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Protein

Chromatin target of PRMT1 protein

Gene

CHTOP

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

Functioni

Plays an important role in the ligand-dependent activation of estrogen receptor target genes (PubMed:19858291). May play a role in the silencing of fetal globin genes (PubMed:20688955). Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (By similarity). Plays an important role in the tumorigenicity of glioblastoma cells. Binds to 5-hydroxymethylcytosine (5hmC) and associates with the methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-methylosome complex associated with 5hmC is recruited to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis (PubMed:25284789).By similarity3 Publications
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 (PubMed:23299939).1 Publication

GO - Molecular functioni

  • methyl-CpG binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • positive regulation of ATPase activity Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of helicase activity Source: UniProtKB
  • positive regulation of histone methylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • RNA export from nucleus Source: Reactome
  • termination of RNA polymerase II transcription Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin target of PRMT1 protein
Alternative name(s):
Friend of PRMT1 protein
Small arginine- and glycine-rich protein
Short name:
SRAG
Gene namesi
Name:CHTOP
Synonyms:C1orf77, FOP
ORF Names:HT031, PP7704
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24511. CHTOP.

Subcellular locationi

  • Nucleus 1 Publication
  • Nucleusnucleolus 1 Publication
  • Nucleusnucleoplasm 1 Publication
  • Nucleus speckle 2 Publications

  • 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 (PubMed:23826332).By similarity1 Publication

GO - Cellular componenti

  • intracellular membrane-bounded organelle Source: HPA
  • nuclear speck Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • transcription export complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi195 – 1951R → A: Loss of 5hmc binding; when associated with A-197; A-199; A-201 and A-203. 1 Publication
Mutagenesisi197 – 1971R → A: Loss of 5hmc binding; when associated with A-195; A-199; A-201 and A-203. 1 Publication
Mutagenesisi199 – 1991R → A: Loss of 5hmc binding; when associated with A-195; A-197; A-201 and A-203. 1 Publication
Mutagenesisi201 – 2011R → A: Loss of 5hmc binding; when associated with A-195; A-197; A-199 and A-203. 1 Publication
Mutagenesisi203 – 2031R → A: Loss of 5hmc binding; when associated with A-195; A-197; A-199 and A-201. 1 Publication

Organism-specific databases

PharmGKBiPA142672526.

Polymorphism and mutation databases

BioMutaiCHTOP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 248247Chromatin target of PRMT1 proteinPRO_0000089263Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei33 – 331PhosphothreonineCombined sources
Modified residuei242 – 2421PhosphothreonineCombined sources

Post-translational modificationi

Asymmetrically methylated by PRMT1 (PubMed:25284789). Symmetrically methylated by PRMT5 (By similarity).By similarity1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9Y3Y2.
MaxQBiQ9Y3Y2.
PaxDbiQ9Y3Y2.
PRIDEiQ9Y3Y2.

PTM databases

iPTMnetiQ9Y3Y2.
PhosphoSiteiQ9Y3Y2.

Expressioni

Tissue specificityi

Expressed in an erythroid progenitor cell line derived from peripheral blood. Expressed in glioblastoma cells (PubMed:25284789).2 Publications

Gene expression databases

BgeeiQ9Y3Y2.
CleanExiHS_C1orf77.
ExpressionAtlasiQ9Y3Y2. baseline and differential.
GenevisibleiQ9Y3Y2. HS.

Organism-specific databases

HPAiHPA028647.
HPA030540.

Interactioni

Subunit structurei

Interacts with PRMT1 and PRMT5 (PubMed:25284789). 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 (By similarity). 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 (PubMed:23299939, PubMed:23826332). Interacts with WDR77 and ERH (PubMed:25284789).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALYREFQ86V818EBI-347794,EBI-347640
DDX39BQ138386EBI-347794,EBI-348622
ERHP840903EBI-347794,EBI-711389
KHDRBS2Q5VWX13EBI-347794,EBI-742808
NXF1Q9UBU99EBI-347794,EBI-398874
PRMT1Q998732EBI-347794,EBI-78738
SMN2Q166373EBI-347794,EBI-395421

Protein-protein interaction databases

BioGridi117547. 46 interactions.
IntActiQ9Y3Y2. 35 interactions.
MINTiMINT-3048425.
STRINGi9606.ENSP00000357683.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3Y2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni153 – 20654Interaction with PRMT1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi194 – 20310GAR motif; involved in 5hmC binding1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi87 – 208122Arg/Gly-richAdd
BLAST

Phylogenomic databases

eggNOGiENOG410IWUS. Eukaryota.
ENOG4111XP9. LUCA.
GeneTreeiENSGT00390000002869.
HOVERGENiHBG058458.
InParanoidiQ9Y3Y2.
OMAiVSIRATM.
OrthoDBiEOG747PM2.
PhylomeDBiQ9Y3Y2.
TreeFamiTF331447.

