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P82979

- SARNP_HUMAN

UniProt

P82979 - SARNP_HUMAN

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Protein

SAP domain-containing ribonucleoprotein

Gene

SARNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA export from nucleus Source: UniProtKB
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. regulation of translation Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Transcription, Transcription regulation, Translation regulation, Transport

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SARNP
Synonyms:HCC1
ORF Names:HSPC316
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:24432. SARNP.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. nuclear speck Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165513309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 210209SAP domain-containing ribonucleoproteinPRO_0000083916Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei10 – 101N6-acetyllysineBy similarity
Modified residuei142 – 1421N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP82979.
PaxDbiP82979.
PRIDEiP82979.

PTM databases

PhosphoSiteiP82979.

Expressioni

Tissue specificityi

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

Inductioni

By EPO/erythropoietin.

Gene expression databases

BgeeiP82979.
ExpressionAtlasiP82979. baseline and differential.
GenevestigatoriP82979.

Organism-specific databases

HPAiHPA030902.
HPA030903.

Interactioni

Subunit structurei

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/THOC4.2 Publications

Protein-protein interaction databases

BioGridi124049. 41 interactions.
IntActiP82979. 5 interactions.
MINTiMINT-5008704.
STRINGi9606.ENSP00000337632.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Helixi13 – 2311Combined sources
Helixi31 – 4414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DO1NMR-A6-47[»]
ProteinModelPortaliP82979.
SMRiP82979. Positions 6-47.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82979.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4235SAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG290157.
GeneTreeiENSGT00390000002944.
HOGENOMiHOG000013054.
InParanoidiP82979.
OrthoDBiEOG7J9VRJ.
PhylomeDBiP82979.
TreeFamiTF319843.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR003034. SAP_dom.
[Graphical view]
PfamiPF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P82979-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATETVELHK LKLAELKQEC LARGLETKGI KQDLIHRLQA YLEEHAEEEA
60 70 80 90 100
NEEDVLGDET EEEETKPIEL PVKEEEPPEK TVDVAAEKKV VKITSEIPQT
110 120 130 140 150
ERMQKRAERF NVPVSLESKK AARAARFGIS SVPTKGLSSD NKPMVNLDKL
160 170 180 190 200
KERAQRFGLN VSSISRKSED DEKLKKRKER FGIVTSSAGT GTTEDTEAKK
210
RKRAERFGIA
Length:210
Mass (Da):23,671
Last modified:January 23, 2007 - v3
Checksum:i96AFDD37EA328126
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271F → V in AAF28994. (PubMed:11042152)Curated
Sequence conflicti153 – 1575RAQRF → ELKDL in AAF28994. (PubMed:11042152)Curated
Sequence conflicti199 – 21012KKRKR…RFGIA → RRGKEQSALGLP in AAF28994. (PubMed:11042152)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8892.1.
PIRiJC7830.
RefSeqiNP_149073.1. NM_033082.3.
UniGeneiHs.505676.

Genome annotation databases

EnsembliENST00000336133; ENSP00000337632; ENSG00000205323.
ENST00000546604; ENSP00000449409; ENSG00000205323.
GeneIDi84324.
KEGGihsa:84324.
UCSCiuc001sht.3. human.

Polymorphism databases

DMDMi18202440.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS8892.1.
PIRi JC7830.
RefSeqi NP_149073.1. NM_033082.3.
UniGenei Hs.505676.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DO1 NMR - A 6-47 [» ]
ProteinModelPortali P82979.
SMRi P82979. Positions 6-47.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124049. 41 interactions.
IntActi P82979. 5 interactions.
MINTi MINT-5008704.
STRINGi 9606.ENSP00000337632.

PTM databases

PhosphoSitei P82979.

Polymorphism databases

DMDMi 18202440.

Proteomic databases

MaxQBi P82979.
PaxDbi P82979.
PRIDEi P82979.

Protocols and materials databases

DNASUi 84324.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336133 ; ENSP00000337632 ; ENSG00000205323 .
ENST00000546604 ; ENSP00000449409 ; ENSG00000205323 .
GeneIDi 84324.
KEGGi hsa:84324.
UCSCi uc001sht.3. human.

Organism-specific databases

CTDi 84324.
GeneCardsi GC12M056146.
HGNCi HGNC:24432. SARNP.
HPAi HPA030902.
HPA030903.
MIMi 610049. gene.
neXtProti NX_P82979.
PharmGKBi PA165513309.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290157.
GeneTreei ENSGT00390000002944.
HOGENOMi HOG000013054.
InParanoidi P82979.
OrthoDBi EOG7J9VRJ.
PhylomeDBi P82979.
TreeFami TF319843.

Miscellaneous databases

ChiTaRSi SARNP. human.
EvolutionaryTracei P82979.
GeneWikii CIP29.
GenomeRNAii 84324.
NextBioi 74056.
PROi P82979.
SOURCEi Search...

Gene expression databases

Bgeei P82979.
ExpressionAtlasi P82979. baseline and differential.
Genevestigatori P82979.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
InterProi IPR003034. SAP_dom.
[Graphical view ]
Pfami PF02037. SAP. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
[Graphical view ]
PROSITEi PS50800. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiSARNP_HUMAN
AccessioniPrimary (citable) accession number: P82979
Secondary accession number(s): A8K393, Q9P066
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3