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Q6NVY1

- HIBCH_HUMAN

UniProt

Q6NVY1 - HIBCH_HUMAN

Protein

3-hydroxyisobutyryl-CoA hydrolase, mitochondrial

Gene

HIBCH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA.1 Publication

    Catalytic activityi

    3-hydroxy-2-methylpropanoyl-CoA + H2O = CoA + 3-hydroxy-2-methylpropanoate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei121 – 1211Substrate
    Binding sitei146 – 1461Substrate; via amide nitrogen
    Binding sitei169 – 1691Substrate
    Binding sitei177 – 1771Substrate

    GO - Molecular functioni

    1. 3-hydroxyisobutyryl-CoA hydrolase activity Source: UniProtKB

    GO - Biological processi

    1. branched-chain amino acid catabolic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome
    4. valine catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Branched-chain amino acid catabolism

    Enzyme and pathway databases

    BRENDAi3.1.2.4. 2681.
    ReactomeiREACT_197. Branched-chain amino acid catabolism.
    SABIO-RKQ6NVY1.
    UniPathwayiUPA00362.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyisobutyryl-CoA hydrolase, mitochondrial (EC:3.1.2.4)
    Alternative name(s):
    3-hydroxyisobutyryl-coenzyme A hydrolase
    Short name:
    HIB-CoA hydrolase
    Short name:
    HIBYL-CoA-H
    Gene namesi
    Name:HIBCH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4908. HIBCH.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    HIBCH deficiency (HIBCHD) [MIM:250620]: The enzyme defect results in accumulation of methacrylyl-CoA, a highly reactive compound, which readily undergoes addition reactions with free sulfhydryl groups. Affected individuals showed delayed development of motor skills, hypotonia, initial poor feeding, and a deterioration in neurological function during first stages of life.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti122 – 1221Y → C in HIBCHD. 1 Publication
    VAR_031870

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi250620. phenotype.
    Orphaneti88639. Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
    PharmGKBiPA29281.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3232MitochondrionBy similarityAdd
    BLAST
    Chaini33 – 3863543-hydroxyisobutyryl-CoA hydrolase, mitochondrialPRO_0000284929Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
    Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
    Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
    Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
    Modified residuei221 – 2211N6-acetyllysine; alternateBy similarity
    Modified residuei221 – 2211N6-succinyllysine; alternateBy similarity
    Modified residuei257 – 2571N6-succinyllysineBy similarity
    Modified residuei297 – 2971N6-acetyllysine; alternateBy similarity
    Modified residuei297 – 2971N6-succinyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-succinyllysineBy similarity
    Modified residuei353 – 3531N6-acetyllysine; alternateBy similarity
    Modified residuei353 – 3531N6-succinyllysine; alternateBy similarity
    Modified residuei360 – 3601N6-acetyllysineBy similarity
    Modified residuei365 – 3651N6-acetyllysineBy similarity
    Modified residuei377 – 3771N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ6NVY1.
    PaxDbiQ6NVY1.
    PeptideAtlasiQ6NVY1.
    PRIDEiQ6NVY1.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00419802.

    PTM databases

    PhosphoSiteiQ6NVY1.

    Expressioni

    Tissue specificityi

    Highly expressed in liver and kidney, also detected in heart, muscle and brain (at protein level). Not detected in lung.1 Publication

    Gene expression databases

    ArrayExpressiQ6NVY1.
    BgeeiQ6NVY1.
    CleanExiHS_HIBCH.
    GenevestigatoriQ6NVY1.

    Organism-specific databases

    HPAiHPA036540.
    HPA036541.

    Interactioni

    Protein-protein interaction databases

    BioGridi117658. 4 interactions.
    IntActiQ6NVY1. 2 interactions.
    STRINGi9606.ENSP00000352706.

    Structurei

    Secondary structure

    1
    386
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 437
    Beta strandi46 – 516
    Helixi54 – 563
    Helixi62 – 7716
    Beta strandi83 – 886
    Beta strandi91 – 955
    Helixi100 – 1078
    Helixi114 – 12916
    Beta strandi135 – 1395
    Beta strandi141 – 1444
    Helixi146 – 1494
    Turni150 – 1534
    Beta strandi154 – 1596
    Beta strandi164 – 1663
    Helixi169 – 1713
    Helixi180 – 1867
    Helixi191 – 1988
    Helixi205 – 2095
    Beta strandi214 – 2163
    Helixi219 – 2213
    Helixi222 – 23110
    Helixi237 – 25014
    Turni253 – 2564
    Helixi262 – 2643
    Helixi265 – 2717
    Beta strandi274 – 2763
    Helixi277 – 28711
    Helixi290 – 29910
    Helixi304 – 31714
    Helixi322 – 33716
    Helixi341 – 3499
    Helixi364 – 3663
    Helixi369 – 3768
    Helixi380 – 3823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BPTX-ray1.50A32-386[»]
    ProteinModelPortaliQ6NVY1.
    SMRiQ6NVY1. Positions 32-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6NVY1.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1024.
    HOVERGENiHBG054809.
    InParanoidiQ6NVY1.
    KOiK05605.
    OMAiVASLCHA.
    PhylomeDBiQ6NVY1.
    TreeFamiTF314329.

    Family and domain databases

    Gene3Di1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    [Graphical view]
    SUPFAMiSSF52096. SSF52096. 2 hits.

    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: Q6NVY1-1) [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

    MGQREMWRLM SRFNAFKRTN TILHHLRMSK HTDAAEEVLL EKKGCTGVIT    50
    LNRPKFLNAL TLNMIRQIYP QLKKWEQDPE TFLIIIKGAG GKAFCAGGDI 100
    RVISEAEKAK QKIAPVFFRE EYMLNNAVGS CQKPYVALIH GITMGGGVGL 150
    SVHGQFRVAT EKCLFAMPET AIGLFPDVGG GYFLPRLQGK LGYFLALTGF 200
    RLKGRDVYRA GIATHFVDSE KLAMLEEDLL ALKSPSKENI ASVLENYHTE 250
    SKIDRDKSFI LEEHMDKINS CFSANTVEEI IENLQQDGSS FALEQLKVIN 300
    KMSPTSLKIT LRQLMEGSSK TLQEVLTMEY RLSQACMRGH DFHEGVRAVL 350
    IDKDQSPKWK PADLKEVTEE DLNNHFKSLG SSDLKF 386
    Length:386
    Mass (Da):43,482
    Last modified:May 1, 2007 - v2
    Checksum:i11B0632ED1DF2FFA
    GO
    Isoform 2 (identifier: Q6NVY1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         338-385: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:338
    Mass (Da):38,012
    Checksum:i747FD3FC0745E844
    GO

    Sequence cautioni

    The sequence AAC52114.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH05190.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAY24178.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD96699.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD96743.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411E → G in AAH67822. (PubMed:15489334)Curated
    Sequence conflicti83 – 831L → V in AAC52114. (PubMed:8824301)Curated
    Sequence conflicti111 – 1111Q → R in BAD96699. 1 PublicationCurated
    Sequence conflicti184 – 19815LPRLQ…FLALT → FATTPRKTWLLPCIN in AAC52114. (PubMed:8824301)CuratedAdd
    BLAST
    Sequence conflicti369 – 3691E → K in BAD96699. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461T → A.3 Publications
    Corresponds to variant rs1058180 [ dbSNP | Ensembl ].
    VAR_031869
    Natural varianti122 – 1221Y → C in HIBCHD. 1 Publication
    VAR_031870

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei338 – 38548Missing in isoform 2. CuratedVSP_024780Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66669 mRNA. Translation: AAC52114.1. Different initiation.
    AK222979 mRNA. Translation: BAD96699.1. Different initiation.
    AK223023 mRNA. Translation: BAD96743.1. Different initiation.
    AC092178 Genomic DNA. Translation: AAY24178.1. Different initiation.
    AC010679 Genomic DNA. Translation: AAX93234.1.
    CH471058 Genomic DNA. Translation: EAX10873.1.
    CH471058 Genomic DNA. Translation: EAX10875.1.
    BC005190 mRNA. Translation: AAH05190.2. Different initiation.
    BC067822 mRNA. Translation: AAH67822.1.
    CCDSiCCDS2304.1. [Q6NVY1-1]
    CCDS46475.1. [Q6NVY1-2]
    RefSeqiNP_055177.2. NM_014362.3. [Q6NVY1-1]
    NP_932164.1. NM_198047.2. [Q6NVY1-2]
    UniGeneiHs.656685.

    Genome annotation databases

    EnsembliENST00000359678; ENSP00000352706; ENSG00000198130. [Q6NVY1-1]
    ENST00000392332; ENSP00000376144; ENSG00000198130. [Q6NVY1-2]
    GeneIDi26275.
    KEGGihsa:26275.
    UCSCiuc002uru.3. human. [Q6NVY1-1]
    uc002urv.3. human. [Q6NVY1-2]

