Q9H2G2 (SLK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
STE20-like serine/threonine-protein kinase
Short name=STE20-like kinase
Short name=hSLK
EC=2.7.11.1

Alternative name(s):
CTCL tumor antigen se20-9
STE20-related serine/threonine-protein kinase
Short name=STE20-related kinase
Serine/threonine-protein kinase 2

Gene names

Name:	SLK
Synonyms:	KIAA0204, STK2

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	1235 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates apoptosis and actin stress fiber dissolution By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Ubiquitously expressed. Highest expression is found in heart and in skeletal muscle. Ref.1
Post-translational modification	Proteolytically cleaved by caspase-3. Autophosphorylated. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily. Contains 1 protein kinase domain. Contains 1 UVR domain.
Sequence caution	The sequence AAH47762.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 611. The sequence AAH47885.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 422. The sequence AAH64804.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 614. The sequence BAA13195.2 differs from that shown. Reason: Frameshift at position 1172.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW protein autophosphorylation Inferred from direct assay PubMed 18239682. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay PubMed 18239682. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay PubMed 18239682. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H2G2-1)

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: Q9H2G2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     929-959: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1235

1235

STE20-like serine/threonine-protein kinase

PRO_0000233239

Regions

Domain

34 – 292

259

Protein kinase

Domain

875 – 910

36

UVR

Nucleotide binding

40 – 48

9

ATP By similarity

Coiled coil

826 – 1069

244

Potential

Coiled coil

1109 – 1183

75

Potential

Compositional bias

16 – 19

4

Poly-Lys

Compositional bias

302 – 652

351

Glu-rich

Sites

Active site

155

1

Proton acceptor By similarity

Binding site

63

1

ATP By similarity

Site

438 – 439

2

Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue

14

1

Phosphoserine Ref.14

Modified residue

189

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12

Modified residue

330

1

Phosphoserine Ref.8

Modified residue

344

1

Phosphoserine Ref.10

Modified residue

347

1

Phosphoserine Ref.9 Ref.14

Modified residue

348

1

Phosphoserine Ref.9 Ref.14

Modified residue

354

1

Phosphoserine By similarity

Modified residue

565

1

Phosphoserine Ref.8 Ref.10 Ref.14

Modified residue

571

1

Phosphoserine Ref.9 Ref.12 Ref.14

Modified residue

655

1

Phosphoserine Ref.8

Modified residue

777

1

Phosphoserine Ref.9

Modified residue

779

1

Phosphoserine Ref.9 Ref.11 Ref.12

Modified residue

818

1

Phosphoserine Ref.9

Modified residue

1097

1

Phosphothreonine Ref.12

Natural variations

Alternative sequence

929 – 959

31

Missing in isoform 2.

VSP_018100

Natural variant

405

1

Q → K in a lung adenocarcinoma sample; somatic mutation. Ref.15

VAR_041080

Natural variant

552

1

C → Y. Ref.15
Corresponds to variant rs805657 [ dbSNP | Ensembl ].

VAR_041081

Natural variant

604

1

E → Q in an ovarian serous carcinoma sample; somatic mutation. Ref.15

VAR_041082

Natural variant

658

1

A → G. Ref.15
Corresponds to variant rs56400929 [ dbSNP | Ensembl ].

VAR_041083

Natural variant

666

1

G → E.
Corresponds to variant rs7071400 [ dbSNP | Ensembl ].

VAR_051666

Natural variant

679

1

I → T. Ref.15
Corresponds to variant rs34326537 [ dbSNP | Ensembl ].

VAR_041084

Natural variant

683

1

K → N. Ref.15
Corresponds to variant rs35389916 [ dbSNP | Ensembl ].

VAR_041085

Natural variant

697

1

T → I. Ref.15
Corresponds to variant rs3740469 [ dbSNP | Ensembl ].

VAR_041086

Experimental info

Mutagenesis

63

1

K → R: Loss of activity. Ref.1

Sequence conflict

5

1

N → S in BAA13195. Ref.3

Secondary structure

1

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1235

Helix Strand Turn

Details...

Beta strand

25 – 28

4

Helix

30 – 32

3

Beta strand

34 – 43

10

Beta strand

46 – 53

8

Turn

54 – 56

3

Beta strand

59 – 66

8

Beta strand

68 – 70

3

Helix

73 – 85

13

Beta strand

94 – 100

7

Beta strand

103 – 109

7

Helix

116 – 123

8

Helix

129 – 148

20

Helix

158 – 160

3

Beta strand

161 – 163

3

Beta strand

169 – 171

3

Helix

181 – 187

7

Helix

199 – 202

4

Turn

207 – 209

3

Turn

212 – 214

3

Helix

215 – 230

16

Turn

234 – 237

4

Helix

240 – 242

3

Helix

243 – 249

7

Helix

258 – 260

3

Helix

263 – 272

10

Turn

277 – 279

3

Helix

283 – 286

4

Helix

290 – 292

3

Helix

298 – 307

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 53A43E7CA29B0ED3	FASTA	1,235	142,695
	10 20 30 40 50 60 MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EDFWEIIGEL GDGAFGKVYK AQNKETSVLA 70 80 90 100 110 120 AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM 130 140 150 160 170 180 LELERPLTES QIQVVCKQTL DALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN 190 200 210 220 230 240 TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP 250 260 270 280 290 300 MRVLLKIAKS EPPTLAQPSR WSSNFKDFLK KCLEKNVDAR WTTSQLLQHP FVTVDSNKPI 310 320 330 340 350 360 RELIAEAKAE VTEEVEDGKE EDEEEETENS LPIPASKRAS SDLSIASSEE DKLSQNACIL 370 380 390 400 410 420 ESVSEKTERS NSEDKLNSKI LNEKPTTDEP EKAVEDINEH ITDAQLEAMT ELHDRTAVIK 430 440 450 460 470 480 ENEREKRPKL ENLPDTEDQE TVDINSVSEG KENNIMITLE TNIEHNLKSE EEKDQEKQQM 490 500 510 520 530 540 FENKLIKSEE IKDTILQTVD LVSQETGEKE ANIQAVDSEV GLTKEDTQEK LGEDDKTQKD 550 560 570 580 590 600 VISNTSDVIG TCEAADVAQK VDEDSAEDTQ SNDGKEVVEV GQKLINKPMV GPEAGGTKEV 610 620 630 640 650 660 PIKEIVEMNE IEEGKNKEQA INSSENIMDI NEEPGTTEGE EITESSSTEE MEVRSVVADT 670 680 690 700 710 720 DQKALGSEVQ DASKVTTQID KEKKEIPVSI KKEPEVTVVS QPTEPQPVLI PSININSDSG 730 740 750 760 770 780 ENKEEIGSLS KTETILPPES ENPKENDNDS GTGSTADTSS IDLNLSISSF LSKTKDSGSI 790 800 810 820 830 840 SLQETRRQKK TLKKTRKFIV DGVEVSVTTS KIVTDSDSKT EELRFLRRQE LRELRFLQKE 850 860 870 880 890 900 EQRAQQQLNS KLQQQREQIF RRFEQEMMSK KRQYDQEIEN LEKQQKQTIE RLEQEHTNRL 910 920 930 940 950 960 RDEAKRIKGE QEKELSKFQN MLKNRKKEVI NEVEKAPKEL RKELMKRRKE ELAQSQHAQE 970 980 990 1000 1010 1020 QEFVQKQQQE LDGSLKKIIQ QQKAELANIE RECLNNKQQL MRAREAAIWE LEERHLQEKH 1030 1040 1050 1060 1070 1080 QLLKQQLKDQ YFMQRHQLLK RHEKETEQMQ RYNQRLIEEL KNRQTQERAR LPKIQRSEAK 1090 1100 1110 1120 1130 1140 TRMAMFKKSL RINSTATPDQ DRDKIKQFAA QEEKRQKNER MAQHQKHENQ MRDLQLQCEA 1150 1160 1170 1180 1190 1200 NVRELHQLQN EKCHLLVEHE TQKLKELDEE HSQELKEWRE KLRPRKKTLE EEFARKLQEQ 1210 1220 1230 EVFFKMTGES ECLNPSTQSR ISKFYPIPSL HSTGS
	Isoform 2 [UniParc]. Checksum: 2CA08AF0591C9AD6	FASTA	1,204	138,996
	10 20 30 40 50 60 MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EDFWEIIGEL GDGAFGKVYK AQNKETSVLA 70 80 90 100 110 120 AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM 130 140 150 160 170 180 LELERPLTES QIQVVCKQTL DALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN 190 200 210 220 230 240 TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP 250 260 270 280 290 300 MRVLLKIAKS EPPTLAQPSR WSSNFKDFLK KCLEKNVDAR WTTSQLLQHP FVTVDSNKPI 310 320 330 340 350 360 RELIAEAKAE VTEEVEDGKE EDEEEETENS LPIPASKRAS SDLSIASSEE DKLSQNACIL 370 380 390 400 410 420 ESVSEKTERS NSEDKLNSKI LNEKPTTDEP EKAVEDINEH ITDAQLEAMT ELHDRTAVIK 430 440 450 460 470 480 ENEREKRPKL ENLPDTEDQE TVDINSVSEG KENNIMITLE TNIEHNLKSE EEKDQEKQQM 490 500 510 520 530 540 FENKLIKSEE IKDTILQTVD LVSQETGEKE ANIQAVDSEV GLTKEDTQEK LGEDDKTQKD 550 560 570 580 590 600 VISNTSDVIG TCEAADVAQK VDEDSAEDTQ SNDGKEVVEV GQKLINKPMV GPEAGGTKEV 610 620 630 640 650 660 PIKEIVEMNE IEEGKNKEQA INSSENIMDI NEEPGTTEGE EITESSSTEE MEVRSVVADT 670 680 690 700 710 720 DQKALGSEVQ DASKVTTQID KEKKEIPVSI KKEPEVTVVS QPTEPQPVLI PSININSDSG 730 740 750 760 770 780 ENKEEIGSLS KTETILPPES ENPKENDNDS GTGSTADTSS IDLNLSISSF LSKTKDSGSI 790 800 810 820 830 840 SLQETRRQKK TLKKTRKFIV DGVEVSVTTS KIVTDSDSKT EELRFLRRQE LRELRFLQKE 850 860 870 880 890 900 EQRAQQQLNS KLQQQREQIF RRFEQEMMSK KRQYDQEIEN LEKQQKQTIE RLEQEHTNRL 910 920 930 940 950 960 RDEAKRIKGE QEKELSKFQN MLKNRKKEEQ EFVQKQQQEL DGSLKKIIQQ QKAELANIER 970 980 990 1000 1010 1020 ECLNNKQQLM RAREAAIWEL EERHLQEKHQ LLKQQLKDQY FMQRHQLLKR HEKETEQMQR 1030 1040 1050 1060 1070 1080 YNQRLIEELK NRQTQERARL PKIQRSEAKT RMAMFKKSLR INSTATPDQD RDKIKQFAAQ 1090 1100 1110 1120 1130 1140 EEKRQKNERM AQHQKHENQM RDLQLQCEAN VRELHQLQNE KCHLLVEHET QKLKELDEEH 1150 1160 1170 1180 1190 1200 SQELKEWREK LRPRKKTLEE EFARKLQEQE VFFKMTGESE CLNPSTQSRI SKFYPIPSLH STGS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of a novel human STE20-like kinase, hSLK." Yamada E., Tsujikawa K., Itoh S., Kameda Y., Kohama Y., Yamamoto H. Biochim. Biophys. Acta 1495:250-262(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF LYS-63. Tissue: Lung carcinoma.
[2]	"Serological detection of cutaneous T-cell lymphoma-associated antigens." Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D. Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[3]	"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain." Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N. DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow.
[4]	Ohara O., Nagase T., Kikuno R., Nomura N. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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].
[7]	"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 2). Tissue: Testis and Uterus.
[8]	"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-189; SER-330; SER-565 AND SER-655, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-189; SER-347; SER-348; SER-571; SER-777; SER-779 AND SER-818, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-344 AND SER-565, MASS SPECTROMETRY.
[11]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-571; SER-779 AND THR-1097, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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].
[14]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-347; SER-348; SER-565 AND SER-571, MASS SPECTROMETRY.
[15]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-405; TYR-552; GLN-604; GLY-658; THR-679; ASN-683 AND ILE-697.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB002804 mRNA. Translation: BAA19655.1.
AF273048 mRNA. Translation: AAG34908.1.
D86959 mRNA. Translation: BAA13195.2. Sequence problems.
AL360170, AL138761 Genomic DNA. Translation: CAH70403.1.
AL360170, AL138761 Genomic DNA. Translation: CAH70404.1.
AL138761, AL360170 Genomic DNA. Translation: CAI12395.1.
AL138761, AL360170 Genomic DNA. Translation: CAI12396.1.
CH471066 Genomic DNA. Translation: EAW49615.1.
CH471066 Genomic DNA. Translation: EAW49616.1.
CH471066 Genomic DNA. Translation: EAW49617.1.
CH471066 Genomic DNA. Translation: EAW49618.1.
BC047762 mRNA. Translation: AAH47762.1. Sequence problems.
BC047885 mRNA. Translation: AAH47885.1. Sequence problems.
BC064804 mRNA. Translation: AAH64804.1. Sequence problems.
BC111565 mRNA. Translation: AAI11566.1.

