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TATD1_HUMAN
ID   TATD1_HUMAN             Reviewed;         297 AA.
AC   Q6P1N9; B2R5J0; Q8TD02; Q9BY40;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Deoxyribonuclease TATDN1;
DE            EC=3.1.21.-;
DE   AltName: Full=Hepatocarcinoma high expression protein;
GN   Name=TATDN1; ORFNames=CDA11;
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] (ISOFORM 1).
RC   TISSUE=Pheochromocytoma;
RA   Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT   "A novel gene expressed in human pheochromocytoma.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Xu Y., Wu C., He G., Huang Y., Cao Y., Ying K., Xie Y., Mao Y.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Skeletal muscle;
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   [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] (ISOFORM 1).
RC   TISSUE=Eye;
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   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   [7]
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   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 5-295.
RG   Structural genomics consortium (SGC);
RT   "Structure of putative deoxyribonuclease TATDN1 isoform A.";
RL   Submitted (JUL-2010) to the PDB data bank.
CC   -!- FUNCTION: Deoxyribonuclease which catalyzes (in vitro) the decatenation
CC       of kinetoplast DNA, which are circular DNA catenated to each other,
CC       producing linear DNA molecules (By similarity). Plays an important role
CC       in chromosomal segregation and cell cycle progression during eye
CC       development probably via its DNA decatenation activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q6GML7}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q17R31};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000250|UniProtKB:Q17R31};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P1N9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P1N9-2; Sequence=VSP_030045;
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       TatD-type hydrolase family. {ECO:0000305}.
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DR   EMBL; AF212250; AAK14933.1; -; mRNA.
DR   EMBL; AY071865; AAL61823.1; -; mRNA.
DR   EMBL; AK312204; BAG35137.1; -; mRNA.
DR   EMBL; CH471060; EAW92066.1; -; Genomic_DNA.
DR   EMBL; CH471060; EAW92067.1; -; Genomic_DNA.
DR   EMBL; BC064964; AAH64964.1; -; mRNA.
DR   CCDS; CCDS55273.1; -. [Q6P1N9-2]
DR   CCDS; CCDS6351.1; -. [Q6P1N9-1]
DR   RefSeq; NP_001139632.1; NM_001146160.1. [Q6P1N9-2]
DR   RefSeq; NP_001304819.1; NM_001317890.1.
DR   RefSeq; NP_001304820.1; NM_001317891.1.
DR   RefSeq; NP_114415.1; NM_032026.3. [Q6P1N9-1]
DR   RefSeq; XP_016869387.1; XM_017013898.1. [Q6P1N9-2]
DR   PDB; 2XIO; X-ray; 1.19 A; A=5-295.
DR   PDBsum; 2XIO; -.
DR   AlphaFoldDB; Q6P1N9; -.
DR   SMR; Q6P1N9; -.
DR   BioGRID; 123823; 86.
DR   IntAct; Q6P1N9; 3.
DR   STRING; 9606.ENSP00000276692; -.
DR   iPTMnet; Q6P1N9; -.
DR   PhosphoSitePlus; Q6P1N9; -.
DR   BioMuta; TATDN1; -.
DR   DMDM; 166227295; -.
DR   EPD; Q6P1N9; -.
DR   jPOST; Q6P1N9; -.
DR   MassIVE; Q6P1N9; -.
DR   MaxQB; Q6P1N9; -.
DR   PaxDb; Q6P1N9; -.
DR   PeptideAtlas; Q6P1N9; -.
DR   PRIDE; Q6P1N9; -.
DR   ProteomicsDB; 66858; -. [Q6P1N9-1]
DR   ProteomicsDB; 66859; -. [Q6P1N9-2]
DR   Antibodypedia; 13907; 95 antibodies from 19 providers.
DR   DNASU; 83940; -.
DR   Ensembl; ENST00000276692.11; ENSP00000276692.6; ENSG00000147687.19. [Q6P1N9-1]
DR   Ensembl; ENST00000519548.5; ENSP00000428336.1; ENSG00000147687.19. [Q6P1N9-2]
DR   GeneID; 83940; -.
