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P54578

- UBP14_HUMAN

UniProt

P54578 - UBP14_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 14

Gene

USP14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).3 Publications

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei114 – 1141Nucleophile1 Publication
    Active sitei435 – 4351Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: ProtInc
    2. endopeptidase inhibitor activity Source: UniProtKB
    3. proteasome binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. tRNA guanylyltransferase activity Source: ProtInc
    6. ubiquitin-specific protease activity Source: FlyBase
    7. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. negative regulation of endopeptidase activity Source: GOC
    2. protein deubiquitination Source: FlyBase
    3. regulation of chemotaxis Source: UniProtKB
    4. regulation of proteasomal protein catabolic process Source: UniProtKB
    5. synaptic transmission Source: Ensembl
    6. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 14 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 14
    Ubiquitin thioesterase 14
    Ubiquitin-specific-processing protease 14
    Gene namesi
    Name:USP14
    Synonyms:TGT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:12612. USP14.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytoplasmic membrane-bounded vesicle Source: UniProtKB
    4. plasma membrane Source: UniProtKB-SubCell
    5. proteasome complex Source: UniProtKB-KW
    6. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Proteasome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37238.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Ubiquitin carboxyl-terminal hydrolase 14PRO_0000080636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei143 – 1431Phosphoserine4 Publications
    Modified residuei235 – 2351Phosphothreonine1 Publication
    Modified residuei449 – 4491N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP54578.
    PaxDbiP54578.
    PeptideAtlasiP54578.
    PRIDEiP54578.

    2D gel databases

    OGPiP54578.

    PTM databases

    PhosphoSiteiP54578.

    Expressioni

    Gene expression databases

    ArrayExpressiP54578.
    BgeeiP54578.
    CleanExiHS_USP14.
    GenevestigatoriP54578.

    Organism-specific databases

    HPAiHPA001308.

    Interactioni

    Subunit structurei

    Homodimer Potential. Associates with the 26S proteasome. Interacts with FANCC, CXCR4 and ERN1.3 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP3CAQ082093EBI-1048016,EBI-352922

    Protein-protein interaction databases

    BioGridi114551. 54 interactions.
    IntActiP54578. 30 interactions.
    MINTiMINT-3020275.
    STRINGi9606.ENSP00000261601.

    Structurei

    Secondary structure

    1
    494
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi110 – 1123
    Helixi114 – 12411
    Helixi127 – 1348
    Beta strandi144 – 1474
    Helixi148 – 16619
    Beta strandi168 – 1703
    Helixi173 – 18210
    Helixi184 – 1874
    Helixi200 – 21213
    Helixi242 – 2465
    Beta strandi249 – 26012
    Beta strandi269 – 27810
    Beta strandi280 – 2823
    Helixi286 – 2927
    Beta strandi297 – 3015
    Turni303 – 3064
    Beta strandi311 – 3199
    Beta strandi322 – 3298
    Beta strandi336 – 3394
    Beta strandi351 – 3544
    Helixi356 – 3583
    Helixi361 – 3666
    Turni367 – 3715
    Helixi372 – 3743
    Turni409 – 4124
    Beta strandi416 – 43015
    Beta strandi433 – 44311
    Beta strandi446 – 4516
    Beta strandi454 – 4585
    Helixi460 – 4634
    Helixi464 – 4674
    Beta strandi468 – 4725
    Beta strandi474 – 4818

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AYNX-ray3.20A/B/C91-494[»]
    2AYOX-ray3.50A91-494[»]
    ProteinModelPortaliP54578.
    SMRiP54578. Positions 6-86, 98-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54578.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 8077Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 483379USPAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiNOG286607.
    HOGENOMiHOG000202292.
    HOVERGENiHBG054185.
    InParanoidiP54578.
    KOiK11843.
    OMAiDWGNLKI.
    OrthoDBiEOG7F7W8H.
    PhylomeDBiP54578.
    TreeFamiTF314494.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    SMARTiSM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS00299. UBIQUITIN_1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54578-1) [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

    MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG    50
    GTLKDDDWGN IKIKNGMTLL MMGSADALPE EPSAKTVFVE DMTEEQLASA 100
    MELPCGLTNL GNTCYMNATV QCIRSVPELK DALKRYAGAL RASGEMASAQ 150
    YITAALRDLF DSMDKTSSSI PPIILLQFLH MAFPQFAEKG EQGQYLQQDA 200
    NECWIQMMRV LQQKLEAIED DSVKETDSSS ASAATPSKKK SLIDQFFGVE 250
    FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK 300
    QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP 350
    LMLDMYELCT PELQEKMVSF RSKFKDLEDK KVNQQPNTSD KKSSPQKEVK 400
    YEPFSFADDI GSNNCGYYDL QAVLTHQGRS SSSGHYVSWV KRKQDEWIKF 450
    DDDKVSIVTP EDILRLSGGG DWHIAYVLLY GPRRVEIMEE ESEQ 494
    Length:494
    Mass (Da):56,069
    Last modified:January 23, 2007 - v3
    Checksum:iE6D4679A86E9DF00
    GO
    Isoform 2 (identifier: P54578-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         66-100: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:459
    Mass (Da):52,386
    Checksum:i3EDE73254891B166
    GO

    Sequence cautioni

    The sequence CR976282 differs from that shown. Reason: Frameshift at position 288.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei66 – 10035Missing in isoform 2. 1 PublicationVSP_047343Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30888 mRNA. Translation: AAB60365.1.
    BT007183 mRNA. Translation: AAP35847.1.
    AP000845 Genomic DNA. No translation available.
    BC003556 mRNA. Translation: AAH03556.1.
    CR976282 mRNA. No translation available.
    CCDSiCCDS32780.1. [P54578-1]
    CCDS32781.1. [P54578-2]
    PIRiG01932.
    RefSeqiNP_001032411.1. NM_001037334.1. [P54578-2]
    NP_005142.1. NM_005151.3. [P54578-1]
    UniGeneiHs.464416.
    Hs.707058.

    Genome annotation databases

    EnsembliENST00000261601; ENSP00000261601; ENSG00000101557. [P54578-1]
    ENST00000582707; ENSP00000464447; ENSG00000101557. [P54578-2]
    GeneIDi9097.
    KEGGihsa:9097.
    UCSCiuc002kkf.1. human. [P54578-1]

    Polymorphism databases

    DMDMi1729927.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U30888 mRNA. Translation: AAB60365.1 .
    BT007183 mRNA. Translation: AAP35847.1 .
    AP000845 Genomic DNA. No translation available.
    BC003556 mRNA. Translation: AAH03556.1 .
    CR976282 mRNA. No translation available.
    CCDSi CCDS32780.1. [P54578-1 ]
    CCDS32781.1. [P54578-2 ]
    PIRi G01932.
    RefSeqi NP_001032411.1. NM_001037334.1. [P54578-2 ]
    NP_005142.1. NM_005151.3. [P54578-1 ]
    UniGenei Hs.464416.
    Hs.707058.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AYN X-ray 3.20 A/B/C 91-494 [» ]
    2AYO X-ray 3.50 A 91-494 [» ]
    ProteinModelPortali P54578.
    SMRi P54578. Positions 6-86, 98-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114551. 54 interactions.
    IntActi P54578. 30 interactions.
    MINTi MINT-3020275.
    STRINGi 9606.ENSP00000261601.

    Chemistry

    ChEMBLi CHEMBL1293295.

    Protein family/group databases

    MEROPSi C19.015.

    PTM databases

    PhosphoSitei P54578.

    Polymorphism databases

    DMDMi 1729927.

    2D gel databases

    OGPi P54578.

    Proteomic databases

    MaxQBi P54578.
    PaxDbi P54578.
    PeptideAtlasi P54578.
    PRIDEi P54578.

    Protocols and materials databases

    DNASUi 9097.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261601 ; ENSP00000261601 ; ENSG00000101557 . [P54578-1 ]
    ENST00000582707 ; ENSP00000464447 ; ENSG00000101557 . [P54578-2 ]
    GeneIDi 9097.
    KEGGi hsa:9097.
    UCSCi uc002kkf.1. human. [P54578-1 ]

    Organism-specific databases

    CTDi 9097.
    GeneCardsi GC18P000148.
    HGNCi HGNC:12612. USP14.
    HPAi HPA001308.
    MIMi 607274. gene.
    neXtProti NX_P54578.
    PharmGKBi PA37238.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG286607.
    HOGENOMi HOG000202292.
    HOVERGENi HBG054185.
    InParanoidi P54578.
    KOi K11843.
    OMAi DWGNLKI.
    OrthoDBi EOG7F7W8H.
    PhylomeDBi P54578.
    TreeFami TF314494.

    Miscellaneous databases

    EvolutionaryTracei P54578.
    GeneWikii USP14.
    GenomeRNAii 9097.
    NextBioi 34093.
    PROi P54578.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54578.
    Bgeei P54578.
    CleanExi HS_USP14.
    Genevestigatori P54578.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    SMARTi SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS00299. UBIQUITIN_1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "tRNA-guanine transglycosylase cDNA from human placenta."
      Deshpande K.L., Katze J.R.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. 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] (ISOFORM 1).
      Tissue: Skin.
    5. Heil O., Ebert L., Hennig S., Henze S., Radelof U., Schneider D., Korn B.
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-308 (ISOFORM 2).
      Tissue: T-cell.
    6. "Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport."
      Reuter T.Y., Medhurst A.L., Waisfisz Q., Zhi Y., Herterich S., Hoehn H., Gross H.J., Joenje H., Hoatlin M.E., Mathew C.G., Huber P.A.
      Exp. Cell Res. 289:211-221(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FANCC.
    7. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    8. "Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome."
      Koulich E., Li X., DeMartino G.N.
      Mol. Biol. Cell 19:1072-1082(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE 26S PROTEASOME, FUNCTION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "USP14 inhibits ER-associated degradation via interaction with IRE1alpha."
      Nagai A., Kadowaki H., Maruyama T., Takeda K., Nishitoh H., Ichijo H.
      Biochem. Biophys. Res. Commun. 379:995-1000(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ERN1.
    11. "Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK activation."
      Mines M.A., Goodwin J.S., Limbird L.E., Cui F.F., Fan G.H.
      J. Biol. Chem. 284:5742-5752(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CXCR4, FUNCTION, SUBCELLULAR LOCATION.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-449, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND THR-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14."
      Hu M., Li P., Song L., Jeffrey P.D., Chenova T.A., Wilkinson K.D., Cohen R.E., Shi Y.
      EMBO J. 24:3747-3756(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 91-494, CATALYTIC ACTIVITY, ACTIVE SITE.

    Entry informationi

    Entry nameiUBP14_HUMAN
    AccessioniPrimary (citable) accession number: P54578
    Secondary accession number(s): J3QRZ5, Q53XY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3