Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q07666 (KHDR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
KH domain-containing, RNA-binding, signal transduction-associated protein 1
Alternative name(s):
GAP-associated tyrosine phosphoprotein p62
Src-associated in mitosis 68 kDa protein
Short name=Sam68
p21 Ras GTPase-activating protein-associated p62
p68
Gene names
Name:KHDRBS1
Synonyms:SAM68
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (Ref.28). Ref.1 Ref.2 Ref.8 Ref.11 Ref.26 Ref.28 UniProtKB Q60749 UniProtKB Q8UUW7

Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. Ref.2 Ref.8 Ref.11 Ref.26 Ref.28

Subunit structure

Self-associates to form homooligomers 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. Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA. Interacts with PTK6 (via SH3 and SH2 domains). Does not interact with TPR. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.17 Ref.28

Subcellular location

Nucleus. Membrane Ref.1 Ref.10 Ref.12 Ref.15.

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. Ref.2

Developmental stage

Isoform 3 is only expressed in growth-arrested cells. Ref.2

Domain

The KH domain is required for binding to RNA By similarity. UniProtKB Q60749

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 methylation on these motifs can modulate protein-protein interactions By similarity. UniProtKB Q91V33

Post-translational modification

Tyrosine phosphorylated by several non-receptor tyrosine kinases, LCK, FYN and JAK3. Negatively correlates with ability to bind RNA but required for many interactions with proteins. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nulear localization of KHDRBS1. Ref.8 Ref.11 Ref.15

Acetylated. Positively correlates with ability to bind RNA. Ref.14

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. Ref.12 Ref.13

Arg-291, Arg-331 and Arg-346 are found to be also dimethylated, probably to asymmetric dimethylarginine. Ref.1 Ref.7 Ref.12 Ref.13

Sequence similarities

Belongs to the KHDRBS family.

Contains 1 KH domain.

Sequence caution

The sequence AAH10132.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentMembrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainSH3-binding
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle arrest

Traceable author statement Ref.2. Source: ProtInc

cell proliferation

Traceable author statement Ref.2. Source: ProtInc

cell surface receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

mRNA processing

Traceable author statement Ref.1. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of RNA export from nucleus

Inferred from direct assay Ref.26. Source: UniProtKB

positive regulation of signal transduction

Inferred from physical interaction Ref.8. Source: GOC

positive regulation of translational initiation

Inferred from direct assay Ref.26. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGrb2-Sos complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) binding

Inferred from direct assay PubMed 21984414. Source: MGI

poly(U) RNA binding

Inferred from direct assay PubMed 21984414. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q07666-1)

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: Q07666-2)

The sequence of this isoform differs from the canonical sequence as follows:
     37-61: Missing.
Note: No experimental confirmation available.
Isoform 3 Ref.2 (identifier: Q07666-3)

Also known as: DeltaKH;

The sequence of this isoform differs from the canonical sequence as follows:
     169-207: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443KH domain-containing, RNA-binding, signal transduction-associated protein 1
PRO_0000050124

Regions

Domain171 – 19727KH
Compositional bias34 – 418Pro-rich
Compositional bias44 – 5512DMA/Gly-rich
Compositional bias59 – 8931Pro-rich
Compositional bias282 – 29211DMA/Gly-rich
Compositional bias295 – 3017Pro-rich
Compositional bias302 – 33231Arg/Gly-rich
Compositional bias334 – 36330Pro-rich