DR   KEGG; hsa:83940; -.
DR   MANE-Select; ENST00000276692.11; ENSP00000276692.6; NM_032026.4; NP_114415.1.
DR   UCSC; uc003yrd.4; human. [Q6P1N9-1]
DR   CTD; 83940; -.
DR   DisGeNET; 83940; -.
DR   GeneCards; TATDN1; -.
DR   HGNC; HGNC:24220; TATDN1.
DR   HPA; ENSG00000147687; Low tissue specificity.
DR   MIM; 619364; gene.
DR   neXtProt; NX_Q6P1N9; -.
DR   OpenTargets; ENSG00000147687; -.
DR   PharmGKB; PA134971804; -.
DR   VEuPathDB; HostDB:ENSG00000147687; -.
DR   eggNOG; KOG3020; Eukaryota.
DR   GeneTree; ENSGT00940000156272; -.
DR   InParanoid; Q6P1N9; -.
DR   OMA; PNEAPRI; -.
DR   OrthoDB; 1224437at2759; -.
DR   PhylomeDB; Q6P1N9; -.
DR   TreeFam; TF324192; -.
DR   PathwayCommons; Q6P1N9; -.
DR   SignaLink; Q6P1N9; -.
DR   BioGRID-ORCS; 83940; 14 hits in 1033 CRISPR screens.
DR   ChiTaRS; TATDN1; human.
DR   EvolutionaryTrace; Q6P1N9; -.
DR   GenomeRNAi; 83940; -.
DR   Pharos; Q6P1N9; Tbio.
DR   PRO; PR:Q6P1N9; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q6P1N9; protein.
DR   Bgee; ENSG00000147687; Expressed in body of pancreas and 105 other tissues.
DR   ExpressionAtlas; Q6P1N9; baseline and differential.
DR   Genevisible; Q6P1N9; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01310; TatD_DNAse; 1.
DR   InterPro; IPR018228; DNase_TatD-rel_CS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001130; TatD-like.
DR   Pfam; PF01026; TatD_DNase; 1.
DR   PIRSF; PIRSF005902; DNase_TatD; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS01091; TATD_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Metal-binding; Nuclease;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..297
FT                   /note="Deoxyribonuclease TATDN1"
FT                   /id="PRO_0000313590"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         112
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   BINDING         222
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q17R31"
FT   MOD_RES         27
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P8M1"
FT   MOD_RES         46
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P8M1"
FT   VAR_SEQ         1..47
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_030045"
FT   CONFLICT        161
FT                   /note="M -> T (in Ref. 5; AAH64964)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           32..42
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           54..64
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          70..74
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           78..82
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           83..87
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           89..101
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          107..116
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           125..134
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          146..152
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           165..167
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           180..188
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          192..195
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           203..210
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           214..216
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          244..247
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           260..262
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           263..274
FT                   /evidence="ECO:0007829|PDB:2XIO"
FT   HELIX           278..293
FT                   /evidence="ECO:0007829|PDB:2XIO"
SQ   SEQUENCE   297 AA;  33602 MW;  D8671A4A50E5D9B5 CRC64;
     MSRFKFIDIG INLTDPMFRG IYRGVQKHQD DLQDVIGRAV EIGVKKFMIT GGNLQDSKDA
     LHLAQTNGMF FSTVGCHPTR CGEFEKNNPD LYLKELLNLA ENNKGKVVAI GECGLDFDRL
     QFCPKDTQLK YFEKQFELSE QTKLPMFLHC RNSHAEFLDI MKRNRDRCVG GVVHSFDGTK
     EAAAALIDLD LYIGFNGCSL KTEANLEVLK SIPSEKLMIE TDAPWCGVKS THAGSKYIRT
     AFPTKKKWES GHCLKDRNEP CHIIQILEIM SAVRDEDPLE LANTLYNNTI KVFFPGI
 
 
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