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Q9UEW8

- STK39_HUMAN

UniProt

Q9UEW8 - STK39_HUMAN

Protein

STE20/SPS1-related proline-alanine-rich protein kinase

Gene

STK39

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    May act as a mediator of stress-activated signals.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921ATPPROSITE-ProRule annotation
    Active sitei192 – 1921Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi69 – 779ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein kinase activity Source: InterPro
    4. protein serine/threonine kinase activity Source: BHF-UCL
    5. receptor signaling protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular hypotonic response Source: BHF-UCL
    2. intracellular signal transduction Source: BHF-UCL
    3. negative regulation of potassium ion transmembrane transport Source: BHF-UCL
    4. negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
    5. negative regulation of rubidium ion transmembrane transporter activity Source: BHF-UCL
    6. negative regulation of rubidium ion transport Source: BHF-UCL
    7. peptidyl-serine phosphorylation Source: BHF-UCL
    8. peptidyl-threonine phosphorylation Source: BHF-UCL
    9. positive regulation of potassium ion transport Source: Ensembl
    10. protein phosphorylation Source: UniProtKB
    11. regulation of inflammatory response Source: Ensembl
    12. response to stress Source: UniProtKB
    13. signal transduction by phosphorylation Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    SignaLinkiQ9UEW8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    STE20/SPS1-related proline-alanine-rich protein kinase (EC:2.7.11.1)
    Short name:
    Ste-20-related kinase
    Alternative name(s):
    DCHT
    Serine/threonine-protein kinase 39
    Gene namesi
    Name:STK39
    Synonyms:SPAK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17717. STK39.

    Subcellular locationi

    Cytoplasm Curated. Nucleus Curated
    Note: Nucleus when caspase-cleaved.Curated

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. basolateral plasma membrane Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. cytoskeleton Source: Ensembl
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38243.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 545545STE20/SPS1-related proline-alanine-rich protein kinasePRO_0000086722Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei309 – 3091Phosphoserine; by PKC/PRKCQ1 Publication
    Modified residuei349 – 3491N6-acetyllysine1 Publication
    Modified residuei354 – 3541PhosphothreonineBy similarity
    Modified residuei370 – 3701Phosphoserine1 Publication
    Modified residuei371 – 3711Phosphoserine1 Publication
    Modified residuei385 – 3851Phosphoserine5 Publications

    Post-translational modificationi

    Phosphorylated at Ser-309 by PRKCQ.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UEW8.
    PaxDbiQ9UEW8.
    PeptideAtlasiQ9UEW8.
    PRIDEiQ9UEW8.

    PTM databases

    PhosphoSiteiQ9UEW8.

    Expressioni

    Tissue specificityi

    Predominantly expressed in brain and pancreas followed by heart, lung, kidney, skeletal muscle, liver, placenta and testis.

    Gene expression databases

    BgeeiQ9UEW8.
    CleanExiHS_STK39.
    GenevestigatoriQ9UEW8.

    Organism-specific databases

    HPAiCAB046022.

    Interactioni

    Subunit structurei

    The phosphorylated form forms a complex with WNK2.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAB39Q9Y3764EBI-2680974,EBI-306905

    Protein-protein interaction databases

    BioGridi118159. 18 interactions.
    IntActiQ9UEW8. 4 interactions.
    MINTiMINT-6783158.
    STRINGi9606.ENSP00000348278.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UEW8.
    SMRiQ9UEW8. Positions 53-397, 452-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 337275Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi360 – 3667Nuclear localization signalSequence Analysis
    Motifi387 – 3915Caspase cleavage related site

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 5342Ala/Pro-richAdd
    BLAST

    Domaini

    PAPA box (proline-alanine repeats) may target the kinase to a specific subcellular location by facilitating interaction with intracellular proteins such as actin or actin-like proteins.

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000234204.
    HOVERGENiHBG108518.
    InParanoidiQ9UEW8.
    KOiK08835.
    OMAiLSVHDSQ.
    OrthoDBiEOG715Q3W.
    PhylomeDBiQ9UEW8.
    TreeFamiTF105339.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR024678. Kinase_OSR1/WNK_CCT.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view]
    PfamiPF12202. OSR1_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [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.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UEW8-1) [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

    MAEPSGSPVH VQLPQQAAPV TAAAAAAPAA ATAAPAPAAP AAPAPAPAPA    50
    AQAVGWPICR DAYELQEVIG SGATAVVQAA LCKPRQERVA IKRINLEKCQ 100
    TSMDELLKEI QAMSQCSHPN VVTYYTSFVV KDELWLVMKL LSGGSMLDII 150
    KYIVNRGEHK NGVLEEAIIA TILKEVLEGL DYLHRNGQIH RDLKAGNILL 200
    GEDGSVQIAD FGVSAFLATG GDVTRNKVRK TFVGTPCWMA PEVMEQVRGY 250
    DFKADMWSFG ITAIELATGA APYHKYPPMK VLMLTLQNDP PTLETGVEDK 300
    EMMKKYGKSF RKLLSLCLQK DPSKRPTAAE LLKCKFFQKA KNREYLIEKL 350
    LTRTPDIAQR AKKVRRVPGS SGHLHKTEDG DWEWSDDEMD EKSEEGKAAF 400
    SQEKSRRVKE ENPEIAVSAS TIPEQIQSLS VHDSQGPPNA NEDYREASSC 450
    AVNLVLRLRN SRKELNDIRF EFTPGRDTAD GVSQELFSAG LVDGHDVVIV 500
    AANLQKIVDD PKALKTLTFK LASGCDGSEI PDEVKLIGFA QLSVS 545
    Length:545
    Mass (Da):59,474
    Last modified:January 11, 2011 - v3
    Checksum:i35E68F400A38A861
    GO
    Isoform 2 (identifier: Q9UEW8-2) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         28-46: Missing.

