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KTI12_HUMAN
ID   KTI12_HUMAN             Reviewed;         354 AA.
AC   Q96EK9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Protein KTI12 homolog;
GN   Name=KTI12; ORFNames=SBBI81;
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 [LARGE SCALE MRNA].
RA   Zhang W., Li N., Wan T., Zhang J., Cao X.;
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-200, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-200, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- INTERACTION:
CC       Q96EK9; Q13643: FHL3; NbExp=3; IntAct=EBI-7951092, EBI-741101;
CC   -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
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DR   EMBL; AF327348; AAL56009.1; -; mRNA.
DR   EMBL; AL445685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012173; AAH12173.1; -; mRNA.
DR   CCDS; CCDS562.1; -.
DR   RefSeq; NP_612426.1; NM_138417.2.
DR   AlphaFoldDB; Q96EK9; -.
DR   SMR; Q96EK9; -.
DR   BioGRID; 125220; 8.
DR   IntAct; Q96EK9; 3.
DR   MINT; Q96EK9; -.
DR   STRING; 9606.ENSP00000360676; -.
DR   iPTMnet; Q96EK9; -.
DR   PhosphoSitePlus; Q96EK9; -.
DR   SwissPalm; Q96EK9; -.
DR   BioMuta; KTI12; -.
DR   DMDM; 74751844; -.
DR   EPD; Q96EK9; -.
DR   jPOST; Q96EK9; -.
DR   MassIVE; Q96EK9; -.
DR   MaxQB; Q96EK9; -.
DR   PaxDb; Q96EK9; -.
DR   PeptideAtlas; Q96EK9; -.
DR   PRIDE; Q96EK9; -.
DR   ProteomicsDB; 76421; -.
DR   Antibodypedia; 32985; 58 antibodies from 14 providers.
DR   DNASU; 112970; -.
DR   Ensembl; ENST00000371614.2; ENSP00000360676.1; ENSG00000198841.4.
DR   GeneID; 112970; -.
DR   KEGG; hsa:112970; -.
DR   MANE-Select; ENST00000371614.2; ENSP00000360676.1; NM_138417.3; NP_612426.1.
DR   UCSC; uc001ctj.2; human.
DR   CTD; 112970; -.
DR   GeneCards; KTI12; -.
DR   HGNC; HGNC:25160; KTI12.
DR   HPA; ENSG00000198841; Low tissue specificity.
DR   neXtProt; NX_Q96EK9; -.
DR   OpenTargets; ENSG00000198841; -.
DR   PharmGKB; PA142671571; -.
DR   VEuPathDB; HostDB:ENSG00000198841; -.
DR   eggNOG; KOG3062; Eukaryota.
DR   GeneTree; ENSGT00390000002443; -.
DR   HOGENOM; CLU_027147_0_0_1; -.
DR   InParanoid; Q96EK9; -.
DR   OMA; LYCEAKA; -.
DR   OrthoDB; 1300128at2759; -.
DR   PhylomeDB; Q96EK9; -.
DR   TreeFam; TF312974; -.
DR   PathwayCommons; Q96EK9; -.
DR   SignaLink; Q96EK9; -.
DR   BioGRID-ORCS; 112970; 516 hits in 1091 CRISPR screens.
DR   GenomeRNAi; 112970; -.
DR   Pharos; Q96EK9; Tdark.
DR   PRO; PR:Q96EK9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q96EK9; protein.
DR   Bgee; ENSG00000198841; Expressed in granulocyte and 110 other tissues.
DR   Genevisible; Q96EK9; HS.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR045106; Kti12.
DR   InterPro; IPR013641; KTI12/PSTK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12435; PTHR12435; 1.
DR   Pfam; PF08433; KTI12; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Protein KTI12 homolog"
FT                   /id="PRO_0000285686"
FT   REGION          116..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         191
FT                   /note="D -> E (in dbSNP:rs2783175)"
FT                   /id="VAR_032046"
SQ   SEQUENCE   354 AA;  38616 MW;  877F297D28AF1E24 CRC64;
     MPLVVFCGLP YSGKSRRAEE LRVALAAEGR AVYVVDDAAV LGAEDPAVYG DSAREKALRG
     ALRASVERRL SRHDVVILDS LNYIKGFRYE LYCLARAART PLCLVYCVRP GGPIAGPQVA
     GANENPGRNV SVSWRPRAEE DGRAQAAGSS VLRELHTADS VVNGSAQADV PKELEREESG
     AAESPALVTP DSEKSAKHGS GAFYSPELLE ALTLRFEAPD SRNRWDRPLF TLVGLEEPLP
     LAGIRSALFE NRAPPPHQST QSQPLASGSF LHQLDQVTSQ VLAGLMEAQK SAVPGDLLTL
     PGTTEHLRFT RPLTMAELSR LRRQFISYTK MHPNNENLPQ LANMFLQYLS QSLH
 
 
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