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O95208

- EPN2_HUMAN

UniProt

O95208 - EPN2_HUMAN

Protein

Epsin-2

Gene

EPN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Plays a role in the formation of clathrin-coated invaginations and endocytosis.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Phosphatidylinositol lipid headgroupBy similarity
    Binding sitei11 – 111Phosphatidylinositol lipid headgroupBy similarity
    Binding sitei25 – 251Phosphatidylinositol lipid headgroupBy similarity
    Binding sitei30 – 301Phosphatidylinositol lipid headgroupBy similarity
    Binding sitei63 – 631Phosphatidylinositol lipid headgroupBy similarity
    Binding sitei73 – 731Phosphatidylinositol lipid headgroupBy similarity

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW

    GO - Biological processi

    1. embryonic organ development Source: Ensembl
    2. endocytosis Source: UniProtKB-KW
    3. in utero embryonic development Source: Ensembl
    4. Notch signaling pathway Source: Ensembl

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epsin-2
    Alternative name(s):
    EPS-15-interacting protein 2
    Gene namesi
    Name:EPN2
    Synonyms:KIAA1065
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:18639. EPN2.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmic vesicleclathrin-coated vesicle 1 Publication
    Note: In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex.

    GO - Cellular componenti

    1. clathrin coat of endocytic vesicle Source: InterPro
    2. Golgi apparatus Source: HPA
    3. intracellular membrane-bounded organelle Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38615.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 641641Epsin-2PRO_0000074516Add
    BLAST

    Post-translational modificationi

    Ubiquitinated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO95208.
    PaxDbiO95208.
    PRIDEiO95208.

    PTM databases

    PhosphoSiteiO95208.

    Miscellaneous databases

    PMAP-CutDBO95208.

    Expressioni

    Tissue specificityi

    Highest expression is found in brain. Detected at lower levels in lung and liver.1 Publication

    Gene expression databases

    ArrayExpressiO95208.
    BgeeiO95208.
    CleanExiHS_EPN2.
    GenevestigatoriO95208.

    Organism-specific databases

    HPAiHPA049809.
    HPA053360.

    Interactioni

    Subunit structurei

    Binds EPS15 By similarity. Binds AP-2 and clathrin.By similarity

    Protein-protein interaction databases

    BioGridi116569. 8 interactions.
    STRINGi9606.ENSP00000320543.

    Structurei

    3D structure databases

    ProteinModelPortaliO95208.
    SMRiO95208. Positions 1-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 144133ENTHPROSITE-ProRule annotationAdd
    BLAST
    Repeati275 – 29420UIM 1Add
    BLAST
    Repeati300 – 31920UIM 2Add
    BLAST
    Repeati352 – 35431
    Repeati364 – 36632
    Repeati377 – 37933
    Repeati391 – 39334
    Repeati409 – 41135
    Repeati427 – 42936
    Repeati537 – 53931
    Repeati552 – 55432
    Repeati637 – 63933

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni352 – 6392886 X 3 AA repeats of [DE]-P-WAdd
    BLAST
    Regioni537 – 6391033 X 3 AA repeats of N-P-FAdd
    BLAST

    Domaini

    The NPF repeat domain is involved in EPS15 binding.
    The DPW repeat domain is involved in AP-2 and clathrin binding.

    Sequence similaritiesi

    Belongs to the epsin family.Curated
    Contains 1 ENTH (epsin N-terminal homology) domain.PROSITE-ProRule annotation
    Contains 2 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG263730.
    HOGENOMiHOG000008298.
    HOVERGENiHBG006690.
    InParanoidiO95208.
    KOiK12471.
    OMAiQEYGKSG.
    OrthoDBiEOG7F511Z.
    PhylomeDBiO95208.
    TreeFamiTF313361.

