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Q9D1J3 (SARNP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SAP domain-containing ribonucleoprotein
Alternative name(s):
Nuclear protein Hcc-1
Gene names
Name:Sarnp
Synonyms:Hcc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

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 By similarity.

Subcellular location

Nucleus By similarity. Nucleus speckle By similarity.

Sequence similarities

Contains 1 SAP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 210209SAP domain-containing ribonucleoprotein
PRO_0000083919

Regions

Domain8 – 4235SAP

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue101N6-acetyllysine Ref.3
Modified residue1421N6-acetyllysine Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9D1J3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 15705691F989E9AB

FASTA21023,533
        10         20         30         40         50         60 
MAAETVELHK LKLAELKQEC LARGLETKGI KQDLINRLQA YLEDHAEEEA NEEDVLGDET 

        70         80         90        100        110        120 
EEEEPKPIEL PVKEEEPPEK AVDMASEKKV VKITSGIPQT ERMQKRAERF NVPVSLESKK 

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

       190        200        210 
FGIVTSSAGT GTTEDTEAKK RKRAERFGIA 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS36092.1.
RefSeqNP_079640.1. NM_025364.2.
UniGeneMm.351579.

3D structure databases

ProteinModelPortalQ9D1J3.
SMRQ9D1J3. Positions 6-47.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9D1J3. 1 interaction.
MINTMINT-1867986.
STRING10090.ENSMUSP00000100863.

PTM databases

PhosphoSiteQ9D1J3.

Proteomic databases

MaxQBQ9D1J3.
PaxDbQ9D1J3.
PRIDEQ9D1J3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056396; ENSMUSP00000137244; ENSMUSG00000051255.
ENSMUST00000105230; ENSMUSP00000100863; ENSMUSG00000078427.
GeneID66118.
KEGGmmu:66118.
UCSCuc007hor.2. mouse.

Organism-specific databases

CTD84324.
MGIMGI:1913368. Sarnp.

Phylogenomic databases

eggNOGNOG290157.
GeneTreeENSGT00390000002944.
HOGENOMHOG000013054.
InParanoidQ9D1J3.
OMASDAKPMV.
OrthoDBEOG7J9VRJ.
PhylomeDBQ9D1J3.
TreeFamTF319843.

Gene expression databases

BgeeQ9D1J3.
CleanExMM_1110005A23RIK.
GenevestigatorQ9D1J3.

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

NextBio320682.
PROQ9D1J3.
SOURCESearch...

Entry information

Entry nameSARNP_MOUSE
AccessionPrimary (citable) accession number: Q9D1J3
Secondary accession number(s): Q3UJZ4, Q9CU18
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot