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Q99615

- DNJC7_HUMAN

UniProt

Q99615 - DNJC7_HUMAN

Protein

DnaJ homolog subfamily C member 7

Gene

DNAJC7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm By similarity.By similarity

    GO - Molecular functioni

    1. heat shock protein binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. chaperone cofactor-dependent protein refolding Source: UniProtKB
    2. protein folding Source: ProtInc

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily C member 7
    Alternative name(s):
    Tetratricopeptide repeat protein 2
    Short name:
    TPR repeat protein 2
    Gene namesi
    Name:DNAJC7
    Synonyms:TPR2, TTC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12392. DNAJC7.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmcytoskeleton
    Note: Colocalizes with NR1I3 to microtubules.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011R → A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-333 and A-409. 1 Publication
    Mutagenesisi333 – 3331R → A: Impairs interaction with HSP90AA1 and HSPA1A/B. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-409. 1 Publication
    Mutagenesisi409 – 4091H → A: Predominantly nuclear localization. Abolishes interaction with HSP90AA1 and HSPA1A/B; when associated with A-101 and A-333. 2 Publications

    Organism-specific databases

    PharmGKBiPA27424.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 494493DnaJ homolog subfamily C member 7PRO_0000071058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ99615.
    PaxDbiQ99615.
    PeptideAtlasiQ99615.
    PRIDEiQ99615.

    PTM databases

    PhosphoSiteiQ99615.

    Miscellaneous databases

    PMAP-CutDBQ99615.

    Expressioni

    Gene expression databases

    ArrayExpressiQ99615.
    BgeeiQ99615.
    CleanExiHS_DNAJC7.
    GenevestigatoriQ99615.

    Organism-specific databases

    HPAiHPA023015.

    Interactioni

    Subunit structurei

    Associates with complexes containing chaperones HSP70 and HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1. Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the interaction is interrupted by UV and heat shock treatments. Interacts with HUS1 and RAD1. Interacts with NR1I3. The DNAJC7-NR1I3 complex may also include HSP90 By similarity. Interacts with HSPA8.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BAG4O954292EBI-357552,EBI-2949658
    vifP125043EBI-357552,EBI-779991From a different organism.

    Protein-protein interaction databases

    BioGridi113117. 30 interactions.
    IntActiQ99615. 17 interactions.
    MINTiMINT-1143801.
    STRINGi9606.ENSP00000406463.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99615.
    SMRiQ99615. Positions 27-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati28 – 6134TPR 1Add
    BLAST
    Repeati62 – 9534TPR 2Add
    BLAST
    Repeati96 – 12934TPR 3Add
    BLAST
    Repeati142 – 17534TPR 4Add
    BLAST
    Repeati177 – 20933TPR 5Add
    BLAST
    Repeati210 – 24334TPR 6Add
    BLAST
    Repeati256 – 28934TPR 7Add
    BLAST
    Repeati294 – 32734TPR 8Add
    BLAST
    Repeati328 – 36134TPR 9Add
    BLAST
    Domaini381 – 45171JPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 J domain.PROSITE-ProRule annotation
    Contains 9 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000210360.
    HOVERGENiHBG051376.
    InParanoidiQ99615.
    KOiK09527.
    OMAiCFQRVLE.
    PhylomeDBiQ99615.
    TreeFamiTF105166.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    1.25.40.10. 3 hits.
    InterProiIPR001623. DnaJ_domain.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00226. DnaJ. 1 hit.
    PF00515. TPR_1. 5 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    PRINTSiPR00625. JDOMAIN.
    SMARTiSM00271. DnaJ. 1 hit.
    SM00028. TPR. 7 hits.
    [Graphical view]
    SUPFAMiSSF46565. SSF46565. 1 hit.
    PROSITEiPS50076. DNAJ_2. 1 hit.
    PS50005. TPR. 8 hits.
    PS50293. TPR_REGION. 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: Q99615-1) [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

    MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY    50
    YTKAIDMCPK NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL 100
    REGKCHLSLG NAMAACRSFQ RALELDHKNA QAQQEFKNAN AVMEYEKIAE 150
    TDFEKRDFRK VVFCMDRALE FAPACHRFKI LKAECLAMLG RYPEAQSVAS 200
    DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA PDHEKACIAC 250
    RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR 300
    GTVNSKLRKL DDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQYEEAVRD 350
    YEKVYQTEKT KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA 400
    YRKRALMHHP DRHSGASAEV QKEEEKKFKE VGEAFTILSD PKKKTRYDSG 450
    QDLDEEGMNM GDFDPNNIFK AFFGGPGGFS FEASGPGNFF FQFG 494
    Length:494
    Mass (Da):56,441
    Last modified:April 13, 2004 - v2
    Checksum:i81C60CF71BFE951D
    GO
    Isoform 2 (identifier: Q99615-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.

    Show »
    Length:438
    Mass (Da):50,097
    Checksum:iC1C5BF7A49DF56B0
    GO

    Sequence cautioni

    The sequence AAB36872.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH33772.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti375 – 3751K → R in BX647209. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 2. 2 PublicationsVSP_044279Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298860 mRNA. Translation: BAG60982.1.
    BX647209 mRNA. No translation available.
    AC105024 Genomic DNA. No translation available.
    AC125257 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60788.1.
    BC003601 mRNA. Translation: AAH03601.1.
    BC011837 mRNA. Translation: AAH11837.2.
    BC033772 mRNA. Translation: AAH33772.1. Different initiation.
    U46571 mRNA. Translation: AAB36872.1. Different initiation.
    CCDSiCCDS45677.1. [Q99615-1]
    CCDS45678.1. [Q99615-2]
    RefSeqiNP_001138238.1. NM_001144766.2. [Q99615-2]
    NP_003306.3. NM_003315.3. [Q99615-1]
    UniGeneiHs.500156.

    Genome annotation databases

    EnsembliENST00000316603; ENSP00000313311; ENSG00000168259. [Q99615-2]
    ENST00000426588; ENSP00000394327; ENSG00000168259. [Q99615-2]
    ENST00000457167; ENSP00000406463; ENSG00000168259. [Q99615-1]
    GeneIDi7266.
    KEGGihsa:7266.
    UCSCiuc002hyo.3. human. [Q99615-1]

    Polymorphism databases

    DMDMi46397879.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK298860 mRNA. Translation: BAG60982.1 .
    BX647209 mRNA. No translation available.
    AC105024 Genomic DNA. No translation available.
    AC125257 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60788.1 .
    BC003601 mRNA. Translation: AAH03601.1 .
    BC011837 mRNA. Translation: AAH11837.2 .
    BC033772 mRNA. Translation: AAH33772.1 . Different initiation.
    U46571 mRNA. Translation: AAB36872.1 . Different initiation.
    CCDSi CCDS45677.1. [Q99615-1 ]
    CCDS45678.1. [Q99615-2 ]
    RefSeqi NP_001138238.1. NM_001144766.2. [Q99615-2 ]
    NP_003306.3. NM_003315.3. [Q99615-1 ]
    UniGenei Hs.500156.

    3D structure databases

    ProteinModelPortali Q99615.
    SMRi Q99615. Positions 27-476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113117. 30 interactions.
    IntActi Q99615. 17 interactions.
    MINTi MINT-1143801.
    STRINGi 9606.ENSP00000406463.

    PTM databases

    PhosphoSitei Q99615.

    Polymorphism databases

    DMDMi 46397879.

    Proteomic databases

    MaxQBi Q99615.
    PaxDbi Q99615.
    PeptideAtlasi Q99615.
    PRIDEi Q99615.

    Protocols and materials databases

    DNASUi 7266.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316603 ; ENSP00000313311 ; ENSG00000168259 . [Q99615-2 ]
    ENST00000426588 ; ENSP00000394327 ; ENSG00000168259 . [Q99615-2 ]
    ENST00000457167 ; ENSP00000406463 ; ENSG00000168259 . [Q99615-1 ]
    GeneIDi 7266.
    KEGGi hsa:7266.
    UCSCi uc002hyo.3. human. [Q99615-1 ]

    Organism-specific databases

    CTDi 7266.
    GeneCardsi GC17M040128.
    HGNCi HGNC:12392. DNAJC7.
    HPAi HPA023015.
    MIMi 601964. gene.
    neXtProti NX_Q99615.
    PharmGKBi PA27424.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000210360.
    HOVERGENi HBG051376.
    InParanoidi Q99615.
    KOi K09527.
    OMAi CFQRVLE.
    PhylomeDBi Q99615.
    TreeFami TF105166.

    Miscellaneous databases

    ChiTaRSi DNAJC7. human.
    GeneWikii DNAJC7.
    GenomeRNAii 7266.
    NextBioi 28407.
    PMAP-CutDB Q99615.
    PROi Q99615.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99615.
    Bgeei Q99615.
    CleanExi HS_DNAJC7.
    Genevestigatori Q99615.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    1.25.40.10. 3 hits.
    InterProi IPR001623. DnaJ_domain.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00226. DnaJ. 1 hit.
    PF00515. TPR_1. 5 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    SM00028. TPR. 7 hits.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    PROSITEi PS50076. DNAJ_2. 1 hit.
    PS50005. TPR. 8 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Salivary gland.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Salivary gland.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Lung and Skin.
    6. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-26; 69-77; 80-90; 138-156; 192-238; 274-291 AND 430-442 (ISOFORM 1), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    7. "Identification and characterization of two novel tetratricopeptide repeat-containing genes."
      Murthy A.E., Bernards A., Church D., Wasmuth J., Gusella J.F.
      DNA Cell Biol. 15:727-735(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-494 (ISOFORM 1).
    8. "Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats."
      Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.
      J. Biol. Chem. 274:34425-34432(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPA8.
    9. "The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9."
      Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K., Yamamoto K.C.
      Biochem. Biophys. Res. Commun. 287:932-940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD9A; HUS1 AND RAD1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-409.
    10. "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system."
      Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C., Obermann W.M.
      EMBO J. 22:3613-3623(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A/B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-101; ARG-333 AND HIS-409.
    11. "Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells."
      Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.
      Mol. Pharmacol. 64:1069-1075(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR1I3.
    12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: FUNCTION, INTERACTION WITH HSP90AB1; HSPA1A/B AND PGR.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDNJC7_HUMAN
    AccessioniPrimary (citable) accession number: Q99615
    Secondary accession number(s): Q7Z784
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 140 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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