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Q9Y316

- MEMO1_HUMAN

UniProt

Q9Y316 - MEMO1_HUMAN

Protein

Protein MEMO1

Gene

MEMO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. regulation of microtubule-based process Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein MEMO1
    Alternative name(s):
    C21orf19-like protein
    Hepatitis C virus NS5A-transactivated protein 7
    Short name:
    HCV NS5A-transactivated protein 7
    Mediator of ErbB2-driven cell motility 1
    Short name:
    Mediator of cell motility 1
    Short name:
    Memo-1
    Gene namesi
    Name:MEMO1
    Synonyms:C2orf4, MEMO, NS5ATP7
    ORF Names:CGI-27
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14014. MEMO1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161W → A: Abolishes interaction with ERBB2. 1 Publication
    Mutagenesisi49 – 491H → A: Abolishes interaction with ERBB2. 1 Publication
    Mutagenesisi54 – 541Y → A: Diminishes interaction with ERBB2. 1 Publication
    Mutagenesisi81 – 811H → A: Abolishes interaction with ERBB2. 1 Publication
    Mutagenesisi192 – 1921H → A: Abolishes interaction with ERBB2. 1 Publication
    Mutagenesisi244 – 2441C → A: Abolishes interaction with ERBB2. 1 Publication

    Organism-specific databases

    PharmGKBiPA162395745.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 297297Protein MEMO1PRO_0000134394Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101PhosphotyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y316.
    PaxDbiQ9Y316.
    PRIDEiQ9Y316.

    PTM databases

    PhosphoSiteiQ9Y316.

    Expressioni

    Gene expression databases

    BgeeiQ9Y316.
    CleanExiHS_MEMO1.
    GenevestigatoriQ9Y316.

    Organism-specific databases

    HPAiHPA042603.

    Interactioni

    Subunit structurei

    Interacts with ERBB2 phosphorylated on 'Tyr-1248'.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046266EBI-1104564,EBI-641062

    Protein-protein interaction databases

    BioGridi119263. 6 interactions.
    IntActiQ9Y316. 4 interactions.
    MINTiMINT-3085289.
    STRINGi9606.ENSP00000295065.

    Structurei

    Secondary structure

    1
    297
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni11 – 155
    Helixi21 – 3212
    Beta strandi43 – 475
    Helixi52 – 6312
    Turni68 – 703
    Beta strandi73 – 797
    Beta strandi81 – 833
    Beta strandi86 – 905
    Beta strandi94 – 963
    Beta strandi103 – 1053
    Helixi107 – 1159
    Beta strandi119 – 1213
    Helixi124 – 1296
    Helixi134 – 1363
    Helixi137 – 1437
    Helixi145 – 1473
    Beta strandi152 – 1587
    Helixi163 – 17715
    Beta strandi182 – 1876
    Beta strandi192 – 1943
    Helixi195 – 1973
    Helixi204 – 2063
    Helixi209 – 22517
    Helixi229 – 23911
    Helixi246 – 26116
    Beta strandi266 – 27712
    Beta strandi286 – 29611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BCZX-ray2.10A/B/C/D5-297[»]
    3BD0X-ray3.01A/B/C/D5-297[»]
    ProteinModelPortaliQ9Y316.
    SMRiQ9Y316. Positions 5-297.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y316.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the MEMO1 family.Curated

    Phylogenomic databases

    eggNOGiCOG1355.
    HOGENOMiHOG000225260.
    HOVERGENiHBG050811.
    KOiK06990.
    OMAiEHSLEMH.
    OrthoDBiEOG7FFMS1.
    PhylomeDBiQ9Y316.
    TreeFamiTF300014.

    Family and domain databases

    HAMAPiMF_00055. MEMO1.
    InterProiIPR002737. MEMO1_fam.
    [Graphical view]
    PANTHERiPTHR11060. PTHR11060. 1 hit.
    PfamiPF01875. Memo. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR04336. AmmeMemoSam_B. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y316-1) [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

    MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPHA    50
    GYTYCGSCAA HAYKQVDPSI TRRIFILGPS HHVPLSRCAL SSVDIYRTPL 100
    YDLRIDQKIY GELWKTGMFE RMSLQTDEDE HSIEMHLPYT AKAMESHKDE 150
    FTIIPVLVGA LSESKEQEFG KLFSKYLADP SNLFVVSSDF CHWGQRFRYS 200
    YYDESQGEIY RSIEHLDKMG MSIIEQLDPV SFSNYLKKYH NTICGRHPIG 250
    VLLNAITELQ KNGMNMSFSF LNYAQSSQCR NWQDSSVSYA AGALTVH 297
    Length:297
    Mass (Da):33,733
    Last modified:November 1, 1999 - v1
    Checksum:iE315FD5587776211
    GO
    Isoform 2 (identifier: Q9Y316-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         49-71: Missing.

    Show »
    Length:274
    Mass (Da):31,307
    Checksum:i1BE5B4A07A5D44D8
    GO
    Isoform 3 (identifier: Q9Y316-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MSNRVVCREASHAGSWYTAS → MPLWRADKCQDVQSASWRPRRAD

    Show »
    Length:300
    Mass (Da):34,294
    Checksum:i0778186B7CCA0ADA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231Q → H in AAH70046. (PubMed:15489334)Curated
    Sequence conflicti172 – 1721L → P in BAG59632. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020MSNRV…WYTAS → MPLWRADKCQDVQSASWRPR RAD in isoform 3. 1 PublicationVSP_047693Add
    BLAST
    Alternative sequencei49 – 7123Missing in isoform 2. 1 PublicationVSP_041092Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF363446 mRNA. Translation: AAL34462.1.
    AB041018 mRNA. Translation: BAD74066.1.
    AB041019 mRNA. Translation: BAD74067.1.
    AF529368 mRNA. Translation: AAQ09602.1.
    AF132961 mRNA. Translation: AAD27736.1.
    AK297128 mRNA. Translation: BAG59632.1.
    AL121652 Genomic DNA. No translation available.
    AL121655 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00467.1.
    CH471053 Genomic DNA. Translation: EAX00469.1.
    CH471053 Genomic DNA. Translation: EAX00470.1.
    CH471053 Genomic DNA. Translation: EAX00472.1.
    BC018733 mRNA. Translation: AAH18733.1.
    BC070046 mRNA. Translation: AAH70046.1.
    BC094681 mRNA. Translation: AAH94681.1.
    CCDSiCCDS1776.1. [Q9Y316-1]
    CCDS46255.1. [Q9Y316-2]
    RefSeqiNP_001131074.1. NM_001137602.1. [Q9Y316-2]
    NP_057039.1. NM_015955.2. [Q9Y316-1]
    XP_005264408.1. XM_005264351.1. [Q9Y316-1]
    UniGeneiHs.444969.

    Genome annotation databases

    EnsembliENST00000295065; ENSP00000295065; ENSG00000162959. [Q9Y316-1]
    ENST00000379383; ENSP00000368691; ENSG00000162959. [Q9Y316-3]
    ENST00000404530; ENSP00000385557; ENSG00000162959. [Q9Y316-1]
    ENST00000426310; ENSP00000400795; ENSG00000162959. [Q9Y316-2]
    GeneIDi51072.
    KEGGihsa:51072.
    UCSCiuc002rnx.3. human. [Q9Y316-1]
    uc010ymu.2. human. [Q9Y316-2]

