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Q9H2G2 (SLK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1235 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-1022272,EBI-1022272

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235STE20-like serine/threonine-protein kinase
PRO_0000233239

Regions

Domain34 – 292259Protein kinase
Domain875 – 91036UVR
Nucleotide binding40 – 489ATP By similarity
Coiled coil826 – 1069244 Potential
Coiled coil1109 – 118375 Potential
Compositional bias16 – 194Poly-Lys
Compositional bias302 – 652351Glu-rich

Sites

Active site1551Proton acceptor By similarity
Binding site631ATP By similarity
Site438 – 4392Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue141Phosphoserine Ref.14
Modified residue1891Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
Modified residue3301Phosphoserine Ref.8
Modified residue3441Phosphoserine Ref.10
Modified residue3471Phosphoserine Ref.9 Ref.14
Modified residue3481Phosphoserine Ref.9 Ref.14
Modified residue3541Phosphoserine By similarity
Modified residue5651Phosphoserine Ref.8 Ref.10 Ref.14
Modified residue5711Phosphoserine Ref.9 Ref.12 Ref.14
Modified residue6551Phosphoserine Ref.8
Modified residue7771Phosphoserine Ref.9
Modified residue7791Phosphoserine Ref.9 Ref.11 Ref.12
Modified residue8181Phosphoserine Ref.9
Modified residue10971Phosphothreonine Ref.12

Natural variations

Alternative sequence929 – 95931Missing in isoform 2.
VSP_018100
Natural variant4051Q → K in a lung adenocarcinoma sample; somatic mutation. Ref.15
VAR_041080
Natural variant5521C → Y. Ref.15
Corresponds to variant rs805657 [ dbSNP | Ensembl ].
VAR_041081
Natural variant6041E → Q in an ovarian serous carcinoma sample; somatic mutation. Ref.15
VAR_041082
Natural variant6581A → G. Ref.15
Corresponds to variant rs56400929 [ dbSNP | Ensembl ].
VAR_041083
Natural variant6661G → E.
Corresponds to variant rs7071400 [ dbSNP | Ensembl ].
VAR_051666
Natural variant6791I → T. Ref.15
Corresponds to variant rs34326537 [ dbSNP | Ensembl ].
VAR_041084
Natural variant6831K → N. Ref.15
Corresponds to variant rs35389916 [ dbSNP | Ensembl ].
VAR_041085
Natural variant6971T → I. Ref.15
Corresponds to variant rs3740469 [ dbSNP | Ensembl ].
VAR_041086

Experimental info

Mutagenesis631K → R: Loss of activity. Ref.1
Sequence conflict51N → S in BAA13195. Ref.3

Secondary structure

....................................................... 1235
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 53A43E7CA29B0ED3

FASTA1,235142,695
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2CA08AF0591C9AD6
Show »

FASTA1,204138,996

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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. expand/collapse author list , 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.
RefSeqNP_055535.2. NM_014720.2.
XP_005270358.1. XM_005270301.1.
UniGeneHs.591922.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J51X-ray2.10A19-320[»]
2JFLX-ray2.20A19-320[»]
2JFMX-ray2.85A19-320[»]
2UV2X-ray2.30A19-320[»]
ProteinModelPortalQ9H2G2.
SMRQ9H2G2. Positions 21-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115096. 9 interactions.
IntActQ9H2G2. 5 interactions.
MINTMINT-4539212.
STRING9606.ENSP00000358770.

Chemistry

BindingDBQ9H2G2.
ChEMBLCHEMBL4202.
GuidetoPHARMACOLOGY2200.

PTM databases

PhosphoSiteQ9H2G2.

Polymorphism databases

DMDM74762732.

Proteomic databases

PaxDbQ9H2G2.
PRIDEQ9H2G2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335753; ENSP00000336824; ENSG00000065613. [Q9H2G2-2]
ENST00000369755; ENSP00000358770; ENSG00000065613. [Q9H2G2-1]
GeneID9748.
KEGGhsa:9748.
UCSCuc001kxo.1. human. [Q9H2G2-1]
uc001kxp.1. human. [Q9H2G2-2]

Organism-specific databases

CTD9748.
GeneCardsGC10P105716.
HGNCHGNC:11088. SLK.
HPAHPA015757.
neXtProtNX_Q9H2G2.
PharmGKBPA35941.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG052712.
InParanoidQ9H2G2.
KOK08836.
OMANIMITLE.
OrthoDBEOG7CNZF6.
PhylomeDBQ9H2G2.
TreeFamTF351445.

Enzyme and pathway databases

SignaLinkQ9H2G2.

Gene expression databases

BgeeQ9H2G2.
CleanExHS_SLK.
GenevestigatorQ9H2G2.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR022165. PKK.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR001943. UVR_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF12474. PKK. 2 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9H2G2.
GeneWikiSLK_(gene).
GenomeRNAi9748.
NextBio36684.
PMAP-CutDBQ9H2G2.
PROQ9H2G2.

Entry information

Entry nameSLK_HUMAN
AccessionPrimary (citable) accession number: Q9H2G2
Secondary accession number(s): D3DRA0 expand/collapse secondary AC list , 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: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM