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Q16816

- PHKG1_HUMAN

UniProt

Q16816 - PHKG1_HUMAN

Protein

Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform

Gene

PHKG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 By similarity.By similarity

    Catalytic activityi

    2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
    ATP + [tau protein] = ADP + [tau protein] phosphate.
    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei49 – 491ATPPROSITE-ProRule annotation
    Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphorylase kinase activity Source: UniProtKB-EC
    3. tau-protein kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glucose metabolic process Source: Reactome
    3. glycogen biosynthetic process Source: InterPro
    4. glycogen catabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    ATP-binding, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09136-MONOMER.
    BRENDAi2.7.11.19. 2681.
    ReactomeiREACT_1008. Glycogen breakdown (glycogenolysis).
    SignaLinkiQ16816.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC:2.7.11.19)
    Short name:
    PHK-gamma-M
    Alternative name(s):
    Phosphorylase kinase subunit gamma-1
    Serine/threonine-protein kinase PHKG1 (EC:2.7.11.1, EC:2.7.11.26)
    Gene namesi
    Name:PHKG1
    Synonyms:PHKG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8930. PHKG1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. phosphorylase kinase complex Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
    PharmGKBiPA33271.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 387386Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoformPRO_0000086508Add
    BLAST

    Proteomic databases

    PaxDbiQ16816.
    PRIDEiQ16816.

    PTM databases

    PhosphoSiteiQ16816.

    Miscellaneous databases

    PMAP-CutDBQ16816.

    Expressioni

    Gene expression databases

    ArrayExpressiQ16816.
    BgeeiQ16816.
    CleanExiHS_PHKG1.
    GenevestigatoriQ16816.

    Organism-specific databases

    HPAiHPA012057.

    Interactioni

    Subunit structurei

    Hexadecamer of 4 heterotetramers, each composed of alpha, beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic subunit, and delta is calmodulin.

    Protein-protein interaction databases

    BioGridi111278. 1 interaction.
    STRINGi9606.ENSP00000297373.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16816.
    SMRiQ16816. Positions 16-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 288269Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni303 – 32725Calmodulin-binding (domain-N)Add
    BLAST
    Regioni343 – 36725Calmodulin-binding (domain-C)Add
    BLAST

    Domaini

    The two calmodulin-binding domains appear to act in concert to bind a single molecule of calmodulin and are pseudosubstrate/autoinhibitory domains.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG106193.
    KOiK00871.
    OMAiQNRYTAE.
    OrthoDBiEOG7JMGDM.
    PhylomeDBiQ16816.
    TreeFamiTF320349.

    Family and domain databases

    InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR011009. Kinase-like_dom.
    IPR002291. Phosph_kin_gamma.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24347. PTHR24347. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01049. PHOSPHBKNASE.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16816-1) [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

    MTRDEALPDS HSAQDFYENY EPKEILGRGV SSVVRRCIHK PTSQEYAVKV    50
    IDVTGGGSFS PEEVRELREA TLKEVDILRK VSGHPNIIQL KDTYETNTFF 100
    FLVFDLMKRG ELFDYLTEKV TLSEKETRKI MRALLEVICT LHKLNIVHRD 150
    LKPENILLDD NMNIKLTDFG FSCQLEPGER LREVCGTPSY LAPEIIECSM 200
    NEDHPGYGKE VDMWSTGVIM YTLLAGSPPF WHRKQMLMLR MIMSGNYQFG 250
    SPEWDDYSDT VKDLVSRFLV VQPQNRYTAE EALAHPFFQQ YLVEEVRHFS 300
    PRGKFKVIAL TVLASVRIYY QYRRVKPVTR EIVIRDPYAL RPLRRLIDAY 350
    AFRIYGHWVK KGQQQNRAAL FENTPKAVLL SLAEEDY 387
    Length:387
    Mass (Da):45,024
    Last modified:January 23, 2007 - v3
    Checksum:i9CB416CB683920AA
    GO
    Isoform 2 (identifier: Q16816-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         106-106: L → LWEDTDTMEMEQKWCLGWDSPKSTNFRAQGRAR

    Note: No experimental confirmation available.

    Show »
    Length:419
    Mass (Da):48,867
    Checksum:i99429FF321971C5E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001F → L in BAH11466. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481V → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040994
    Natural varianti323 – 3231R → C.1 Publication
    Corresponds to variant rs149458708 [ dbSNP | Ensembl ].
    VAR_040995

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei106 – 1061L → LWEDTDTMEMEQKWCLGWDS PKSTNFRAQGRAR in isoform 2. 1 PublicationVSP_044716

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80590 mRNA. Translation: CAA56681.1.
    AF254253
    , AF254250, AF254251, AF254252 Genomic DNA. Translation: AAL36972.1.
    AK293180 mRNA. Translation: BAH11466.1.
    AC092101 Genomic DNA. Translation: AAS07453.1.
    CH471140 Genomic DNA. Translation: EAX07987.1.
    BC051327 mRNA. Translation: AAH51327.1.
    BC069679 mRNA. Translation: AAH69679.1.
    BC069738 mRNA. Translation: AAH69738.1.
    BC069754 mRNA. Translation: AAH69754.1.
    BC074753 mRNA. Translation: AAH74753.1.
    CCDSiCCDS5525.1. [Q16816-1]
    CCDS59057.1. [Q16816-2]
    RefSeqiNP_001245388.1. NM_001258459.1. [Q16816-2]
    NP_006204.1. NM_006213.4. [Q16816-1]
    UniGeneiHs.730821.

