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SAP domain-containing ribonucleoprotein (Cytokine-induced protein of 29 kDa) (Nuclear protein Hcc-1) (Proliferation-associated cytokine-inducible protein CIP29)

 SARNP_HUMAN             Reviewed;         210 AA.
P82979; A8K393; Q9P066;
29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
07-NOV-2018, entry version 166.
RecName: Full=SAP domain-containing ribonucleoprotein;
AltName: Full=Cytokine-induced protein of 29 kDa;
AltName: Full=Nuclear protein Hcc-1;
AltName: Full=Proliferation-associated cytokine-inducible protein CIP29;
Name=SARNP; Synonyms=HCC1; ORFNames=HSPC316;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 110-119;
157-167 AND 181-199, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=11356193; DOI=10.1016/S0014-5793(01)02409-7;
Choong M.L., Tan L.K., Lo S.L., Ren E.-C., Ou K.L., Ong S.-E.,
Liang R.C.M.Y., Seow T.K., Chung M.C.M.;
"An integrated approach in the discovery and characterization of a
novel nuclear protein over-expressed in liver and pancreatic tumors.";
FEBS Lett. 496:109-116(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary cancer;
PubMed=11922608; DOI=10.1006/bbrc.2002.6680;
Fukuda S., Wu D.W., Stark K., Pelus L.M.;
"Cloning and characterization of a proliferation-associated cytokine-
inducible protein, CIP29.";
Biochem. Biophys. Res. Commun. 292:593-600(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-10 AND 127-135, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
Submitted (JUL-2004) to UniProtKB.
[8]
FUNCTION.
PubMed=15338056; DOI=10.1007/s00018-004-4205-x;
Leaw C.L., Ren E.C., Choong M.L.;
"Hcc-1 is a novel component of the nuclear matrix with growth
inhibitory function.";
Cell. Mol. Life Sci. 61:2264-2273(2004).
[9]
FUNCTION, AND INTERACTION WITH DDX39A AND FUS.
PubMed=17196963; DOI=10.1016/j.yexcr.2006.11.014;
Sugiura T., Sakurai K., Nagano Y.;
"Intracellular characterization of DDX39, a novel growth-associated
RNA helicase.";
Exp. Cell Res. 313:782-790(2007).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TREX COMPLEX,
AND INTERACTION WITH DDX39B.
PubMed=20844015; DOI=10.1101/gad.1898610;
Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A.,
Reed R.;
"ATP is required for interactions between UAP56 and two conserved mRNA
export proteins, Aly and CIP29, to assemble the TREX complex.";
Genes Dev. 24:2043-2053(2010).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
STRUCTURE BY NMR OF 6-47.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SAP domain of human nuclear protein HCC-
1.";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: Binds both single-stranded and double-stranded DNA with
higher affinity for the single-stranded form. Specifically binds
to scaffold/matrix attachment region DNA. Also binds single-
stranded RNA. Enhances RNA unwinding activity of DDX39A. May
participate in important transcriptional or translational control
of cell growth, metabolism and carcinogenesis. Component of the
TREX complex which is thought to couple mRNA transcription,
processing and nuclear export, and specifically associates with
spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to
spliced mRNAs by a transcription-independent mechanism, binds to
mRNA upstream of the exon-junction complex (EJC) and is recruited
in a splicing- and cap-dependent manner to a region near the 5'
end of the mRNA where it functions in mRNA export to the cytoplasm
via the TAP/NFX1 pathway. The TREX complex is essential for the
export of Kaposi's sarcoma-associated herpesvirus (KSHV)
intronless mRNAs and infectious virus production.
{ECO:0000269|PubMed:15338056, ECO:0000269|PubMed:17196963,
ECO:0000269|PubMed:20844015}.
-!- SUBUNIT: Interacts with DDX39A. Interacts with FUS. Component of
the transcription/export (TREX) complex at least composed of
ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex;
TREX seems to have dynamic structure involving ATP-dependent
remodeling; in the complex interacts directly with DDX39B in a
ATP-dependent manner which bridges it to ALYREF/THOC4.
{ECO:0000269|PubMed:17196963, ECO:0000269|PubMed:20844015}.
-!- INTERACTION:
O00148:DDX39A; NbExp=4; IntAct=EBI-347495, EBI-348253;
Q13838:DDX39B; NbExp=5; IntAct=EBI-347495, EBI-348622;
Q01081:U2AF1; NbExp=3; IntAct=EBI-347495, EBI-632461;
P26368:U2AF2; NbExp=3; IntAct=EBI-347495, EBI-742339;
-!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle.
