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Q92688

- AN32B_HUMAN

UniProt

Q92688 - AN32B_HUMAN

Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member B

Gene

ANP32B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity By similarity. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome.By similarity1 Publication

    GO - Molecular functioni

    1. histone binding Source: UniProt
    2. RNA polymerase binding Source: UniProt

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProt
    2. negative regulation of cell differentiation Source: UniProt
    3. nucleosome assembly Source: UniProt
    4. positive regulation of protein export from nucleus Source: UniProt

    Keywords - Molecular functioni

    Chaperone

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acidic leucine-rich nuclear phosphoprotein 32 family member B
    Alternative name(s):
    Acidic protein rich in leucines
    Putative HLA-DR-associated protein I-2
    Short name:
    PHAPI2
    Silver-stainable protein SSP29
    Gene namesi
    Name:ANP32B
    Synonyms:APRIL, PHAPI2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:16677. ANP32B.

    Subcellular locationi

    Isoform 1 : Nucleus
    Note: Accumulates in the nuclei at the S phase.By similarity
    Isoform 2 : Cytoplasm
    Note: Lacks a nuclear localization signal.

    GO - Cellular componenti

    1. cytoplasm Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24812.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 251251Acidic leucine-rich nuclear phosphoprotein 32 family member BPRO_0000137595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei86 – 861N6-acetyllysine1 Publication
    Modified residuei244 – 2441Phosphothreonine4 Publications

    Post-translational modificationi

    Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92688.
    PaxDbiQ92688.
    PRIDEiQ92688.

    PTM databases

    PhosphoSiteiQ92688.

    Miscellaneous databases

    PMAP-CutDBQ92688.

    Expressioni

    Tissue specificityi

    Expressed in heart, lung, pancreas, prostate and in spleen, thymus and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ92688.
    BgeeiQ92688.
    CleanExiHS_ANP32B.
    GenevestigatoriQ92688.

    Interactioni

    Subunit structurei

    Monomer. Interacts with histones H3 and H4.1 Publication

    Protein-protein interaction databases

    BioGridi115795. 34 interactions.
    IntActiQ92688. 13 interactions.
    STRINGi9606.ENSP00000345848.

    Structurei

    Secondary structure

    1
    251
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 119
    Helixi16 – 183
    Beta strandi20 – 234
    Helixi39 – 435
    Beta strandi46 – 527
    Beta strandi68 – 736
    Helixi82 – 865
    Beta strandi92 – 943
    Beta strandi96 – 994
    Helixi104 – 1096
    Beta strandi117 – 1193
    Helixi124 – 1263
    Helixi131 – 1366
    Beta strandi157 – 1593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ELLNMR-A1-161[»]
    2RR6NMR-A1-161[»]
    ProteinModelPortaliQ92688.
    SMRiQ92688. Positions 1-161.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92688.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati16 – 4025LRR 11 PublicationAdd
    BLAST
    Repeati43 – 6422LRR 21 PublicationAdd
    BLAST
    Repeati65 – 8420LRR 31 PublicationAdd
    BLAST
    Repeati89 – 11022LRR 41 PublicationAdd
    BLAST
    Domaini123 – 16139LRRCTAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi146 – 251106Asp/Glu-rich (highly acidic)Add
    BLAST

    Domaini

    Histone binding is mediated by the concave surface of the LRR region.

    Sequence similaritiesi

    Belongs to the ANP32 family.Curated
    Contains 4 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG322008.
    HOGENOMiHOG000007361.
    HOVERGENiHBG053102.
    InParanoidiQ92688.
    OMAiDEVSGEX.
    OrthoDBiEOG7TJ3KH.
    PhylomeDBiQ92688.
    TreeFamiTF317206.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view]
    SMARTiSM00446. LRRcap. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92688-1) [UniParc]FASTAAdd to Basket

    Also known as: Anp32b1, PHAPI2b

    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

    MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI    50
    NVGLISVSNL PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL 100
    KDISTLEPLK KLECLKSLDL FNCEVTNLND YRESVFKLLP QLTYLDGYDR 150
    EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE DDEDGEEEEF DEEDDEDEDV 200
    EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR KRETDDEGED 250
    D 251
    Length:251
    Mass (Da):28,788
    Last modified:February 1, 1997 - v1
    Checksum:i93A1AADF8EDE7D53
    GO
    Isoform 2 (identifier: Q92688-2) [UniParc]FASTAAdd to Basket

    Also known as: Anp32b2, PHAPI2b

    The sequence of this isoform differs from the canonical sequence as follows:
         196-251: Missing.

    Note: No canonical donor splice site.

    Show »
    Length:195
    Mass (Da):22,277
    Checksum:iC504A0E604F16F73
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 22Missing in CAA69265. (PubMed:9473664)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei196 – 25156Missing in isoform 2. 1 PublicationVSP_019304Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07569 mRNA. Translation: CAA68855.1.
    U70439 mRNA. Translation: AAB37579.1.
    Y07969 mRNA. Translation: CAA69265.1.
    Y07570 mRNA. Translation: CAA68856.1.
    AK313733 mRNA. Translation: BAG36474.1.
    AL354726 Genomic DNA. Translation: CAI15260.1.
    CH471105 Genomic DNA. Translation: EAW58865.1.
    BC013003 mRNA. Translation: AAH13003.1.
    BC019658 mRNA. Translation: AAH19658.1.
    CCDSiCCDS6732.1. [Q92688-1]
    RefSeqiNP_006392.1. NM_006401.2. [Q92688-1]
    UniGeneiHs.730654.

    Genome annotation databases

    EnsembliENST00000339399; ENSP00000345848; ENSG00000136938. [Q92688-1]
    GeneIDi10541.
    KEGGihsa:10541.
    UCSCiuc004aya.3. human. [Q92688-1]

    Polymorphism databases

    DMDMi26390818.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y07569 mRNA. Translation: CAA68855.1 .
    U70439 mRNA. Translation: AAB37579.1 .
    Y07969 mRNA. Translation: CAA69265.1 .
    Y07570 mRNA. Translation: CAA68856.1 .
    AK313733 mRNA. Translation: BAG36474.1 .
    AL354726 Genomic DNA. Translation: CAI15260.1 .
    CH471105 Genomic DNA. Translation: EAW58865.1 .
    BC013003 mRNA. Translation: AAH13003.1 .
    BC019658 mRNA. Translation: AAH19658.1 .
    CCDSi CCDS6732.1. [Q92688-1 ]
    RefSeqi NP_006392.1. NM_006401.2. [Q92688-1 ]
    UniGenei Hs.730654.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ELL NMR - A 1-161 [» ]
    2RR6 NMR - A 1-161 [» ]
    ProteinModelPortali Q92688.
    SMRi Q92688. Positions 1-161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115795. 34 interactions.
    IntActi Q92688. 13 interactions.
    STRINGi 9606.ENSP00000345848.

    PTM databases

    PhosphoSitei Q92688.

    Polymorphism databases

    DMDMi 26390818.

    Proteomic databases

    MaxQBi Q92688.
    PaxDbi Q92688.
    PRIDEi Q92688.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339399 ; ENSP00000345848 ; ENSG00000136938 . [Q92688-1 ]
    GeneIDi 10541.
    KEGGi hsa:10541.
    UCSCi uc004aya.3. human. [Q92688-1 ]

    Organism-specific databases

    CTDi 10541.
    GeneCardsi GC09P100745.
    HGNCi HGNC:16677. ANP32B.
    neXtProti NX_Q92688.
    PharmGKBi PA24812.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322008.
    HOGENOMi HOG000007361.
    HOVERGENi HBG053102.
    InParanoidi Q92688.
    OMAi DEVSGEX.
    OrthoDBi EOG7TJ3KH.
    PhylomeDBi Q92688.
    TreeFami TF317206.

    Miscellaneous databases

    ChiTaRSi ANP32B. human.
    EvolutionaryTracei Q92688.
    GeneWikii ANP32B.
    GenomeRNAii 10541.
    NextBioi 39993.
    PMAP-CutDB Q92688.
    PROi Q92688.

    Gene expression databases

    ArrayExpressi Q92688.
    Bgeei Q92688.
    CleanExi HS_ANP32B.
    Genevestigatori Q92688.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR003603. U2A'_phosphoprotein32A_C.
    [Graphical view ]
    SMARTi SM00446. LRRcap. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Vaesen M., Barnikol-Watanabe S., Kratzin H.D., Hilschmann N.
      Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Molecular cloning and partial characterization of a new silver-stainable protein."
      Zhu L., Henning D., Valdez B.C.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Expression analysis and chromosomal mapping of a novel human gene, APRIL, encoding an acidic protein rich in leucines."
      Mencinger M., Panagopoulos I., Contreras J.A., Mitelman F., Aman P.
      Biochim. Biophys. Acta 1395:176-180(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Pancreas.
    4. "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).
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Muscle and Testis.
    8. "The Anp32 family of proteins containing leucine-rich repeats."
      Matilla A., Radrizzani M.
      Cerebellum 4:7-18(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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 THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 THR-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain."
      Tochio N., Umehara T., Munemasa Y., Suzuki T., Sato S., Tsuda K., Koshiba S., Kigawa T., Nagai R., Yokoyama S.
      J. Mol. Biol. 401:97-114(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-161, FUNCTION, SUBUNIT, INTERACTION WITH HISTONES H3 AND H4, LEUCINE-RICH REPEATS.

    Entry informationi

    Entry nameiAN32B_HUMAN
    AccessioniPrimary (citable) accession number: Q92688
    Secondary accession number(s): B2R9C7
    , O00655, P78458, P78459
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 131 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3