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Q96S53

- TESK2_HUMAN

UniProt

Q96S53 - TESK2_HUMAN

Protein

Dual specificity testis-specific protein kinase 2

Gene

TESK2

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 129 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity
    Manganese.By similarity

    Enzyme regulationi

    Activated by autophosphorylation on Ser-219.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei87 – 871ATPPROSITE-ProRule annotation
    Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi64 – 729ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein kinase activity Source: ProtInc
    5. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
    6. protein serine/threonine kinase activity Source: UniProtKB
    7. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. focal adhesion assembly Source: UniProtKB
    3. protein phosphorylation Source: UniProtKB
    4. spermatogenesis Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity testis-specific protein kinase 2 (EC:2.7.12.1)
    Alternative name(s):
    Testicular protein kinase 2
    Gene namesi
    Name:TESK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11732. TESK2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36449.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 571571Dual specificity testis-specific protein kinase 2PRO_0000086749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei219 – 2191Phosphoserine; by autocatalysisBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ96S53.
    PRIDEiQ96S53.

    PTM databases

    PhosphoSiteiQ96S53.

    Expressioni

    Tissue specificityi

    Predominantly expressed in testis and prostate. Found predominantly in non-germinal Sertoli cells.2 Publications

    Gene expression databases

    ArrayExpressiQ96S53.
    BgeeiQ96S53.
    CleanExiHS_TESK2.
    GenevestigatoriQ96S53.

    Organism-specific databases

    HPAiHPA027257.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-1384110,EBI-352572

    Protein-protein interaction databases

    BioGridi115689. 3 interactions.
    IntActiQ96S53. 6 interactions.
    STRINGi9606.ENSP00000361158.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96S53.
    SMRiQ96S53. Positions 48-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 313256Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231415.
    HOVERGENiHBG058204.
    InParanoidiQ96S53.
    KOiK08842.
    OMAiNVLDPYY.
    OrthoDBiEOG7V7664.
    PhylomeDBiQ96S53.
    TreeFamiTF318014.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q96S53-1) [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

    MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF    50
    SRLTRLDDFT CEKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANMLK 100
    EVQLMNRLSH PNILRFMGVC VHQGQLHALT EYINSGNLEQ LLDSNLHLPW 150
    TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK NCLIKRDENG YSAVVADFGL 200
    AEKIPDVSMG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF SYGIILCEII 250
    ARIQADPDYL PRTENFGLDY DAFQHMVGDC PPDFLQLTFN CCNMDPKLRP 300
    SFVEIGKTLE EILSRLQEEE QERDRKLQPT ARGLLEKAPG VKRLSSLDDK 350
    IPHKSPCPRR TIWLSRSQSD IFSRKPPRTV SVLDPYYRPR DGAARTPKVN 400
    PFSARQDLMG GKIKFFDLPS KSVISLVFDL DAPGPGTMPL ADWQEPLAPP 450
    IRRWRSLPGS PEFLHQEACP FVGREESLSD GPPPRLSSLK YRVKEIPPFR 500
    ASALPAAQAH EAMDCSILQE ENGFGSRPQG TSPCPAGASE EMEVEERPAG 550
    STPATFSTSG IGLQTQGKQD G 571
    Length:571
    Mass (Da):63,639
    Last modified:December 1, 2001 - v1
    Checksum:iD83B0E58321A46FA
    GO
    Isoform 2 (identifier: Q96S53-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         116-131: Missing.

    Show »
    Length:555
    Mass (Da):61,887
    Checksum:iEFA1A38A53B68FD9
    GO
    Isoform 3 (identifier: Q96S53-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         265-293: Missing.

    Show »
    Length:542
    Mass (Da):60,332
    Checksum:iA4BE7D25116F20E1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti455 – 4551R → C in AAH33085. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111G → A in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
    VAR_041214

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei116 – 13116Missing in isoform 2. 1 PublicationVSP_004930Add
    BLAST
    Alternative sequencei265 – 29329Missing in isoform 3. 1 PublicationVSP_004931Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132545 mRNA. Translation: CAB41970.1.
    AB057597 mRNA. Translation: BAB62909.1.
    AK027573 mRNA. Translation: BAG51348.1.
    AL451136, AL359540 Genomic DNA. Translation: CAI13092.1.
    AL451136, AL359540 Genomic DNA. Translation: CAI13093.1.
    AL359540, AL451136 Genomic DNA. Translation: CAI21723.1.
    AL359540, AL451136 Genomic DNA. Translation: CAI21724.1.
    CH471059 Genomic DNA. Translation: EAX06987.1.
    BC033085 mRNA. Translation: AAH33085.1.
    CCDSiCCDS41323.1. [Q96S53-1]
    RefSeqiNP_009101.2. NM_007170.2. [Q96S53-1]
    XP_006710350.1. XM_006710287.1. [Q96S53-1]
    UniGeneiHs.591499.

