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P82979 (SARNP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SAP domain-containing ribonucleoprotein
Alternative name(s):
Cytokine-induced protein of 29 kDa
Nuclear protein Hcc-1
Proliferation-associated cytokine-inducible protein CIP29
Gene names
Name:SARNP
Synonyms:HCC1
ORF Names:HSPC316
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.9 Ref.11

Subunit structure

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. Ref.9 Ref.11

Subcellular location

Nucleus. Nucleus speckle Ref.1 Ref.11.

Tissue specificity

Low expression in spleen, liver, pancreas, testis, thymus, heart, and kidney. Increased levels are seen in hepatocellular carcinoma and pancreatic adenocarcinoma. Ref.1

Induction

By EPO/erythropoietin.

Sequence similarities

Contains 1 SAP domain.

Sequence caution

The sequence AAF28994.1 differs from that shown. Reason: Frameshift at positions 134 and 149.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 210209SAP domain-containing ribonucleoprotein
PRO_0000083916

Regions

Domain8 – 4235SAP

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.10 Ref.12
Modified residue101N6-acetyllysine By similarity
Modified residue1421N6-acetyllysine By similarity

Experimental info

Sequence conflict1271F → V in AAF28994. Ref.3
Sequence conflict153 – 1575RAQRF → ELKDL in AAF28994. Ref.3
Sequence conflict199 – 21012KKRKR…RFGIA → RRGKEQSALGLP in AAF28994. Ref.3

Secondary structure

....... 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82979 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 96AFDD37EA328126

FASTA21023,671
        10         20         30         40         50         60 
MATETVELHK LKLAELKQEC LARGLETKGI KQDLIHRLQA YLEEHAEEEA NEEDVLGDET 

        70         80         90        100        110        120 
EEEETKPIEL PVKEEEPPEK TVDVAAEKKV VKITSEIPQT ERMQKRAERF NVPVSLESKK 

       130        140        150        160        170        180 
AARAARFGIS SVPTKGLSSD NKPMVNLDKL KERAQRFGLN VSSISRKSED DEKLKKRKER 

       190        200        210 
FGIVTSSAGT GTTEDTEAKK RKRAERFGIA 

« Hide

References

« Hide 'large scale' references
[1]"An integrated approach in the discovery and characterization of a novel nuclear protein over-expressed in liver and pancreatic tumors."
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.
FEBS Lett. 496:109-116(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 110-119; 157-167 AND 181-199, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Liver.
[2]"Cloning and characterization of a proliferation-associated cytokine-inducible protein, CIP29."
Fukuda S., Wu D.W., Stark K., Pelus L.M.
Biochem. Biophys. Res. Commun. 292:593-600(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary cancer.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
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. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Fetal brain.
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[7]Bienvenut W.V., Potts A., Brablan J., Quadroni M.
Submitted (JUL-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-10 AND 127-135, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]"Hcc-1 is a novel component of the nuclear matrix with growth inhibitory function."
Leaw C.L., Ren E.C., Choong M.L.
Cell. Mol. Life Sci. 61:2264-2273(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Intracellular characterization of DDX39, a novel growth-associated RNA helicase."
Sugiura T., Sakurai K., Nagano Y.
Exp. Cell Res. 313:782-790(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DDX39A AND FUS.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex."
Dufu K., Livingstone M.J., Seebacher J., Gygi S.P., Wilson S.A., Reed R.
Genes Dev. 24:2043-2053(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TREX COMPLEX, INTERACTION WITH DDX39B.
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Solution structure of the SAP domain of human nuclear protein HCC-1."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 6-47.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ409089 Genomic DNA. Translation: CAC37950.1.
AF486281 mRNA. Translation: AAM09686.1.
AF161434 mRNA. Translation: AAF28994.1. Sequence problems.
AK290508 mRNA. Translation: BAF83197.1.
CH471054 Genomic DNA. Translation: EAW96838.1.
BC007099 mRNA. Translation: AAH07099.1.
CCDSCCDS8892.1.
PIRJC7830.
RefSeqNP_149073.1. NM_033082.3.
UniGeneHs.505676.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO1NMR-A6-47[»]
ProteinModelPortalP82979.
SMRP82979. Positions 6-47.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124049. 39 interactions.
IntActP82979. 5 interactions.
MINTMINT-5008704.
STRING9606.ENSP00000337632.

PTM databases

PhosphoSiteP82979.

Polymorphism databases

DMDM18202440.

Proteomic databases

MaxQBP82979.
PaxDbP82979.
PRIDEP82979.

Protocols and materials databases

DNASU84324.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336133; ENSP00000337632; ENSG00000205323.
ENST00000546604; ENSP00000449409; ENSG00000205323.
GeneID84324.
KEGGhsa:84324.
UCSCuc001sht.3. human.

Organism-specific databases

CTD84324.
GeneCardsGC12M056146.
HGNCHGNC:24432. SARNP.
HPAHPA030902.
HPA030903.
MIM610049. gene.
neXtProtNX_P82979.
PharmGKBPA165513309.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290157.
HOGENOMHOG000013054.
InParanoidP82979.
OrthoDBEOG7J9VRJ.
PhylomeDBP82979.
TreeFamTF319843.

Gene expression databases

ArrayExpressP82979.
BgeeP82979.
GenevestigatorP82979.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
InterProIPR003034. SAP_dom.
[Graphical view]
PfamPF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSARNP. human.
EvolutionaryTraceP82979.
GeneWikiCIP29.
GenomeRNAi84324.
NextBio74056.
PROP82979.
SOURCESearch...

Entry information

Entry nameSARNP_HUMAN
AccessionPrimary (citable) accession number: P82979
Secondary accession number(s): A8K393, Q9P066
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM