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Q60749

- KHDR1_MOUSE

UniProt

Q60749 - KHDR1_MOUSE

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Protein

KH domain-containing, RNA-binding, signal transduction-associated protein 1

Gene
Khdrbs1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. May not be involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species.By similarity3 Publications

GO - Molecular functioni

  1. poly(A) binding Source: MGI
  2. poly(U) RNA binding Source: MGI
  3. protein binding Source: IntAct
  4. RNA binding Source: UniProtKB
  5. SH3/SH2 adaptor activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell surface receptor signaling pathway Source: UniProtKB
  3. negative regulation of transcription, DNA-templated Source: MGI
  4. positive regulation of RNA export from nucleus Source: UniProtKB
  5. positive regulation of signal transduction Source: GOC
  6. positive regulation of translational initiation Source: UniProtKB
  7. regulation of RNA export from nucleus Source: MGI
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Khdrbs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:893579. Khdrbs1.

Subcellular locationi

Nucleus. Membrane 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. Grb2-Sos complex Source: Ensembl
  3. membrane Source: UniProtKB
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443KH domain-containing, RNA-binding, signal transduction-associated protein 1PRO_0000050125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine By similarityBy similarity
Modified residuei21 – 211N6-acetyllysine1 Publication
Modified residuei29 – 291Phosphoserine By similarity
Modified residuei45 – 451Asymmetric dimethylarginine; alternate By similarityBy similarity
Modified residuei45 – 451Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei52 – 521Asymmetric dimethylarginine; alternate By similarityBy similarity
Modified residuei52 – 521Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei58 – 581Phosphoserine By similarity
Modified residuei113 – 1131Phosphoserine1 Publication
Modified residuei175 – 1751N6-acetyllysine By similarity
Modified residuei291 – 2911Omega-N-methylated arginine; by PRMT1 By similarityBy similarity
Modified residuei304 – 3041Asymmetric dimethylarginine; alternate By similarityBy similarity
Modified residuei304 – 3041Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei310 – 3101Omega-N-methylarginine; alternate By similarityBy similarity
Modified residuei310 – 3101Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei315 – 3151Omega-N-methylarginine; alternate By similarityBy similarity
Modified residuei315 – 3151Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei320 – 3201Dimethylated arginine; alternate By similarityBy similarity
Modified residuei320 – 3201Omega-N-methylarginine; alternate By similarity
Modified residuei320 – 3201Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei325 – 3251Omega-N-methylarginine; alternate By similarityBy similarity
Modified residuei325 – 3251Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei331 – 3311Dimethylated arginine; alternate By similarityBy similarity
Modified residuei331 – 3311Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei340 – 3401Omega-N-methylarginine; alternate By similarityBy similarity
Modified residuei340 – 3401Omega-N-methylated arginine; by PRMT1; alternate By similarity
Modified residuei346 – 3461Omega-N-methylated arginine; by PRMT1 By similarityBy similarity
Modified residuei435 – 4351Phosphotyrosine; by PTK6 By similarity
Modified residuei440 – 4401Phosphotyrosine; by PTK6 By similarity
Modified residuei443 – 4431Phosphotyrosine; by PTK6 By similarity

Post-translational modificationi

Tyrosine phosphorylated by several non-receptor tyrosine kinases, LCK, FYN and JAK3. Phosphorylation by PTK6 negatively regulates its RNA binding ability. Phosphorylation by PTK6 at Tyr-440 dictates the nulear localization of KHDRBS1.1 Publication
Acetylated. Positively correlates with ability to bind RNA By similarity.By similarity
Arginine methylation is required for nuclear localization. Inhibits interaction with Src-like SH3 domains, but not interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 By similarity.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ60749.
PaxDbiQ60749.
PRIDEiQ60749.

PTM databases

PhosphoSiteiQ60749.

Expressioni

Gene expression databases

BgeeiQ60749.
GenevestigatoriQ60749.

Interactioni

Subunit structurei

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. Forms a complex with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA By similarity. Interacts with PTK6 (via SH3 and SH2 domains). Does not interact with TPR By similarity.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CrebbpP454817EBI-519077,EBI-296306
FynP3968813EBI-519077,EBI-524514
Prmt1Q9JIF02EBI-519077,EBI-519055

Protein-protein interaction databases

BioGridi203068. 14 interactions.
DIPiDIP-2861N.
IntActiQ60749. 12 interactions.
MINTiMINT-1613905.

Structurei

3D structure databases

ProteinModelPortaliQ60749.
SMRiQ60749. Positions 98-276.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 19727KHAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 418Pro-rich
Compositional biasi44 – 5512Arg/Gly-richAdd
BLAST
Compositional biasi59 – 8931Pro-richAdd
BLAST
Compositional biasi282 – 29211Arg/Gly-richAdd
BLAST
Compositional biasi295 – 3017Pro-rich
Compositional biasi302 – 33231Arg/Gly-richAdd
BLAST
Compositional biasi334 – 36330Pro-richAdd
BLAST

Domaini

The KH domain is required for binding to RNA.1 Publication
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.By similarity

Sequence similaritiesi

Belongs to the KHDRBS family.
Contains 1 KH domain.

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiCOG5176.
GeneTreeiENSGT00550000074434.
HOVERGENiHBG079164.
InParanoidiB2KG38.
KOiK13198.
OMAiFMELSYL.
OrthoDBiEOG75MVX3.
PhylomeDBiQ60749.
TreeFamiTF314878.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60749-1 [UniParc]FASTAAdd to Basket

« Hide

MQRRDDPASR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRPRGGGGG    50
PRGGARASPA TQPPPLLPPS TPGPDATVVG SAPTPLLPPS ATAAVKMEPE 100
NKYLPELMAE KDSLDPSFTH AMQLLSVEIE KIQKGESKKD DEENYLDLFS 150
HKNMKLKERV LIPVKQYPKF NFVGKILGPQ GNTIKRLQEE TGAKISVLGK 200
GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA YALMAHAMEE 250
VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVSVRG RGAAPPPPPV 300
PRGRGVGPPR GALVRGTPVR GSITRGATVT RGVPPPPTVR GAPTPRARTA 350
GIQRIPLPPT PAPETYEDYG YDDTYAEQSY EGYEGYYSQS QGESEYYDYG 400
HGELQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY 443
Length:443
Mass (Da):48,371
Last modified:April 12, 2005 - v2
Checksum:iD33DE960BEA9E5AA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041L → P in AAA64997. 1 Publication
Sequence conflicti147 – 1471D → N AA sequence 1 Publication
Sequence conflicti174 – 1741G → R in AAA86693. 1 Publication
Sequence conflicti197 – 1971V → VS in AAA86693. 1 Publication
Sequence conflicti225 – 2306MDLHVF → LGENGL AA sequence 1 Publication
Sequence conflicti327 – 3271A → S in AAA86693. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17961 mRNA. Translation: AAA86693.1.
U17046 mRNA. Translation: AAA64997.1.
AK050520 mRNA. Translation: BAC34303.1.
AK152084 mRNA. Translation: BAE30934.1.
AL669834 Genomic DNA. Translation: CAM13766.1.
CU210913 Genomic DNA. Translation: CAQ51789.1.
BC002051 mRNA. Translation: AAH02051.1.
CCDSiCCDS18703.1.
PIRiI49140.
S43974.
RefSeqiNP_035447.3. NM_011317.4.
UniGeneiMm.489797.
Mm.8256.

Genome annotation databases

EnsembliENSMUST00000066257; ENSMUSP00000066516; ENSMUSG00000028790.
ENSMUST00000129342; ENSMUSP00000115402; ENSMUSG00000028790.
GeneIDi20218.
KEGGimmu:20218.
UCSCiuc008uyd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U17961 mRNA. Translation: AAA86693.1 .
U17046 mRNA. Translation: AAA64997.1 .
AK050520 mRNA. Translation: BAC34303.1 .
AK152084 mRNA. Translation: BAE30934.1 .
AL669834 Genomic DNA. Translation: CAM13766.1 .
CU210913 Genomic DNA. Translation: CAQ51789.1 .
BC002051 mRNA. Translation: AAH02051.1 .
CCDSi CCDS18703.1.
PIRi I49140.
S43974.
RefSeqi NP_035447.3. NM_011317.4.
UniGenei Mm.489797.
Mm.8256.

3D structure databases

ProteinModelPortali Q60749.
SMRi Q60749. Positions 98-276.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203068. 14 interactions.
DIPi DIP-2861N.
IntActi Q60749. 12 interactions.
MINTi MINT-1613905.

PTM databases

PhosphoSitei Q60749.

Proteomic databases

MaxQBi Q60749.
PaxDbi Q60749.
PRIDEi Q60749.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000066257 ; ENSMUSP00000066516 ; ENSMUSG00000028790 .
ENSMUST00000129342 ; ENSMUSP00000115402 ; ENSMUSG00000028790 .
GeneIDi 20218.
KEGGi mmu:20218.
UCSCi uc008uyd.2. mouse.

Organism-specific databases

CTDi 10657.
MGIi MGI:893579. Khdrbs1.

Phylogenomic databases

eggNOGi COG5176.
GeneTreei ENSGT00550000074434.
HOVERGENi HBG079164.
InParanoidi B2KG38.
KOi K13198.
OMAi FMELSYL.
OrthoDBi EOG75MVX3.
PhylomeDBi Q60749.
TreeFami TF314878.

Miscellaneous databases

ChiTaRSi KHDRBS1. mouse.
NextBioi 297827.
PROi Q60749.
SOURCEi Search...

Gene expression databases

Bgeei Q60749.
Genevestigatori Q60749.

Family and domain databases

Gene3Di 3.30.1370.10. 1 hit.
InterProi IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view ]
Pfami PF00013. KH_1. 1 hit.
[Graphical view ]
SMARTi SM00322. KH. 1 hit.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 1 hit.
PROSITEi PS50084. KH_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and cDNA sequence of a murine protein homologous to the human p62 tyrosine phosphoprotein that associates with the Ras GTPase-activating protein p120 GAP."
    Agger R., Freimuth P.
    Gene 158:307-308(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-120 AND 139-150.
    Strain: BALB/c X DBA/2.
    Tissue: Dendritic cell.
  2. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1."
    Richard S., Yu D., Blumer K.J., Hausladen D., Olszowy M.W., Connelly P.A., Shaw A.S.
    Mol. Cell. Biol. 15:186-197(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FYN; GRB2 AND PLCG1.
    Tissue: Thymus.
  3. "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.
    , 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: C57BL/6J.
    Tissue: Bone marrow and Pancreas.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  6. Cited for: PROTEIN SEQUENCE OF 57-71; 103-131; 139-152; 158-165; 222-230; 273-282 AND 433-443, FUNCTION, PHOSPHORYLATION AT SER-113, INTERACTION WITH SRC.
  7. "Self-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domain."
    Chen T., Damaj B.B., Herrera C., Lasko P., Richard S.
    Mol. Cell. Biol. 17:5707-5718(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, HOMOOLIGOMERIZATION.
  8. "A mammalian germ cell-specific RNA-binding protein interacts with ubiquitously expressed proteins involved in splice site selection."
    Elliott D.J., Bourgeois C.F., Klink A., Stevenin J., Cooke H.J.
    Proc. Natl. Acad. Sci. U.S.A. 97:5717-5722(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBMY1A1.
  9. "Physical and functional interaction between the transcriptional cofactor CBP and the KH domain protein Sam68."
    Hong W., Resnick R.J., Rakowski C., Shalloway D., Taylor S.J., Blobel G.A.
    Mol. Cancer Res. 1:48-55(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBP.
  10. "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: INTERACTION WITH PRMT1.
  11. "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 LYS-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiKHDR1_MOUSE
AccessioniPrimary (citable) accession number: Q60749
Secondary accession number(s): A2ACH3
, B2KG38, Q3U8T3, Q60735, Q7M4N5, Q99M33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi