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Q9Y3Y2 (CHTOP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromatin target of PRMT1 protein
Alternative name(s):
Friend of PRMT1 protein
Small arginine- and glycine-rich protein
Short name=SRAG
Gene names
Name:CHTOP
Synonyms:C1orf77, FOP
ORF Names:HT031, PP7704
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the ligand-dependent activation of estrogen receptor target genes. May play a role in the silencing of fetal globin genes. Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Ref.9 Ref.10 Ref.15

Required for effective mRNA nuclear export and is a 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. Stimulates DDX39B ATPase and helicase activities. In cooperation with ALYREF/THOC4 enhances NXF1 RNA binding activity. Ref.9 Ref.10 Ref.15

Subunit structure

Interacts with PRMT1 and PRMT5. Interacts with the 5FMC complex; the interaction is methylation-dependent. Interacts with FYTTD1, SET and PRC1 complex members CBX4, RNF2 and PHC2; the interactions are methylation-independent. Interacts with ZNF148. 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 (methylated) with ALYREF/THOC4 and with DDX39B in a methylation-independent manner. Interacts (methylated) with NXF1; the interaction is mutually exclusive with the NXF1:THOC5 interaction. Ref.15 Ref.16

Subcellular location

Nucleus. Nucleusnucleolus. Nucleusnucleoplasm By similarity. Nucleus speckle. Note: Mostly associated with facultative heterochromatin By similarity. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Ref.8 Ref.15 Ref.16

Tissue specificity

Expressed in an erythroid progenitor cell line derived from peripheral blood. Ref.9

Post-translational modification

Asymmetrically methylated by PRMT1. Symmetrically methylated by PRMT5 By similarity. Ref.15

Sequence caution

The sequence AAH02733.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH70027.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAL55869.1 differs from that shown. Reason: Frameshift at position 181.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT1Q998732EBI-347794,EBI-78738

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y3Y2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y3Y2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     73-73: Q → QK
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9Y3Y2-4)

Also known as: SRAG-5;

The sequence of this isoform differs from the canonical sequence as follows:
     134-179: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 248247Chromatin target of PRMT1 protein
PRO_0000089263

Regions

Region153 – 20654Interaction with PRMT1 By similarity
Compositional bias87 – 208122Arg/Gly-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.14
Modified residue331Phosphothreonine Ref.11 Ref.13
Modified residue2421Phosphothreonine Ref.7 Ref.11

Natural variations

Alternative sequence731Q → QK in isoform 2.
VSP_017277
Alternative sequence134 – 17946Missing in isoform 3.
VSP_040496

Experimental info

Sequence conflict721K → N in AAH59949. Ref.5
Sequence conflict1801R → P in CAB43362. Ref.6
Sequence conflict2381Y → H in CAB43362. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 3D97D16610FCE0E6

FASTA24826,397
        10         20         30         40         50         60 
MAAQSAPKVV LKSTTKMSLN ERFTNMLKNK QPTPVNIRAS MQQQQQLASA RNRRLAQQME 

        70         80         90        100        110        120 
NRPSVQAALK LKQSLKQRLG KSNIQARLGR PIGALARGAI GGRGLPIIQR GLPRGGLRGG 

       130        140        150        160        170        180 
RATRTLLRGG MSLRGQNLLR GGRAVAPRMG LRRGGVRGRG GPGRGGLGRG AMGRGGIGGR 

       190        200        210        220        230        240 
GRGMIGRGRG GFGGRGRGRG RGRGALARPV LTKEQLDNQL DAYMSKTKGH LDAELDAYMA 


QTDPETND 

« Hide

Isoform 2 [UniParc].

Checksum: 938006D98E4F28FE
Show »

FASTA24926,525
Isoform 3 (SRAG-5) [UniParc].

