SARNP_HUMAN
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 03-AUG-2022, entry version 185.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 110-119; 157-167 AND
RP 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 novel
RT 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 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT 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., 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 [5]
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 [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 project:
RT 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 inhibitory
RT 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 RNA
RT helicase.";
RL Exp. Cell Res. 313:782-790(2007).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TREX COMPLEX, AND
RP 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., 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, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA 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-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 to
CC scaffold/matrix attachment region DNA. Also binds single-stranded RNA.
CC Enhances RNA unwinding activity of DDX39A. May participate in important
CC transcriptional or translational control of cell growth, metabolism and
CC carcinogenesis. Component of the TREX complex which is thought to
CC couple mRNA transcription, processing and nuclear export, and
CC specifically associates with spliced mRNA and not with unspliced pre-
CC mRNA. TREX is recruited to spliced mRNAs by a transcription-independent
CC mechanism, binds to mRNA upstream of the exon-junction complex (EJC)
CC and is recruited in a splicing- and cap-dependent manner to a region
CC near the 5' end of the mRNA where it functions in mRNA export to the
CC cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for
CC the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless
CC mRNAs and infectious virus production. {ECO:0000269|PubMed:15338056,
CC ECO:0000269|PubMed:17196963, ECO:0000269|PubMed:20844015}.
CC -!- SUBUNIT: Interacts with DDX39A. Interacts with FUS. Component of the
CC transcription/export (TREX) complex at least composed of ALYREF/THOC4,
CC DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX seems to have
CC dynamic structure involving ATP-dependent remodeling; in the complex
CC interacts directly with DDX39B in a ATP-dependent manner which bridges
CC it to ALYREF/THOC4. {ECO:0000269|PubMed:17196963,
CC ECO:0000269|PubMed:20844015}.
CC -!- INTERACTION:
CC P82979; O00148: DDX39A; NbExp=4; IntAct=EBI-347495, EBI-348253;
CC P82979; Q13838: DDX39B; NbExp=4; IntAct=EBI-347495, EBI-348622;
CC P82979; Q01081: U2AF1; NbExp=3; IntAct=EBI-347495, EBI-632461;
CC P82979; P26368: U2AF2; NbExp=3; IntAct=EBI-347495, EBI-742339;
CC P82979; O76024: WFS1; NbExp=3; IntAct=EBI-347495, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle.
CC -!- TISSUE SPECIFICITY: Low expression in spleen, liver, pancreas, testis,
CC thymus, heart, and kidney. Increased levels are seen in hepatocellular
CC carcinoma and pancreatic adenocarcinoma. {ECO:0000269|PubMed:11356193}.
CC -!- INDUCTION: By EPO/erythropoietin.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28994.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CIP29ID42967ch12q13.html";
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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 PDB; 2DO1; NMR; -; A=6-47.
DR PDBsum; 2DO1; -.
DR AlphaFoldDB; P82979; -.
DR SMR; P82979; -.
DR BioGRID; 124049; 111.
DR IntAct; P82979; 43.
DR MINT; P82979; -.
DR STRING; 9606.ENSP00000337632; -.
DR GlyGen; P82979; 3 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P82979; -.
DR MetOSite; P82979; -.
DR PhosphoSitePlus; P82979; -.
DR SwissPalm; P82979; -.
DR BioMuta; SARNP; -.
DR DMDM; 18202440; -.
DR EPD; P82979; -.
DR jPOST; P82979; -.
DR MassIVE; P82979; -.
DR MaxQB; P82979; -.
DR PaxDb; P82979; -.
DR PeptideAtlas; P82979; -.
DR PRIDE; P82979; -.
DR ProteomicsDB; 57726; -.
DR TopDownProteomics; P82979; -.
DR Antibodypedia; 15547; 211 antibodies from 31 providers.
DR DNASU; 84324; -.
DR Ensembl; ENST00000336133.8; ENSP00000337632.3; ENSG00000205323.9.
DR Ensembl; ENST00000546604.5; ENSP00000449409.1; ENSG00000205323.9.
DR GeneID; 84324; -.
DR KEGG; hsa:84324; -.
DR MANE-Select; ENST00000336133.8; ENSP00000337632.3; NM_033082.4; NP_149073.1.
DR UCSC; uc001sht.4; human.
DR CTD; 84324; -.
DR DisGeNET; 84324; -.
DR GeneCards; SARNP; -.
DR HGNC; HGNC:24432; SARNP.
DR HPA; ENSG00000205323; Low tissue specificity.
DR MIM; 610049; gene.
DR neXtProt; NX_P82979; -.
DR OpenTargets; ENSG00000205323; -.
DR PharmGKB; PA165513309; -.
DR VEuPathDB; HostDB:ENSG00000205323; -.
DR eggNOG; KOG0720; Eukaryota.
DR eggNOG; KOG4259; Eukaryota.
DR GeneTree; ENSGT00390000002944; -.
DR HOGENOM; CLU_073926_1_0_1; -.
DR InParanoid; P82979; -.
DR OMA; ETPTKKH; -.
DR OrthoDB; 1120366at2759; -.
DR PhylomeDB; P82979; -.
DR TreeFam; TF319843; -.
DR PathwayCommons; P82979; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; P82979; -.
DR BioGRID-ORCS; 84324; 276 hits in 1078 CRISPR screens.
DR ChiTaRS; SARNP; human.
DR EvolutionaryTrace; P82979; -.
DR GeneWiki; CIP29; -.
DR GenomeRNAi; 84324; -.
DR Pharos; P82979; Tbio.
DR PRO; PR:P82979; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P82979; protein.
DR Bgee; ENSG00000205323; Expressed in ganglionic eminence and 152 other tissues.
DR ExpressionAtlas; P82979; baseline and differential.
DR Genevisible; P82979; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA-binding;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Transcription; Transcription regulation; Translation regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..210
FT /note="SAP domain-containing ribonucleoprotein"
FT /id="PRO_0000083916"
FT DOMAIN 8..42
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 45..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1J3"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1J3"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D1J3"
FT CONFLICT 127
FT /note="F -> V (in Ref. 3; AAF28994)"
FT /evidence="ECO:0000305"
FT CONFLICT 153..157
FT /note="RAQRF -> ELKDL (in Ref. 3; AAF28994)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..210
FT /note="KKRKRAERFGIA -> RRGKEQSALGLP (in Ref. 3; AAF28994)"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2DO1"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2DO1"
FT HELIX 31..44
FT /evidence="ECO:0007829|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
