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Q99471

- PFD5_HUMAN

UniProt

Q99471 - PFD5_HUMAN

Protein

Prefoldin subunit 5

Gene

PFDN5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
    4. negative regulation of transcription, DNA-templated Source: BHF-UCL
    5. protein folding Source: Reactome
    6. regulation of transcription, DNA-templated Source: ProtInc
    7. retina development in camera-type eye Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Enzyme and pathway databases

    ReactomeiREACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prefoldin subunit 5
    Alternative name(s):
    C-Myc-binding protein Mm-1
    Myc modulator 1
    Gene namesi
    Name:PFDN5
    Synonyms:MM1, PFD5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8869. PFDN5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: ProtInc
    3. prefoldin complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33210.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 154153Prefoldin subunit 5PRO_0000153661Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei42 – 421N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99471.
    PaxDbiQ99471.
    PeptideAtlasiQ99471.
    PRIDEiQ99471.

    2D gel databases

    OGPiQ99471.

    PTM databases

    PhosphoSiteiQ99471.

    Expressioni

    Tissue specificityi

    Highly expressed in pancreas and skeletal muscle and moderately in other tissues.

    Gene expression databases

    BgeeiQ99471.
    CleanExiHS_PFDN5.
    GenevestigatoriQ99471.

    Organism-specific databases

    HPAiHPA008587.

    Interactioni

    Subunit structurei

    Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to MYC; interacts with its N-terminal domain.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    vIRF-3Q9DUN18EBI-357275,EBI-1647907From a different organism.

    Protein-protein interaction databases

    BioGridi111226. 53 interactions.
    DIPiDIP-28155N.
    IntActiQ99471. 29 interactions.
    MINTiMINT-5003456.
    STRINGi9606.ENSP00000334188.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99471.
    SMRiQ99471. Positions 11-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prefoldin subunit alpha family.Curated

    Phylogenomic databases

    eggNOGiCOG1730.
    HOGENOMiHOG000207562.
    HOVERGENiHBG004539.
    InParanoidiQ99471.
    KOiK04797.
    OMAiFVECECI.
    PhylomeDBiQ99471.
    TreeFamiTF106509.

    Family and domain databases

    Gene3Di1.10.287.370. 1 hit.
    HAMAPiMF_00308. PfdA.
    InterProiIPR011599. PFD_alpha.
    IPR009053. Prefoldin.
    IPR004127. Prefoldin_subunit_alpha.
    [Graphical view]
    PfamiPF02996. Prefoldin. 1 hit.
    [Graphical view]
    SUPFAMiSSF46579. SSF46579. 1 hit.
    TIGRFAMsiTIGR00293. TIGR00293. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q99471-1) [UniParc]FASTAAdd to Basket

    Also known as: MM1-alpha

    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

    MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL    50
    NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK 100
    DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA 150
    TAKA 154
    Length:154
    Mass (Da):17,328
    Last modified:January 11, 2001 - v2
    Checksum:i0DA1F3644548CB14
    GO
    Isoform 2 (identifier: Q99471-2) [UniParc]FASTAAdd to Basket

    Also known as: MM1-beta

    The sequence of this isoform differs from the canonical sequence as follows:
         59-154: GKELLVPLTS...LGAAQATAKA → DVCPWEAA

    Note: Does not repress transcription activity of MYC.

    Show »
    Length:66
    Mass (Da):7,481
    Checksum:iC07E3472E5BD2A76
    GO
    Isoform 3 (identifier: Q99471-3) [UniParc]FASTAAdd to Basket

    Also known as: MM1-gamma

    The sequence of this isoform differs from the canonical sequence as follows:
         25-69: Missing.

    Show »
    Length:109
    Mass (Da):12,379
    Checksum:i899AFF472DCC00D7
    GO

    Sequence cautioni

    The sequence BAA14006.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei25 – 6945Missing in isoform 3. 1 PublicationVSP_043103Add
    BLAST
    Alternative sequencei59 – 15496GKELL…ATAKA → DVCPWEAA in isoform 2. 1 PublicationVSP_043104Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89667 mRNA. Translation: BAA14006.1. Different initiation.
    AB055802 Genomic DNA. Translation: BAB32643.1.
    AB055803 mRNA. Translation: BAB32644.1.
    AB055804 mRNA. Translation: BAB32645.1.
    AB055805 mRNA. Translation: BAB32646.1.
    BT007195 mRNA. Translation: AAP35859.1.
    AK292623 mRNA. Translation: BAF85312.1.
    AC073611 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96683.1.
    CH471054 Genomic DNA. Translation: EAW96685.1.
    BC003373 mRNA. No translation available.
    BC062671 mRNA. Translation: AAH62671.1.
    CCDSiCCDS8853.1. [Q99471-1]
    CCDS8854.1. [Q99471-3]
    RefSeqiNP_002615.2. NM_002624.3. [Q99471-1]
    NP_665904.1. NM_145897.2. [Q99471-3]
    UniGeneiHs.655327.

    Genome annotation databases

    EnsembliENST00000243040; ENSP00000243040; ENSG00000123349. [Q99471-2]
    ENST00000334478; ENSP00000334188; ENSG00000123349. [Q99471-1]
    ENST00000351500; ENSP00000266964; ENSG00000123349. [Q99471-3]
    ENST00000551018; ENSP00000447942; ENSG00000123349. [Q99471-1]
    GeneIDi5204.
    KEGGihsa:5204.
    UCSCiuc001scl.3. human. [Q99471-1]
    uc001scm.3. human. [Q99471-3]

    Polymorphism databases

    DMDMi12231038.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89667 mRNA. Translation: BAA14006.1 . Different initiation.
    AB055802 Genomic DNA. Translation: BAB32643.1 .
    AB055803 mRNA. Translation: BAB32644.1 .
    AB055804 mRNA. Translation: BAB32645.1 .
    AB055805 mRNA. Translation: BAB32646.1 .
    BT007195 mRNA. Translation: AAP35859.1 .
    AK292623 mRNA. Translation: BAF85312.1 .
    AC073611 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96683.1 .
    CH471054 Genomic DNA. Translation: EAW96685.1 .
    BC003373 mRNA. No translation available.
    BC062671 mRNA. Translation: AAH62671.1 .
    CCDSi CCDS8853.1. [Q99471-1 ]
    CCDS8854.1. [Q99471-3 ]
    RefSeqi NP_002615.2. NM_002624.3. [Q99471-1 ]
    NP_665904.1. NM_145897.2. [Q99471-3 ]
    UniGenei Hs.655327.

    3D structure databases

    ProteinModelPortali Q99471.
    SMRi Q99471. Positions 11-149.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111226. 53 interactions.
    DIPi DIP-28155N.
    IntActi Q99471. 29 interactions.
    MINTi MINT-5003456.
    STRINGi 9606.ENSP00000334188.

    PTM databases

    PhosphoSitei Q99471.

    Polymorphism databases

    DMDMi 12231038.

    2D gel databases

    OGPi Q99471.

    Proteomic databases

    MaxQBi Q99471.
    PaxDbi Q99471.
    PeptideAtlasi Q99471.
    PRIDEi Q99471.

    Protocols and materials databases

    DNASUi 5204.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243040 ; ENSP00000243040 ; ENSG00000123349 . [Q99471-2 ]
    ENST00000334478 ; ENSP00000334188 ; ENSG00000123349 . [Q99471-1 ]
    ENST00000351500 ; ENSP00000266964 ; ENSG00000123349 . [Q99471-3 ]
    ENST00000551018 ; ENSP00000447942 ; ENSG00000123349 . [Q99471-1 ]
    GeneIDi 5204.
    KEGGi hsa:5204.
    UCSCi uc001scl.3. human. [Q99471-1 ]
    uc001scm.3. human. [Q99471-3 ]

    Organism-specific databases

    CTDi 5204.
    GeneCardsi GC12P053689.
    HGNCi HGNC:8869. PFDN5.
    HPAi HPA008587.
    MIMi 604899. gene.
    neXtProti NX_Q99471.
    PharmGKBi PA33210.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1730.
    HOGENOMi HOG000207562.
    HOVERGENi HBG004539.
    InParanoidi Q99471.
    KOi K04797.
    OMAi FVECECI.
    PhylomeDBi Q99471.
    TreeFami TF106509.

    Enzyme and pathway databases

    Reactomei REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.

    Miscellaneous databases

    ChiTaRSi PFDN5. human.
    GeneWikii PFDN5.
    GenomeRNAii 5204.
    NextBioi 20126.
    PROi Q99471.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99471.
    CleanExi HS_PFDN5.
    Genevestigatori Q99471.

    Family and domain databases

    Gene3Di 1.10.287.370. 1 hit.
    HAMAPi MF_00308. PfdA.
    InterProi IPR011599. PFD_alpha.
    IPR009053. Prefoldin.
    IPR004127. Prefoldin_subunit_alpha.
    [Graphical view ]
    Pfami PF02996. Prefoldin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46579. SSF46579. 1 hit.
    TIGRFAMsi TIGR00293. TIGR00293. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc."
      Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.
      J. Biol. Chem. 273:29794-29800(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer."
      Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H., Iguchi-Ariga S.M.M., Nagashima K., Ariga H.
      J. Biol. Chem. 276:45137-45144(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
      Tissue: Blood and Fibroblast.
    3. "Distinct localizations and repression activities of MM-1 isoforms toward c-Myc."
      Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M., Ariga H.
      J. Cell. Biochem. 97:145-155(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
      Tissue: B-cell and Placenta.
    4. "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).
    5. "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).
      Tissue: Thymus.
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Placenta.
    9. "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin."
      Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J., Klein H.L., Cowan N.J.
      Cell 93:863-873(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "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-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPFD5_HUMAN
    AccessioniPrimary (citable) accession number: Q99471
    Secondary accession number(s): A8K9A8
    , Q54AA8, Q9C083, Q9C084
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 131 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3