Amino acid modifications

Modified residue201Phosphoserine Ref.16 Ref.21 PubMed 16083285
Modified residue291Phosphoserine Ref.21
Modified residue451Asymmetric dimethylarginine; by PRMT1 Ref.12
Modified residue521Asymmetric dimethylarginine; partial; by PRMT1 Ref.12
Modified residue581Phosphoserine Ref.20
Modified residue1131Phosphoserine By similarity UniProtKB Q60749
Modified residue1751N6-acetyllysine Ref.23
Modified residue2911Omega-N-methylated arginine; by PRMT1 Ref.13
Modified residue3041Asymmetric dimethylarginine; by PRMT1 Ref.12
Modified residue3101Omega-N-methylarginine; by PRMT1 Ref.12
Modified residue3151Omega-N-methylarginine; by PRMT1 Ref.12
Modified residue3201Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.7 Ref.12
Modified residue3201Omega-N-methylarginine; by PRMT1 Ref.7 Ref.12
Modified residue3251Omega-N-methylarginine; by PRMT1 Ref.12 Ref.13
Modified residue3311Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.7
Modified residue3311Omega-N-methylated arginine; by PRMT1 Ref.7 Ref.13
Modified residue3401Omega-N-methylarginine; by PRMT1 Ref.7 Ref.13
Modified residue3461Omega-N-methylated arginine; by PRMT1 Ref.13
Modified residue4351Phosphotyrosine; by PTK6 Ref.15
Modified residue4401Phosphotyrosine; by PTK6 Ref.15
Modified residue4431Phosphotyrosine; by PTK6 Ref.15

Natural variations

Alternative sequence37 – 6125Missing in isoform 2.
VSP_051719
Alternative sequence169 – 20739Missing in isoform 3. Ref.2
VSP_051720

Experimental info

Mutagenesis4351Y → F: No effect on the nuclear localization. Ref.15
Mutagenesis4401Y → F: Completely blocks nuclear localization. Ref.15
Mutagenesis4431Y → F: No effect on the nuclear localization. Ref.15

Secondary structure

..... 443
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 59FB4DB6FB4DBE98

FASTA44348,227
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 36B5B877E35D9A2C
Show »

FASTA41845,861
Isoform 3 (DeltaKH) [UniParc].

Checksum: 0E6334E3447CCA5F
Show »

FASTA40444,027

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62."
Wong G., Muller O., Clark R., Conroy L., Moran M.F., Polakis P., McCormick F.
Cell 69:551-558(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, RNA-BINDING, METHYLATION, INTERACTION WITH RASA1.
Tissue: Fetal brain.
[2]"A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain."
Barlat I., Maurier F., Duchesne M., Guitard E., Tocque B., Schweighoffer F.
J. Biol. Chem. 272:3129-3132(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Placenta.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"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].
[5]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].
[6]"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 1).
Tissue: Lymph and Placenta.
[7]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 18-31; 57-96; 103-131; 139-152; 176-185; 292-302 AND 316-340, METHYLATION AT ARG-320; ARG-331 AND ARG-340, MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[8]"Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling."
Fusaki N., Iwamatsu A., Iwashima M., Fujisawa J.
J. Biol. Chem. 272:6214-6219(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 102-110 AND 169-175 (ISOFORMS 1/2), FUNCTION, PHOSPHORYLATION, INTERACTION WITH LCK; FYN; PTPN6; PLCG1; GRB2; CBL; JAK3 AND PIK3R1.
[9]"T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis."
Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J., Cooke H.J., Artzt K., Eperon I.C.
Hum. Mol. Genet. 8:959-969(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KHDRBS3.
Tissue: Testis.
[10]"Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding ability."
Derry J.J., Richard S., Valderrama Carvajal H., Ye X., Vasioukhin V., Cochrane A.W., Chen T., Tyner A.L.
Mol. Cell. Biol. 20:6114-6126(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PTK6.
[11]"Human leptin signaling in human peripheral blood mononuclear cells: activation of the JAK-STAT pathway."
Sanchez-Margalet V., Martin-Romero C.
Cell. Immunol. 211:30-36(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STAT3.
[12]"Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1."
Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.
Mol. Biol. Cell 14:274-287(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 AND ARG-325, SUBCELLULAR LOCATION.
[13]"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC."
Ong S.E., Mittler G., Mann M.
Nat. Methods 1:119-126(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity."
Babic I., Jakymiw A., Fujita D.J.
Oncogene 23:3781-3789(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION, INTERACTION WITH RNA.
[15]"Tyrosine phosphorylation of sam68 by breast tumor kinase regulates intranuclear localization and cell cycle progression."
Lukong K.E., Larocque D., Tyner A.L., Richard S.
J. Biol. Chem. 280:38639-38647(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-435; TYR-440 AND TYR-443, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-435; TYR-440 AND TYR-443.
[16]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; RBMX; NCOA5 AND PPP1CA.
[18]"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."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"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].
[26]"The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway."
Coyle J.H., Bor Y.C., Rekosh D., Hammarskjold M.L.
RNA 17:1344-1356(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA."
Rajanala K., Nandicoori V.K.
PLoS ONE 7:E29921-E29921(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ABSENCE OF FUNCTION IN UNSPLICED RNA EXPORT, ABSENCE OF INTERACTION WITH TPR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88108 mRNA. Translation: AAA59990.1.
U78971 mRNA. Translation: AAB47504.1.
AK091346 mRNA. Translation: BAC03643.1.
AL139249, AL445248 Genomic DNA. Translation: CAI21971.1.
AL139249, AL445248 Genomic DNA. Translation: CAI21972.1.
AL445248, AL139249 Genomic DNA. Translation: CAH71944.1.
AL445248, AL139249 Genomic DNA. Translation: CAH71945.1.
CH471059 Genomic DNA. Translation: EAX07576.1.
CH471059 Genomic DNA. Translation: EAX07577.1.
BC000717 mRNA. Translation: AAH00717.1.
BC010132 mRNA. Translation: AAH10132.1. Sequence problems.
BC019109 mRNA. Translation: AAH19109.1.
PIRA38219.
RefSeqNP_001258807.1. NM_001271878.1.
NP_006550.1. NM_006559.2.
UniGeneHs.445893.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XA6NMR-A/B97-135[»]
3QHEX-ray2.40B/D365-419[»]
ProteinModelPortalQ07666.
SMRQ07666. Positions 67-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115900. 127 interactions.
DIPDIP-29007N.
IntActQ07666. 64 interactions.
MINTMINT-102826.
STRING9606.ENSP00000313829.

