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Q07666

- KHDR1_HUMAN

UniProt

Q07666 - KHDR1_HUMAN

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Protein

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

Gene

KHDRBS1

Organism
Homo sapiens (Human)
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. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824).1 Publication
Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. cell cycle arrest Source: ProtInc
  2. cell proliferation Source: ProtInc
  3. cell surface receptor signaling pathway Source: UniProtKB
  4. G2/M transition of mitotic cell cycle Source: UniProtKB
  5. mRNA processing Source: ProtInc
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. positive regulation of RNA export from nucleus Source: UniProtKB
  8. positive regulation of signal transduction Source: GOC
  9. positive regulation of translational initiation Source: UniProtKB
  10. regulation of RNA export from nucleus Source: UniProtKB
  11. signal transduction Source: ProtInc
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

SignaLinkiQ07666.

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:KHDRBS1Imported
Synonyms:SAM681 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18116. KHDRBS1.

Subcellular locationi

Nucleus 1 Publication. 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi435 – 4351Y → F: No effect on the nuclear localization. 1 Publication
Mutagenesisi440 – 4401Y → F: Completely blocks nuclear localization. 1 Publication
Mutagenesisi443 – 4431Y → F: No effect on the nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA30092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443KH domain-containing, RNA-binding, signal transduction-associated protein 1PRO_0000050124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine2 Publications
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei45 – 451Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei52 – 521Asymmetric dimethylarginine; partial; by PRMT11 Publication
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei113 – 1131PhosphoserineBy similarity
Modified residuei175 – 1751N6-acetyllysine2 Publications
Modified residuei304 – 3041Asymmetric dimethylarginine; by PRMT11 Publication
Modified residuei310 – 3101Omega-N-methylarginine; by PRMT11 Publication
Modified residuei315 – 3151Omega-N-methylarginine; by PRMT11 Publication
Modified residuei320 – 3201Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei320 – 3201Omega-N-methylarginine; by PRMT11 Publication
Modified residuei325 – 3251Omega-N-methylarginine; by PRMT12 Publications
Modified residuei331 – 3311Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei331 – 3311Omega-N-methylated arginine; by PRMT12 Publications
Modified residuei340 – 3401Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei340 – 3401Omega-N-methylarginine; by PRMT11 Publication
Modified residuei435 – 4351Phosphotyrosine; by PTK61 Publication
Modified residuei440 – 4401Phosphotyrosine; by PTK61 Publication
Modified residuei443 – 4431Phosphotyrosine; by PTK61 Publication

Post-translational modificationi

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 KHDRBS1.5 Publications
Acetylated. Positively correlates with ability to bind RNA.2 Publications
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/FBP30.4 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ07666.
PaxDbiQ07666.
PRIDEiQ07666.

PTM databases

PhosphoSiteiQ07666.

Miscellaneous databases

PMAP-CutDBQ07666.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Isoform 3 is only expressed in growth-arrested cells.1 Publication

Gene expression databases

BgeeiQ07666.
CleanExiHS_KHDRBS1.
ExpressionAtlasiQ07666. baseline and differential.
GenevestigatoriQ07666.

Organism-specific databases

HPAiCAB005355.
HPA051280.
HPA056813.

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 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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FYNP062414EBI-1364,EBI-515315
GRB2P629938EBI-1364,EBI-401755
HCKP086314EBI-1364,EBI-346340
HNRNPA1P096512EBI-1364,EBI-352662
JAK3P523332EBI-1364,EBI-518246
LCKP062395EBI-1364,EBI-1348
LckP062402EBI-1364,EBI-1401From a different organism.
PIK3R1P237272EBI-1364,EBI-520244From a different organism.
PLCG1P191742EBI-1364,EBI-79387
SMARCA2P515312EBI-1364,EBI-679562
SRCP129313EBI-1364,EBI-621482
STAT3P407632EBI-1364,EBI-518675
VAV1P154983EBI-1364,EBI-625518

Protein-protein interaction databases

BioGridi115900. 135 interactions.
DIPiDIP-29007N.
IntActiQ07666. 65 interactions.
MINTiMINT-102826.
STRINGi9606.ENSP00000313829.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi100 – 11314
Helixi119 – 13416

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XA6NMR-A/B97-135[»]
3QHEX-ray2.40B/D365-419[»]
ProteinModelPortaliQ07666.
SMRiQ07666. Positions 98-276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07666.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 19727KHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Domaini