    Polymorphism databases

    DMDMi7388490.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF363446 mRNA. Translation: AAL34462.1 .
    AB041018 mRNA. Translation: BAD74066.1 .
    AB041019 mRNA. Translation: BAD74067.1 .
    AF529368 mRNA. Translation: AAQ09602.1 .
    AF132961 mRNA. Translation: AAD27736.1 .
    AK297128 mRNA. Translation: BAG59632.1 .
    AL121652 Genomic DNA. No translation available.
    AL121655 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAX00467.1 .
    CH471053 Genomic DNA. Translation: EAX00469.1 .
    CH471053 Genomic DNA. Translation: EAX00470.1 .
    CH471053 Genomic DNA. Translation: EAX00472.1 .
    BC018733 mRNA. Translation: AAH18733.1 .
    BC070046 mRNA. Translation: AAH70046.1 .
    BC094681 mRNA. Translation: AAH94681.1 .
    CCDSi CCDS1776.1. [Q9Y316-1 ]
    CCDS46255.1. [Q9Y316-2 ]
    RefSeqi NP_001131074.1. NM_001137602.1. [Q9Y316-2 ]
    NP_057039.1. NM_015955.2. [Q9Y316-1 ]
    XP_005264408.1. XM_005264351.1. [Q9Y316-1 ]
    UniGenei Hs.444969.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BCZ X-ray 2.10 A/B/C/D 5-297 [» ]
    3BD0 X-ray 3.01 A/B/C/D 5-297 [» ]
    ProteinModelPortali Q9Y316.
    SMRi Q9Y316. Positions 5-297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119263. 6 interactions.
    IntActi Q9Y316. 4 interactions.
    MINTi MINT-3085289.
    STRINGi 9606.ENSP00000295065.

    PTM databases

    PhosphoSitei Q9Y316.

    Polymorphism databases

    DMDMi 7388490.

    Proteomic databases

    MaxQBi Q9Y316.
    PaxDbi Q9Y316.
    PRIDEi Q9Y316.

    Protocols and materials databases

    DNASUi 51072.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295065 ; ENSP00000295065 ; ENSG00000162959 . [Q9Y316-1 ]
    ENST00000379383 ; ENSP00000368691 ; ENSG00000162959 . [Q9Y316-3 ]
    ENST00000404530 ; ENSP00000385557 ; ENSG00000162959 . [Q9Y316-1 ]
    ENST00000426310 ; ENSP00000400795 ; ENSG00000162959 . [Q9Y316-2 ]
    GeneIDi 51072.
    KEGGi hsa:51072.
    UCSCi uc002rnx.3. human. [Q9Y316-1 ]
    uc010ymu.2. human. [Q9Y316-2 ]

    Organism-specific databases

    GeneCardsi GC02M032092.
    HGNCi HGNC:14014. MEMO1.
    HPAi HPA042603.
    MIMi 611786. gene.
    neXtProti NX_Q9Y316.
    PharmGKBi PA162395745.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1355.
    HOGENOMi HOG000225260.
    HOVERGENi HBG050811.
    KOi K06990.
    OMAi EHSLEMH.
    OrthoDBi EOG7FFMS1.
    PhylomeDBi Q9Y316.
    TreeFami TF300014.

    Miscellaneous databases

    ChiTaRSi MEMO1. human.
    EvolutionaryTracei Q9Y316.
    GenomeRNAii 51072.
    NextBioi 53687.
    PROi Q9Y316.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y316.
    CleanExi HS_MEMO1.
    Genevestigatori Q9Y316.

    Family and domain databases

    HAMAPi MF_00055. MEMO1.
    InterProi IPR002737. MEMO1_fam.
    [Graphical view ]
    PANTHERi PTHR11060. PTHR11060. 1 hit.
    Pfami PF01875. Memo. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR04336. AmmeMemoSam_B. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "From PREDs and open reading frames to cDNA isolation: revisiting the human chromosome 21 transcription map."
      Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.
      Genomics 78:46-54(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of two isoforms of C2orf4 gene."
      Shibuya K., Kudoh J., Shimizu N.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
      Tissue: Heart and Skeletal muscle.
    3. "Cloning and identification of human gene 7 transactivated by hepatitis C virus NS5A protein."
      Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "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).
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: B-cell, PNS and Testis.
    9. Cited for: FUNCTION, INTERACTION WITH ERBB2.
    10. "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
      Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
      Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site."
      Qiu C., Lienhard S., Hynes N.E., Badache A., Leahy D.J.
      J. Biol. Chem. 283:2734-2740(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-297, INTERACTION WITH ERBB2, MUTAGENESIS OF TRP-16; HIS-49; TYR-54; HIS-81; HIS-192 AND CYS-244.

    Entry informationi

    Entry nameiMEMO1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y316
    Secondary accession number(s): B4DLS0
    , D6W575, Q5R2V8, Q5R2V9, Q6NSL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 121 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 2
      Human chromosome 2: 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
    5. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3