    Genome annotation databases

    EnsembliENST00000297373; ENSP00000297373; ENSG00000164776. [Q16816-1]
    ENST00000452681; ENSP00000445440; ENSG00000164776. [Q16816-2]
    GeneIDi5260.
    KEGGihsa:5260.
    UCSCiuc003try.2. human. [Q16816-1]

    Polymorphism databases

    DMDMi2833281.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80590 mRNA. Translation: CAA56681.1 .
    AF254253
    , AF254250 , AF254251 , AF254252 Genomic DNA. Translation: AAL36972.1 .
    AK293180 mRNA. Translation: BAH11466.1 .
    AC092101 Genomic DNA. Translation: AAS07453.1 .
    CH471140 Genomic DNA. Translation: EAX07987.1 .
    BC051327 mRNA. Translation: AAH51327.1 .
    BC069679 mRNA. Translation: AAH69679.1 .
    BC069738 mRNA. Translation: AAH69738.1 .
    BC069754 mRNA. Translation: AAH69754.1 .
    BC074753 mRNA. Translation: AAH74753.1 .
    CCDSi CCDS5525.1. [Q16816-1 ]
    CCDS59057.1. [Q16816-2 ]
    RefSeqi NP_001245388.1. NM_001258459.1. [Q16816-2 ]
    NP_006204.1. NM_006213.4. [Q16816-1 ]
    UniGenei Hs.730821.

    3D structure databases

    ProteinModelPortali Q16816.
    SMRi Q16816. Positions 16-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111278. 1 interaction.
    STRINGi 9606.ENSP00000297373.

    Chemistry

    BindingDBi Q16816.
    ChEMBLi CHEMBL4004.
    GuidetoPHARMACOLOGYi 2145.

    PTM databases

    PhosphoSitei Q16816.

    Polymorphism databases

    DMDMi 2833281.

    Proteomic databases

    PaxDbi Q16816.
    PRIDEi Q16816.

    Protocols and materials databases

    DNASUi 5260.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297373 ; ENSP00000297373 ; ENSG00000164776 . [Q16816-1 ]
    ENST00000452681 ; ENSP00000445440 ; ENSG00000164776 . [Q16816-2 ]
    GeneIDi 5260.
    KEGGi hsa:5260.
    UCSCi uc003try.2. human. [Q16816-1 ]

    Organism-specific databases

    CTDi 5260.
    GeneCardsi GC07M056115.
    HGNCi HGNC:8930. PHKG1.
    HPAi HPA012057.
    MIMi 172470. gene.
    neXtProti NX_Q16816.
    Orphaneti 715. Glycogen storage disease due to muscle phosphorylase kinase deficiency.
    PharmGKBi PA33271.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG106193.
    KOi K00871.
    OMAi QNRYTAE.
    OrthoDBi EOG7JMGDM.
    PhylomeDBi Q16816.
    TreeFami TF320349.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09136-MONOMER.
    BRENDAi 2.7.11.19. 2681.
    Reactomei REACT_1008. Glycogen breakdown (glycogenolysis).
    SignaLinki Q16816.

    Miscellaneous databases

    GeneWikii PHKG1.
    GenomeRNAii 5260.
    NextBioi 20318.
    PMAP-CutDB Q16816.
    PROi Q16816.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16816.
    Bgeei Q16816.
    CleanExi HS_PHKG1.
    Genevestigatori Q16816.

    Family and domain databases

    InterProi IPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
    IPR011009. Kinase-like_dom.
    IPR002291. Phosph_kin_gamma.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24347. PTHR24347. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01049. PHOSPHBKNASE.
    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. "Human cDNA encoding the muscle isoform of the phosphorylase kinase gamma subunit (PHKG1)."
      Wehner M., Kilimann M.W.
      Hum. Genet. 96:616-618(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    2. Burwinkel B. Jr., Kilimann M.W. Sr.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 2).
      Tissue: Adrenal gland.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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 1).
      Tissue: Salivary gland.
    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: VARIANTS [LARGE SCALE ANALYSIS] MET-48 AND CYS-323.

    Entry informationi

    Entry nameiPHKG1_HUMAN
    AccessioniPrimary (citable) accession number: Q16816
    Secondary accession number(s): B7Z1D0, F5H2S1, Q75LP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 145 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 7
      Human chromosome 7: 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