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Q9H2G2

- SLK_HUMAN

UniProt

Q9H2G2 - SLK_HUMAN

Protein

STE20-like serine/threonine-protein kinase

Gene

SLK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Mediates apoptosis and actin stress fiber dissolution.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei63 – 631ATPPROSITE-ProRule annotation
    Active sitei155 – 1551Proton acceptorPROSITE-ProRule annotation
    Sitei438 – 4392Cleavage; by caspase-3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi40 – 489ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. protein homodimerization activity Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. protein autophosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9H2G2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    STE20-like serine/threonine-protein kinase (EC:2.7.11.1)
    Short name:
    STE20-like kinase
    Short name:
    hSLK
    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 namesi
    Name:SLK
    Synonyms:KIAA0204, STK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:11088. SLK.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631K → R: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA35941.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12351235STE20-like serine/threonine-protein kinasePRO_0000233239Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine2 Publications
    Modified residuei189 – 1891Phosphoserine5 Publications
    Modified residuei330 – 3301Phosphoserine2 Publications
    Modified residuei344 – 3441Phosphoserine2 Publications
    Modified residuei347 – 3471Phosphoserine3 Publications
    Modified residuei348 – 3481Phosphoserine3 Publications
    Modified residuei354 – 3541PhosphoserineBy similarity
    Modified residuei565 – 5651Phosphoserine4 Publications
    Modified residuei571 – 5711Phosphoserine4 Publications
    Modified residuei655 – 6551Phosphoserine2 Publications
    Modified residuei777 – 7771Phosphoserine2 Publications
    Modified residuei779 – 7791Phosphoserine4 Publications
    Modified residuei818 – 8181Phosphoserine2 Publications
    Modified residuei1097 – 10971Phosphothreonine2 Publications

    Post-translational modificationi

    Proteolytically cleaved by caspase-3.
    Autophosphorylated.7 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H2G2.
    PaxDbiQ9H2G2.
    PRIDEiQ9H2G2.

    PTM databases

    PhosphoSiteiQ9H2G2.

    Miscellaneous databases

    PMAP-CutDBQ9H2G2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highest expression is found in heart and in skeletal muscle.1 Publication

    Gene expression databases

    BgeeiQ9H2G2.
    CleanExiHS_SLK.
    GenevestigatoriQ9H2G2.

    Organism-specific databases

    HPAiHPA015757.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1022272,EBI-1022272

    Protein-protein interaction databases

    BioGridi115096. 9 interactions.
    IntActiQ9H2G2. 5 interactions.
    MINTiMINT-4539212.
    STRINGi9606.ENSP00000358770.

