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Q9BVP2

- GNL3_HUMAN

UniProt

Q9BVP2 - GNL3_HUMAN

Protein

Guanine nucleotide-binding protein-like 3

Gene

GNL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    May be required to maintain the proliferative capacity of stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence proteasomal degradation By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi178 – 1814GTPSequence Analysis
    Nucleotide bindingi261 – 2688GTPSequence Analysis
    Nucleotide bindingi305 – 3084GTPSequence Analysis

    GO - Molecular functioni

    1. GTPase activity Source: RefGenome
    2. GTP binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. GTP catabolic process Source: GOC
    3. regulation of cell proliferation Source: UniProtKB
    4. ribosome biogenesis Source: RefGenome

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein-like 3
    Alternative name(s):
    E2-induced gene 3 protein
    Novel nucleolar protein 47
    Short name:
    NNP47
    Nucleolar GTP-binding protein 3
    Nucleostemin
    Gene namesi
    Name:GNL3
    Synonyms:E2IG3, NS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:29931. GNL3.

    Subcellular locationi

    Nucleus By similarity. Nucleusnucleolus By similarity
    Note: Shuttles between the nucleus and nucleolus.By similarity

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. membrane Source: UniProtKB
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: Ensembl
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134952132.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 549549Guanine nucleotide-binding protein-like 3PRO_0000122444Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei79 – 791N6-acetyllysine1 Publication
    Modified residuei529 – 5291Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BVP2.
    PaxDbiQ9BVP2.
    PRIDEiQ9BVP2.

    2D gel databases

    SWISS-2DPAGEQ9BVP2.

    PTM databases

    PhosphoSiteiQ9BVP2.

    Expressioni

    Tissue specificityi

    Increased levels in lung tissue in cancer patients.1 Publication

    Gene expression databases

    ArrayExpressiQ9BVP2.
    BgeeiQ9BVP2.
    CleanExiHS_GNL3.
    GenevestigatoriQ9BVP2.

    Organism-specific databases

    HPAiCAB020770.

    Interactioni

    Subunit structurei

    Interacts with MDM2; this interaction stabilizes MDM2. Interaction with MDM2 occurs in the nucleoplasm and is triggered by a nucleolar release mechanism, such as mitosis-induced nucleolar disassembly By similarity. Indirectly interacts with TP53, via MDM2-binding By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDM2Q009873EBI-641642,EBI-389668
    PPP2R5AQ151723EBI-641642,EBI-641666
    STAT3P407632EBI-641642,EBI-518675

    Protein-protein interaction databases

    BioGridi117690. 64 interactions.
    IntActiQ9BVP2. 18 interactions.
    MINTiMINT-1405256.
    STRINGi9606.ENSP00000395772.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BVP2.
    SMRiQ9BVP2. Positions 130-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini131 – 312182CP-type GPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 4645BasicBy similarityAdd
    BLAST
    Regioni282 – 456175IntermediateBy similarityAdd
    BLAST
    Regioni465 – 54379AcidicBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili56 – 9540Sequence AnalysisAdd
    BLAST

    Domaini

    The basic domain (B) allows nucleolar localization in the absence of GTP. The intermediate domain (I) inhibits nucleolar localization by the B domain and is required for exit from the nucleolus. Exit from the nucleolus to the nucleoplasm requires both the I and the acidic (A) domains, and may be triggered by GTP hydrolysis By similarity.By similarity
    In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.

    Sequence similaritiesi

    Belongs to the TRAFAC class YlqF/YawG GTPase family.PROSITE-ProRule annotation
    Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1161.
    HOGENOMiHOG000207716.
    HOVERGENiHBG051747.
    InParanoidiQ9BVP2.
    KOiK14538.
    OMAiPKKLYCQ.
    OrthoDBiEOG7J9VPR.
    PhylomeDBiQ9BVP2.
    TreeFamiTF313085.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR014813. Gnl3_N_dom.
    IPR006073. GTP_binding_domain.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF08701. GN3L_Grn1. 1 hit.
    PF01926. MMR_HSR1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51721. G_CP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BVP2-1) [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

    MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV    50
    PNSAPFKEAL LREAELRKQR LEELKQQQKL DRQKELEKKR KLETNPDIKP 100
    SNVEPMEKEF GLCKTENKAK SGKQNSKKLY CQELKKVIEA SDVVLEVLDA 150
    RDPLGCRCPQ VEEAIVQSGQ KKLVLILNKS DLVPKENLES WLNYLKKELP 200
    TVVFRASTKP KDKGKITKRV KAKKNAAPFR SEVCFGKEGL WKLLGGFQET 250
    CSKAIRVGVI GFPNVGKSSI INSLKQEQMC NVGVSMGLTR SMQVVPLDKQ 300
    ITIIDSPSFI VSPLNSSSAL ALRSPASIEV VKPMEAASAI LSQADARQVV 350
    LKYTVPGYRN SLEFFTVLAQ RRGMHQKGGI PNVEGAAKLL WSEWTGASLA 400
    YYCHPPTSWT PPPYFNESIV VDMKSGFNLE ELEKNNAQSI RAIKGPHLAN 450
    SILFQSSGLT NGIIEEKDIH EELPKRKERK QEEREDDKDS DQETVDEEVD 500
    ENSSGMFAAE ETGEALSEET TAGEQSTRSF ILDKIIEEDD AYDFSTDYV 549
    Length:549
    Mass (Da):61,993
    Last modified:May 5, 2009 - v2
    Checksum:iF3928FE1C77C77F4
    GO
    Isoform 2 (identifier: Q9BVP2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-12: Missing.

    Show »
    Length:537
    Mass (Da):60,540
    Checksum:i342BCB22B4234056
    GO

    Sequence cautioni

    The sequence AAF09482.1 differs from that shown. Reason: Frameshift at position 516.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31R → K in AAV74413. (PubMed:16012751)Curated
    Sequence conflicti86 – 861L → Q in AAV74413. (PubMed:16012751)Curated
    Sequence conflicti436 – 4361N → D in AAV74413. (PubMed:16012751)Curated
    Sequence conflicti463 – 4631I → M in BAB55169. (PubMed:14702039)Curated
    Sequence conflicti495 – 4951V → A in AAV74413. (PubMed:16012751)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391R → Q.3 Publications
    Corresponds to variant rs11177 [ dbSNP | Ensembl ].
    VAR_022160
    Natural varianti367 – 3671V → M.4 Publications
    Corresponds to variant rs2289247 [ dbSNP | Ensembl ].
    VAR_022161

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1212Missing in isoform 2. 1 PublicationVSP_013411Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191018 mRNA. Translation: AAF09482.1. Frameshift.
    AY825265 mRNA. Translation: AAV74413.1.
    AK027514 mRNA. Translation: BAB55168.1.
    AK027516 mRNA. Translation: BAB55169.1.
    AK315484 mRNA. Translation: BAG37868.1.
    AC104446 Genomic DNA. No translation available.
    BC001024 mRNA. Translation: AAH01024.1.
    CCDSiCCDS2861.1. [Q9BVP2-1]
    CCDS43100.1. [Q9BVP2-2]
    RefSeqiNP_055181.3. NM_014366.4. [Q9BVP2-1]
    NP_996561.1. NM_206825.1. [Q9BVP2-2]
    NP_996562.1. NM_206826.1. [Q9BVP2-2]
    UniGeneiHs.313544.