    Family and domain databases

    Gene3Di1.25.40.90. 1 hit.
    InterProiIPR008942. ENTH_VHS.
    IPR027319. Epsin-2_metazoa.
    IPR013809. Epsin-like_N.
    IPR001026. Epsin_dom_N.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view]
    PANTHERiPTHR12276:SF50. PTHR12276:SF50. 1 hit.
    PfamiPF01417. ENTH. 1 hit.
    [Graphical view]
    SMARTiSM00273. ENTH. 1 hit.
    SM00726. UIM. 2 hits.
    [Graphical view]
    SUPFAMiSSF48464. SSF48464. 1 hit.
    PROSITEiPS50942. ENTH. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95208-1) [UniParc]FASTAAdd to Basket

    Also known as: 2b

    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

    MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV    50
    VAFSEIMSMV WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI 100
    FAIQTLKDFQ YIDRDGKDQG INVREKSKQL VALLKDEERL KAERAQALKT 150
    KERMAQVATG MGSNQITFGR GSSQPNLSTS HSEQEYGKAG GSPASYHGSP 200
    EASLCPQHRT GAPLGQSEEL QPLSQRHPFL PHLGLASRPN GDWSQPCLTC 250
    DRAARATSPR VSSELEQARP QTSGEEELQL QLALAMSREV AEQEERLRRG 300
    DDLRLQMALE ESRRDTVKIP KKKEHGSLPQ QTTLLDLMDA LPSSGPAAQK 350
    AEPWGPSAST NQTNPWGGPA APASTSDPWP SFGTKPAASI DPWGVPTGAT 400
    VQSVPKNSDP WAASQQPASS AGKRASDAWG AVSTTKPVSV SGSFELFSNL 450
    NGTIKDDFSE FDNLRTSKKT AESVTSLPSQ NNGTTSPDPF ESQPLTVASS 500
    KPSSARKTPE SFLGPNAALV NLDSLVTRPA PPAQSLNPFL APGAPATSAP 550
    VNPFQVNQPQ PLTLNQLRGS PVLGTSTSFG PGPGVESMAV ASMTSAAPQP 600
    ALGATGSSLT PLGPAMMNMV GSVGIPPSAA QATGTTNPFL L 641
    Length:641
    Mass (Da):68,482
    Last modified:December 16, 2008 - v3
    Checksum:i0BE24CBD824F357A
    GO
    Isoform 2 (identifier: O95208-2) [UniParc]FASTAAdd to Basket

    Also known as: 2a

    The sequence of this isoform differs from the canonical sequence as follows:
         200-256: Missing.

    Note: Contains a phosphoserine at position 192. Contains a phosphoserine at position 195.

    Show »
    Length:584
    Mass (Da):62,300
    Checksum:iD668242ECACD26EF
    GO
    Isoform 3 (identifier: O95208-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.
         200-256: Missing.

    Note: No experimental confirmation available. Contains a phosphoserine at position 153. Contains a phosphoserine at position 156.

    Show »
    Length:545
    Mass (Da):57,919
    Checksum:iC8D6661429926997
    GO
    Isoform 4 (identifier: O95208-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-285: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:356
    Mass (Da):36,729
    Checksum:iEF6741C03E5744A3
    GO

    Sequence cautioni

    The sequence BAA83017.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAG52540.1 differs from that shown. Reason: Erroneous termination at position 324. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti256 – 2561A → AS in AAC78609. (PubMed:10567358)Curated
    Sequence conflicti547 – 5471T → N in AAC78608. (PubMed:10567358)Curated
    Sequence conflicti547 – 5471T → N in AAC78609. (PubMed:10567358)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti401 – 4011V → A.5 Publications
    Corresponds to variant rs6587220 [ dbSNP | Ensembl ].
    VAR_053080
    Natural varianti531 – 5311P → T.
    Corresponds to variant rs1062727 [ dbSNP | Ensembl ].
    VAR_047923
    Natural varianti532 – 5321P → T.
    Corresponds to variant rs1062727 [ dbSNP | Ensembl ].
    VAR_053081

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 285285Missing in isoform 4. 1 PublicationVSP_047003Add
    BLAST
    Alternative sequencei1 – 3939Missing in isoform 3. 1 PublicationVSP_009154Add
    BLAST
    Alternative sequencei200 – 25657Missing in isoform 2 and isoform 3. 2 PublicationsVSP_009155Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF062084 mRNA. Translation: AAC78608.1.
    AF062085 mRNA. Translation: AAC78609.1.
    AB028988 mRNA. Translation: BAA83017.2. Different initiation.
    AK001996 mRNA. Translation: BAG51000.1.
    AK024115 mRNA. Translation: BAB14831.1.
    AK092366 mRNA. Translation: BAG52540.1. Sequence problems.
    AC106017 Genomic DNA. No translation available.
    AC124066 Genomic DNA. No translation available.
    CH471212 Genomic DNA. Translation: EAW50876.1.
    BC093972 mRNA. Translation: AAH93972.1.
    BC093974 mRNA. Translation: AAH93974.1.
    CCDSiCCDS11203.1. [O95208-1]
    CCDS11204.1. [O95208-2]
    CCDS42277.1. [O95208-5]
    RefSeqiNP_001096134.1. NM_001102664.1. [O95208-5]
    NP_055779.2. NM_014964.4. [O95208-1]
    NP_683723.2. NM_148921.3. [O95208-2]
    UniGeneiHs.743983.