    Structurei

    Secondary structure

    1
    1235
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 284
    Helixi30 – 323
    Beta strandi34 – 4310
    Beta strandi46 – 538
    Turni54 – 563
    Beta strandi59 – 668
    Beta strandi68 – 703
    Helixi73 – 8513
    Beta strandi94 – 1007
    Beta strandi103 – 1097
    Helixi116 – 1238
    Helixi129 – 14820
    Helixi158 – 1603
    Beta strandi161 – 1633
    Beta strandi169 – 1713
    Helixi181 – 1877
    Helixi199 – 2024
    Turni207 – 2093
    Turni212 – 2143
    Helixi215 – 23016
    Turni234 – 2374
    Helixi240 – 2423
    Helixi243 – 2497
    Helixi258 – 2603
    Helixi263 – 27210
    Turni277 – 2793
    Helixi283 – 2864
    Helixi290 – 2923
    Helixi298 – 30710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J51X-ray2.10A19-320[»]
    2JFLX-ray2.20A19-320[»]
    2JFMX-ray2.85A19-320[»]
    2UV2X-ray2.30A19-320[»]
    ProteinModelPortaliQ9H2G2.
    SMRiQ9H2G2. Positions 21-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H2G2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 292259Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini875 – 91036UVRPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili826 – 1069244Sequence AnalysisAdd
    BLAST
    Coiled coili1109 – 118375Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi16 – 194Poly-Lys
    Compositional biasi302 – 652351Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 UVR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG052712.
    InParanoidiQ9H2G2.
    KOiK08836.
    OMAiNIMITLE.
    OrthoDBiEOG7CNZF6.
    PhylomeDBiQ9H2G2.
    TreeFamiTF351445.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF00069. Pkinase. 1 hit.
    PF12474. PKK. 2 hits.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50151. UVR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H2G2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EDFWEIIGEL GDGAFGKVYK     50
    AQNKETSVLA AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY 100
    ENNLWILIEF CAGGAVDAVM LELERPLTES QIQVVCKQTL DALNYLHDNK 150
    IIHRDLKAGN ILFTLDGDIK LADFGVSAKN TRTIQRRDSF IGTPYWMAPE 200
    VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP MRVLLKIAKS 250
    EPPTLAQPSR WSSNFKDFLK KCLEKNVDAR WTTSQLLQHP FVTVDSNKPI 300
    RELIAEAKAE VTEEVEDGKE EDEEEETENS LPIPASKRAS SDLSIASSEE 350
    DKLSQNACIL ESVSEKTERS NSEDKLNSKI LNEKPTTDEP EKAVEDINEH 400
    ITDAQLEAMT ELHDRTAVIK ENEREKRPKL ENLPDTEDQE TVDINSVSEG 450
    KENNIMITLE TNIEHNLKSE EEKDQEKQQM FENKLIKSEE IKDTILQTVD 500
    LVSQETGEKE ANIQAVDSEV GLTKEDTQEK LGEDDKTQKD VISNTSDVIG 550
    TCEAADVAQK VDEDSAEDTQ SNDGKEVVEV GQKLINKPMV GPEAGGTKEV 600
    PIKEIVEMNE IEEGKNKEQA INSSENIMDI NEEPGTTEGE EITESSSTEE 650
    MEVRSVVADT DQKALGSEVQ DASKVTTQID KEKKEIPVSI KKEPEVTVVS 700
    QPTEPQPVLI PSININSDSG ENKEEIGSLS KTETILPPES ENPKENDNDS 750
    GTGSTADTSS IDLNLSISSF LSKTKDSGSI SLQETRRQKK TLKKTRKFIV 800
    DGVEVSVTTS KIVTDSDSKT EELRFLRRQE LRELRFLQKE EQRAQQQLNS 850
    KLQQQREQIF RRFEQEMMSK KRQYDQEIEN LEKQQKQTIE RLEQEHTNRL 900
    RDEAKRIKGE QEKELSKFQN MLKNRKKEVI NEVEKAPKEL RKELMKRRKE 950
    ELAQSQHAQE QEFVQKQQQE LDGSLKKIIQ QQKAELANIE RECLNNKQQL 1000
    MRAREAAIWE LEERHLQEKH QLLKQQLKDQ YFMQRHQLLK RHEKETEQMQ 1050
    RYNQRLIEEL KNRQTQERAR LPKIQRSEAK TRMAMFKKSL RINSTATPDQ 1100
    DRDKIKQFAA QEEKRQKNER MAQHQKHENQ MRDLQLQCEA NVRELHQLQN 1150
    EKCHLLVEHE TQKLKELDEE HSQELKEWRE KLRPRKKTLE EEFARKLQEQ 1200
    EVFFKMTGES ECLNPSTQSR ISKFYPIPSL HSTGS 1235
    Length:1,235
    Mass (Da):142,695
    Last modified:March 1, 2001 - v1
    Checksum:i53A43E7CA29B0ED3
    GO
    Isoform 2 (identifier: Q9H2G2-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,204
    Mass (Da):138,996
    Checksum:i2CA08AF0591C9AD6
    GO

    Sequence cautioni

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51N → S in BAA13195. (PubMed:9039502)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti405 – 4051Q → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041080
    Natural varianti552 – 5521C → Y.1 Publication
    Corresponds to variant rs805657 [ dbSNP | Ensembl ].
    VAR_041081
    Natural varianti604 – 6041E → Q in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_041082
    Natural varianti658 – 6581A → G.1 Publication
    Corresponds to variant rs56400929 [ dbSNP | Ensembl ].
    VAR_041083
    Natural varianti666 – 6661G → E.
    Corresponds to variant rs7071400 [ dbSNP | Ensembl ].
    VAR_051666
    Natural varianti679 – 6791I → T.1 Publication
    Corresponds to variant rs34326537 [ dbSNP | Ensembl ].
    VAR_041084
    Natural varianti683 – 6831K → N.1 Publication
    Corresponds to variant rs35389916 [ dbSNP | Ensembl ].
    VAR_041085
    Natural varianti697 – 6971T → I.1 Publication
    Corresponds to variant rs3740469 [ dbSNP | Ensembl ].
    VAR_041086

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei929 – 95931Missing in isoform 2. 3 PublicationsVSP_018100Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS7553.1. [Q9H2G2-1]
    RefSeqiNP_055535.2. NM_014720.2. [Q9H2G2-1]
    XP_005270358.1. XM_005270301.1. [Q9H2G2-2]
    UniGeneiHs.591922.

    Genome annotation databases

    EnsembliENST00000335753; ENSP00000336824; ENSG00000065613. [Q9H2G2-2]
    ENST00000369755; ENSP00000358770; ENSG00000065613. [Q9H2G2-1]
    GeneIDi9748.
    KEGGihsa:9748.
    UCSCiuc001kxo.1. human. [Q9H2G2-1]
    uc001kxp.1. human. [Q9H2G2-2]

    Polymorphism databases

    DMDMi74762732.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS7553.1. [Q9H2G2-1 ]
    RefSeqi NP_055535.2. NM_014720.2. [Q9H2G2-1 ]
    XP_005270358.1. XM_005270301.1. [Q9H2G2-2 ]
    UniGenei Hs.591922.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q9H2G2.
    SMRi Q9H2G2. Positions 21-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115096. 9 interactions.
    IntActi Q9H2G2. 5 interactions.
    MINTi MINT-4539212.
    STRINGi 9606.ENSP00000358770.

    Chemistry

    BindingDBi Q9H2G2.
    ChEMBLi CHEMBL4202.
    GuidetoPHARMACOLOGYi 2200.

    PTM databases

    PhosphoSitei Q9H2G2.

    Polymorphism databases

    DMDMi 74762732.

    Proteomic databases

    MaxQBi Q9H2G2.
    PaxDbi Q9H2G2.
    PRIDEi Q9H2G2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335753 ; ENSP00000336824 ; ENSG00000065613 . [Q9H2G2-2 ]
    ENST00000369755 ; ENSP00000358770 ; ENSG00000065613 . [Q9H2G2-1 ]
    GeneIDi 9748.
    KEGGi hsa:9748.
    UCSCi uc001kxo.1. human. [Q9H2G2-1 ]
    uc001kxp.1. human. [Q9H2G2-2 ]

    Organism-specific databases

    CTDi 9748.
    GeneCardsi GC10P105716.
    HGNCi HGNC:11088. SLK.
    HPAi HPA015757.
    neXtProti NX_Q9H2G2.
    PharmGKBi PA35941.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG052712.
    InParanoidi Q9H2G2.
    KOi K08836.
    OMAi NIMITLE.
    OrthoDBi EOG7CNZF6.
    PhylomeDBi Q9H2G2.
    TreeFami TF351445.

    Enzyme and pathway databases

    SignaLinki Q9H2G2.

    Miscellaneous databases

    EvolutionaryTracei Q9H2G2.
    GeneWikii SLK_(gene).
    GenomeRNAii 9748.
    NextBioi 36684.
    PMAP-CutDB Q9H2G2.
    PROi Q9H2G2.

    Gene expression databases

    Bgeei Q9H2G2.
    CleanExi HS_SLK.
    Genevestigatori Q9H2G2.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF00069. Pkinase. 1 hit.
    PF12474. PKK. 2 hits.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50151. UVR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiSLK_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2G2
    Secondary accession number(s): D3DRA0
    , D3DRA1, O00211, Q6P1Z4, Q86WU7, Q86WW1, Q92603, Q9NQL0, Q9NQL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3