    Genome annotation databases

    EnsembliENST00000372084; ENSP00000361156; ENSG00000070759. [Q96S53-3]
    ENST00000372086; ENSP00000361158; ENSG00000070759. [Q96S53-1]
    GeneIDi10420.
    KEGGihsa:10420.
    UCSCiuc001cns.1. human. [Q96S53-1]
    uc009vxr.1. human. [Q96S53-3]

    Polymorphism databases

    DMDMi25009462.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132545 mRNA. Translation: CAB41970.1 .
    AB057597 mRNA. Translation: BAB62909.1 .
    AK027573 mRNA. Translation: BAG51348.1 .
    AL451136 , AL359540 Genomic DNA. Translation: CAI13092.1 .
    AL451136 , AL359540 Genomic DNA. Translation: CAI13093.1 .
    AL359540 , AL451136 Genomic DNA. Translation: CAI21723.1 .
    AL359540 , AL451136 Genomic DNA. Translation: CAI21724.1 .
    CH471059 Genomic DNA. Translation: EAX06987.1 .
    BC033085 mRNA. Translation: AAH33085.1 .
    CCDSi CCDS41323.1. [Q96S53-1 ]
    RefSeqi NP_009101.2. NM_007170.2. [Q96S53-1 ]
    XP_006710350.1. XM_006710287.1. [Q96S53-1 ]
    UniGenei Hs.591499.

    3D structure databases

    ProteinModelPortali Q96S53.
    SMRi Q96S53. Positions 48-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115689. 3 interactions.
    IntActi Q96S53. 6 interactions.
    STRINGi 9606.ENSP00000361158.

    Chemistry

    ChEMBLi CHEMBL2069163.

    PTM databases

    PhosphoSitei Q96S53.

    Polymorphism databases

    DMDMi 25009462.

    Proteomic databases

    PaxDbi Q96S53.
    PRIDEi Q96S53.

    Protocols and materials databases

    DNASUi 10420.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372084 ; ENSP00000361156 ; ENSG00000070759 . [Q96S53-3 ]
    ENST00000372086 ; ENSP00000361158 ; ENSG00000070759 . [Q96S53-1 ]
    GeneIDi 10420.
    KEGGi hsa:10420.
    UCSCi uc001cns.1. human. [Q96S53-1 ]
    uc009vxr.1. human. [Q96S53-3 ]

    Organism-specific databases

    CTDi 10420.
    GeneCardsi GC01M045809.
    HGNCi HGNC:11732. TESK2.
    HPAi HPA027257.
    MIMi 604746. gene.
    neXtProti NX_Q96S53.
    PharmGKBi PA36449.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231415.
    HOVERGENi HBG058204.
    InParanoidi Q96S53.
    KOi K08842.
    OMAi NVLDPYY.
    OrthoDBi EOG7V7664.
    PhylomeDBi Q96S53.
    TreeFami TF318014.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.

    Miscellaneous databases

    ChiTaRSi TESK2. human.
    GeneWikii TESK2.
    GenomeRNAii 10420.
    NextBioi 39492.
    PROi Q96S53.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96S53.
    Bgeei Q96S53.
    CleanExi HS_TESK2.
    Genevestigatori Q96S53.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis."
      Rosok O., Pedeutour F., Ree A.H., Aasheim H.-C.
      Genomics 61:44-54(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells."
      Toshima J., Toshima J.Y., Takeuchi K., Mori R., Mizuno K.
      J. Biol. Chem. 276:31449-31458(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3).
      Tissue: Brain.
    7. "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: VARIANT [LARGE SCALE ANALYSIS] ALA-11.

    Entry informationi

    Entry nameiTESK2_HUMAN
    AccessioniPrimary (citable) accession number: Q96S53
    Secondary accession number(s): Q5T422
    , Q5T423, Q8N520, Q9Y3Q6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 129 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    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