ID ZN830_HUMAN Reviewed; 372 AA. AC Q96NB3; Q96F60; Q96GZ5; Q9BU38; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 09-DEC-2015, entry version 114. DE RecName: Full=Zinc finger protein 830; DE AltName: Full=Coiled-coil domain-containing protein 16; GN Name=ZNF830; Synonyms=CCDC16; 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], AND VARIANT GLN-99. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-372, AND VARIANTS GLN-99 RP AND THR-154. RC TISSUE=Colon, and 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-362, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [6] RP IDENTIFICATION AS PART OF THE XAB2 COMPLEX. RX PubMed=17981804; DOI=10.1074/jbc.M706647200; RA Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., RA Nakatsu Y., Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., RA Tanaka K.; RT "Isolation of XAB2 complex involved in pre-mRNA splicing, RT transcription, and transcription-coupled repair."; RL J. Biol. Chem. 283:940-950(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION RP 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION RP BY 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] GLN-99, AND IDENTIFICATION BY MASS RP 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., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: May act as a regulator of the cell cycle in embryos by CC participating in control of M phase. CC {ECO:0000250|UniProtKB:Q8R1N0}. CC -!- SUBUNIT: Component of the XAB2 complex, a multimeric protein CC complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. CC {ECO:0000269|PubMed:17981804}. CC -!- INTERACTION: CC O60306:AQR; NbExp=2; IntAct=EBI-3920997, EBI-2512328; CC Q13123:IK; NbExp=2; IntAct=EBI-3920997, EBI-713456; CC Q15365:PCBP1; NbExp=2; IntAct=EBI-3920997, EBI-946095; CC Q13356:PPIL2; NbExp=2; IntAct=EBI-3920997, EBI-7705988; CC Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-3920997, EBI-538479; CC Q13435:SF3B2; NbExp=2; IntAct=EBI-3920997, EBI-749111; CC Q13573:SNW1; NbExp=2; IntAct=EBI-3920997, EBI-632715; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8R1N0}. CC Note=Excluded from nucleolus. {ECO:0000250|UniProtKB:Q8R1N0}. CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK055707; BAB70992.1; -; mRNA. DR EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002913; AAH02913.2; -; mRNA. DR EMBL; BC009044; AAH09044.1; -; mRNA. DR EMBL; BC011584; AAH11584.2; -; mRNA. DR CCDS; CCDS32618.1; -. DR RefSeq; NP_443089.3; NM_052857.3. DR UniGene; Hs.413678; -. DR ProteinModelPortal; Q96NB3; -. DR BioGrid; 124850; 21. DR IntAct; Q96NB3; 13. DR STRING; 9606.ENSP00000354518; -. DR PhosphoSite; Q96NB3; -. DR BioMuta; ZNF830; -. DR DMDM; 313104066; -. DR MaxQB; Q96NB3; -. DR PaxDb; Q96NB3; -. DR PRIDE; Q96NB3; -. DR DNASU; 91603; -. DR Ensembl; ENST00000361952; ENSP00000354518; ENSG00000198783. DR GeneID; 91603; -. DR KEGG; hsa:91603; -. DR UCSC; uc002hih.4; human. DR CTD; 91603; -. DR GeneCards; ZNF830; -. DR HGNC; HGNC:28291; ZNF830. DR HPA; HPA024754; -. DR HPA; HPA027211; -. DR neXtProt; NX_Q96NB3; -. DR PharmGKB; PA162410767; -. DR eggNOG; KOG3032; Eukaryota. DR eggNOG; ENOG4111GTR; LUCA. DR GeneTree; ENSGT00390000012151; -. DR HOGENOM; HOG000246999; -. DR HOVERGEN; HBG105347; -. DR InParanoid; Q96NB3; -. DR KO; K13104; -. DR OMA; VLGKQHR; -. DR PhylomeDB; Q96NB3; -. DR TreeFam; TF315895; -. DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER). DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR GenomeRNAi; 91603; -. DR NextBio; 77315; -. DR PRO; PR:Q96NB3; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; Q96NB3; -. DR CleanEx; HS_ZNF830; -. DR ExpressionAtlas; Q96NB3; baseline and differential. DR Genevisible; Q96NB3; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl. DR GO; GO:0006281; P:DNA repair; TAS:Reactome. DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl. DR GO; GO:0044773; P:mitotic DNA damage checkpoint; IEA:Ensembl. DR GO; GO:0007067; P:mitotic nuclear division; IBA:GO_Central. DR GO; GO:0033260; P:nuclear DNA replication; IEA:Ensembl. DR GO; GO:0006289; P:nucleotide-excision repair; TAS:Reactome. DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Cell division; Coiled coil; KW Complete proteome; Developmental protein; Metal-binding; Mitosis; KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc; KW Zinc-finger. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}. FT CHAIN 2 372 Zinc finger protein 830. FT /FTId=PRO_0000076193. FT ZN_FING 53 75 C2H2-type. FT COILED 312 349 {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330}. FT MOD_RES 351 351 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:17525332, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 362 362 Phosphoserine. FT {ECO:0000244|PubMed:17525332}. FT VARIANT 16 16 I -> V (in dbSNP:rs8073825). FT /FTId=VAR_030940. FT VARIANT 93 93 S -> P (in dbSNP:rs8078059). FT /FTId=VAR_030941. FT VARIANT 99 99 H -> Q (in dbSNP:rs931196). FT {ECO:0000244|PubMed:21269460, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_024059. FT VARIANT 135 135 F -> L (in dbSNP:rs8078217). FT /FTId=VAR_030942. FT VARIANT 154 154 S -> T (in dbSNP:rs3744355). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_024060. SQ SEQUENCE 372 AA; 41999 MW; A06403B117672C8C CRC64; MASSASARTP AGKRVINQEE LRRLMKEKQR LSTSRKRIES PFAKYNRLGQ LSCALCNTPV KSELLWQTHV LGKQHREKVA ELKGAKEASQ GSSASSAPHS VKRKAPDADD QDVKRAKATL VPQVQPSTSA WTTNFDKIGK EFIRATPSKP SGLSLLPDYE DEEEEEEEEE GDGERKRGDA SKPLSDAQGK EHSVSSSREV TSSVLPNDFF STNPPKAPII PHSGSIEKAE IHEKVVERRE NTAEALPEGF FDDPEVDARV RKVDAPKDQM DKEWDEFQKA MRQVNTISEA IVAEEDEEGR LDRQIGEIDE QIECYRRVEK LRNRQDEIKN KLKEILTIKE LQKKEEENAD SDDEGELQDL LSQDWRVKGA LL //