The KH domain is required for binding to RNA.By similarity
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.Sequence Analysis
Contains 1 KH domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiCOG5176.
GeneTreeiENSGT00550000074434.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ07666.
KOiK13198.
OMAiFMELSYL.
OrthoDBiEOG75MVX3.
PhylomeDBiQ07666.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q07666-1) [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
MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG
60 70 80 90 100
SRGGARASPA TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE
110 120 130 140 150
NKYLPELMAE KDSLDPSFTH AMQLLTAEIE KIQKGDSKKD DEENYLDLFS
160 170 180 190 200
HKNMKLKERV LIPVKQYPKF NFVGKILGPQ GNTIKRLQEE TGAKISVLGK
210 220 230 240 250
GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA YALMAHAMEE
260 270 280 290 300
VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV
310 320 330 340 350
PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA
360 370 380 390 400
GIQRIPLPPP PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG
410 420 430 440
HGEVQDSYEA YGQDDWNGTR PSLKAPPARP VKGAYREHPY GRY
Length:443
Mass (Da):48,227
Last modified:November 1, 1996 - v1
Checksum:i59FB4DB6FB4DBE98
GO
Isoform 2Curated (identifier: Q07666-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-61: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:418
Mass (Da):45,861
Checksum:i36B5B877E35D9A2C
GO
Isoform 31 Publication (identifier: Q07666-3) [UniParc]FASTAAdd to Basket

Also known as: DeltaKH1 Publication

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

Show »
Length:404
Mass (Da):44,027
Checksum:i0E6334E3447CCA5F
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei37 – 6125Missing in isoform 2. 1 PublicationVSP_051719Add
BLAST
Alternative sequencei169 – 20739Missing in isoform 3. 1 PublicationVSP_051720Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS350.1. [Q07666-1]
CCDS60067.1. [Q07666-3]
PIRiA38219.
RefSeqiNP_001258807.1. NM_001271878.1. [Q07666-3]
NP_006550.1. NM_006559.2. [Q07666-1]
UniGeneiHs.445893.

Genome annotation databases

EnsembliENST00000327300; ENSP00000313829; ENSG00000121774. [Q07666-1]
ENST00000492989; ENSP00000417731; ENSG00000121774. [Q07666-3]
GeneIDi10657.
KEGGihsa:10657.
UCSCiuc001bua.2. human. [Q07666-3]
uc001bub.4. human. [Q07666-1]

Polymorphism databases

DMDMi62511098.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS350.1. [Q07666-1 ]
CCDS60067.1. [Q07666-3 ]
PIRi A38219.
RefSeqi NP_001258807.1. NM_001271878.1. [Q07666-3 ]
NP_006550.1. NM_006559.2. [Q07666-1 ]
UniGenei Hs.445893.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XA6 NMR - A/B 97-135 [» ]
3QHE X-ray 2.40 B/D 365-419 [» ]
ProteinModelPortali Q07666.
SMRi Q07666. Positions 98-276.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115900. 135 interactions.
DIPi DIP-29007N.
IntActi Q07666. 65 interactions.
MINTi MINT-102826.
STRINGi 9606.ENSP00000313829.

Chemistry

BindingDBi Q07666.
ChEMBLi CHEMBL1795190.

PTM databases

PhosphoSitei Q07666.

Polymorphism databases

DMDMi 62511098.

Proteomic databases

MaxQBi Q07666.
PaxDbi Q07666.
PRIDEi Q07666.

Protocols and materials databases

DNASUi 10657.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327300 ; ENSP00000313829 ; ENSG00000121774 . [Q07666-1 ]
ENST00000492989 ; ENSP00000417731 ; ENSG00000121774 . [Q07666-3 ]
GeneIDi 10657.
KEGGi hsa:10657.
UCSCi uc001bua.2. human. [Q07666-3 ]
uc001bub.4. human. [Q07666-1 ]

Organism-specific databases

CTDi 10657.
GeneCardsi GC01P032479.
HGNCi HGNC:18116. KHDRBS1.
HPAi CAB005355.
HPA051280.
HPA056813.
MIMi 602489. gene.
neXtProti NX_Q07666.
PharmGKBi PA30092.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5176.
GeneTreei ENSGT00550000074434.
HOGENOMi HOG000230771.
HOVERGENi HBG079164.
InParanoidi Q07666.
KOi K13198.
OMAi FMELSYL.
OrthoDBi EOG75MVX3.
PhylomeDBi Q07666.
TreeFami TF314878.

Enzyme and pathway databases

SignaLinki Q07666.

Miscellaneous databases

ChiTaRSi KHDRBS1. human.
EvolutionaryTracei Q07666.
GeneWikii KHDRBS1.
GenomeRNAii 10657.
NextBioi 40517.
PMAP-CutDB Q07666.
PROi Q07666.
SOURCEi Search...

Gene expression databases

Bgeei Q07666.
CleanExi HS_KHDRBS1.
ExpressionAtlasi Q07666. baseline and differential.
Genevestigatori Q07666.

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. "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 brainImported.
  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: Placenta1 Publication.
  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.
    , 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: BrainImported.
  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.
    , 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. 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: LymphImported and PlacentaImported.
  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, IDENTIFICATION BY 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: Testis1 Publication.
  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. 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. 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.

Entry informationi

Entry nameiKHDR1_HUMAN
AccessioniPrimary (citable) accession number: Q07666
Secondary accession number(s): D3DPP3
, Q6PJX7, Q8NB97, Q99760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 148 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, 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
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3