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O95433

- AHSA1_HUMAN

UniProt

O95433 - AHSA1_HUMAN

Protein

Activator of 90 kDa heat shock protein ATPase homolog 1

Gene

AHSA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Cochaperone that stimulates HSP90 ATPase activity By similarity. May affect a step in the endoplasmic reticulum to Golgi trafficking.By similarity

    GO - Molecular functioni

    1. ATPase activator activity Source: MGI
    2. chaperone binding Source: MGI
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of ATPase activity Source: GOC
    2. response to stress Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activator of 90 kDa heat shock protein ATPase homolog 1
    Short name:
    AHA1
    Alternative name(s):
    p38
    Gene namesi
    Name:AHSA1
    Synonyms:C14orf3
    ORF Names:HSPC322
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:1189. AHSA1.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Endoplasmic reticulum 1 Publication
    Note: May transiently interact with the endoplasmic reticulum.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB-SubCell
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25515.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 338337Activator of 90 kDa heat shock protein ATPase homolog 1PRO_0000215820Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei3 – 31N6-acetyllysine1 Publication
    Modified residuei193 – 1931Phosphoserine2 Publications
    Modified residuei212 – 2121N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95433.
    PaxDbiO95433.
    PeptideAtlasiO95433.
    PRIDEiO95433.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00030706.

    PTM databases

    PhosphoSiteiO95433.

    Expressioni

    Tissue specificityi

    Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.1 Publication

    Inductioni

    By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG).1 Publication

    Gene expression databases

    ArrayExpressiO95433.
    BgeeiO95433.
    CleanExiHS_AHSA1.
    GenevestigatoriO95433.

    Organism-specific databases

    HPAiCAB006244.
    HPA000903.

    Interactioni

    Subunit structurei

    Interacts with HSPCA/HSP90 and with the cytoplasmic tail of the vesicular stomatitis virus glycoprotein (VSV G). Interacts with GCH1. Interacts with SRPK1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GCH1P307933EBI-448610,EBI-958183
    HSP90AA1P079004EBI-448610,EBI-296047
    HSP90AB1P082383EBI-448610,EBI-352572

    Protein-protein interaction databases

    BioGridi115846. 21 interactions.
    IntActiO95433. 24 interactions.
    MINTiMINT-5002315.
    STRINGi9606.ENSP00000216479.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi206 – 21712
    Helixi219 – 2257
    Helixi229 – 2357
    Turni253 – 2564
    Beta strandi261 – 2655
    Turni266 – 2683
    Beta strandi269 – 2768
    Beta strandi285 – 2906
    Beta strandi298 – 30811
    Helixi309 – 3179
    Turni318 – 3236
    Helixi324 – 3307

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X53NMR-A204-335[»]
    ProteinModelPortaliO95433.
    SMRiO95433. Positions 25-146, 204-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95433.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AHA1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5580.
    HOGENOMiHOG000242852.
    HOVERGENiHBG065806.
    InParanoidiO95433.
    OMAiPEVSHEN.
    PhylomeDBiO95433.
    TreeFamiTF313680.

    Family and domain databases

    Gene3Di3.30.530.20. 1 hit.
    InterProiIPR013538. Activator_of_Hsp90_ATPase.
    IPR015310. AHSA1_N.
    IPR023393. START-like_dom.
    [Graphical view]
    PfamiPF09229. Aha1_N. 1 hit.
    PF08327. AHSA1. 1 hit.
    [Graphical view]
    SMARTiSM01000. Aha1_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF103111. SSF103111. 1 hit.

    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: O95433-1) [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

    MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTDKL KTLFLAVQVQ    50
    NEEGKCEVTE VSKLDGEASI NNRKGKLIFF YEWSVKLNWT GTSKSGVQYK 100
    GHVEIPNLSD ENSVDEVEIS VSLAKDEPDT NLVALMKEEG VKLLREAMGI 150
    YISTLKTEFT QGMILPTMNG ESVDPVGQPA LKTEERKAKP APSKTQARPV 200
    GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA TLEADRGGKF 250
    HMVDGNVSGE FTDLVPEKHI VMKWRFKSWP EGHFATITLT FIDKNGETEL 300
    CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF 338
    Length:338
    Mass (Da):38,274
    Last modified:May 1, 1999 - v1
    Checksum:iE6B686DDD8D7D729
    GO
    Isoform 2 (identifier: O95433-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         283-338: HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF → SHCHSG

    Note: No experimental confirmation available.

