Full text data of PARP12
PARP12
(ZC3HDC1)
[Confidence: low (only semi-automatic identification from reviews)]
Poly [ADP-ribose] polymerase 12; PARP-12; 2.4.2.30 (ADP-ribosyltransferase diphtheria toxin-like 12; ARTD12; Zinc finger CCCH domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Poly [ADP-ribose] polymerase 12; PARP-12; 2.4.2.30 (ADP-ribosyltransferase diphtheria toxin-like 12; ARTD12; Zinc finger CCCH domain-containing protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H0J9
ID PAR12_HUMAN Reviewed; 701 AA.
AC Q9H0J9; Q9H610; Q9NP36; Q9NTI3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Poly [ADP-ribose] polymerase 12;
DE Short=PARP-12;
DE EC=2.4.2.30;
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 12;
DE Short=ARTD12;
DE AltName: Full=Zinc finger CCCH domain-containing protein 1;
GN Name=PARP12; Synonyms=ZC3HDC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 444-701.
RC TISSUE=Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP IDENTIFICATION BY 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 [6]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-
RT ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
CC -!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
CC nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- SIMILARITY: Contains 4 C3H1-type zinc fingers.
CC -!- SIMILARITY: Contains 1 PARP catalytic domain.
CC -!- SIMILARITY: Contains 2 WWE domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL136766; CAB66700.1; -; mRNA.
DR EMBL; AL137255; CAB70657.1; -; mRNA.
DR EMBL; AC004849; AAS00360.1; -; Genomic_DNA.
DR EMBL; AC025816; AAF66161.1; -; Genomic_DNA.
DR EMBL; AC004961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081541; AAH81541.1; -; mRNA.
DR EMBL; AK026346; BAB15457.1; -; mRNA.
DR PIR; T46327; T46327.
DR RefSeq; NP_073587.1; NM_022750.2.
DR UniGene; Hs.12646; -.
DR UniGene; Hs.308710; -.
DR PDB; 2PQF; X-ray; 2.20 A; A/B/C/D/E/F=489-684.
DR PDBsum; 2PQF; -.
DR ProteinModelPortal; Q9H0J9; -.
DR SMR; Q9H0J9; 5-231, 496-680.
DR IntAct; Q9H0J9; 4.
DR STRING; 9606.ENSP00000263549; -.
DR PhosphoSite; Q9H0J9; -.
DR DMDM; 47117630; -.
DR PaxDb; Q9H0J9; -.
DR PRIDE; Q9H0J9; -.
DR Ensembl; ENST00000263549; ENSP00000263549; ENSG00000059378.
DR GeneID; 64761; -.
DR KEGG; hsa:64761; -.
DR UCSC; uc003vvl.1; human.
DR CTD; 64761; -.
DR GeneCards; GC07M139723; -.
DR HGNC; HGNC:21919; PARP12.
DR HPA; HPA003584; -.
DR MIM; 612481; gene.
DR neXtProt; NX_Q9H0J9; -.
DR PharmGKB; PA134953063; -.
DR eggNOG; NOG83866; -.
DR HOGENOM; HOG000236279; -.
DR HOVERGEN; HBG050384; -.
DR InParanoid; Q9H0J9; -.
DR KO; K15259; -.
DR OMA; RWQFLDR; -.
DR OrthoDB; EOG7P5T0J; -.
DR PhylomeDB; Q9H0J9; -.
DR ChiTaRS; PARP12; human.
DR EvolutionaryTrace; Q9H0J9; -.
DR GeneWiki; PARP12; -.
DR GenomeRNAi; 64761; -.
DR NextBio; 66743; -.
DR PRO; PR:Q9H0J9; -.
DR ArrayExpress; Q9H0J9; -.
DR Bgee; Q9H0J9; -.
DR CleanEx; HS_PARP12; -.
DR Genevestigator; Q9H0J9; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.228.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Metal-binding; NAD; Nucleus;
KW Polymorphism; Reference proteome; Repeat; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1 701 Poly [ADP-ribose] polymerase 12.
FT /FTId=PRO_0000211341.
FT DOMAIN 298 361 WWE 1.
FT DOMAIN 364 458 WWE 2.
FT DOMAIN 484 698 PARP catalytic.
FT ZN_FING 94 119 C3H1-type 1.
FT ZN_FING 150 179 C3H1-type 2.
FT ZN_FING 180 202 C3H1-type 3.
FT ZN_FING 270 297 C3H1-type 4.
FT ZN_FING 271 296 C3H1-type 3.
FT COMPBIAS 58 61 Poly-Ala.
FT VARIANT 293 293 V -> I (in dbSNP:rs34111764).
FT /FTId=VAR_050463.
FT VARIANT 463 463 V -> M (in dbSNP:rs35456446).
FT /FTId=VAR_050464.
FT VARIANT 620 620 A -> V (in dbSNP:rs17161356).
FT /FTId=VAR_050465.
FT CONFLICT 444 450 VQKNLVY -> MGGFGQH (in Ref. 4).
FT CONFLICT 462 462 Y -> C (in Ref. 4; BAB15457).
FT STRAND 499 502
FT HELIX 508 518
FT STRAND 524 533
FT HELIX 535 550
FT TURN 551 554
FT STRAND 559 565
FT HELIX 568 570
FT HELIX 571 577
FT TURN 581 584
FT STRAND 593 600
FT HELIX 601 605
FT STRAND 611 623
FT STRAND 626 629
FT STRAND 649 653
FT STRAND 655 657
FT STRAND 660 664
FT HELIX 666 668
FT STRAND 669 679
SQ SEQUENCE 701 AA; 79064 MW; 35152182F24CD215 CRC64;
MAQAGVVGEV TQVLCAAGGA LELPELRRRL RMGLSADALE RLLRQRGRFV VAVRAGGAAA
APERVVLAAS PLRLCRAHQG SKPGCVGLCA QLHLCRFMVY GACKFLRAGK NCRNSHSLTT
EHNLSVLRTH GVDHLSYNEL CQLLFQNDPW LLPEICQHYN KGDGPHGSCA FQKQCIKLHI
CQYFLQGECK FGTSCKRSHD FSNSENLEKL EKLGMSSDLV SRLPTIYRNA HDIKNKSSAP
SRVPPLFVPQ GTSERKDSSG SVSPNTLSQE EGDQICLYHI RKSCSFQDKC HRVHFHLPYR
WQFLDRGKWE DLDNMELIEE AYCNPKIERI LCSESASTFH SHCLNFNAMT YGATQARRLS
TASSVTKPPH FILTTDWIWY WSDEFGSWQE YGRQGTVHPV TTVSSSDVEK AYLAYCTPGS
DGQAATLKFQ AGKHNYELDF KAFVQKNLVY GTTKKVCRRP KYVSPQDVTT MQTCNTKFPG
PKSIPDYWDS SALPDPGFQK ITLSSSSEEY QKVWNLFNRT LPFYFVQKIE RVQNLALWEV
YQWQKGQMQK QNGGKAVDER QLFHGTSAIF VDAICQQNFD WRVCGVHGTS YGKGSYFARD
AAYSHHYSKS DTQTHTMFLA RVLVGEFVRG NASFVRPPAK EGWSNAFYDS CVNSVSDPSI
FVIFEKHQVY PEYVIQYTTS SKPSVTPSIL LALGSLFSSR Q
//
ID PAR12_HUMAN Reviewed; 701 AA.
AC Q9H0J9; Q9H610; Q9NP36; Q9NTI3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 107.
DE RecName: Full=Poly [ADP-ribose] polymerase 12;
DE Short=PARP-12;
DE EC=2.4.2.30;
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 12;
DE Short=ARTD12;
DE AltName: Full=Zinc finger CCCH domain-containing protein 1;
GN Name=PARP12; Synonyms=ZC3HDC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 444-701.
RC TISSUE=Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP IDENTIFICATION BY 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 [6]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP NOMENCLATURE.
RX PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
RA Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
RT "Toward a unified nomenclature for mammalian ADP-
RT ribosyltransferases.";
RL Trends Biochem. Sci. 35:208-219(2010).
CC -!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
CC nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
CC -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC -!- SIMILARITY: Contains 4 C3H1-type zinc fingers.
CC -!- SIMILARITY: Contains 1 PARP catalytic domain.
CC -!- SIMILARITY: Contains 2 WWE domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AL136766; CAB66700.1; -; mRNA.
DR EMBL; AL137255; CAB70657.1; -; mRNA.
