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)

Q96HS1

- PGAM5_HUMAN

UniProt

Q96HS1 - PGAM5_HUMAN

Protein

Serine/threonine-protein phosphatase PGAM5, mitochondrial

Gene

PGAM5

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 99 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression. Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore.3 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB
    2. phosphatase activity Source: UniProtKB
    3. phosphoprotein phosphatase activity Source: UniProtKB-EC
    4. protein complex binding Source: UniProtKB

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. necroptotic process Source: UniProtKB
    3. positive regulation of GTPase activity Source: GOC

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Necrosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PGAM5, mitochondrial (EC:3.1.3.16)
    Alternative name(s):
    Bcl-XL-binding protein v68
    Phosphoglycerate mutase family member 5
    Gene namesi
    Name:PGAM5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:28763. PGAM5.

    Subcellular locationi

    Mitochondrion outer membrane 1 Publication; Single-pass membrane protein 1 Publication
    Note: Isoform 2 overexpression results in the formation of disconnected punctuate mitochondria distributed throughout the cytoplasm. Isoform 1 overexpression results in the clustering of mitochondria around the nucleus.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial outer membrane Source: UniProtKB-SubCell
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791E → A: Loss of interaction with KEAP1; when associated with A-80. 1 Publication
    Mutagenesisi80 – 801S → A: Loss of interaction with KEAP1; when associated with A-79. 1 Publication
    Mutagenesisi105 – 1051H → A: Loss of phosphatase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485574.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Serine/threonine-protein phosphatase PGAM5, mitochondrialPRO_0000288782Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei116 – 1161N6-acetyllysine1 Publication
    Modified residuei144 – 1441N6-acetyllysine1 Publication
    Modified residuei191 – 1911N6-acetyllysine1 Publication

    Post-translational modificationi

    Both isoform 1 and isoform 2 are phosphorylated by the RIPK1/RIPK3 complex under necrotic conditions. This phosphorylation increases PGAM5 phosphatase activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96HS1.
    PaxDbiQ96HS1.
    PRIDEiQ96HS1.

    PTM databases

    PhosphoSiteiQ96HS1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96HS1.
    BgeeiQ96HS1.
    CleanExiHS_PGAM5.
    GenevestigatoriQ96HS1.

    Organism-specific databases

    HPAiHPA036978.
    HPA036979.

    Interactioni

    Subunit structurei

    Dimer. Forms a ternary complex with NFE2L2 and KEAP1. Interacts with BCL2L1 and MAP3K5. Upon TNF-induced necrosis, forms in complex with RIPK1, RIPK3 and MLKL; the formation of this complex leads to PGAM5 phosphorylation. Isoform 2, but not isoform 1, interacts with DNM1L; this interaction leads to DNM1L dephosphorylation and activation and eventually to mitochondria fragmentation.4 Publications

    Protein-protein interaction databases

    BioGridi128154. 42 interactions.
    DIPiDIP-50735N.
    IntActiQ96HS1. 28 interactions.
    MINTiMINT-1385191.

    Structurei

    Secondary structure

    1
    289
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi98 – 1047
    Helixi115 – 1173
    Helixi122 – 13615
    Beta strandi143 – 1508
    Helixi151 – 16212
    Beta strandi169 – 1724
    Helixi173 – 1753
    Helixi197 – 21115
    Beta strandi223 – 2297
    Helixi231 – 24111
    Helixi246 – 2516
    Beta strandi259 – 2646
    Beta strandi270 – 2778
    Helixi283 – 2853

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MXOX-ray1.70A/B90-289[»]
    3O0TX-ray1.90A/B90-289[»]
    ProteinModelPortaliQ96HS1.
    SMRiQ96HS1. Positions 89-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96HS1.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni77 – 826Interaction with KEAP1

    Domaini

    The N-terminal 35 amino acids, including the potential transmembrane alpha-helix, function as a non-cleaved mitochondrial targeting sequence that targets the protein to the cytosolic side of the outer mitochondrial membrane.1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71348.
    HOGENOMiHOG000261217.
    HOVERGENiHBG105576.
    InParanoidiQ96HS1.
    KOiK15637.
    OMAiWLRMSLN.
    OrthoDBiEOG7966H1.
    PhylomeDBiQ96HS1.
    TreeFamiTF314977.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    [Graphical view]
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96HS1-1) [UniParc]FASTAAdd to Basket

    Also known as: PGAM5-L

    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

    MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRAGGDAEPR PAEPPAWAGG    50
    ARPGPGVWDP NWDRREPLSL INVRKRNVES GEEELASKLD HYKAKATRHI 100
    FLIRHSQYHV DGSLEKDRTL TPLGREQAEL TGLRLASLGL KFNKIVHSSM 150
    TRAIETTDII SRHLPGVCKV STDLLREGAP IEPDPPVSHW KPEAVQYYED 200
    GARIEAAFRN YIHRADARQE EDSYEIFICH ANVIRYIVCR ALQFPPEGWL 250
    RLSLNNGSIT HLVIRPNGRV ALRTLGDTGF MPPDKITRS 289
    Length:289
    Mass (Da):32,004
    Last modified:May 29, 2007 - v2
    Checksum:iEE20D2F0A99FCD83
    GO
    Isoform 2 (identifier: Q96HS1-2) [UniParc]FASTAAdd to Basket

    Also known as: PGAM5-S

    The sequence of this isoform differs from the canonical sequence as follows:
         240-289: RALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKITRS → SIPPLLSAGDFVLLGS

    Show »
    Length:255
    Mass (Da):28,020
    Checksum:i07B881D6D8BE033C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241G → C in AAK60627. (PubMed:15489334)Curated
    Isoform 2 (identifier: Q96HS1-2)
    Sequence conflicti252 – 2521L → V in AAH08196. (PubMed:16541075)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei240 – 28950RALQF…KITRS → SIPPLLSAGDFVLLGS in isoform 2. 1 PublicationVSP_025761Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU249757 mRNA. Translation: ABX39494.1.
    AC135586 Genomic DNA. No translation available.
    BC008196 mRNA. Translation: AAH08196.1.
    AF357523 mRNA. Translation: AAK60627.1.
    CCDSiCCDS53845.1. [Q96HS1-1]
    CCDS9280.1. [Q96HS1-2]
    RefSeqiNP_001164014.1. NM_001170543.1. [Q96HS1-1]
    NP_612642.2. NM_138575.3. [Q96HS1-2]
    UniGeneiHs.102558.

    Genome annotation databases

    EnsembliENST00000317555; ENSP00000321503; ENSG00000247077. [Q96HS1-2]
    ENST00000498926; ENSP00000438465; ENSG00000247077. [Q96HS1-1]
    GeneIDi192111.
    KEGGihsa:192111.
    UCSCiuc001uku.3. human. [Q96HS1-2]
    uc009zyv.3. human. [Q96HS1-1]

    Polymorphism databases

    DMDMi150417955.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU249757 mRNA. Translation: ABX39494.1 .
    AC135586 Genomic DNA. No translation available.
    BC008196 mRNA. Translation: AAH08196.1 .
    AF357523 mRNA. Translation: AAK60627.1 .
    CCDSi CCDS53845.1. [Q96HS1-1 ]
    CCDS9280.1. [Q96HS1-2 ]
    RefSeqi NP_001164014.1. NM_001170543.1. [Q96HS1-1 ]
    NP_612642.2. NM_138575.3. [Q96HS1-2 ]
    UniGenei Hs.102558.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MXO X-ray 1.70 A/B 90-289 [» ]
    3O0T X-ray 1.90 A/B 90-289 [» ]
    ProteinModelPortali Q96HS1.
    SMRi Q96HS1. Positions 89-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128154. 42 interactions.
    DIPi DIP-50735N.
    IntActi Q96HS1. 28 interactions.
    MINTi MINT-1385191.

    PTM databases

    PhosphoSitei Q96HS1.

    Polymorphism databases

    DMDMi 150417955.

    Proteomic databases

    MaxQBi Q96HS1.
    PaxDbi Q96HS1.
    PRIDEi Q96HS1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317555 ; ENSP00000321503 ; ENSG00000247077 . [Q96HS1-2 ]
    ENST00000498926 ; ENSP00000438465 ; ENSG00000247077 . [Q96HS1-1 ]
    GeneIDi 192111.
    KEGGi hsa:192111.
    UCSCi uc001uku.3. human. [Q96HS1-2 ]
    uc009zyv.3. human. [Q96HS1-1 ]

    Organism-specific databases

    CTDi 192111.
    GeneCardsi GC12P133287.
    H-InvDB HIX0017319.
    HGNCi HGNC:28763. PGAM5.
    HPAi HPA036978.
    HPA036979.
    MIMi 614939. gene.
    neXtProti NX_Q96HS1.
    PharmGKBi PA143485574.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71348.
    HOGENOMi HOG000261217.
    HOVERGENi HBG105576.
    InParanoidi Q96HS1.
    KOi K15637.
    OMAi WLRMSLN.
    OrthoDBi EOG7966H1.
    PhylomeDBi Q96HS1.
    TreeFami TF314977.

    Miscellaneous databases

    EvolutionaryTracei Q96HS1.
    GenomeRNAii 192111.
    NextBioi 89319.
    PROi Q96HS1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96HS1.
    Bgeei Q96HS1.
    CleanExi HS_PGAM5.
    Genevestigatori Q96HS1.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    [Graphical view ]
    Pfami PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-regulated Keap1-dependent ubiquitin ligase complex."
      Lo S.-C., Hannink M.
      J. Biol. Chem. 281:37893-37903(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING, SUBUNIT, INTERACTION WITH BCL2L1 AND KEAP1, MUTAGENESIS OF GLU-79 AND SER-80.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Cervix.
    4. "In vitro selection and characterization of Bcl-X(L)-binding proteins from a mix of tissue-specific mRNA display libraries."
      Hammond P.W., Alpin J., Rise C.E., Wright M., Kreider B.L.
      J. Biol. Chem. 276:20898-20906(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-157.
      Tissue: Kidney.
    5. "PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria."
      Lo S.-C., Hannink M.
      Exp. Cell Res. 314:1789-1803(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH NFE2L2 AND KEAP1, FUNCTION, SUBCELLULAR LOCATION.
    6. "Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1."
      Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S., Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.
      Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K5, MUTAGENESIS OF HIS-105.
    7. "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-116; LYS-144 AND LYS-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways."
      Wang Z., Jiang H., Chen S., Du F., Wang X.
      Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH RIPK1; RIPK3 AND MLKL, INTERACTION WITH DNM1L.
    11. "Crystal structure of human phosphoglycerate mutase family member 5 (PGAM5)."
      Structural genomics consortium (SGC)
      Submitted (SEP-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 90-289.

    Entry informationi

    Entry nameiPGAM5_HUMAN
    AccessioniPrimary (citable) accession number: Q96HS1
    Secondary accession number(s): A9LN06, C9IZY7, Q96JB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 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 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3