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UniProtKB/Swiss-Prot entry Q07666


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KHDR1_HUMAN
Primary accession number Q07666
Secondary accession numbers Q6PJX7 Q8NB97 Q99760
Integrated into Swiss-Prot on April 12, 2005
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 79)
Name and origin of the protein
Protein name KH domain-containing, RNA-binding, signal transduction-associated protein 1
Synonyms p21 Ras GTPase-activating protein-associated p62
GAP-associated tyrosine phosphoprotein p62
Src-associated in mitosis 68 kDa protein
Sam68
p68
Gene name
Name: KHDRBS1
Synonyms: SAM68
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, RNA-BINDING, METHYLATION, AND INTERACTION WITH RASA1.
TISSUE=Fetal brain;
DOI=10.1016/0092-8674(92)90455-L; PubMed=1374686 [NCBI, ExPASy, EBI, Israel, Japan]
Wong G., Muller O., Clark R., Conroy L., Moran M.F., Polakis P., McCormick F.;
"Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62.";
Cell 69:551-558(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Placenta;
DOI=10.1074/jbc.272.6.3129; PubMed=9013542 [NCBI, ExPASy, EBI, Israel, Japan]
Barlat I., Maurier F., Duchesne M., Guitard E., Tocque B., Schweighoffer F.;
"A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain.";
J. Biol. Chem. 272:3129-3132(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 102-110 AND 169-175 (ISOFORMS 1/2), FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH LCK; FYN; PTPN6; PLCG1; GRB2; CBL; JAK3 AND PIK3R1.
DOI=10.1074/jbc.272.10.6214; PubMed=9045636 [NCBI, ExPASy, EBI, Israel, Japan]
Fusaki N., Iwamatsu A., Iwashima M., Fujisawa J.;
"Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling.";
J. Biol. Chem. 272:6214-6219(1997).
[7]
INTERACTION WITH KHDRBS3.
TISSUE=Testis;
DOI=10.1093/hmg/8.6.959; PubMed=10332027 [NCBI, ExPASy, EBI, Israel, Japan]
Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J., Cooke H.J., Artzt K., Eperon I.C.;
"T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis.";
Hum. Mol. Genet. 8:959-969(1999).
[8]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH STAT3.
DOI=10.1006/cimm.2001.1815; PubMed=11585385 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez-Margalet V., Martin-Romero C.;
"Human leptin signaling in human peripheral blood mononuclear cells: activation of the JAK-STAT pathway.";
Cell. Immunol. 211:30-36(2001).
[9]
METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 AND ARG-325, AND SUBCELLULAR LOCATION.
DOI=10.1091/mbc.E02-08-0484; PubMed=12529443 [NCBI, ExPASy, EBI, Israel, Japan]
Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.;
"Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1.";
Mol. Biol. Cell 14:274-287(2003).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-291; ARG-325; ARG-331; ARG-340 AND ARG-346, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[11]
ACETYLATION, AND INTERACTION WITH RNA.
DOI=10.1038/sj.onc.1207484; PubMed=15021911 [NCBI, ExPASy, EBI, Israel, Japan]
Babic I., Jakymiw A., Fujita D.J.;
"The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity.";
Oncogene 23:3781-3789(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-20, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-33, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
Comments
  • FUNCTION: Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.
  • FUNCTION: Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.
  • SUBUNIT: Self-associates to form homo-oligomers when bound to RNA, oligomerization appears to be limited when binding to proteins. Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1, PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN through the Arg/Gly-rich-flanked Pro-rich regions (By similarity).
  • INTERACTION:
    P22681:CBL; NbExp=1; IntAct=EBI-1364, EBI-518228;
    P46108-1:CRK; NbExp=1; IntAct=EBI-1364, EBI-287556;
    P06241:FYN; NbExp=2; IntAct=EBI-1364, EBI-515315;
    P62993:GRB2; NbExp=2; IntAct=EBI-1364, EBI-401755;
    P08631:HCK; NbExp=2; IntAct=EBI-1364, EBI-346340;
    P52333:JAK3; NbExp=1; IntAct=EBI-1364, EBI-518246;