IPI

IPI00022827.
IPI00247439.

RefSeq

NP_055535.2. NM_014720.2.

UniGene

Hs.591922.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J51	X-ray	2.10	A	19-320	[»]
2JFL	X-ray	2.20	A	19-320	[»]
2JFM	X-ray	2.85	A	19-320	[»]
2UV2	X-ray	2.30	A	19-320	[»]

ProteinModelPortal

Q9H2G2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H2G2. 5 interactions.

MINT

MINT-4539212.

STRING

9606.ENSP00000358770.

PTM databases

PhosphoSite

Q9H2G2.

Polymorphism databases

DMDM

74762732.

Proteomic databases

PaxDb

Q9H2G2.

PRIDE

Q9H2G2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335753; ENSP00000336824; ENSG00000065613.
ENST00000369755; ENSP00000358770; ENSG00000065613.

GeneID

9748.

KEGG

hsa:9748.

UCSC

uc001kxo.1. human.
uc001kxp.1. human.

Organism-specific databases

CTD

9748.

GeneCards

GC10P105716.

HGNC

HGNC:11088. SLK.

HPA

HPA015757.

neXtProt

NX_Q9H2G2.

PharmGKB

PA35941.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG052712.

InParanoid

Q9H2G2.

KO

K08836.

OMA

DARWTTS.

PhylomeDB

Q9H2G2.

Gene expression databases

Bgee

Q9H2G2.

CleanEx

HS_SLK.

Genevestigator

Q9H2G2.

GermOnline

ENSG00000065613. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR022165. PKK.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001943. UVR_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF12474. PKK. 2 hits.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9H2G2.

ChEMBL

CHEMBL4202.

EvolutionaryTrace

Q9H2G2.

GenomeRNAi

9748.

NextBio

36684.

PMAP-CutDB

Q9H2G2.

Entry information

Entry name

SLK_HUMAN

Accession

Primary (citable) accession number: Q9H2G2
Secondary accession number(s): D3DRA0 , D3DRA1, O00211, Q6P1Z4, Q86WU7, Q86WW1, Q92603, Q9NQL0, Q9NQL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 114 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.