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PHF13_HUMAN
ID   PHF13_HUMAN             Reviewed;         300 AA.
AC   Q86YI8; B3KUQ7; Q59FB6; Q5TH65; Q8N551; Q9UJP2;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=PHD finger protein 13;
DE   AltName: Full=Survival time-associated PHD finger protein in ovarian cancer 1;
DE            Short=SPOC1;
GN   Name=PHF13;
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].
RC   TISSUE=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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-20.
RC   TISSUE=Lung, and Testis;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-300.
RA   Rhodes S., Huckle E.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GSK3B, PROTEASOMAL
RP   DEGRADATION, AND INDUCTION.
RX   PubMed=19638409; DOI=10.1242/jcs.047365;
RA   Kinkley S., Staege H., Mohrmann G., Rohaly G., Schaub T., Kremmer E.,
RA   Winterpacht A., Will H.;
RT   "SPOC1: a novel PHD-containing protein modulating chromatin structure and
RT   mitotic chromosome condensation.";
RL   J. Cell Sci. 122:2946-2956(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 250-300 IN COMPLEX WITH
RP   TRIMETHYLATED HISTONE H3 AND ZINC IONS, AND X-RAY CRYSTALLOGRAPHY (1.85
RP   ANGSTROMS) OF 232-281.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of PHF13 in complex with tri-methylated histone H3K4.";
RL   Submitted (SEP-2010) to the PDB data bank.
CC   -!- FUNCTION: Modulates chromatin structure. Required for normal chromosome
CC       condensation during the early stages of mitosis. Required for normal
CC       chromosome separation during mitosis. {ECO:0000269|PubMed:19638409}.
CC   -!- SUBUNIT: Interacts with histone H3 that is trimethylated at 'Lys-4'
CC       (H3K4me3). Interacts with GSK3B. {ECO:0000269|PubMed:19638409,
CC       ECO:0000269|Ref.8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19638409}. Nucleus,
CC       nucleoplasm {ECO:0000269|PubMed:19638409}. Note=Predominantly bound to
CC       chromatin, but a minor proportion is also detected in the nucleoplasm.
CC   -!- INDUCTION: Expression levels are tightly regulated during the cell
CC       cycle. Strongly up-regulated during late G2 phase and M phase of the
CC       mitotic cell cycle. Down-regulated at the G1-S phase transition of the
CC       cell cycle. {ECO:0000269|PubMed:19638409}.
CC   -!- PTM: Subject to proteasomal degradation. Stable when bound to
CC       chromatin. The soluble form is rapidly degraded.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32792.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD92781.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK315110; BAG37568.1; -; mRNA.
DR   EMBL; AK097715; BAG53519.1; -; mRNA.
DR   EMBL; AB209544; BAD92781.1; ALT_INIT; mRNA.
DR   EMBL; AL031447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71561.1; -; Genomic_DNA.
DR   EMBL; BC032792; AAH32792.2; ALT_INIT; mRNA.
DR   EMBL; BC038516; AAH38516.1; -; mRNA.
DR   EMBL; AL121733; CAB57324.1; -; mRNA.
DR   CCDS; CCDS85.1; -.
DR   RefSeq; NP_722519.2; NM_153812.2.
DR   PDB; 3O70; X-ray; 1.85 A; A=232-281.
DR   PDB; 3O7A; X-ray; 1.67 A; A=229-280.
DR   PDBsum; 3O70; -.
DR   PDBsum; 3O7A; -.
DR   AlphaFoldDB; Q86YI8; -.
DR   SMR; Q86YI8; -.
DR   BioGRID; 127151; 10.
DR   IntAct; Q86YI8; 6.
DR   MINT; Q86YI8; -.
DR   STRING; 9606.ENSP00000366876; -.
DR   BindingDB; Q86YI8; -.
DR   ChEMBL; CHEMBL1764945; -.
DR   iPTMnet; Q86YI8; -.
DR   PhosphoSitePlus; Q86YI8; -.
DR   BioMuta; PHF13; -.
DR   DMDM; 229462750; -.
DR   EPD; Q86YI8; -.
DR   MassIVE; Q86YI8; -.
DR   PaxDb; Q86YI8; -.