    P06239:LCK; NbExp=3; IntAct=EBI-1364, EBI-1348;
    P06240:Lck (xeno); NbExp=1; IntAct=EBI-1364, EBI-1401;
    P07948:LYN; NbExp=1; IntAct=EBI-1364, EBI-79452;
    P19174:PLCG1; NbExp=1; IntAct=EBI-1364, EBI-79387;
    P29350:PTPN6; NbExp=1; IntAct=EBI-1364, EBI-78260;
    P51531:SMARCA2; NbExp=2; IntAct=EBI-1364, EBI-679562;
    P40763:STAT3; NbExp=1; IntAct=EBI-1364, EBI-518675;
  • SUBCELLULAR LOCATION: Nucleus. Membrane.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ07666-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ07666-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_051719.
    Name3
    SynonymsDeltaKH
    Isoform IDQ07666-3
    Features which should be applied to build the isoform sequence: VSP_051720.
  • TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined. Isoform 1 is expressed at lower levels in brain, skeletal muscle, and liver whereas isoform 3 is intensified in skeletal muscle and in liver.
  • DEVELOPMENTAL STAGE: Isoform 3 is only expressed in growth-arrested cells.
  • DOMAIN: The KH domain is required for binding to RNA (By similarity).
  • DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs which can be asymmetric dimethylated on arginine residues to give the DMA/Gly-rich regions. Selective methlylation on these motifs can modulate protein-protein interactions (By similarity).
  • PTM: Tyrosine phosphorylated by several non-receptor tyrosine kinases, for example LCK, FYN and JAK3. Negatively correlates with ability to bind RNA but required for many interactions with proteins.
  • PTM: Acetylated. Positively correlates with ability to bind RNA.
  • PTM: Arginine methylation is required for nuclear localization. Also can affect interaction with other proteins. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30.
  • PTM: Arg-291, Arg-331 and Arg-346 are found to be also dimethylated, probably to asymmetric dimethylarginine.
  • SIMILARITY: Belongs to the KHDRBS family.
  • SIMILARITY: Contains 1 KH domain.
  • SEQUENCE CAUTION:
    • Sequence=AAH10132.1; Type=Miscellaneous discrepancy; Note=Intron retention
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M88108; AAA59990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U78971; AAB47504.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK091346; BAC03643.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139249; CAI21971.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445248; CAI21971.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139249; CAI21972.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445248; CAI21972.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445248; CAH71944.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139249; CAH71944.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445248; CAH71945.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139249; CAH71945.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000717; AAH00717.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010132; AAH10132.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019109; AAH19109.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A38219; A38219.
RefSeq NP_006550.1; -.
UniGene Hs.445893
3D structure databases
HSSP Q9UNW9; 1DTJ. [HSSP ENTRY / PDB]
ModBase Q07666.
Protein-protein interaction databases
DIP DIP:29007N; -.
IntAct Q07666; -.
PTM databases
PhosphoSite Q07666; -.
Organism-specific databases
H-InvDB HIX0000361; -.
HGNC HGNC:18116; KHDRBS1.
GenAtlas KHDRBS1.
HPA CAB005355; -.
MIM 602489; gene. [NCBI / EBI]
PharmGKB PA30092; -.
GeneCards Q07666.
Gene expression databases
ArrayExpress Q07666; -.
CleanEx HS_KHDRBS1; -.
GermOnline ENSG00000121774; Homo sapiens.
Ontologies
GO
GO:0016020; Cellular component: membrane (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0005070; Molecular function: SH3/SH2 adaptor activity (inferred from physical interaction from UniProtKB).
GO:0016564; Molecular function: transcription repressor activity (inferred from sequence or structural similarity from UniProtKB).