    Genome annotation databases

    EnsembliENST00000394799; ENSP00000378278; ENSG00000163938. [Q9BVP2-2]
    ENST00000418458; ENSP00000395772; ENSG00000163938. [Q9BVP2-1]
    GeneIDi26354.
    KEGGihsa:26354.
    UCSCiuc003dfd.3. human. [Q9BVP2-1]

    Polymorphism databases

    DMDMi229462872.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191018 mRNA. Translation: AAF09482.1 . Frameshift.
    AY825265 mRNA. Translation: AAV74413.1 .
    AK027514 mRNA. Translation: BAB55168.1 .
    AK027516 mRNA. Translation: BAB55169.1 .
    AK315484 mRNA. Translation: BAG37868.1 .
    AC104446 Genomic DNA. No translation available.
    BC001024 mRNA. Translation: AAH01024.1 .
    CCDSi CCDS2861.1. [Q9BVP2-1 ]
    CCDS43100.1. [Q9BVP2-2 ]
    RefSeqi NP_055181.3. NM_014366.4. [Q9BVP2-1 ]
    NP_996561.1. NM_206825.1. [Q9BVP2-2 ]
    NP_996562.1. NM_206826.1. [Q9BVP2-2 ]
    UniGenei Hs.313544.

    3D structure databases

    ProteinModelPortali Q9BVP2.
    SMRi Q9BVP2. Positions 130-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117690. 64 interactions.
    IntActi Q9BVP2. 18 interactions.
    MINTi MINT-1405256.
    STRINGi 9606.ENSP00000395772.

    PTM databases

    PhosphoSitei Q9BVP2.

    Polymorphism databases

    DMDMi 229462872.

    2D gel databases

    SWISS-2DPAGE Q9BVP2.

    Proteomic databases

    MaxQBi Q9BVP2.
    PaxDbi Q9BVP2.
    PRIDEi Q9BVP2.

    Protocols and materials databases

    DNASUi 26354.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394799 ; ENSP00000378278 ; ENSG00000163938 . [Q9BVP2-2 ]
    ENST00000418458 ; ENSP00000395772 ; ENSG00000163938 . [Q9BVP2-1 ]
    GeneIDi 26354.
    KEGGi hsa:26354.
    UCSCi uc003dfd.3. human. [Q9BVP2-1 ]

    Organism-specific databases

    CTDi 26354.
    GeneCardsi GC03P052718.
    H-InvDB HIX0003367.
    HGNCi HGNC:29931. GNL3.
    HPAi CAB020770.
    MIMi 608011. gene.
    neXtProti NX_Q9BVP2.
    PharmGKBi PA134952132.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1161.
    HOGENOMi HOG000207716.
    HOVERGENi HBG051747.
    InParanoidi Q9BVP2.
    KOi K14538.
    OMAi PKKLYCQ.
    OrthoDBi EOG7J9VPR.
    PhylomeDBi Q9BVP2.
    TreeFami TF313085.

    Miscellaneous databases

    ChiTaRSi GNL3. human.
    GeneWikii GNL3.
    GenomeRNAii 26354.
    NextBioi 48693.
    PROi Q9BVP2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BVP2.
    Bgeei Q9BVP2.
    CleanExi HS_GNL3.
    Genevestigatori Q9BVP2.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR014813. Gnl3_N_dom.
    IPR006073. GTP_binding_domain.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF08701. GN3L_Grn1. 1 hit.
    PF01926. MMR_HSR1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51721. G_CP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Effects of estrogen on global gene expression: identification of novel targets of estrogen action."
      Charpentier A.H., Bednarek A.K., Daniel R.L., Hawkins K.A., Laflin K.J., Gaddis S., MacLeod M.C., Aldaz C.M.
      Cancer Res. 60:5977-5983(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-39 AND MET-367.
    2. "Cloning of the nucleostemin gene and its function in transforming human embryonic bone marrow mesenchymal stem cells into F6 tumor cells."
      Han C., Zhang X., Xu W., Wang W., Qian H., Chen Y.
      Int. J. Mol. Med. 16:205-213(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANTS GLN-39 AND MET-367.
    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).
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1), VARIANTS GLN-39 AND MET-367.
      Tissue: Eye.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A nucleolar mechanism controlling cell proliferation in stem and cancer cells."
      Tsai R.Y.L., McKay R.D.G.
      Genes Dev. 16:2991-3003(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGNL3_HUMAN
    AccessioniPrimary (citable) accession number: Q9BVP2
    Secondary accession number(s): B2RDC1
    , Q5PU80, Q96SV6, Q96SV7, Q9UJY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 122 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 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3