    Show »
    Length:526
    Mass (Da):57,937
    Checksum:iA1DD278DEE7A4334
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411A → AAP in AAC72238. (PubMed:10980603)Curated
    Sequence conflicti41 – 411A → AAP in AAD01901. 1 PublicationCurated
    Sequence conflicti173 – 1731L → F in AAD01901. 1 PublicationCurated
    Sequence conflicti416 – 4161A → V in AHW56588. (PubMed:24722188)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei28 – 4619Missing in isoform 2. 1 PublicationVSP_055889Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF099989 mRNA. Translation: AAC72238.1.
    KJ534948 mRNA. Translation: AHW56588.1.
    AF030403 mRNA. Translation: AAD01901.1.
    AC016723 Genomic DNA. Translation: AAY15003.1.
    AC017069 Genomic DNA. Translation: AAY14897.1.
    AC067940 Genomic DNA. Translation: AAY24032.1.
    AF017635 mRNA. Translation: AAB70552.1.
    CCDSiCCDS42770.1.
    RefSeqiNP_037365.2. NM_013233.2.
    UniGeneiHs.276271.

    Genome annotation databases

    EnsembliENST00000355999; ENSP00000348278; ENSG00000198648. [Q9UEW8-1]
    GeneIDi27347.
    KEGGihsa:27347.
    UCSCiuc002uea.3. human.

    Polymorphism databases

    DMDMi317373508.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF099989 mRNA. Translation: AAC72238.1 .
    KJ534948 mRNA. Translation: AHW56588.1 .
    AF030403 mRNA. Translation: AAD01901.1 .
    AC016723 Genomic DNA. Translation: AAY15003.1 .
    AC017069 Genomic DNA. Translation: AAY14897.1 .
    AC067940 Genomic DNA. Translation: AAY24032.1 .
    AF017635 mRNA. Translation: AAB70552.1 .
    CCDSi CCDS42770.1.
    RefSeqi NP_037365.2. NM_013233.2.
    UniGenei Hs.276271.

    3D structure databases

    ProteinModelPortali Q9UEW8.
    SMRi Q9UEW8. Positions 53-397, 452-545.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118159. 18 interactions.
    IntActi Q9UEW8. 4 interactions.
    MINTi MINT-6783158.
    STRINGi 9606.ENSP00000348278.

    Chemistry

    BindingDBi Q9UEW8.
    ChEMBLi CHEMBL1163108.
    GuidetoPHARMACOLOGYi 2224.

    PTM databases

    PhosphoSitei Q9UEW8.

    Polymorphism databases

    DMDMi 317373508.

    Proteomic databases

    MaxQBi Q9UEW8.
    PaxDbi Q9UEW8.
    PeptideAtlasi Q9UEW8.
    PRIDEi Q9UEW8.

    Protocols and materials databases

    DNASUi 27347.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355999 ; ENSP00000348278 ; ENSG00000198648 . [Q9UEW8-1 ]
    GeneIDi 27347.
    KEGGi hsa:27347.
    UCSCi uc002uea.3. human.

    Organism-specific databases

    CTDi 27347.
    GeneCardsi GC02M168774.
    H-InvDB HIX0023910.
    HGNCi HGNC:17717. STK39.
    HPAi CAB046022.
    MIMi 607648. gene.
    neXtProti NX_Q9UEW8.
    PharmGKBi PA38243.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000234204.
    HOVERGENi HBG108518.
    InParanoidi Q9UEW8.
    KOi K08835.
    OMAi LSVHDSQ.
    OrthoDBi EOG715Q3W.
    PhylomeDBi Q9UEW8.
    TreeFami TF105339.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki Q9UEW8.

    Miscellaneous databases

    GeneWikii STK39.
    GenomeRNAii 27347.
    NextBioi 50438.
    PROi Q9UEW8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UEW8.
    CleanExi HS_STK39.
    Genevestigatori Q9UEW8.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR024678. Kinase_OSR1/WNK_CCT.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    [Graphical view ]
    Pfami PF12202. OSR1_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SPAK, a STE20/SPS1-related kinase that activates the p38 pathway."
      Johnston A.M., Naselli G., Gonez L.J., Martin R.M., Harrison L.C., de Aizpurua H.J.
      Oncogene 19:4290-4297(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "New human member of the Ste20 family."
      Melnick M.B., Petitt M., Perrimon N., Comb M.J.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Baytel D., Don J.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 279-545 (ISOFORM 1).
      Tissue: Testis.
    6. "SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway."
      Li Y., Hu J., Vita R., Sun B., Tabata H., Altman A.
      EMBO J. 23:1112-1122(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-309.
    7. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-385, 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-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSTK39_HUMAN
    AccessioniPrimary (citable) accession number: Q9UEW8
    Secondary accession number(s): O14774
    , Q53S90, Q53SL7, Q53SS1, Q9UER4, X5D9C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 141 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3