Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q86V86

- PIM3_HUMAN

UniProt

Q86V86 - PIM3_HUMAN

Protein

Serine/threonine-protein kinase pim-3

Gene

PIM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis, promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regulation of cell cycle progression, protein synthesis and by regulation of MYC transcriptional activity. Additionally to this role on tumorigenesis, can also negatively regulate insulin secretion by inhibiting the activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the control of energy metabolism and regulation of AMPK activity in modulating MYC and PPARGC1A protein levels and cell growth.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691ATPPROSITE-ProRule annotation
    Active sitei170 – 1701Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi46 – 549ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell cycle Source: UniProtKB-KW
    3. histone phosphorylation Source: Ensembl
    4. negative regulation of apoptotic process Source: UniProtKB
    5. negative regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    6. protein autophosphorylation Source: Ensembl
    7. protein phosphorylation Source: UniProtKB
    8. regulation of mitotic cell cycle Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ86V86.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase pim-3 (EC:2.7.11.1)
    Gene namesi
    Name:PIM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:19310. PIM3.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA134980758.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326Serine/threonine-protein kinase pim-3PRO_0000086533Add
    BLAST

    Post-translational modificationi

    Ubiquitinated, leading to proteasomal degradation.1 Publication
    Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ86V86.
    PRIDEiQ86V86.

    PTM databases

    PhosphoSiteiQ86V86.

    Expressioni

    Tissue specificityi

    Detected in various tissues, including the heart, brain, lung, kidney, spleen, placenta, skeletal muscle, and peripheral blood leukocytes. Not found or barely expressed in the normal adult endoderm-derived organs such as colon, thymus, liver, or small intestine. However, expression is augmented in premalignant and malignant lesions of these organs.3 Publications

    Gene expression databases

    BgeeiQ86V86.
    CleanExiHS_PIM3.
    GenevestigatoriQ86V86.

    Interactioni

    Subunit structurei

    Interacts with BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation of PIM3, ubiquitination and proteasomal degradation. Interacts with SOCS6 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi136104. 2 interactions.
    IntActiQ86V86. 2 interactions.
    MINTiMINT-6823599.
    STRINGi9606.ENSP00000353824.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86V86.
    SMRiQ86V86. Positions 40-293.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 293254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231357.
    HOVERGENiHBG106681.
    InParanoidiQ86V86.
    KOiK08807.
    OMAiRVTEWGT.
    OrthoDBiEOG7NW6B0.
    PhylomeDBiQ86V86.
    TreeFamiTF320810.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. 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.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q86V86-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLSKFGSLA HLCGPGGVDH LPVKILQPAK ADKESFEKAY QVGAVLGSGG    50
    FGTVYAGSRI ADGLPVAVKH VVKERVTEWG SLGGATVPLE VVLLRKVGAA 100
    GGARGVIRLL DWFERPDGFL LVLERPEPAQ DLFDFITERG ALDEPLARRF 150
    FAQVLAAVRH CHSCGVVHRD IKDENLLVDL RSGELKLIDF GSGALLKDTV 200
    YTDFDGTRVY SPPEWIRYHR YHGRSATVWS LGVLLYDMVC GDIPFEQDEE 250
    ILRGRLLFRR RVSPECQQLI RWCLSLRPSE RPSLDQIAAH PWMLGADGGV 300
    PESCDLRLCT LDPDDVASTT SSSESL 326
    Length:326
    Mass (Da):35,891
    Last modified:November 25, 2008 - v3
    Checksum:i41FDEFAC4367A162
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371E → K in AAI41856. (PubMed:15489334)Curated
    Sequence conflicti300 – 3001V → A in BAD42438. (PubMed:15540201)Curated
    Sequence conflicti300 – 3001V → A in BAF84694. (PubMed:16141072)Curated
    Sequence conflicti300 – 3001V → A in AAI41856. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB114795 mRNA. Translation: BAD42438.1.
    AK292005 mRNA. Translation: BAF84694.1.
    CR536608, BX539320 Genomic DNA. Translation: CAO03523.1.
    BX539320, CR536608 Genomic DNA. Translation: CAO03581.1.
    BC052239 mRNA. No translation available.
    BC141855 mRNA. Translation: AAI41856.1.
    CCDSiCCDS33678.1.
    RefSeqiNP_001001852.2. NM_001001852.3.
    UniGeneiHs.530381.

    Genome annotation databases

    EnsembliENST00000360612; ENSP00000353824; ENSG00000198355.
    GeneIDi415116.
    KEGGihsa:415116.
    UCSCiuc003bjb.3. human.

    Polymorphism databases

    DMDMi215274221.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB114795 mRNA. Translation: BAD42438.1 .
    AK292005 mRNA. Translation: BAF84694.1 .
    CR536608 , BX539320 Genomic DNA. Translation: CAO03523.1 .
    BX539320 , CR536608 Genomic DNA. Translation: CAO03581.1 .
    BC052239 mRNA. No translation available.
    BC141855 mRNA. Translation: AAI41856.1 .
    CCDSi CCDS33678.1.
    RefSeqi NP_001001852.2. NM_001001852.3.
    UniGenei Hs.530381.

    3D structure databases

    ProteinModelPortali Q86V86.
    SMRi Q86V86. Positions 40-293.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 136104. 2 interactions.
    IntActi Q86V86. 2 interactions.
    MINTi MINT-6823599.
    STRINGi 9606.ENSP00000353824.

    Chemistry

    BindingDBi Q86V86.
    ChEMBLi CHEMBL5407.
    GuidetoPHARMACOLOGYi 2160.

    PTM databases

    PhosphoSitei Q86V86.

    Polymorphism databases

    DMDMi 215274221.

    Proteomic databases

    PaxDbi Q86V86.
    PRIDEi Q86V86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360612 ; ENSP00000353824 ; ENSG00000198355 .
    GeneIDi 415116.
    KEGGi hsa:415116.
    UCSCi uc003bjb.3. human.

    Organism-specific databases

    CTDi 415116.
    GeneCardsi GC22P050354.
    H-InvDB HIX0203204.
    HGNCi HGNC:19310. PIM3.
    MIMi 610580. gene.
    neXtProti NX_Q86V86.
    PharmGKBi PA134980758.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231357.
    HOVERGENi HBG106681.
    InParanoidi Q86V86.
    KOi K08807.
    OMAi RVTEWGT.
    OrthoDBi EOG7NW6B0.
    PhylomeDBi Q86V86.
    TreeFami TF320810.

    Enzyme and pathway databases

    SignaLinki Q86V86.

    Miscellaneous databases

    ChiTaRSi PIM3. human.
    GenomeRNAii 415116.
    NextBioi 108679.
    PROi Q86V86.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q86V86.
    CleanExi HS_PIM3.
    Genevestigatori Q86V86.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami 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.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Aberrant expression of serine/threonine kinase Pim-3 in hepatocellular carcinoma development and its role in the proliferation of human hepatoma cell lines."
      Fujii C., Nakamoto Y., Lu P., Tsuneyama K., Popivanova B.K., Kaneko S., Mukaida N.
      Int. J. Cancer 114:209-218(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Small intestine.
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Tissue: Lymph.
    5. Cited for: IDENTIFICATION FROM ESTS.
    6. "Protein phosphatase 2A regulates the stability of Pim protein kinases."
      Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
      J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP2CA, PHOSPHORYLATION, UBIQUITINATION.
    7. "Pim-3, a proto-oncogene with serine/threonine kinase activity, is aberrantly expressed in human pancreatic cancer and phosphorylates bad to block bad-mediated apoptosis in human pancreatic cancer cell lines."
      Li Y.Y., Popivanova B.K., Nagai Y., Ishikura H., Fujii C., Mukaida N.
      Cancer Res. 66:6741-6747(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BAD, TISSUE SPECIFICITY.
    8. "Proto-oncogene, Pim-3 with serine/threonine kinase activity, is aberrantly expressed in human colon cancer cells and can prevent Bad-mediated apoptosis."
      Popivanova B.K., Li Y.Y., Zheng H., Omura K., Fujii C., Tsuneyama K., Mukaida N.
      Cancer Sci. 98:321-328(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BAD, TISSUE SPECIFICITY.
    9. "Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."
      Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
      Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDKN1B.
    10. "Aberrant Pim-3 expression is involved in gastric adenoma-adenocarcinoma sequence and cancer progression."
      Zheng H.C., Tsuneyama K., Takahashi H., Miwa S., Sugiyama T., Popivanova B.K., Fujii C., Nomoto K., Mukaida N., Takano Y.
      J. Cancer Res. Clin. Oncol. 134:481-488(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION.

    Entry informationi

    Entry nameiPIM3_HUMAN
    AccessioniPrimary (citable) accession number: Q86V86
    Secondary accession number(s): A5D8X8
    , A8K7J0, B1B0P0, Q68BM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 21, 2003
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 108 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 22
      Human chromosome 22: 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