Family and domain databases

InterProiIPR025715. FoP_C.
[Graphical view]
PfamiPF13865. FoP_duplication. 1 hit.
[Graphical view]
SMARTiSM01218. FoP_duplication. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y3Y2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAQSAPKVV LKSTTKMSLN ERFTNMLKNK QPTPVNIRAS MQQQQQLASA
60 70 80 90 100
RNRRLAQQME NRPSVQAALK LKQSLKQRLG KSNIQARLGR PIGALARGAI
110 120 130 140 150
GGRGLPIIQR GLPRGGLRGG RATRTLLRGG MSLRGQNLLR GGRAVAPRMG
160 170 180 190 200
LRRGGVRGRG GPGRGGLGRG AMGRGGIGGR GRGMIGRGRG GFGGRGRGRG
210 220 230 240
RGRGALARPV LTKEQLDNQL DAYMSKTKGH LDAELDAYMA QTDPETND
Length:248
Mass (Da):26,397
Last modified:October 11, 2004 - v2
Checksum:i3D97D16610FCE0E6
GO
Isoform 2 (identifier: Q9Y3Y2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-73: Q → QK

Note: No experimental confirmation available.
Show »
Length:249
Mass (Da):26,525
Checksum:i938006D98E4F28FE
GO
Isoform 3 (identifier: Q9Y3Y2-4) [UniParc]FASTAAdd to basket

Also known as: SRAG-5

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

Show »
Length:202
Mass (Da):21,918
Checksum:i20AEC438CB993D76
GO

Sequence cautioni

The sequence AAH02733.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH70027.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL55869.1 differs from that shown. Reason: Frameshift at position 181. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721K → N in AAH59949 (PubMed:15489334).Curated
Sequence conflicti180 – 1801R → P in CAB43362 (PubMed:17974005).Curated
Sequence conflicti238 – 2381Y → H in CAB43362 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei73 – 731Q → QK in isoform 2. 1 PublicationVSP_017277
Alternative sequencei134 – 17946Missing in isoform 3. CuratedVSP_040496Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1048.1. [Q9Y3Y2-1]
CCDS72917.1. [Q9Y3Y2-3]
PIRiT08660.
RefSeqiNP_001193541.1. NM_001206612.1. [Q9Y3Y2-3]
NP_001231593.1. NM_001244664.1.
NP_001304006.1. NM_001317077.1. [Q9Y3Y2-4]
NP_056422.2. NM_015607.3. [Q9Y3Y2-1]
UniGeneiHs.611057.

Genome annotation databases

EnsembliENST00000368690; ENSP00000357679; ENSG00000160679. [Q9Y3Y2-3]
ENST00000368694; ENSP00000357683; ENSG00000160679. [Q9Y3Y2-1]
ENST00000403433; ENSP00000385228; ENSG00000160679. [Q9Y3Y2-4]
GeneIDi26097.
KEGGihsa:26097.
UCSCiuc001fcm.3. human. [Q9Y3Y2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1048.1. [Q9Y3Y2-1]
CCDS72917.1. [Q9Y3Y2-3]
PIRiT08660.
RefSeqiNP_001193541.1. NM_001206612.1. [Q9Y3Y2-3]
NP_001231593.1. NM_001244664.1.
NP_001304006.1. NM_001317077.1. [Q9Y3Y2-4]
NP_056422.2. NM_015607.3. [Q9Y3Y2-1]
UniGeneiHs.611057.

3D structure databases

ProteinModelPortaliQ9Y3Y2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117547. 46 interactions.
IntActiQ9Y3Y2. 35 interactions.
MINTiMINT-3048425.
STRINGi9606.ENSP00000357683.

PTM databases

iPTMnetiQ9Y3Y2.
PhosphoSiteiQ9Y3Y2.

Polymorphism and mutation databases

BioMutaiCHTOP.

Proteomic databases

EPDiQ9Y3Y2.
MaxQBiQ9Y3Y2.
PaxDbiQ9Y3Y2.
PRIDEiQ9Y3Y2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368690; ENSP00000357679; ENSG00000160679. [Q9Y3Y2-3]
ENST00000368694; ENSP00000357683; ENSG00000160679. [Q9Y3Y2-1]
ENST00000403433; ENSP00000385228; ENSG00000160679. [Q9Y3Y2-4]
GeneIDi26097.
KEGGihsa:26097.
UCSCiuc001fcm.3. human. [Q9Y3Y2-1]

Organism-specific databases

CTDi26097.
GeneCardsiCHTOP.
H-InvDBHIX0001086.
HGNCiHGNC:24511. CHTOP.
HPAiHPA028647.
HPA030540.
MIMi614206. gene.
neXtProtiNX_Q9Y3Y2.
PharmGKBiPA142672526.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWUS. Eukaryota.
ENOG4111XP9. LUCA.
GeneTreeiENSGT00390000002869.
HOVERGENiHBG058458.
InParanoidiQ9Y3Y2.
OMAiVSIRATM.
OrthoDBiEOG747PM2.
PhylomeDBiQ9Y3Y2.
TreeFamiTF331447.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-72187. mRNA 3'-end processing.

Miscellaneous databases

ChiTaRSiCHTOP. human.
GenomeRNAii26097.
PROiQ9Y3Y2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3Y2.
CleanExiHS_C1orf77.
ExpressionAtlasiQ9Y3Y2. baseline and differential.
GenevisibleiQ9Y3Y2. HS.

Family and domain databases

InterProiIPR025715. FoP_C.
[Graphical view]
PfamiPF13865. FoP_duplication. 1 hit.
[Graphical view]
SMARTiSM01218. FoP_duplication. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: FUNCTION, IDENTIFICATION IN THE TREX COMPLEX, METHYLATION, SUBCELLULAR LOCATION, INTERACTION WITH NXF1; DDX39B AND ALYREF.
  15. "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.
  16. Cited for: FUNCTION, INTERACTION WITH PRMT1; PRMT5; WDR77 AND ERH, METHYLATION, MUTAGENESIS OF ARG-195; ARG-197; ARG-199; ARG-201 AND ARG-203.

Entry informationi

Entry nameiCHTOP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3Y2
Secondary accession number(s): D3DV55
, Q0VAQ8, Q2VPI9, Q5T7Y8, Q5T7Y9, Q5T7Z0, Q6NSM4, Q6PB28, Q8WYT9, Q9BUC5, Q9H034, Q9H2L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 129 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.