ID SARNP_HUMAN Reviewed; 210 AA. AC P82979; A8K393; Q9P066; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 29-APR-2015, entry version 135. DE RecName: Full=SAP domain-containing ribonucleoprotein; DE AltName: Full=Cytokine-induced protein of 29 kDa; DE AltName: Full=Nuclear protein Hcc-1; DE AltName: Full=Proliferation-associated cytokine-inducible protein CIP29; GN Name=SARNP; Synonyms=HCC1; ORFNames=HSPC316; 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 [GENOMIC DNA], PROTEIN SEQUENCE OF 110-119; RP 157-167 AND 181-199, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=11356193; DOI=10.1016/S0014-5793(01)02409-7; RA Choong M.L., Tan L.K., Lo S.L., Ren E.-C., Ou K.L., Ong S.-E., RA Liang R.C.M.Y., Seow T.K., Chung M.C.M.; RT "An integrated approach in the discovery and characterization of a RT novel nuclear protein over-expressed in liver and pancreatic tumors."; RL FEBS Lett. 496:109-116(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mammary cancer; RX PubMed=11922608; DOI=10.1006/bbrc.2002.6680; RA Fukuda S., Wu D.W., Stark K., Pelus L.M.; RT "Cloning and characterization of a proliferation-associated cytokine- RT inducible protein, CIP29."; RL Biochem. Biophys. Res. Commun. 292:593-600(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal brain; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 [7] RP PROTEIN SEQUENCE OF 2-10 AND 127-135, ACETYLATION AT ALA-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V., Potts A., Brablan J., Quadroni M.; RL Submitted (JUL-2004) to UniProtKB. RN [8] RP FUNCTION. RX PubMed=15338056; DOI=10.1007/s00018-004-4205-x; RA Leaw C.L., Ren E.C., Choong M.L.; RT "Hcc-1 is a novel component of the nuclear matrix with growth RT inhibitory function."; RL Cell. Mol. Life Sci. 61:2264-2273(2004). RN [9] RP FUNCTION, AND INTERACTION WITH DDX39A AND FUS. RX PubMed=17196963; DOI=10.1016/j.yexcr.2006.11.014; RA Sugiura T., Sakurai K., Nagano Y.; RT "Intracellular characterization of DDX39, a novel growth-associated RT RNA helicase."; RL Exp. Cell Res. 313:782-790(2007). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [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 [11] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TREX COMPLEX, RP AND INTERACTION WITH DDX39B. RX PubMed=20844015; DOI=10.1101/gad.1898610; RA Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., RA Reed R.; RT "ATP is required for interactions between UAP56 and two conserved mRNA RT export proteins, Aly and CIP29, to assemble the TREX complex."; RL Genes Dev. 24:2043-2053(2010). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [13] RP STRUCTURE BY NMR OF 6-47. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SAP domain of human nuclear protein HCC- RT 1."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: Binds both single-stranded and double-stranded DNA with CC higher affinity for the single-stranded form. Specifically binds CC to scaffold/matrix attachment region DNA. Also binds single- CC stranded RNA. Enhances RNA unwinding activity of DDX39A. May CC participate in important transcriptional or translational control CC of cell growth, metabolism and carcinogenesis. Component of the CC TREX complex which is thought to couple mRNA transcription, CC processing and nuclear export, and specifically associates with CC spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to CC spliced mRNAs by a transcription-independent mechanism, binds to CC mRNA upstream of the exon-junction complex (EJC) and is recruited CC in a splicing- and cap-dependent manner to a region near the 5' CC end of the mRNA where it functions in mRNA export to the cytoplasm CC via the TAP/NFX1 pathway. The TREX complex is essential for the CC export of Kaposi's sarcoma-associated herpesvirus (KSHV) CC intronless mRNAs and infectious virus production. CC {ECO:0000269|PubMed:15338056, ECO:0000269|PubMed:17196963, CC ECO:0000269|PubMed:20844015}. CC -!- SUBUNIT: Interacts with DDX39A. Interacts with FUS. Component of CC the transcription/export (TREX) complex at least composed of CC ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; CC TREX seems to have dynamic structure involving ATP-dependent CC remodeling; in the complex interacts directly with DDX39B in a CC ATP-dependent manner which bridges it to ALYREF/THOC4. CC {ECO:0000269|PubMed:17196963, ECO:0000269|PubMed:20844015}. CC -!