    Show »
    Length:288
    Mass (Da):32,340
    Checksum:i4ACB777F0ED29F4E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 682EA → CL in AAF29000. (PubMed:11042152)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei283 – 33856HFATI…GARLF → SHCHSG in isoform 2. 1 PublicationVSP_055797Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ243310 mRNA. Translation: CAB45684.1.
    AF164791 mRNA. Translation: AAF80755.1.
    AK300766 mRNA. Translation: BAG62431.1.
    AK313824 mRNA. Translation: BAG36559.1.
    AF111168 Genomic DNA. Translation: AAD09623.1.
    CH471061 Genomic DNA. Translation: EAW81291.1.
    BC000321 mRNA. Translation: AAH00321.1.
    BC007398 mRNA. Translation: AAH07398.2.
    AF161440 mRNA. Translation: AAF29000.1.
    CCDSiCCDS9863.1.
    PIRiJC7769.
    RefSeqiNP_036243.1. NM_012111.2.
    UniGeneiHs.204041.

    Genome annotation databases

    EnsembliENST00000216479; ENSP00000216479; ENSG00000100591. [O95433-1]
    ENST00000535854; ENSP00000440108; ENSG00000100591. [O95433-2]
    GeneIDi10598.
    KEGGihsa:10598.
    UCSCiuc001xtw.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ243310 mRNA. Translation: CAB45684.1 .
    AF164791 mRNA. Translation: AAF80755.1 .
    AK300766 mRNA. Translation: BAG62431.1 .
    AK313824 mRNA. Translation: BAG36559.1 .
    AF111168 Genomic DNA. Translation: AAD09623.1 .
    CH471061 Genomic DNA. Translation: EAW81291.1 .
    BC000321 mRNA. Translation: AAH00321.1 .
    BC007398 mRNA. Translation: AAH07398.2 .
    AF161440 mRNA. Translation: AAF29000.1 .
    CCDSi CCDS9863.1.
    PIRi JC7769.
    RefSeqi NP_036243.1. NM_012111.2.
    UniGenei Hs.204041.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X53 NMR - A 204-335 [» ]
    ProteinModelPortali O95433.
    SMRi O95433. Positions 25-146, 204-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115846. 21 interactions.
    IntActi O95433. 24 interactions.
    MINTi MINT-5002315.
    STRINGi 9606.ENSP00000216479.

    PTM databases

    PhosphoSitei O95433.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00030706.

    Proteomic databases

    MaxQBi O95433.
    PaxDbi O95433.
    PeptideAtlasi O95433.
    PRIDEi O95433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216479 ; ENSP00000216479 ; ENSG00000100591 . [O95433-1 ]
    ENST00000535854 ; ENSP00000440108 ; ENSG00000100591 . [O95433-2 ]
    GeneIDi 10598.
    KEGGi hsa:10598.
    UCSCi uc001xtw.3. human.

    Organism-specific databases

    CTDi 10598.
    GeneCardsi GC14P077924.
    HGNCi HGNC:1189. AHSA1.
    HPAi CAB006244.
    HPA000903.
    MIMi 608466. gene.
    neXtProti NX_O95433.
    PharmGKBi PA25515.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5580.
    HOGENOMi HOG000242852.
    HOVERGENi HBG065806.
    InParanoidi O95433.
    OMAi PEVSHEN.
    PhylomeDBi O95433.
    TreeFami TF313680.

    Miscellaneous databases

    ChiTaRSi AHSA1. human.
    EvolutionaryTracei O95433.
    GeneWikii AHSA1.
    GenomeRNAii 10598.
    NextBioi 40246.
    PROi O95433.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95433.
    Bgeei O95433.
    CleanExi HS_AHSA1.
    Genevestigatori O95433.

    Family and domain databases

    Gene3Di 3.30.530.20. 1 hit.
    InterProi IPR013538. Activator_of_Hsp90_ATPase.
    IPR015310. AHSA1_N.
    IPR023393. START-like_dom.
    [Graphical view ]
    Pfami PF09229. Aha1_N. 1 hit.
    PF08327. AHSA1. 1 hit.
    [Graphical view ]
    SMARTi SM01000. Aha1_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103111. SSF103111. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of a novel gene underexpressed in Down syndrome."
      Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E., Scott H.S.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lung and Ovary.
    7. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-338 (ISOFORM 1).
      Tissue: Umbilical cord blood.
    8. "p38: a novel protein that associates with the vesicular stomatitis virus glycoprotein."
      Sevier C.S., Machamer C.E.
      Biochem. Biophys. Res. Commun. 287:574-582(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VSV G, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. Cited for: INTERACTION WITH HSPCA, IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION.
    10. "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
      Lotz G.P., Lin H., Harst A., Obermann W.M.J.
      J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPCA.
    11. "A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions."
      Swick L., Kapatos G.
      J. Neurochem. 97:1447-1455(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCH1.
    12. "Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
      Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
      Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRPK1.
    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 ALA-2; LYS-3 AND LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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-193, 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-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The solution structure of the C-terminal domain of human activator of 90 kDa heat shock protein ATPase homolog 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 204-335.

    Entry informationi

    Entry nameiAHSA1_HUMAN
    AccessioniPrimary (citable) accession number: O95433
    Secondary accession number(s): B2R9L2
    , B4DUR9, Q96IL6, Q9P060
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 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 14
      Human chromosome 14: 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