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THYN1_HUMAN
ID   THYN1_HUMAN             Reviewed;         225 AA.
AC   Q9P016; Q567Q2; Q9H3L4; Q9HC20;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Thymocyte nuclear protein 1;
DE   AltName: Full=Thymocyte protein Thy28;
GN   Name=THYN1; Synonyms=THY28; ORFNames=HSPC144, MDS012, My0054;
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   Ge H.P., Yu L., Cui W.C., Fan Y.X., Yang Y.M., Zhao S.Y.;
RT   "Cloning and characterization of a novel human cDNA homology to chicken
RT   thymocyte protein cThy28kD mRNA.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Mao Y.M., Xie Y., Zhou Z.X.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT   "Novel genes expressed in hematopoietic stem/progenitor cells from
RT   myelodysplastic syndrome patients.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Spinal cord, and 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   [6]
RP   PURIFICATION.
RX   PubMed=15939300; DOI=10.1016/j.pep.2005.03.008;
RA   Song A.X., Chang Y.G., Gao Y.G., Lin X.J., Shi Y.H., Lin D.H., Hang Q.H.,
RA   Hu H.Y.;
RT   "Identification, expression, and purification of a unique stable domain
RT   from human HSPC144 protein.";
RL   Protein Expr. Purif. 42:146-152(2005).
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 55-221.
RX   PubMed=19237743; DOI=10.1107/s0907444908041474;
RA   Yu F., Song A., Xu C., Sun L., Li J., Tang L., Yu M., Yeates T.O., Hu H.,
RA   He J.;
RT   "Determining the DUF55-domain structure of human thymocyte nuclear protein
RT   1 from crystals partially twinned by tetartohedry.";
RL   Acta Crystallogr. D 65:212-219(2009).
CC   -!- FUNCTION: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting
CC       that it acts as a specific reader of 5hmC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9P016-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9P016-2; Sequence=VSP_021789;
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
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DR   EMBL; AF087886; AAP97185.1; -; mRNA.
DR   EMBL; AF059619; AAG43118.1; -; mRNA.
DR   EMBL; AF182413; AAG14949.1; -; mRNA.
DR   EMBL; AF161493; AAF29108.1; -; mRNA.
DR   EMBL; BC006978; AAH06978.1; -; mRNA.
DR   EMBL; BC093074; AAH93074.1; -; mRNA.
DR   CCDS; CCDS8496.1; -. [Q9P016-1]
DR   CCDS; CCDS8497.1; -. [Q9P016-2]
DR   RefSeq; NP_001032381.1; NM_001037304.1. [Q9P016-2]
DR   RefSeq; NP_001032382.1; NM_001037305.1. [Q9P016-1]
DR   RefSeq; NP_054893.1; NM_014174.2. [Q9P016-1]
DR   RefSeq; NP_954994.1; NM_199297.1. [Q9P016-2]
DR   RefSeq; NP_954995.1; NM_199298.1. [Q9P016-1]
DR   PDB; 3EOP; X-ray; 2.30 A; A/B=55-221.
DR   PDB; 5J3E; X-ray; 2.60 A; A/B=1-225.
DR   PDBsum; 3EOP; -.
DR   PDBsum; 5J3E; -.
DR   AlphaFoldDB; Q9P016; -.
DR   BMRB; Q9P016; -.
DR   SMR; Q9P016; -.
DR   BioGRID; 118856; 26.
DR   IntAct; Q9P016; 9.
DR   MINT; Q9P016; -.
DR   STRING; 9606.ENSP00000341657; -.
DR   GlyGen; Q9P016; 1 site, 2 O-linked glycans (1 site).
DR   iPTMnet; Q9P016; -.
DR   PhosphoSitePlus; Q9P016; -.
DR   SwissPalm; Q9P016; -.
DR   BioMuta; THYN1; -.
DR   DMDM; 74734762; -.
DR   EPD; Q9P016; -.
DR   jPOST; Q9P016; -.
DR   MassIVE; Q9P016; -.
DR   MaxQB; Q9P016; -.
DR   PaxDb; Q9P016; -.
DR   PeptideAtlas; Q9P016; -.
DR   PRIDE; Q9P016; -.