-!- TISSUE SPECIFICITY: Low expression in spleen, liver, pancreas,
testis, thymus, heart, and kidney. Increased levels are seen in
hepatocellular carcinoma and pancreatic adenocarcinoma.
{ECO:0000269|PubMed:11356193}.
-!- INDUCTION: By EPO/erythropoietin.
-!- SEQUENCE CAUTION:
Sequence=AAF28994.1; Type=Frameshift; Positions=134, 149; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CIP29ID42967ch12q13.html";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ409089; CAC37950.1; -; Genomic_DNA.
EMBL; AF486281; AAM09686.1; -; mRNA.
EMBL; AF161434; AAF28994.1; ALT_SEQ; mRNA.
EMBL; AK290508; BAF83197.1; -; mRNA.
EMBL; CH471054; EAW96838.1; -; Genomic_DNA.
EMBL; BC007099; AAH07099.1; -; mRNA.
CCDS; CCDS8892.1; -.
PIR; JC7830; JC7830.
RefSeq; NP_149073.1; NM_033082.3.
UniGene; Hs.505676; -.
PDB; 2DO1; NMR; -; A=6-47.
PDBsum; 2DO1; -.
ProteinModelPortal; P82979; -.
SMR; P82979; -.
BioGrid; 124049; 77.
IntAct; P82979; 16.
MINT; P82979; -.
STRING; 9606.ENSP00000337632; -.
iPTMnet; P82979; -.
PhosphoSitePlus; P82979; -.
BioMuta; SARNP; -.
DMDM; 18202440; -.
EPD; P82979; -.
MaxQB; P82979; -.
PaxDb; P82979; -.
PeptideAtlas; P82979; -.
PRIDE; P82979; -.
ProteomicsDB; 57726; -.
TopDownProteomics; P82979; -.
DNASU; 84324; -.
Ensembl; ENST00000336133; ENSP00000337632; ENSG00000205323.
Ensembl; ENST00000546604; ENSP00000449409; ENSG00000205323.
GeneID; 84324; -.
KEGG; hsa:84324; -.
UCSC; uc001sht.4; human.
CTD; 84324; -.
DisGeNET; 84324; -.
EuPathDB; HostDB:ENSG00000205323.8; -.
GeneCards; SARNP; -.
HGNC; HGNC:24432; SARNP.
HPA; HPA030902; -.
HPA; HPA030903; -.
MIM; 610049; gene.
neXtProt; NX_P82979; -.
OpenTargets; ENSG00000205323; -.
PharmGKB; PA165513309; -.
eggNOG; KOG4259; Eukaryota.
eggNOG; ENOG4111IA4; LUCA.
GeneTree; ENSGT00390000002944; -.
HOGENOM; HOG000013054; -.
InParanoid; P82979; -.
KO; K18732; -.
PhylomeDB; P82979; -.
TreeFam; TF319843; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72187; mRNA 3'-end processing.
ChiTaRS; SARNP; human.
EvolutionaryTrace; P82979; -.
GeneWiki; CIP29; -.
GenomeRNAi; 84324; -.
PRO; PR:P82979; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000205323; Expressed in 175 organ(s), highest expression level in testis.
ExpressionAtlas; P82979; baseline and differential.
Genevisible; P82979; HS.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0000346; C:transcription export complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
Gene3D; 1.10.720.30; -; 1.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
Pfam; PF02037; SAP; 1.
SMART; SM00513; SAP; 1.
SUPFAM; SSF68906; SSF68906; 1.
PROSITE; PS50800; SAP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; DNA-binding; mRNA transport; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding; Transcription;
Transcription regulation; Translation regulation; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.7}.
CHAIN 2 210 SAP domain-containing ribonucleoprotein.
/FTId=PRO_0000083916.
DOMAIN 8 42 SAP. {ECO:0000255|PROSITE-
ProRule:PRU00186}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.7}.
MOD_RES 10 10 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D1J3}.
MOD_RES 142 142 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D1J3}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000250|UniProtKB:Q9D1J3}.
CONFLICT 127 127 F -> V (in Ref. 3; AAF28994).
{ECO:0000305}.
CONFLICT 153 157 RAQRF -> ELKDL (in Ref. 3; AAF28994).
{ECO:0000305}.
CONFLICT 199 210 KKRKRAERFGIA -> RRGKEQSALGLP (in Ref. 3;
AAF28994). {ECO:0000305}.
TURN 8 10 {ECO:0000244|PDB:2DO1}.
HELIX 13 23 {ECO:0000244|PDB:2DO1}.
HELIX 31 44 {ECO:0000244|PDB:2DO1}.
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


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