Checksum: 20AEC438CB993D76
Show »

FASTA20221,918

References

« Hide 'large scale' references
[1]Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hypothalamus.
[2]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-248 (ISOFORM 1).
Tissue: Eye, Liver, Placenta and Uterus.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-248 (ISOFORM 1).
Tissue: Fetal brain and Lymph node.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Identification of the small protein rich in arginine and glycine (SRAG): a newly identified nucleolar protein that can regulate cell proliferation."
Zullo A.J., Michaud M., Zhang W., Grusby M.J.
J. Biol. Chem. 284:12504-12511(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, RNA-BINDING.
[9]"Fetal globin expression is regulated by Friend of Prmt1."
van Dijk T.B., Gillemans N., Pourfarzad F., van Lom K., von Lindern M., Grosveld F., Philipsen S.
Blood 116:4349-4352(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]"Friend of Prmt1, a novel chromatin target of protein arginine methyltransferases."
van Dijk T.B., Gillemans N., Stein C., Fanis P., Demmers J., van de Corput M., Essers J., Grosveld F., Bauer U.M., Philipsen S.
Mol. Cell. Biol. 30:260-272(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33 AND THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"Chtop is a component of the dynamic TREX mRNA export complex."
Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B., Philipsen S., Wilson S.A.
EMBO J. 32:473-486(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE TREX COMPLEX, METHYLATION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; DDX39B AND ALYREF.
[16]"Mapping interactions between mRNA export factors in living cells."
Teng I.F., Wilson S.A.
PLoS ONE 8:E67676-E67676(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ALYREF AND NXF1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF261137 mRNA. Translation: AAG44673.1.
AF318362 mRNA. Translation: AAL55869.1. Frameshift.
AL162258 Genomic DNA. Translation: CAI19678.1.
AL162258 Genomic DNA. Translation: CAI19679.1.
AL162258 Genomic DNA. Translation: CAI19680.1.
CH471121 Genomic DNA. Translation: EAW53290.1.
CH471121 Genomic DNA. Translation: EAW53295.1.
BC002733 mRNA. Translation: AAH02733.1. Different initiation.
BC059949 mRNA. Translation: AAH59949.1.
BC070027 mRNA. Translation: AAH70027.1. Different initiation.
BC108721 mRNA. Translation: AAI08722.1.
BC120961 mRNA. Translation: AAI20962.1.
BC120962 mRNA. Translation: AAI20963.1.
AL050260 mRNA. Translation: CAB43362.2.
AL512704 mRNA. Translation: CAC21650.2.
PIRT08660.
RefSeqNP_001193541.1. NM_001206612.1.
NP_001231593.1. NM_001244664.1.
NP_056422.2. NM_015607.3.
UniGeneHs.611057.

3D structure databases

ProteinModelPortalQ9Y3Y2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117547. 11 interactions.
IntActQ9Y3Y2. 11 interactions.
MINTMINT-3048425.

PTM databases

PhosphoSiteQ9Y3Y2.

Proteomic databases

PaxDbQ9Y3Y2.
PRIDEQ9Y3Y2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368690; ENSP00000357679; ENSG00000160679. [Q9Y3Y2-4]
ENST00000368694; ENSP00000357683; ENSG00000160679. [Q9Y3Y2-1]
ENST00000403433; ENSP00000385228; ENSG00000160679. [Q9Y3Y2-4]
GeneID26097.
KEGGhsa:26097.
UCSCuc001fcm.2. human. [Q9Y3Y2-1]
uc001fcn.2. human. [Q9Y3Y2-3]

Organism-specific databases

CTD26097.
GeneCardsGC01P153607.
H-InvDBHIX0001086.
HGNCHGNC:24511. CHTOP.
HPAHPA028647.
MIM614206. gene.
neXtProtNX_Q9Y3Y2.
PharmGKBPA142672526.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43697.
HOVERGENHBG058458.
InParanoidQ9Y3Y2.
OMAVSIRATM.
OrthoDBEOG747PM2.
PhylomeDBQ9Y3Y2.
TreeFamTF331447.

Gene expression databases

ArrayExpressQ9Y3Y2.
BgeeQ9Y3Y2.
CleanExHS_C1orf77.
GenevestigatorQ9Y3Y2.

Family and domain databases

InterProIPR025715. FoP_duplication.
[Graphical view]
PfamPF13865. FoP_duplication. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHTOP. human.
GenomeRNAi26097.
NextBio48073.
PROQ9Y3Y2.
SOURCESearch...

Entry information

Entry nameCHTOP_HUMAN
AccessionPrimary (citable) accession number: Q9Y3Y2
Secondary accession number(s): D3DV55 expand/collapse secondary AC list , Q0VAQ8, Q2VPI9, Q5T7Y8, Q5T7Y9, Q5T7Z0, Q6NSM4, Q6PB28, Q8WYT9, Q9BUC5, Q9H034, Q9H2L0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 107 of the entry and version 2 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

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM