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ONCO_HUMAN
ID   ONCO_HUMAN              Reviewed;         109 AA.
AC   P0CE72; B9EJH7; P32930; Q6ISI5; Q75MW0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Oncomodulin-1;
DE            Short=OM;
DE   AltName: Full=Parvalbumin beta;
GN   Name=OCM; Synonyms=OCM1, OCMN;
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 [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   PubMed=8354278; DOI=10.1111/j.1432-1033.1993.tb18084.x;
RA   Foehr U.G., Weber B.R., Muentener M., Staudenmann W., Hughes G.J.,
RA   Frutiger S., Banville D., Schaefer B.W., Heizmann C.W.;
RT   "Human alpha and beta parvalbumins. Structure and tissue-specific
RT   expression.";
RL   Eur. J. Biochem. 215:719-727(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   STRUCTURE BY NMR, AND CALCIUM-BINDING SITES.
RX   PubMed=15610002; DOI=10.1021/bi048388o;
RA   Babini E., Bertini I., Capozzi F., Del Bianco C., Hollender D., Kiss T.,
RA   Luchinat C., Quattrone A.;
RT   "Solution structure of human beta-parvalbumin and structural comparison
RT   with its paralog alpha-parvalbumin and with their rat orthologs.";
RL   Biochemistry 43:16076-16085(2004).
CC   -!- FUNCTION: Has some calmodulin-like activity with respect to enzyme
CC       activation and growth regulation. Binds two calcium ions.
CC   -!- INTERACTION:
CC       P0CE72; P12532: CKMT1B; NbExp=6; IntAct=EBI-11955379, EBI-1050662;
CC       P0CE72; O00560: SDCBP; NbExp=3; IntAct=EBI-11955379, EBI-727004;
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   EMBL; L20348; AAA02869.1; -; Genomic_DNA.
DR   EMBL; L20345; AAA02869.1; JOINED; Genomic_DNA.
DR   EMBL; L20346; AAA02869.1; JOINED; Genomic_DNA.
DR   EMBL; L20347; AAA02869.1; JOINED; Genomic_DNA.
DR   EMBL; AC004983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471144; EAW87352.1; -; Genomic_DNA.
DR   EMBL; BC069468; AAH69468.1; -; mRNA.
DR   EMBL; BC069512; AAH69512.1; -; mRNA.
DR   EMBL; BC069550; AAH69550.1; -; mRNA.
DR   EMBL; BC113706; AAI13707.1; -; mRNA.
DR   EMBL; BC113704; AAI13705.1; -; mRNA.
DR   EMBL; BC147028; AAI47029.1; -; mRNA.
DR   EMBL; BC147029; AAI47030.1; -; mRNA.
DR   CCDS; CCDS43548.1; -.
DR   PIR; S35041; PVHUO.
DR   RefSeq; NP_001091091.1; NM_001097622.1.
DR   RefSeq; XP_011513787.1; XM_011515485.2.
DR   PDB; 1TTX; NMR; -; A=1-109.
DR   PDBsum; 1TTX; -.
DR   AlphaFoldDB; P0CE72; -.
DR   BMRB; P0CE72; -.
DR   SMR; P0CE72; -.
DR   BioGRID; 576309; 5.
DR   IntAct; P0CE72; 2.
DR   STRING; 9606.ENSP00000242104; -.
DR   iPTMnet; P0CE72; -.
DR   PhosphoSitePlus; P0CE72; -.
DR   BioMuta; OCM; -.
DR   DMDM; 292630843; -.
DR   MassIVE; P0CE72; -.
DR   PaxDb; P0CE72; -.
DR   PeptideAtlas; P0CE72; -.
DR   PRIDE; P0CE72; -.
DR   Antibodypedia; 64205; 70 antibodies from 10 providers.
DR   DNASU; 654231; -.
DR   Ensembl; ENST00000242104.6; ENSP00000242104.5; ENSG00000122543.11.
DR   Ensembl; ENST00000416608.5; ENSP00000401365.1; ENSG00000122543.11.
DR   GeneID; 654231; -.
DR   KEGG; hsa:654231; -.
DR   MANE-Select; ENST00000242104.6; ENSP00000242104.5; NM_001097622.2; NP_001091091.1.
DR   UCSC; uc003spe.5; human.
DR   CTD; 654231; -.
DR   DisGeNET; 654231; -.
DR   GeneCards; OCM; -.
DR   HGNC; HGNC:8105; OCM.
DR   HPA; ENSG00000122543; Tissue enhanced (brain).
DR   MIM; 164795; gene.
DR   neXtProt; NX_P0CE72; -.
DR   OpenTargets; ENSG00000122543; -.
DR   PharmGKB; PA31894; -.
DR   VEuPathDB; HostDB:ENSG00000122543; -.
DR   eggNOG; KOG0027; Eukaryota.
DR   GeneTree; ENSGT00940000161875; -.
DR   HOGENOM; CLU_157356_0_0_1; -.
DR   InParanoid; P0CE72; -.
DR   OMA; PTICWIL; -.
DR   OrthoDB; 1524081at2759; -.
DR   PhylomeDB; P0CE72; -.
DR   TreeFam; TF332342; -.
DR   PathwayCommons; P0CE72; -.
DR   SignaLink; P0CE72; -.
DR   BioGRID-ORCS; 654231; 18 hits in 983 CRISPR screens.
DR   ChiTaRS; OCM; human.
DR   EvolutionaryTrace; P0CE72; -.
DR   GenomeRNAi; 654231; -.
DR   Pharos; P0CE72; Tbio.
DR   PRO; PR:P0CE72; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P0CE72; protein.
DR   Bgee; ENSG00000122543; Expressed in amygdala and 87 other tissues.
DR   Genevisible; P0CE72; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR008080; Parvalbumin.
DR   PANTHER; PTHR11653; PTHR11653; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Metal-binding; Reference proteome;
KW   Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02631"
FT   CHAIN           2..109
FT                   /note="Oncomodulin-1"
FT                   /id="PRO_0000073582"
FT   DOMAIN          39..74
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          78..109
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         52
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         91
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         93
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         97
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   BINDING         102
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT                   ECO:0000269|PubMed:15610002, ECO:0007744|PDB:1TTX"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02631"
FT   CONFLICT        20
FT                   /note="R -> Q (in Ref. 1; AAA02869)"
FT                   /evidence="ECO:0000305"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           8..18
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           41..51
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           80..90
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:1TTX"
FT   HELIX           100..108
FT                   /evidence="ECO:0007829|PDB:1TTX"
SQ   SEQUENCE   109 AA;  12184 MW;  C5793E2FF4A058A0 CRC64;
     MSITDVLSAD DIAAALQECR DPDTFEPQKF FQTSGLSKMS ANQVKDVFRF IDNDQSGYLD
     EEELKFFLQK FESGARELTE SETKSLMAAA DNDGDGKIGA EEFQEMVHS
 
 
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