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Q9H2G2

- SLK_HUMAN

UniProt

Q9H2G2 - SLK_HUMAN

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Protein

STE20-like serine/threonine-protein kinase

Gene
SLK, KIAA0204, STK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 631ATP By similarity
Active sitei155 – 1551Proton acceptor By similarity
Sitei438 – 4392Cleavage; by caspase-3 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi40 – 489ATP By similarity

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
  5. receptor signaling protein serine/threonine kinase activity Source: RefGenome

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. protein autophosphorylation Source: UniProtKB
  3. signal transduction by phosphorylation Source: GOC
Complete GO annotation...

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
Complete GO annotation...

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 – 141Phosphoserine1 Publication
Modified residuei189 – 1891Phosphoserine4 Publications
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei347 – 3471Phosphoserine2 Publications
Modified residuei348 – 3481Phosphoserine2 Publications
Modified residuei354 – 3541Phosphoserine By similarity
Modified residuei565 – 5651Phosphoserine3 Publications
Modified residuei571 – 5711Phosphoserine3 Publications
Modified residuei655 – 6551Phosphoserine1 Publication
Modified residuei777 – 7771Phosphoserine1 Publication
Modified residuei779 – 7791Phosphoserine3 Publications
Modified residuei818 – 8181Phosphoserine1 Publication
Modified residuei1097 – 10971Phosphothreonine1 Publication

Post-translational modificationi

Proteolytically cleaved by caspase-3.
Autophosphorylated.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiQ9H2G2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 292259Protein kinaseAdd
BLAST
Domaini875 – 91036UVRAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili826 – 1069244 Reviewed predictionAdd
BLAST
Coiled coili1109 – 118375 Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 UVR domain.

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.

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. VSP_018100Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51N → S in BAA13195. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 127 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

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