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PHOCN_HUMAN
ID   PHOCN_HUMAN             Reviewed;         225 AA.
AC   Q9Y3A3; B4DML0; Q53SE0; Q7Z4Y6; Q9H2P3; Q9H5J1; Q9Y4T8;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=MOB-like protein phocein;
DE   AltName: Full=2C4D;
DE   AltName: Full=Class II mMOB1;
DE   AltName: Full=Mob1 homolog 3;
DE            Short=Mob3;
DE   AltName: Full=Mps one binder kinase activator-like 3;
DE   AltName: Full=Preimplantation protein 3;
GN   Name=MOB4; Synonyms=MOB3, MOBKL3, PHOCN, PREI3; ORFNames=CGI-95;
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., Todokoro K., Kotani S.;
RT   "Human MOB3.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Hu P.R., Yu L., Zhao Y., Yue P., Li M.Z., Zhao S.Y.;
RT   "Cloning of a novel human cDNA homology to murine B6D2F1 clone 2C4D mRNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Adrenal gland;
RA   Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Trachea;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
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   [10]
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   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Urinary bladder;
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   [12]
RP   PROTEIN SEQUENCE OF 57-70 AND 166-175, INTERACTION WITH STRN; STRN3 AND THE
RP   PPA2 COMPLEX, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=11319234; DOI=10.1074/jbc.m102398200;
RA   Moreno C.S., Lane W.S., Pallas D.C.;
RT   "A mammalian homolog of yeast MOB1 is both a member and a putative
RT   substrate of striatin family-protein phosphatase 2A complexes.";
RL   J. Biol. Chem. 276:24253-24260(2001).
RN   [13]
RP   INTERACTION WITH CTTNBP2NL.
RX   PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA   Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA   Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA   Aebersold R., Raught B., Gingras A.C.;
RT   "A PP2A phosphatase high density interaction network identifies a novel
RT   striatin-interacting phosphatase and kinase complex linked to the cerebral
RT   cavernous malformation 3 (CCM3) protein.";
RL   Mol. Cell. Proteomics 8:157-171(2009).
RN   [14]
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).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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: May play a role in membrane trafficking, specifically in
CC       membrane budding reactions. {ECO:0000250}.
CC   -!- SUBUNIT: Binds STRN4 (By similarity). Interacts with DNM1 and EPS15 (By
CC       similarity). Interacts with nucleoside diphosphate kinase (By
CC       similarity). Binds STRN and STRN3. Part of a ternary complex containing
CC       MOB4/PHOCN, STRN and/or STRN3 and PPA2. Interacts with CTTNBP2 (By
CC       similarity). Interacts with CTTNBP2NL. {ECO:0000250,
CC       ECO:0000269|PubMed:11319234, ECO:0000269|PubMed:18782753}.
CC   -!- INTERACTION:
CC       Q9Y3A3; Q9P2B4: CTTNBP2NL; NbExp=6; IntAct=EBI-713935, EBI-1774273;
CC       Q9Y3A3; O43815: STRN; NbExp=5; IntAct=EBI-713935, EBI-1046642;
CC       Q9Y3A3; Q13033-2: STRN3; NbExp=4; IntAct=EBI-713935, EBI-1053876;
CC       Q9Y3A3; Q9Y228: TRAF3IP3; NbExp=2; IntAct=EBI-713935, EBI-765817;
CC       Q9Y3A3-1; Q13033: STRN3; NbExp=2; IntAct=EBI-713946, EBI-1053857;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:11319234}. Membrane {ECO:0000269|PubMed:11319234};
CC       Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Golgi
CC       apparatus, Golgi stack membrane {ECO:0000269|PubMed:11319234};
CC       Peripheral membrane protein {ECO:0000269|PubMed:11319234}. Note=In a
CC       perinuclear punctate pattern. Associated with membranes and the Golgi
CC       stacks.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y3A3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y3A3-2; Sequence=VSP_012303;
CC       Name=3;
CC         IsoId=Q9Y3A3-3; Sequence=VSP_041091;
CC   -!- PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:11319234}.
CC   -!- SIMILARITY: Belongs to the MOB1/phocein family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP97221.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB45697.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB015441; BAB19057.1; -; mRNA.
DR   EMBL; AF093825; AAP97221.1; ALT_INIT; mRNA.
DR   EMBL; AJ580638; CAE45270.1; -; mRNA.
DR   EMBL; AF151853; AAD34090.1; -; mRNA.
DR   EMBL; AF250319; AAG44567.1; -; mRNA.
DR   EMBL; AL080070; CAB45697.1; ALT_FRAME; mRNA.
DR   EMBL; AK027043; BAB15635.1; -; mRNA.
DR   EMBL; AK292938; BAF85627.1; -; mRNA.
DR   EMBL; AK297514; BAG59922.1; -; mRNA.
DR   EMBL; CR457371; CAG33652.1; -; mRNA.
DR   EMBL; AC020550; AAX93147.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70164.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70167.1; -; Genomic_DNA.
DR   EMBL; BC005237; AAH05237.1; -; mRNA.
DR   CCDS; CCDS2321.1; -. [Q9Y3A3-1]
DR   CCDS; CCDS2322.1; -. [Q9Y3A3-2]
DR   CCDS; CCDS46480.1; -. [Q9Y3A3-3]
DR   PIR; T12466; T12466.
DR   RefSeq; NP_001094289.1; NM_001100819.2. [Q9Y3A3-3]
DR   RefSeq; NP_001191023.1; NM_001204094.1. [Q9Y3A3-2]
DR   RefSeq; NP_056202.2; NM_015387.4. [Q9Y3A3-1]
DR   RefSeq; NP_955776.1; NM_199482.3. [Q9Y3A3-2]
DR   PDB; 5YF4; X-ray; 1.90 A; A=53-210.
