Reviewed, UniProtKB/Swiss-Prot Q07666 (KHDR1_HUMAN)

Names and origin

Protein names

Recommended name:
    KH domain-containing, RNA-binding, signal transduction-associated protein 1
Alternative name(s):
    p21 Ras GTPase-activating protein-associated p62
    GAP-associated tyrosine phosphoprotein p62
    Src-associated in mitosis 68 kDa protein
      Short name=Sam68
    p68

Gene names

Name:	KHDRBS1
Synonyms:	SAM68

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. Ref.2 Ref.7 Ref.9 Ref.1 UniProtKB Q60749 UniProtKB Q8UUW7 Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase. Ref.2 Ref.7 Ref.9
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.
Subcellular location	Nucleus. Membrane. Ref.1 Ref.10
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 methlylation on these motifs can modulate protein-protein interactions By similarity. UniProtKB Q91V33
Post-translational modification	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. Ref.7 Ref.9 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Acetylated. Positively correlates with ability to bind RNA. Ref.12 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.10 Ref.11 Arg-291, Arg-331 and Arg-346 are found to be also dimethylated, probably to asymmetric dimethylarginine. Ref.1 Ref.10 Ref.6 Ref.11
Sequence similarities	Belongs to the KHDRBS family. Contains 1 KH domain.
Sequence caution	The sequence AAH10132.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Biological process	Cell cycle Transcription Transcription regulation
Cellular component	Membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	SH3-binding
Ligand	RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB cell cycle arrest Ref.2 Traceable author statement. Source: ProtInc cell proliferation Ref.2 Traceable author statement. Source: ProtInc cell surface receptor linked signal transduction Ref.7 Inferred from direct assay. Source: UniProtKB mRNA processing Ref.1 Traceable author statement. Source: ProtInc negative regulation of transcription Inferred from sequence or structural similarity. Source: UniProtKB regulation of RNA export from nucleus Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Ref.1 Inferred from direct assay. Source: UniProtKB nucleus Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Ref.1 Traceable author statement. Source: ProtInc RNA binding Ref.1 Inferred from direct assay. Source: UniProtKB SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW SH3/SH2 adaptor activity Ref.7 Inferred from physical interaction. Source: UniProtKB transcription repressor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBL	P22681	1	EBI-1364,EBI-518228
CRK	P46108-1	1	EBI-1364,EBI-287556
FYN	P06241	2	EBI-1364,EBI-515315
GRB2	P62993	2	EBI-1364,EBI-401755
HCK	P08631	2	EBI-1364,EBI-346340
JAK3	P52333	1	EBI-1364,EBI-518246
LCK	P06239	3	EBI-1364,EBI-1348
Lck	P06240	1	EBI-1364,EBI-1401	From a different organism.
LYN	P07948	1	EBI-1364,EBI-79452
PLCG1	P19174	1	EBI-1364,EBI-79387
PTPN6	P29350	1	EBI-1364,EBI-78260
SMARCA2	P51531	2	EBI-1364,EBI-679562
STAT3	P40763	1	EBI-1364,EBI-518675
TOB1	P50616	1	EBI-1364,EBI-723281

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 443	443	KH domain-containing, RNA-binding, signal transduction-associated protein 1		PRO_0000050124
Regions
	Domain	171 – 197	27	KH
	Compositional bias	34 – 41	8	Pro-rich
	Compositional bias	44 – 55	12	DMA/Gly-rich
	Compositional bias	59 – 89	31	Pro-rich
	Compositional bias	282 – 292	11	DMA/Gly-rich
	Compositional bias	295 – 301	7	Pro-rich
	Compositional bias	302 – 332	31	Arg/Gly-rich
	Compositional bias	334 – 363	30	Pro-rich
Amino acid modifications
	Modified residue	15	1	Phosphoserine Ref.19
	Modified residue	18	1	Phosphoserine Ref.14 Ref.15 Ref.19
	Modified residue	20	1	Phosphoserine Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
	Modified residue	29	1	Phosphoserine Ref.19
	Modified residue	33	1	Phosphothreonine Ref.15
	Modified residue	45	1	Asymmetric dimethylarginine; by PRMT1 Ref.10
	Modified residue	52	1	Asymmetric dimethylarginine; partial; by PRMT1 Ref.10
	Modified residue	58	1	Phosphoserine Ref.18
	Modified residue	113	1	Phosphoserine By similarity UniProtKB Q60749
	Modified residue	291	1	Omega-N-methylated arginine; by PRMT1 Ref.11
	Modified residue	304	1	Asymmetric dimethylarginine; by PRMT1 Ref.10
	Modified residue	310	1	Omega-N-methylarginine; by PRMT1 Ref.10
	Modified residue	315	1	Omega-N-methylarginine; by PRMT1 Ref.10
	Modified residue	320	1	Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.10 Ref.6
	Modified residue	320	1	Omega-N-methylarginine; by PRMT1 Ref.10 Ref.6
	Modified residue	325	1	Omega-N-methylarginine; by PRMT1 Ref.10 Ref.11
	Modified residue	331	1	Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.6 Ref.11
	Modified residue	331	1	Omega-N-methylated arginine; by PRMT1 Ref.6 Ref.11
	Modified residue	340	1	Omega-N-methylarginine; by PRMT1 Ref.6 Ref.11
	Modified residue	346	1	Omega-N-methylated arginine; by PRMT1 Ref.11
Natural variations
	Alternative sequence	37 – 61	25	Missing in isoform 2.		VSP_051719
	Alternative sequence	169 – 207	39	Missing in isoform 3. Ref.2		VSP_051720