GO:0007050; Biological process: cell cycle arrest (traceable author statement from ProtInc).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0007166; Biological process: cell surface receptor linked signal transduction (inferred from direct assay from UniProtKB).
GO:0000086; Biological process: G2/M transition of mitotic cell cycle (inferred from sequence or structural similarity from UniProtKB).
GO:0006397; Biological process: mRNA processing (traceable author statement from ProtInc).
GO:0016481; Biological process: negative regulation of transcription (inferred from sequence or structural similarity from UniProtKB).
GO:0046831; Biological process: regulation of RNA export from nucleus (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004087; KH.
IPR004088; KH_type_1.
Graphical view of domain structure.
Pfam PF00013; KH_1; 1.
Pfam graphical view of domain structure.
SMART SM00322; KH; 1.
SMART graphical view of domain structure.
PROSITE PS50084; KH_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q07666.
Genome annotation databases
Ensembl ENSG00000121774; Homo sapiens. [Contig view]
GeneID 10657; -.
KEGG hsa:10657; -.
Phylogenomic databases
HOGENOM Q07666; -.
HOVERGEN Q07666; -.
Other
SOURCE KHDRBS1; Homo sapiens.
ProtoNet Q07666.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative splicing; Cell cycle; Direct protein sequencing; Membrane; Methylation; Nucleus; Phosphoprotein; RNA-binding; SH3-binding; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   443  443     KH domain-containing, RNA-binding, signal transduction-associated protein 1. PRO_0000050124
DOMAIN   171   197  27     KH. 
COMPBIAS   34    41  8     Pro-rich. 
COMPBIAS   44    55  12     DMA/Gly-rich. 
COMPBIAS   59    89  31     Pro-rich. 
COMPBIAS   282   292  11     DMA/Gly-rich. 
COMPBIAS   295   301  7     Pro-rich. 
COMPBIAS   302   332  31     Arg/Gly-rich. 
COMPBIAS   334   363  30     Pro-rich. 
MOD_RES   18    18        Phosphoserine. 
MOD_RES   20    20        Phosphoserine. 
MOD_RES   33    33        Phosphothreonine. 
MOD_RES   45    45        Asymmetric dimethylarginine; by PRMT1. 
MOD_RES   52    52        Asymmetric dimethylarginine; partial; by PRMT1. 
MOD_RES   113   113        Phosphoserine (By similarity). 
MOD_RES   291   291        Omega-N-methylated arginine; by PRMT1. 
MOD_RES   304   304        Asymmetric dimethylarginine; by PRMT1. 
MOD_RES   310   310        Omega-N-methylarginine; by PRMT1. 
MOD_RES   315   315        Omega-N-methylarginine; by PRMT1. 
MOD_RES   320   320        Omega-N-methylarginine; by PRMT1. 
MOD_RES   325   325        Omega-N-methylarginine; by PRMT1. 
MOD_RES   331   331        Omega-N-methylated arginine; by PRMT1. 
MOD_RES   340   340        Omega-N-methylarginine; by PRMT1. 
MOD_RES   346   346        Omega-N-methylated arginine; by PRMT1. 
VAR_SEQ   37    61        Missing (in isoform 2). VSP_051719
VAR_SEQ   169   207        Missing (in isoform 3). VSP_051720
Sequence information
Length: 443 AA [This is the length of the unprocessed precursor] Molecular weight: 48227 Da [This is the MW of the unprocessed precursor] CRC64: 59FB4DB6FB4DBE98 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG SRGGARASPA 

        70         80         90        100        110        120 
TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE NKYLPELMAE KDSLDPSFTH 

       130        140        150        160        170        180 
AMQLLTAEIE KIQKGDSKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ 

       190        200        210        220        230        240 
GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA 

       250        260        270        280        290        300 
YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV 

       310        320        330        340        350        360 
PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA GIQRIPLPPP 

       370        380        390        400        410        420 
PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG HGEVQDSYEA YGQDDWNGTR 

       430        440 
PSLKAPPARP VKGAYREHPY GRY 

Q07666 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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