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O43447

- PPIH_HUMAN

UniProt

O43447 - PPIH_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase H

Gene

PPIH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone.3 Publications

    Catalytic activityi

    Peptidylproline (omega=180) = peptidylproline (omega=0).

    Enzyme regulationi

    Inhibited by cyclosporin A.

    GO - Molecular functioni

    1. cyclosporin A binding Source: ProtInc
    2. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL
    3. protein binding Source: IntAct
    4. ribonucleoprotein complex binding Source: BHF-UCL

    GO - Biological processi

    1. mRNA splicing, via spliceosome Source: BHF-UCL
    2. positive regulation of viral genome replication Source: UniProtKB
    3. protein complex assembly Source: ProtInc
    4. protein folding Source: ProtInc
    5. protein peptidyl-prolyl isomerization Source: GOC

    Keywords - Molecular functioni

    Chaperone, Isomerase, Rotamase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase H (EC:5.2.1.8)
    Short name:
    PPIase H
    Alternative name(s):
    Rotamase H
    Small nuclear ribonucleoprotein particle-specific cyclophilin H
    Short name:
    CypH
    U-snRNP-associated cyclophilin SnuCyp-20
    Short name:
    USA-CYP
    Gene namesi
    Name:PPIH
    Synonyms:CYP20, CYPH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:14651. PPIH.

    Subcellular locationi

    Nucleus speckle 1 Publication. Cytoplasm 1 Publication
    Note: Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nuclear speck Source: BHF-UCL
    3. spliceosomal complex Source: BHF-UCL
    4. U4/U6 snRNP Source: BHF-UCL
    5. U4/U6 x U5 tri-snRNP complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331W → F: Abolishes inhibition by cyclosporin A. 1 Publication

    Organism-specific databases

    PharmGKBiPA33586.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 177176Peptidyl-prolyl cis-trans isomerase HPRO_0000064162Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43447.
    PaxDbiO43447.
    PRIDEiO43447.

    PTM databases

    PhosphoSiteiO43447.

    Expressioni

    Gene expression databases

    ArrayExpressiO43447.
    BgeeiO43447.
    CleanExiHS_PPIH.
    GenevestigatoriO43447.

    Organism-specific databases

    HPAiHPA059019.

    Interactioni

    Subunit structurei

    Interacts directly with PRPF4. Part of a heteromeric complex containing PPIH, PRPF3 and PRPF4 that is stable in the absence of RNA. Component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Heterodimer with PRPF18.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRPF4O431722EBI-1055615,EBI-718395

    Protein-protein interaction databases

    BioGridi115728. 20 interactions.
    IntActiO43447. 8 interactions.
    MINTiMINT-270606.
    STRINGi9606.ENSP00000306614.

    Structurei

    Secondary structure

    1
    177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 198
    Beta strandi22 – 3110
    Turni33 – 353
    Helixi37 – 4812
    Beta strandi67 – 693
    Turni70 – 723
    Beta strandi73 – 764
    Turni79 – 813
    Beta strandi82 – 843
    Beta strandi109 – 1124
    Beta strandi124 – 1296
    Helixi132 – 1343
    Turni135 – 1373
    Beta strandi140 – 1467
    Helixi148 – 1558
    Helixi161 – 1633
    Beta strandi165 – 1673
    Beta strandi169 – 1768

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MZWX-ray2.00A1-177[»]
    1QOIX-ray2.00A1-177[»]
    ProteinModelPortaliO43447.
    SMRiO43447. Positions 5-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43447.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 176163PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0652.
    HOGENOMiHOG000065981.
    HOVERGENiHBG001065.
    InParanoidiO43447.
    KOiK09567.
    OMAiTPKFPDE.
    OrthoDBiEOG79GT7W.
    PhylomeDBiO43447.
    TreeFamiTF312958.

    Family and domain databases

    Gene3Di2.40.100.10. 1 hit.
    InterProiIPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view]
    PfamiPF00160. Pro_isomerase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSiPR00153. CSAPPISMRASE.
    SUPFAMiSSF50891. SSF50891. 1 hit.
    PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 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: O43447-1) [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

    MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGE    50
    FRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF 100
    KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV 150
    MRKIENVPTG PNNKPKLPVV ISQCGEM 177
    Length:177
    Mass (Da):19,208
    Last modified:June 1, 1998 - v1
    Checksum:i566BCE6361E0F339
    GO
    Isoform 2 (identifier: O43447-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-51: MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEF → MIAGDSDR

    Note: No experimental confirmation available.

    Show »
    Length:134
    Mass (Da):14,492
    Checksum:iE55350B73F8A1C3B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5151MAVAN…CTGEF → MIAGDSDR in isoform 2. 1 PublicationVSP_056587Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF016371 mRNA. Translation: AAC51927.1.
    AF036331 mRNA. Translation: AAC60793.1.
    AK294288 mRNA. Translation: BAH11725.1.
    AC098484 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX07155.1.
    BC003412 mRNA. Translation: AAH03412.1.
    CCDSiCCDS469.1.
    RefSeqiNP_006338.1. NM_006347.3.
    XP_005270419.1. XM_005270362.1.
    XP_005270421.1. XM_005270364.2.
    XP_006710356.1. XM_006710293.1.
    UniGeneiHs.256639.