DR EMBL; AC004849; AAS00360.1; -; Genomic_DNA.
DR EMBL; AC025816; AAF66161.1; -; Genomic_DNA.
DR EMBL; AC004961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081541; AAH81541.1; -; mRNA.
DR EMBL; AK026346; BAB15457.1; -; mRNA.
DR PIR; T46327; T46327.
DR RefSeq; NP_073587.1; NM_022750.2.
DR UniGene; Hs.12646; -.
DR UniGene; Hs.308710; -.
DR PDB; 2PQF; X-ray; 2.20 A; A/B/C/D/E/F=489-684.
DR PDBsum; 2PQF; -.
DR ProteinModelPortal; Q9H0J9; -.
DR SMR; Q9H0J9; 5-231, 496-680.
DR IntAct; Q9H0J9; 4.
DR STRING; 9606.ENSP00000263549; -.
DR PhosphoSite; Q9H0J9; -.
DR DMDM; 47117630; -.
DR PaxDb; Q9H0J9; -.
DR PRIDE; Q9H0J9; -.
DR Ensembl; ENST00000263549; ENSP00000263549; ENSG00000059378.
DR GeneID; 64761; -.
DR KEGG; hsa:64761; -.
DR UCSC; uc003vvl.1; human.
DR CTD; 64761; -.
DR GeneCards; GC07M139723; -.
DR HGNC; HGNC:21919; PARP12.
DR HPA; HPA003584; -.
DR MIM; 612481; gene.
DR neXtProt; NX_Q9H0J9; -.
DR PharmGKB; PA134953063; -.
DR eggNOG; NOG83866; -.
DR HOGENOM; HOG000236279; -.
DR HOVERGEN; HBG050384; -.
DR InParanoid; Q9H0J9; -.
DR KO; K15259; -.
DR OMA; RWQFLDR; -.
DR OrthoDB; EOG7P5T0J; -.
DR PhylomeDB; Q9H0J9; -.
DR ChiTaRS; PARP12; human.
DR EvolutionaryTrace; Q9H0J9; -.
DR GeneWiki; PARP12; -.
DR GenomeRNAi; 64761; -.
DR NextBio; 66743; -.
DR PRO; PR:Q9H0J9; -.
DR ArrayExpress; Q9H0J9; -.
DR Bgee; Q9H0J9; -.
DR CleanEx; HS_PARP12; -.
DR Genevestigator; Q9H0J9; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.228.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Metal-binding; NAD; Nucleus;
KW Polymorphism; Reference proteome; Repeat; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1 701 Poly [ADP-ribose] polymerase 12.
FT /FTId=PRO_0000211341.
FT DOMAIN 298 361 WWE 1.
FT DOMAIN 364 458 WWE 2.
FT DOMAIN 484 698 PARP catalytic.
FT ZN_FING 94 119 C3H1-type 1.
FT ZN_FING 150 179 C3H1-type 2.
FT ZN_FING 180 202 C3H1-type 3.
FT ZN_FING 270 297 C3H1-type 4.
FT ZN_FING 271 296 C3H1-type 3.
FT COMPBIAS 58 61 Poly-Ala.
FT VARIANT 293 293 V -> I (in dbSNP:rs34111764).
FT /FTId=VAR_050463.
FT VARIANT 463 463 V -> M (in dbSNP:rs35456446).
FT /FTId=VAR_050464.
FT VARIANT 620 620 A -> V (in dbSNP:rs17161356).
FT /FTId=VAR_050465.
FT CONFLICT 444 450 VQKNLVY -> MGGFGQH (in Ref. 4).
FT CONFLICT 462 462 Y -> C (in Ref. 4; BAB15457).
FT STRAND 499 502
FT HELIX 508 518
FT STRAND 524 533
FT HELIX 535 550
FT TURN 551 554
FT STRAND 559 565
FT HELIX 568 570
FT HELIX 571 577
FT TURN 581 584
FT STRAND 593 600
FT HELIX 601 605
FT STRAND 611 623
FT STRAND 626 629
FT STRAND 649 653
FT STRAND 655 657
FT STRAND 660 664
FT HELIX 666 668
FT STRAND 669 679
SQ SEQUENCE 701 AA; 79064 MW; 35152182F24CD215 CRC64;
MAQAGVVGEV TQVLCAAGGA LELPELRRRL RMGLSADALE RLLRQRGRFV VAVRAGGAAA
APERVVLAAS PLRLCRAHQG SKPGCVGLCA QLHLCRFMVY GACKFLRAGK NCRNSHSLTT
EHNLSVLRTH GVDHLSYNEL CQLLFQNDPW LLPEICQHYN KGDGPHGSCA FQKQCIKLHI
CQYFLQGECK FGTSCKRSHD FSNSENLEKL EKLGMSSDLV SRLPTIYRNA HDIKNKSSAP
SRVPPLFVPQ GTSERKDSSG SVSPNTLSQE EGDQICLYHI RKSCSFQDKC HRVHFHLPYR
WQFLDRGKWE DLDNMELIEE AYCNPKIERI LCSESASTFH SHCLNFNAMT YGATQARRLS
TASSVTKPPH FILTTDWIWY WSDEFGSWQE YGRQGTVHPV TTVSSSDVEK AYLAYCTPGS
DGQAATLKFQ AGKHNYELDF KAFVQKNLVY GTTKKVCRRP KYVSPQDVTT MQTCNTKFPG
PKSIPDYWDS SALPDPGFQK ITLSSSSEEY QKVWNLFNRT LPFYFVQKIE RVQNLALWEV
YQWQKGQMQK QNGGKAVDER QLFHGTSAIF VDAICQQNFD WRVCGVHGTS YGKGSYFARD
AAYSHHYSKS DTQTHTMFLA RVLVGEFVRG NASFVRPPAK EGWSNAFYDS CVNSVSDPSI
FVIFEKHQVY PEYVIQYTTS SKPSVTPSIL LALGSLFSSR Q
//
MIM
612481
*RECORD*
*FIELD* NO
612481
*FIELD* TI
*612481 POLY(ADP-RIBOSE) POLYMERASE FAMILY, MEMBER 12; PARP12
;;ZC3HDC1;;
FLJ22693
read more*FIELD* TX
CLONING
By database searching with evolutionarily conserved sequences in the
TIPARP gene (612480), Katoh and Katoh (2003) identified 2 human genes,
FLJ22693 (PARP12) and ZAP (ZC3HAV1; 607312), that encode deduced
proteins with the same conserved regions: a WWE domain, a PARP-like
domain, and a TPH domain. The N-terminal region of the TPH domain in all
3 genes contains a CCCH-type zinc finger. Katoh and Katoh (2003) noted
that PARP12 and ZCH3HAV1 share 27.5% and 26% overall amino acid sequence
identity with TIPARP, respectively. The PARP12 gene encodes a deduced
701-amino acid protein.
*FIELD* RF
1. Katoh, M.; Katoh, M.: Identification and characterization of human
TIPARP gene within the CCNL amplicon at human chromosome 3q25.31. Int.
J. Oncol. 23: 541-547, 2003.
*FIELD* CD
Carol A. Bocchini: 12/15/2008
*FIELD* ED
carol: 12/16/2008
*RECORD*
*FIELD* NO
612481
*FIELD* TI
*612481 POLY(ADP-RIBOSE) POLYMERASE FAMILY, MEMBER 12; PARP12
;;ZC3HDC1;;
FLJ22693
read more*FIELD* TX
CLONING
By database searching with evolutionarily conserved sequences in the
TIPARP gene (612480), Katoh and Katoh (2003) identified 2 human genes,
FLJ22693 (PARP12) and ZAP (ZC3HAV1; 607312), that encode deduced
proteins with the same conserved regions: a WWE domain, a PARP-like
domain, and a TPH domain. The N-terminal region of the TPH domain in all
3 genes contains a CCCH-type zinc finger. Katoh and Katoh (2003) noted
that PARP12 and ZCH3HAV1 share 27.5% and 26% overall amino acid sequence
identity with TIPARP, respectively. The PARP12 gene encodes a deduced
701-amino acid protein.
*FIELD* RF
1. Katoh, M.; Katoh, M.: Identification and characterization of human
TIPARP gene within the CCNL amplicon at human chromosome 3q25.31. Int.
J. Oncol. 23: 541-547, 2003.
*FIELD* CD
Carol A. Bocchini: 12/15/2008
*FIELD* ED
carol: 12/16/2008