Chemistry

BindingDBQ07666.
ChEMBLCHEMBL1795190.

PTM databases

PhosphoSiteQ07666.

Polymorphism databases

DMDM62511098.

Proteomic databases

PaxDbQ07666.
PRIDEQ07666.

Protocols and materials databases

DNASU10657.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327300; ENSP00000313829; ENSG00000121774. [Q07666-1]
ENST00000492989; ENSP00000417731; ENSG00000121774. [Q07666-3]
GeneID10657.
KEGGhsa:10657.
UCSCuc001bua.2. human. [Q07666-3]
uc001bub.4. human. [Q07666-1]

Organism-specific databases

CTD10657.
GeneCardsGC01P032479.
HGNCHGNC:18116. KHDRBS1.
HPACAB005355.
HPA051280.
HPA056813.
MIM602489. gene.
neXtProtNX_Q07666.
PharmGKBPA30092.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5176.
HOGENOMHOG000230771.
HOVERGENHBG079164.
InParanoidQ07666.
KOK13198.
OMAFMELSYL.
OrthoDBEOG75MVX3.
PhylomeDBQ07666.
TreeFamTF314878.

Enzyme and pathway databases

SignaLinkQ07666.

Gene expression databases

ArrayExpressQ07666.
BgeeQ07666.
CleanExHS_KHDRBS1.
GenevestigatorQ07666.

Family and domain databases

InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamPF00013. KH_1. 1 hit.
[Graphical view]
SMARTSM00322. KH. 1 hit.
[Graphical view]
PROSITEPS50084. KH_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKHDRBS1. human.
EvolutionaryTraceQ07666.
GeneWikiKHDRBS1.
GenomeRNAi10657.
NextBio40517.
PMAP-CutDBQ07666.
PROQ07666.
SOURCESearch...

Entry information

Entry nameKHDR1_HUMAN
AccessionPrimary (citable) accession number: Q07666
Secondary accession number(s): D3DPP3 expand/collapse secondary AC list , Q6PJX7, Q8NB97, Q99760
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 141 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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