Q07666 (KHDR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	KHDRBS1
Synonyms:	SAM68

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
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. 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 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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/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-dependent 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 translational initiation Inferred from direct assay Ref.26. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Grb2-Sos complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: Compara membrane Inferred from direct assay Ref.1. Source: UniProtKB nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc RNA binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FYN	P06241	3	EBI-1364,EBI-515315
GRB2	P62993	8	EBI-1364,EBI-401755
HCK	P08631	2	EBI-1364,EBI-346340
JAK3	P52333	2	EBI-1364,EBI-518246
LCK	P06239	3	EBI-1364,EBI-1348
Lck	P06240	2	EBI-1364,EBI-1401	From a different organism.
PIK3R1	P23727	2	EBI-1364,EBI-520244	From a different organism.
PLCG1	P19174	2	EBI-1364,EBI-79387
SMARCA2	P51531	2	EBI-1364,EBI-679562
SRC	P12931	3	EBI-1364,EBI-621482
STAT3	P40763	2	EBI-1364,EBI-518675

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

20

1

Phosphoserine Ref.16 Ref.21 PubMed 16083285

Modified residue

29

1

Phosphoserine Ref.21

Modified residue

45

1

Asymmetric dimethylarginine; by PRMT1 Ref.12

Modified residue

52

1

Asymmetric dimethylarginine; partial; by PRMT1 Ref.12

Modified residue

58

1

Phosphoserine Ref.20

Modified residue

113

1

Phosphoserine By similarity UniProtKB Q60749

Modified residue

175

1

N6-acetyllysine Ref.23

Modified residue

291

1

Omega-N-methylated arginine; by PRMT1 Ref.13

Modified residue

304

1

Asymmetric dimethylarginine; by PRMT1 Ref.12

Modified residue

310

1

Omega-N-methylarginine; by PRMT1 Ref.12

Modified residue

315

1

Omega-N-methylarginine; by PRMT1 Ref.12

Modified residue

320

1

Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.7 Ref.12

Modified residue

320

1

Omega-N-methylarginine; by PRMT1 Ref.7 Ref.12

Modified residue

325

1

Omega-N-methylarginine; by PRMT1 Ref.12 Ref.13

Modified residue

331

1

Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.7

Modified residue

331

1

Omega-N-methylated arginine; by PRMT1 Ref.7 Ref.13

Modified residue

340

1

Omega-N-methylarginine; by PRMT1 Ref.7 Ref.13

Modified residue

346

1

Omega-N-methylated arginine; by PRMT1 Ref.13

Modified residue

435

1

Phosphotyrosine; by PTK6 Ref.15

Modified residue

440

1

Phosphotyrosine; by PTK6 Ref.15

Modified residue

443

1

Phosphotyrosine; by PTK6 Ref.15

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

Experimental info

Mutagenesis

435

1

Y → F: No effect on the nuclear localization. Ref.15

Mutagenesis

440

1

Y → F: Completely blocks nuclear localization. Ref.15

Mutagenesis

443

1

Y → F: No effect on the nuclear localization. Ref.15

Secondary structure

1

.

.

.

.

.

443

Helix Strand Turn

Details...

Helix

100 – 113

14

Helix

119 – 134

16

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 [UniParc]. 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) [UniParc]. 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] [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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

IPI

IPI00008575.
IPI00082310.
IPI00385834.

PIR

A38219.

RefSeq

NP_001258807.1. NM_001271878.1.
NP_006550.1. NM_006559.2.

UniGene

Hs.445893.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XA6	NMR	-	A/B	97-135	[»]
3QHE	X-ray	2.40	B/D	365-419	[»]

ProteinModelPortal

Q07666.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29007N.

IntAct

Q07666. 45 interactions.

MINT

MINT-102826.

STRING

9606.ENSP00000313829.

PTM databases

PhosphoSite

Q07666.

Polymorphism databases

DMDM

62511098.

Proteomic databases

PaxDb

Q07666.

PRIDE

Q07666.

Protocols and materials databases

DNASU

10657.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000327300; ENSP00000313829; ENSG00000121774.
ENST00000492989; ENSP00000417731; ENSG00000121774.

GeneID

10657.

KEGG

hsa:10657.

UCSC

uc001bua.1. human.
uc001bub.3. human.

Organism-specific databases

CTD

10657.

GeneCards

GC01P032479.

HGNC

HGNC:18116. KHDRBS1.

HPA

CAB005355.

MIM

602489. gene.

neXtProt

NX_Q07666.

PharmGKB

PA30092.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5176.

HOGENOM

HOG000230771.

HOVERGEN

HBG079164.

InParanoid

Q07666.

KO

K13198.

OMA

FMELSYL.

OrthoDB

EOG4JHCGB.

PhylomeDB

Q07666.

Enzyme and pathway databases

SignaLink

Q07666.

Gene expression databases

ArrayExpress

Q07666.

Bgee

Q07666.

CleanEx

HS_KHDRBS1.

Genevestigator

Q07666.

GermOnline

ENSG00000121774. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[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

BindingDB

Q07666.

ChEMBL

CHEMBL1795190.

ChiTaRS

KHDRBS1. human.

EvolutionaryTrace

Q07666.

GenomeRNAi

10657.

NextBio

40517.

PMAP-CutDB

Q07666.

SOURCE

Search...

Entry information

Entry name

KHDR1_HUMAN

Accession

Primary (citable) accession number: Q07666
Secondary accession number(s): D3DPP3 , Q6PJX7, Q8NB97, Q99760

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.