DR   PDB; 7K36; EM; 3.30 A; H=1-225.
DR   PDBsum; 5YF4; -.
DR   PDBsum; 7K36; -.
DR   AlphaFoldDB; Q9Y3A3; -.
DR   SMR; Q9Y3A3; -.
DR   BioGRID; 117369; 115.
DR   CORUM; Q9Y3A3; -.
DR   IntAct; Q9Y3A3; 91.
DR   MINT; Q9Y3A3; -.
DR   STRING; 9606.ENSP00000315702; -.
DR   iPTMnet; Q9Y3A3; -.
DR   MetOSite; Q9Y3A3; -.
DR   PhosphoSitePlus; Q9Y3A3; -.
DR   SwissPalm; Q9Y3A3; -.
DR   BioMuta; MOB4; -.
DR   DMDM; 56749365; -.
DR   OGP; Q9Y3A3; -.
DR   EPD; Q9Y3A3; -.
DR   jPOST; Q9Y3A3; -.
DR   MassIVE; Q9Y3A3; -.
DR   MaxQB; Q9Y3A3; -.
DR   PaxDb; Q9Y3A3; -.
DR   PeptideAtlas; Q9Y3A3; -.
DR   PRIDE; Q9Y3A3; -.
DR   ProteomicsDB; 85993; -. [Q9Y3A3-1]
DR   ProteomicsDB; 85994; -. [Q9Y3A3-2]
DR   ProteomicsDB; 85995; -. [Q9Y3A3-3]
DR   Antibodypedia; 53879; 213 antibodies from 34 providers.
DR   DNASU; 25843; -.
DR   Ensembl; ENST00000233892.8; ENSP00000233892.4; ENSG00000115540.15. [Q9Y3A3-2]
DR   Ensembl; ENST00000323303.9; ENSP00000315702.4; ENSG00000115540.15. [Q9Y3A3-1]
DR   Ensembl; ENST00000409360.1; ENSP00000387289.1; ENSG00000115540.15. [Q9Y3A3-2]
DR   Ensembl; ENST00000448447.6; ENSP00000405354.2; ENSG00000115540.15. [Q9Y3A3-3]
DR   GeneID; 25843; -.
DR   KEGG; hsa:25843; -.
DR   MANE-Select; ENST00000323303.9; ENSP00000315702.4; NM_015387.5; NP_056202.2.
DR   UCSC; uc002uum.4; human. [Q9Y3A3-1]
DR   CTD; 25843; -.
DR   DisGeNET; 25843; -.
DR   GeneCards; MOB4; -.
DR   HGNC; HGNC:17261; MOB4.
DR   HPA; ENSG00000115540; Low tissue specificity.
DR   MIM; 609361; gene.
DR   neXtProt; NX_Q9Y3A3; -.
DR   OpenTargets; ENSG00000115540; -.
DR   PharmGKB; PA162396053; -.
DR   VEuPathDB; HostDB:ENSG00000115540; -.
DR   eggNOG; KOG1852; Eukaryota.
DR   GeneTree; ENSGT01050000244956; -.
DR   HOGENOM; CLU_056981_3_0_1; -.
DR   InParanoid; Q9Y3A3; -.
DR   OMA; CKRFTTY; -.
DR   PhylomeDB; Q9Y3A3; -.
DR   TreeFam; TF314078; -.
DR   PathwayCommons; Q9Y3A3; -.
DR   SignaLink; Q9Y3A3; -.
DR   BioGRID-ORCS; 25843; 167 hits in 1012 CRISPR screens.
DR   ChiTaRS; MOB4; human.
DR   GeneWiki; MOBKL3; -.
DR   GenomeRNAi; 25843; -.
DR   Pharos; Q9Y3A3; Tbio.
DR   PRO; PR:Q9Y3A3; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9Y3A3; protein.
DR   Bgee; ENSG00000115540; Expressed in adrenal tissue and 204 other tissues.
DR   ExpressionAtlas; Q9Y3A3; baseline and differential.
DR   Genevisible; Q9Y3A3; HS.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..225
FT                   /note="MOB-like protein phocein"
FT                   /id="PRO_0000193576"
FT   BINDING         92
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..32
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_012303"
FT   VAR_SEQ         20..40
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041091"
FT   CONFLICT        90
FT                   /note="S -> G (in Ref. 7; BAB15635)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="L -> P (in Ref. 6; CAB45697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="F -> S (in Ref. 7; BAB15635)"
FT                   /evidence="ECO:0000305"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   HELIX           38..49
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   HELIX           54..58
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   HELIX           68..88
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   HELIX           121..137
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   TURN            139..141
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:7K36"
FT   HELIX           155..173
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   HELIX           175..185
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   HELIX           187..197
FT                   /evidence="ECO:0007829|PDB:5YF4"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:5YF4"
SQ   SEQUENCE   225 AA;  26032 MW;  D0EF1219711458BA CRC64;
     MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP
     PEGQDEGVWK YEHLRQFCLE LNGLAVKLQS ECHPDTCTQM TATEQWIFLC AAHKTPKECP
     AIDYTRHTLD GAACLLNSNK YFPSRVSIKE SSVAKLGSVC RRIYRIFSHA YFHHRQIFDE
     YENETFLCHR FTKFVMKYNL MSKDNLIVPI LEEEVQNSVS GESEA
 
 
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