DR   ProteomicsDB; 83534; -. [Q9P016-1]
DR   ProteomicsDB; 83535; -. [Q9P016-2]
DR   Antibodypedia; 33170; 162 antibodies from 25 providers.
DR   DNASU; 29087; -.
DR   Ensembl; ENST00000341541.8; ENSP00000341657.3; ENSG00000151500.15. [Q9P016-1]
DR   Ensembl; ENST00000352327.5; ENSP00000341452.5; ENSG00000151500.15. [Q9P016-2]
DR   Ensembl; ENST00000392594.7; ENSP00000376373.3; ENSG00000151500.15. [Q9P016-1]
DR   Ensembl; ENST00000392595.6; ENSP00000376374.2; ENSG00000151500.15. [Q9P016-1]
DR   GeneID; 29087; -.
DR   KEGG; hsa:29087; -.
DR   MANE-Select; ENST00000341541.8; ENSP00000341657.3; NM_014174.3; NP_054893.1.
DR   UCSC; uc001qhf.4; human. [Q9P016-1]
DR   CTD; 29087; -.
DR   DisGeNET; 29087; -.
DR   GeneCards; THYN1; -.
DR   HGNC; HGNC:29560; THYN1.
DR   HPA; ENSG00000151500; Low tissue specificity.
DR   MIM; 613739; gene.
DR   neXtProt; NX_Q9P016; -.
DR   OpenTargets; ENSG00000151500; -.
DR   PharmGKB; PA128394653; -.
DR   VEuPathDB; HostDB:ENSG00000151500; -.
DR   eggNOG; KOG3383; Eukaryota.
DR   GeneTree; ENSGT00390000013297; -.
DR   HOGENOM; CLU_041799_2_0_1; -.
DR   InParanoid; Q9P016; -.
DR   OMA; DVQFIRM; -.
DR   OrthoDB; 1522853at2759; -.
DR   PhylomeDB; Q9P016; -.
DR   TreeFam; TF332126; -.
DR   PathwayCommons; Q9P016; -.
DR   SignaLink; Q9P016; -.
DR   BioGRID-ORCS; 29087; 8 hits in 1078 CRISPR screens.
DR   ChiTaRS; THYN1; human.
DR   EvolutionaryTrace; Q9P016; -.
DR   GeneWiki; THYN1; -.
DR   GenomeRNAi; 29087; -.
DR   Pharos; Q9P016; Tbio.
DR   PRO; PR:Q9P016; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9P016; protein.
DR   Bgee; ENSG00000151500; Expressed in oocyte and 208 other tissues.
DR   ExpressionAtlas; Q9P016; baseline and differential.
DR   Genevisible; Q9P016; HS.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   InterPro; IPR002740; EVE_domain.
DR   InterPro; IPR015947; PUA-like_sf.
DR   Pfam; PF01878; EVE; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..225
FT                   /note="Thymocyte nuclear protein 1"
FT                   /id="PRO_0000262564"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           5..10
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        32..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         161..225
FT                   /note="VDVQFVRMMKRFIPLAELKSYHQAHKATGGPLKNMVLFTRQRLSIQPLTQEE
FT                   FDFVLSLEEKEPS -> KSLILF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT                   /id="VSP_021789"
FT   CONFLICT        29
FT                   /note="G -> V (in Ref. 5; AAH93074)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="E -> G (in Ref. 2; AAG43118)"
FT                   /evidence="ECO:0000305"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           78..81
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           96..104
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          110..115
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          122..135
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          159..174
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           175..188
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   TURN            191..194
FT                   /evidence="ECO:0007829|PDB:5J3E"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           210..218
FT                   /evidence="ECO:0007829|PDB:3EOP"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:3EOP"
SQ   SEQUENCE   225 AA;  25697 MW;  76E6034A6404C962 CRC64;
     MSRPRKRLAG TSGSDKGLSG KRTKTENSGE ALAKVEDSNP QKTSATKNCL KNLSSHWLMK
     SEPESRLEKG VDVKFSIEDL KAQPKQTTCW DGVRNYQARN FLRAMKLGEE AFFYHSNCKE
     PGIAGLMKIV KEAYPDHTQF EKNNPHYDPS SKEDNPKWSM VDVQFVRMMK RFIPLAELKS
     YHQAHKATGG PLKNMVLFTR QRLSIQPLTQ EEFDFVLSLE EKEPS
 
 
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