91810)"
FT /evidence="ECO:0000305"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5BRK"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:5TWG"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5TWG"
FT TURN 42..45
FT /evidence="ECO:0007829|PDB:4J1V"
FT HELIX 53..75
FT /evidence="ECO:0007829|PDB:4J1V"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4J1V"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4J1V"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4J1V"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4JIZ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1PI1"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:4J1V"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4J1V"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4JIZ"
FT HELIX 144..165
FT /evidence="ECO:0007829|PDB:4J1V"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:4J1V"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5TWG"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:4J1V"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:4J1V"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:4J1V"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:4J1V"
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