DR   PeptideAtlas; Q86YI8; -.
DR   PRIDE; Q86YI8; -.
DR   ProteomicsDB; 70418; -.
DR   Antibodypedia; 13124; 142 antibodies from 20 providers.
DR   DNASU; 148479; -.
DR   Ensembl; ENST00000377648.5; ENSP00000366876.4; ENSG00000116273.6.
DR   GeneID; 148479; -.
DR   KEGG; hsa:148479; -.
DR   MANE-Select; ENST00000377648.5; ENSP00000366876.4; NM_153812.3; NP_722519.2.
DR   UCSC; uc001aob.5; human.
DR   CTD; 148479; -.
DR   DisGeNET; 148479; -.
DR   GeneCards; PHF13; -.
DR   HGNC; HGNC:22983; PHF13.
DR   HPA; ENSG00000116273; Low tissue specificity.
DR   neXtProt; NX_Q86YI8; -.
DR   OpenTargets; ENSG00000116273; -.
DR   PharmGKB; PA134901883; -.
DR   VEuPathDB; HostDB:ENSG00000116273; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   GeneTree; ENSGT00530000063882; -.
DR   HOGENOM; CLU_047981_0_0_1; -.
DR   InParanoid; Q86YI8; -.
DR   OMA; HAFQSEG; -.
DR   OrthoDB; 982722at2759; -.
DR   PhylomeDB; Q86YI8; -.
DR   TreeFam; TF331373; -.
DR   PathwayCommons; Q86YI8; -.
DR   SignaLink; Q86YI8; -.
DR   BioGRID-ORCS; 148479; 24 hits in 1082 CRISPR screens.
DR   ChiTaRS; PHF13; human.
DR   EvolutionaryTrace; Q86YI8; -.
DR   GenomeRNAi; 148479; -.
DR   Pharos; Q86YI8; Tbio.
DR   PRO; PR:Q86YI8; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q86YI8; protein.
DR   Bgee; ENSG00000116273; Expressed in secondary oocyte and 190 other tissues.
DR   ExpressionAtlas; Q86YI8; baseline and differential.
DR   Genevisible; Q86YI8; HS.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0035064; F:methylated histone binding; NAS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IMP:UniProtKB.
DR   CDD; cd15632; PHD_PHF13; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR041947; PHD_PHF13.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Chromatin regulator;
KW   DNA condensation; Metal-binding; Mitosis; Nucleus; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..300
FT                   /note="PHD finger protein 13"
FT                   /id="PRO_0000059304"
FT   ZN_FING         232..280
FT                   /note="PHD-type"
FT   REGION          109..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..248
FT                   /note="Interaction with trimethylated histone H3 (H3K4)"
FT   MOTIF           110..127
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        151..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         20
FT                   /note="K -> E (in dbSNP:rs17853850)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_055285"
FT   CONFLICT        111
FT                   /note="K -> R (in Ref. 1; BAG53519)"
FT                   /evidence="ECO:0000305"
FT   STRAND          246..248
FT                   /evidence="ECO:0007829|PDB:3O7A"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:3O7A"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:3O7A"
FT   TURN            258..262
FT                   /evidence="ECO:0007829|PDB:3O7A"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:3O7A"
FT   HELIX           275..278
FT                   /evidence="ECO:0007829|PDB:3O7A"
SQ   SEQUENCE   300 AA;  33582 MW;  197663A113B995F2 CRC64;
     MDSDSCAAAF HPEEYSPSCK RRRTVEDFNK FCTFVLAYAG YIPYPKEELP LRSSPSPANS
     TAGTIDSDGW DAGFSDIASS VPLPVSDRCF SHLQPTLLQR AKPSNFLLDR KKTDKLKKKK
     KRKRRDSDAP GKEGYRGGLL KLEAADPYVE TPTSPTLQDI PQAPSDPCSG WDSDTPSSGS
     CATVSPDQVK EIKTEGKRTI VRQGKQVVFR DEDSTGNDED IMVDSDDDSW DLVTCFCMKP
     FAGRPMIECN ECHTWIHLSC AKIRKSNVPE VFVCQKCRDS KFDIRRSNRS RTGSRKLFLD
 
 
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