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 59FB4DB6FB4DBE98	FASTA	443	48,227
	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
	Isoform 2. Checksum: 36B5B877E35D9A2C	FASTA	418	45,861
	10 20 30 40 50 60 MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPP LLPPSATGPD ATVGGPAPTP 70 80 90 100 110 120 LLPPSATASV KMEPENKYLP ELMAEKDSLD PSFTHAMQLL TAEIEKIQKG DSKKDDEENY 130 140 150 160 170 180 LDLFSHKNMK LKERVLIPVK QYPKFNFVGK ILGPQGNTIK RLQEETGAKI SVLGKGSMRD 190 200 210 220 230 240 KAKEEELRKG GDPKYAHLNM DLHVFIEVFG PPCEAYALMA HAMEEVKKFL VPDMMDDICQ 250 260 270 280 290 300 EQFLELSYLN GVPEPSRGRG VPVRGRGAAP PPPPVPRGRG VGPPRGALVR GTPVRGAITR 310 320 330 340 350 360 GATVTRGVPP PPTVRGAPAP RARTAGIQRI PLPPPPAPET YEEYGYDDTY AEQSYEGYEG 370 380 390 400 410 YYSQSQGDSE YYDYGHGEVQ DSYEAYGQDD WNGTRPSLKA PPARPVKGAY REHPYGRY
	Isoform 3 (DeltaKH). Checksum: 0E6334E3447CCA5F	FASTA	404	44,027
	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 LIPVKQYPKE EELRKGGDPK 190 200 210 220 230 240 YAHLNMDLHV FIEVFGPPCE AYALMAHAME EVKKFLVPDM MDDICQEQFL ELSYLNGVPE 250 260 270 280 290 300 PSRGRGVPVR GRGAAPPPPP VPRGRGVGPP RGALVRGTPV RGAITRGATV TRGVPPPPTV 310 320 330 340 350 360 RGAPAPRART AGIQRIPLPP PPAPETYEEY GYDDTYAEQS YEGYEGYYSQ SQGDSEYYDY 370 380 390 400 GHGEVQDSYE AYGQDDWNGT RPSLKAPPAR PVKGAYREHP YGRY

References

	« Hide 'large scale' referencesShow '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: 1374686] [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: 9013542] [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. , 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: 14702039] [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. , 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph and Placenta.
[6]	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.
[7]	"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: 9045636] [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.
[8]	"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: 10332027] [Abstract] Cited for: INTERACTION WITH KHDRBS3. Tissue: Testis.
[9]	"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: 11585385] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH STAT3.
[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: 12529443] [Abstract] Cited for: METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 AND ARG-325, SUBCELLULAR LOCATION.
[11]	"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: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-291; ARG-325; ARG-331; ARG-340 AND ARG-346, MASS SPECTROMETRY.
[12]	"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: 15021911] [Abstract] Cited for: ACETYLATION, INTERACTION WITH RNA.
[13]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
[14]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-20, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-33, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
[17]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, MASS SPECTROMETRY.
[18]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, MASS SPECTROMETRY.
[19]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-18; SER-20 AND SER-29, MASS SPECTROMETRY.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. BC000717 mRNA. Translation: AAH00717.1. BC010132 mRNA. Translation: AAH10132.1. Sequence problems. BC019109 mRNA. Translation: AAH19109.1.
IPI	IPI00008575. IPI00082310. IPI00385834.
PIR	A38219.
RefSeq	NP_006550.1.
UniGene	Hs.709204
3D structure databases
HSSP	HSSP built from PDB template 1DTJ based on UniProtKB Q9UNW9.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:29007N.
IntAct	Q07666. 19 interactions.
PTM databases
PhosphoSite	Q07666.
Proteomic databases
PRIDE	Q07666.
Genome annotation databases
Ensembl	ENSG00000121774. Homo sapiens. [Contig view]
GeneID	10657.
KEGG	hsa:10657.
Organism-specific databases
GeneCards	GC01P032294.
H-InvDB	HIX0000361.
HGNC	HGNC:18116. KHDRBS1.
HPA	CAB005355.
MIM	602489. gene.
PharmGKB	PA30092.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q07666.
HOVERGEN	Q07666.
OMA	Q07666. VRQAPSR.
Gene expression databases
ArrayExpress	Q07666.
Bgee	Q07666.
CleanEx	HS_KHDRBS1.
GermOnline	ENSG00000121774. Homo sapiens.
Family and domain databases
InterPro	IPR004087. KH. IPR004088. KH_type_1. IPR018111. KH_type_1_subgr. [Graphical view]
Pfam	PF00013. KH_1. 1 hit. [Graphical view]
SMART	SM00322. KH. 1 hit. [Graphical view]
PROSITE	PS50084. KH_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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Entry information

Entry name

KHDR1_HUMAN

Accession

Primary (citable) accession number: Q07666
Secondary accession number(s): Q6PJX7, Q8NB97, Q99760

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)