    Polymorphism databases

    DMDMi146324905.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66669 mRNA. Translation: AAC52114.1 . Different initiation.
    AK222979 mRNA. Translation: BAD96699.1 . Different initiation.
    AK223023 mRNA. Translation: BAD96743.1 . Different initiation.
    AC092178 Genomic DNA. Translation: AAY24178.1 . Different initiation.
    AC010679 Genomic DNA. Translation: AAX93234.1 .
    CH471058 Genomic DNA. Translation: EAX10873.1 .
    CH471058 Genomic DNA. Translation: EAX10875.1 .
    BC005190 mRNA. Translation: AAH05190.2 . Different initiation.
    BC067822 mRNA. Translation: AAH67822.1 .
    CCDSi CCDS2304.1. [Q6NVY1-1 ]
    CCDS46475.1. [Q6NVY1-2 ]
    RefSeqi NP_055177.2. NM_014362.3. [Q6NVY1-1 ]
    NP_932164.1. NM_198047.2. [Q6NVY1-2 ]
    UniGenei Hs.656685.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BPT X-ray 1.50 A 32-386 [» ]
    ProteinModelPortali Q6NVY1.
    SMRi Q6NVY1. Positions 32-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117658. 4 interactions.
    IntActi Q6NVY1. 2 interactions.
    STRINGi 9606.ENSP00000352706.

    PTM databases

    PhosphoSitei Q6NVY1.

    Polymorphism databases

    DMDMi 146324905.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00419802.

    Proteomic databases

    MaxQBi Q6NVY1.
    PaxDbi Q6NVY1.
    PeptideAtlasi Q6NVY1.
    PRIDEi Q6NVY1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359678 ; ENSP00000352706 ; ENSG00000198130 . [Q6NVY1-1 ]
    ENST00000392332 ; ENSP00000376144 ; ENSG00000198130 . [Q6NVY1-2 ]
    GeneIDi 26275.
    KEGGi hsa:26275.
    UCSCi uc002uru.3. human. [Q6NVY1-1 ]
    uc002urv.3. human. [Q6NVY1-2 ]

    Organism-specific databases

    CTDi 26275.
    GeneCardsi GC02M191054.
    HGNCi HGNC:4908. HIBCH.
    HPAi HPA036540.
    HPA036541.
    MIMi 250620. phenotype.
    610690. gene.
    neXtProti NX_Q6NVY1.
    Orphaneti 88639. Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency.
    PharmGKBi PA29281.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1024.
    HOVERGENi HBG054809.
    InParanoidi Q6NVY1.
    KOi K05605.
    OMAi VASLCHA.
    PhylomeDBi Q6NVY1.
    TreeFami TF314329.

    Enzyme and pathway databases

    UniPathwayi UPA00362 .
    BRENDAi 3.1.2.4. 2681.
    Reactomei REACT_197. Branched-chain amino acid catabolism.
    SABIO-RK Q6NVY1.

    Miscellaneous databases

    EvolutionaryTracei Q6NVY1.
    GenomeRNAii 26275.
    NextBioi 48577.
    PROi Q6NVY1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6NVY1.
    Bgeei Q6NVY1.
    CleanExi HS_HIBCH.
    Genevestigatori Q6NVY1.

    Family and domain databases

    Gene3Di 1.10.12.10. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR029045. ClpP/crotonase-like_dom.
    IPR014748. Crontonase_C.
    [Graphical view ]
    SUPFAMi SSF52096. SSF52096. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure and tissue-specific expression of human beta-hydroxyisobutyryl-coenzyme A hydrolase."
      Hawes J.W., Jaskiewicz J., Shimomura Y., Huang B., Bunting J., Harper E.T., Harris R.A.
      J. Biol. Chem. 271:26430-26434(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-46.
      Tissue: Small intestine.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-46.
    5. "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], VARIANT ALA-46.
      Tissue: Testis.
    6. "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-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Crystal structure of human beta-hydroxyisobutyryl-COA hydrolase in complex with quercetin."
      Structural genomics consortium (SGC)
      Submitted (JAN-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-386 IN COMPLEX WITH 3-HYDROXY-2-METHYLPROPANOIC ACID AND QUERCETIN.
    9. "Mutations in the gene encoding 3-hydroxyisobutyryl-CoA hydrolase results in progressive infantile neurodegeneration."
      Loupatty F.J., Clayton P.T., Ruiter J.P.N., Ofman R., Ijlst L., Brown G.K., Thorburn D.R., Harris R.A., Duran M., Desousa C., Krywawych S., Heales S.J.R., Wanders R.J.A.
      Am. J. Hum. Genet. 80:195-199(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIBCHD CYS-122.

    Entry informationi

    Entry nameiHIBCH_HUMAN
    AccessioniPrimary (citable) accession number: Q6NVY1
    Secondary accession number(s): D3DPI4
    , Q53GA8, Q53GF2, Q53RF7, Q53TC6, Q92931, Q9BS94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 98 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 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3