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Q9D1J3

- SARNP_MOUSE

UniProt

Q9D1J3 - SARNP_MOUSE

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Protein
SAP domain-containing ribonucleoprotein
Gene
Sarnp, Hcc1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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 By similarity.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW

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):
Nuclear protein Hcc-1
Gene namesi
Name:Sarnp
Synonyms:Hcc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1913368. Sarnp.

Subcellular locationi

Nucleus By similarity. Nucleus speckle By similarity

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 210209SAP domain-containing ribonucleoprotein
PRO_0000083919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei10 – 101N6-acetyllysine1 Publication
Modified residuei142 – 1421N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D1J3.
PaxDbiQ9D1J3.
PRIDEiQ9D1J3.

PTM databases

PhosphoSiteiQ9D1J3.

Expressioni

Gene expression databases

BgeeiQ9D1J3.
CleanExiMM_1110005A23RIK.
GenevestigatoriQ9D1J3.

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 By similarity.

Protein-protein interaction databases

IntActiQ9D1J3. 1 interaction.
MINTiMINT-1867986.
STRINGi10090.ENSMUSP00000100863.

Structurei

3D structure databases

ProteinModelPortaliQ9D1J3.
SMRiQ9D1J3. Positions 6-47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4235SAP
Add
BLAST

Sequence similaritiesi

Contains 1 SAP domain.

Phylogenomic databases

eggNOGiNOG290157.
GeneTreeiENSGT00390000002944.
HOGENOMiHOG000013054.
InParanoidiQ9D1J3.
OMAiSDAKPMV.
OrthoDBiEOG7J9VRJ.
PhylomeDBiQ9D1J3.
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.

Q9D1J3-1 [UniParc]FASTAAdd to Basket

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MAAETVELHK LKLAELKQEC LARGLETKGI KQDLINRLQA YLEDHAEEEA    50
NEEDVLGDET EEEEPKPIEL PVKEEEPPEK AVDMASEKKV VKITSGIPQT 100
ERMQKRAERF NVPVSLESKK AARAARFGIS SVPTKGLSSD TKPMVNLDKL 150
KERAQRFGLN VSSISRKSED DEKLKKRKER FGIVTSSAGT GTTEDTEAKK 200
RKRAERFGIA 210
Length:210
Mass (Da):23,533
Last modified:January 23, 2007 - v3
Checksum:i15705691F989E9AB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK003453 mRNA. Translation: BAB22799.1.
AK018773 mRNA. Translation: BAB31400.1.
AK088266 mRNA. Translation: BAC40246.1.
AK146248 mRNA. Translation: BAE27010.1.
BC027510 mRNA. Translation: AAH27510.1.
CCDSiCCDS36092.1.
RefSeqiNP_079640.1. NM_025364.2.
UniGeneiMm.351579.

Genome annotation databases

EnsembliENSMUST00000056396; ENSMUSP00000137244; ENSMUSG00000051255.
ENSMUST00000105230; ENSMUSP00000100863; ENSMUSG00000078427.
GeneIDi66118.
KEGGimmu:66118.
UCSCiuc007hor.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK003453 mRNA. Translation: BAB22799.1 .
AK018773 mRNA. Translation: BAB31400.1 .
AK088266 mRNA. Translation: BAC40246.1 .
AK146248 mRNA. Translation: BAE27010.1 .
BC027510 mRNA. Translation: AAH27510.1 .
CCDSi CCDS36092.1.
RefSeqi NP_079640.1. NM_025364.2.
UniGenei Mm.351579.

3D structure databases

ProteinModelPortali Q9D1J3.
SMRi Q9D1J3. Positions 6-47.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9D1J3. 1 interaction.
MINTi MINT-1867986.
STRINGi 10090.ENSMUSP00000100863.

PTM databases

PhosphoSitei Q9D1J3.

Proteomic databases

MaxQBi Q9D1J3.
PaxDbi Q9D1J3.
PRIDEi Q9D1J3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000056396 ; ENSMUSP00000137244 ; ENSMUSG00000051255 .
ENSMUST00000105230 ; ENSMUSP00000100863 ; ENSMUSG00000078427 .
GeneIDi 66118.
KEGGi mmu:66118.
UCSCi uc007hor.2. mouse.

Organism-specific databases

CTDi 84324.
MGIi MGI:1913368. Sarnp.

Phylogenomic databases

eggNOGi NOG290157.
GeneTreei ENSGT00390000002944.
HOGENOMi HOG000013054.
InParanoidi Q9D1J3.
OMAi SDAKPMV.
OrthoDBi EOG7J9VRJ.
PhylomeDBi Q9D1J3.
TreeFami TF319843.

Miscellaneous databases

NextBioi 320682.
PROi Q9D1J3.
SOURCEi Search...

Gene expression databases

Bgeei Q9D1J3.
CleanExi MM_1110005A23RIK.
Genevestigatori Q9D1J3.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c, C57BL/6J and NOD.
    Tissue: Cerebellum, Embryo and Thymus.
  2. "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: Mammary gland.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-10 AND LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSARNP_MOUSE
AccessioniPrimary (citable) accession number: Q9D1J3
Secondary accession number(s): Q3UJZ4, Q9CU18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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