    Genome annotation databases

    EnsembliENST00000304979; ENSP00000306614; ENSG00000171960.
    ENST00000372550; ENSP00000361630; ENSG00000171960.
    GeneIDi10465.
    KEGGihsa:10465.
    UCSCiuc001chq.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF016371 mRNA. Translation: AAC51927.1 .
    AF036331 mRNA. Translation: AAC60793.1 .
    AK294288 mRNA. Translation: BAH11725.1 .
    AC098484 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX07155.1 .
    BC003412 mRNA. Translation: AAH03412.1 .
    CCDSi CCDS469.1.
    RefSeqi NP_006338.1. NM_006347.3.
    XP_005270419.1. XM_005270362.1.
    XP_005270421.1. XM_005270364.2.
    XP_006710356.1. XM_006710293.1.
    UniGenei Hs.256639.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MZW X-ray 2.00 A 1-177 [» ]
    1QOI X-ray 2.00 A 1-177 [» ]
    ProteinModelPortali O43447.
    SMRi O43447. Positions 5-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115728. 20 interactions.
    IntActi O43447. 8 interactions.
    MINTi MINT-270606.
    STRINGi 9606.ENSP00000306614.

    Chemistry

    DrugBanki DB00172. L-Proline.

    PTM databases

    PhosphoSitei O43447.

    Proteomic databases

    MaxQBi O43447.
    PaxDbi O43447.
    PRIDEi O43447.

    Protocols and materials databases

    DNASUi 10465.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000304979 ; ENSP00000306614 ; ENSG00000171960 .
    ENST00000372550 ; ENSP00000361630 ; ENSG00000171960 .
    GeneIDi 10465.
    KEGGi hsa:10465.
    UCSCi uc001chq.3. human.

    Organism-specific databases

    CTDi 10465.
    GeneCardsi GC01P043097.
    HGNCi HGNC:14651. PPIH.
    HPAi HPA059019.
    MIMi 606095. gene.
    neXtProti NX_O43447.
    PharmGKBi PA33586.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0652.
    HOGENOMi HOG000065981.
    HOVERGENi HBG001065.
    InParanoidi O43447.
    KOi K09567.
    OMAi TPKFPDE.
    OrthoDBi EOG79GT7W.
    PhylomeDBi O43447.
    TreeFami TF312958.

    Miscellaneous databases

    ChiTaRSi PPIH. human.
    EvolutionaryTracei O43447.
    GeneWikii PPIH.
    GenomeRNAii 10465.
    NextBioi 39685.
    PROi O43447.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43447.
    Bgeei O43447.
    CleanExi HS_PPIH.
    Genevestigatori O43447.

    Family and domain databases

    Gene3Di 2.40.100.10. 1 hit.
    InterProi IPR029000. Cyclophilin-like_dom.
    IPR024936. Cyclophilin-type_PPIase.
    IPR020892. Cyclophilin-type_PPIase_CS.
    IPR002130. Cyclophilin-type_PPIase_dom.
    [Graphical view ]
    Pfami PF00160. Pro_isomerase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
    PRINTSi PR00153. CSAPPISMRASE.
    SUPFAMi SSF50891. SSF50891. 1 hit.
    PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
    PS50072. CSA_PPIASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated with U4/U6 snRNPs."
      Horowitz D.S., Kobayashi R., Krainer A.R.
      RNA 3:1374-1387(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 154-164, INTERACTION WITH PRPF3; PRPF4 AND U4/U6 SNRNPS.
      Tissue: Liver.
    2. "The 20kD protein of human [U4/U6.U5] tri-snRNPs is a novel cyclophilin that forms a complex with the U4/U6-specific 60kD and 90kD proteins."
      Teigelkamp S., Achsel T., Mundt C., Goethel S.-F., Cronshagen U., Lane W.S., Marahiel M., Luehrmann R.
      RNA 4:127-141(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 62-67; 71-81 AND 153-164, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE U4/U5/U6 TRI-SNRNP COMPLEX.
      Tissue: Liver.
    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] (ISOFORM 2).
      Tissue: Amygdala.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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: Placenta.
    7. "A cyclophilin functions in pre-mRNA splicing."
      Horowitz D.S., Lee E.J., Mabon S.A., Misteli T.
      EMBO J. 21:470-480(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TRP-133, INTERACTION WITH PRPF4 AND PRPF18.
    8. "The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
      Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
      RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Crystal structure of the human U4/U6 small nuclear ribonucleoprotein particle-specific SnuCyp-20, a nuclear cyclophilin."
      Reidt U., Reuter K., Achsel T., Ingelfinger D., Luehrmann R., Ficner R.
      J. Biol. Chem. 275:7439-7442(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177.
    12. "Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide."
      Reidt U., Wahl M.C., Fasshauer D., Horowitz D.S., Luehrmann R., Ficner R.
      J. Mol. Biol. 331:45-56(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-177 IN COMPLEX WITH PRPF4, FUNCTION.

    Entry informationi

    Entry nameiPPIH_HUMAN
    AccessioniPrimary (citable) accession number: O43447
    Secondary accession number(s): A6NNE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 129 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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