- INTERACTION: CC O00148:DDX39A; NbExp=4; IntAct=EBI-347495, EBI-348253; CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. CC -!- TISSUE SPECIFICITY: Low expression in spleen, liver, pancreas, CC testis, thymus, heart, and kidney. Increased levels are seen in CC hepatocellular carcinoma and pancreatic adenocarcinoma. CC {ECO:0000269|PubMed:11356193}. CC -!- INDUCTION: By EPO/erythropoietin. CC -!- SIMILARITY: Contains 1 SAP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00186}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF28994.1; Type=Frameshift; Positions=134, 149; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/CIP29ID42967ch12q13.html"; 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; AJ409089; CAC37950.1; -; Genomic_DNA. DR EMBL; AF486281; AAM09686.1; -; mRNA. DR EMBL; AF161434; AAF28994.1; ALT_SEQ; mRNA. DR EMBL; AK290508; BAF83197.1; -; mRNA. DR EMBL; CH471054; EAW96838.1; -; Genomic_DNA. DR EMBL; BC007099; AAH07099.1; -; mRNA. DR CCDS; CCDS8892.1; -. DR PIR; JC7830; JC7830. DR RefSeq; NP_149073.1; NM_033082.3. DR UniGene; Hs.505676; -. DR PDB; 2DO1; NMR; -; A=6-47. DR PDBsum; 2DO1; -. DR ProteinModelPortal; P82979; -. DR SMR; P82979; 6-47. DR BioGrid; 124049; 41. DR IntAct; P82979; 5. DR MINT; MINT-5008704; -. DR STRING; 9606.ENSP00000337632; -. DR PhosphoSite; P82979; -. DR BioMuta; SARNP; -. DR DMDM; 18202440; -. DR MaxQB; P82979; -. DR PaxDb; P82979; -. DR PRIDE; P82979; -. DR DNASU; 84324; -. DR Ensembl; ENST00000336133; ENSP00000337632; ENSG00000205323. DR Ensembl; ENST00000546604; ENSP00000449409; ENSG00000205323. DR GeneID; 84324; -. DR KEGG; hsa:84324; -. DR UCSC; uc001sht.3; human. DR CTD; 84324; -. DR GeneCards; GC12M056146; -. DR HGNC; HGNC:24432; SARNP. DR HPA; HPA030902; -. DR HPA; HPA030903; -. DR MIM; 610049; gene. DR neXtProt; NX_P82979; -. DR PharmGKB; PA165513309; -. DR eggNOG; NOG290157; -. DR GeneTree; ENSGT00390000002944; -. DR HOGENOM; HOG000013054; -. DR InParanoid; P82979; -. DR KO; K18732; -. DR OrthoDB; EOG7J9VRJ; -. DR PhylomeDB; P82979; -. DR TreeFam; TF319843; -. DR ChiTaRS; SARNP; human. DR EvolutionaryTrace; P82979; -. DR GeneWiki; CIP29; -. DR GenomeRNAi; 84324; -. DR NextBio; 74056; -. DR PRO; PR:P82979; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P82979; -. DR ExpressionAtlas; P82979; baseline and differential. DR Genevestigator; P82979; -. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0000346; C:transcription export complex; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.720.30; -; 1. DR InterPro; IPR003034; SAP_dom. DR Pfam; PF02037; SAP; 1. DR SMART; SM00513; SAP; 1. DR PROSITE; PS50800; SAP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; DNA-binding; mRNA transport; Nucleus; KW Reference proteome; RNA-binding; Transcription; KW Transcription regulation; Translation regulation; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:19413330, FT ECO:0000269|PubMed:22223895, FT ECO:0000269|Ref.7}. FT CHAIN 2 210 SAP domain-containing ribonucleoprotein. FT /FTId=PRO_0000083916. FT DOMAIN 8 42 SAP. {ECO:0000255|PROSITE- FT ProRule:PRU00186}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000269|PubMed:19413330, FT ECO:0000269|PubMed:22223895, FT ECO:0000269|Ref.7}. FT MOD_RES 10 10 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9D1J3}. FT MOD_RES 142 142 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9D1J3}. FT CONFLICT 127 127 F -> V (in Ref. 3; AAF28994). FT {ECO:0000305}. FT CONFLICT 153 157 RAQRF -> ELKDL (in Ref. 3; AAF28994). FT {ECO:0000305}. FT CONFLICT 199 210 KKRKRAERFGIA -> RRGKEQSALGLP (in Ref. 3; FT AAF28994). {ECO:0000305}. FT TURN 8 10 {ECO:0000244|PDB:2DO1}. FT HELIX 13 23 {ECO:0000244|PDB:2DO1}. FT HELIX 31 44 {ECO:0000244|PDB:2DO1}. SQ SEQUENCE 210 AA; 23671 MW; 96AFDD37EA328126 CRC64; MATETVELHK LKLAELKQEC LARGLETKGI KQDLIHRLQA YLEEHAEEEA NEEDVLGDET EEEETKPIEL PVKEEEPPEK TVDVAAEKKV VKITSEIPQT ERMQKRAERF NVPVSLESKK AARAARFGIS SVPTKGLSSD NKPMVNLDKL KERAQRFGLN VSSISRKSED DEKLKKRKER FGIVTSSAGT GTTEDTEAKK RKRAERFGIA //