    Genome annotation databases

    EnsembliENST00000314728; ENSP00000320543; ENSG00000072134. [O95208-1]
    ENST00000347697; ENSP00000261495; ENSG00000072134. [O95208-2]
    ENST00000395618; ENSP00000378980; ENSG00000072134. [O95208-5]
    ENST00000395620; ENSP00000378982; ENSG00000072134. [O95208-2]
    GeneIDi22905.
    KEGGihsa:22905.
    UCSCiuc002gvd.4. human. [O95208-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF062084 mRNA. Translation: AAC78608.1 .
    AF062085 mRNA. Translation: AAC78609.1 .
    AB028988 mRNA. Translation: BAA83017.2 . Different initiation.
    AK001996 mRNA. Translation: BAG51000.1 .
    AK024115 mRNA. Translation: BAB14831.1 .
    AK092366 mRNA. Translation: BAG52540.1 . Sequence problems.
    AC106017 Genomic DNA. No translation available.
    AC124066 Genomic DNA. No translation available.
    CH471212 Genomic DNA. Translation: EAW50876.1 .
    BC093972 mRNA. Translation: AAH93972.1 .
    BC093974 mRNA. Translation: AAH93974.1 .
    CCDSi CCDS11203.1. [O95208-1 ]
    CCDS11204.1. [O95208-2 ]
    CCDS42277.1. [O95208-5 ]
    RefSeqi NP_001096134.1. NM_001102664.1. [O95208-5 ]
    NP_055779.2. NM_014964.4. [O95208-1 ]
    NP_683723.2. NM_148921.3. [O95208-2 ]
    UniGenei Hs.743983.

    3D structure databases

    ProteinModelPortali O95208.
    SMRi O95208. Positions 1-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116569. 8 interactions.
    STRINGi 9606.ENSP00000320543.

    PTM databases

    PhosphoSitei O95208.

    Proteomic databases

    MaxQBi O95208.
    PaxDbi O95208.
    PRIDEi O95208.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314728 ; ENSP00000320543 ; ENSG00000072134 . [O95208-1 ]
    ENST00000347697 ; ENSP00000261495 ; ENSG00000072134 . [O95208-2 ]
    ENST00000395618 ; ENSP00000378980 ; ENSG00000072134 . [O95208-5 ]
    ENST00000395620 ; ENSP00000378982 ; ENSG00000072134 . [O95208-2 ]
    GeneIDi 22905.
    KEGGi hsa:22905.
    UCSCi uc002gvd.4. human. [O95208-1 ]

    Organism-specific databases

    CTDi 22905.
    GeneCardsi GC17P019118.
    H-InvDB HIX0013614.
    HGNCi HGNC:18639. EPN2.
    HPAi HPA049809.
    HPA053360.
    MIMi 607263. gene.
    neXtProti NX_O95208.
    PharmGKBi PA38615.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG263730.
    HOGENOMi HOG000008298.
    HOVERGENi HBG006690.
    InParanoidi O95208.
    KOi K12471.
    OMAi QEYGKSG.
    OrthoDBi EOG7F511Z.
    PhylomeDBi O95208.
    TreeFami TF313361.

    Miscellaneous databases

    ChiTaRSi EPN2. human.
    GeneWikii EPN2.
    GenomeRNAii 22905.
    NextBioi 43557.
    PMAP-CutDB O95208.
    PROi O95208.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95208.
    Bgeei O95208.
    CleanExi HS_EPN2.
    Genevestigatori O95208.

    Family and domain databases

    Gene3Di 1.25.40.90. 1 hit.
    InterProi IPR008942. ENTH_VHS.
    IPR027319. Epsin-2_metazoa.
    IPR013809. Epsin-like_N.
    IPR001026. Epsin_dom_N.
    IPR003903. Ubiquitin-int_motif.
    [Graphical view ]
    PANTHERi PTHR12276:SF50. PTHR12276:SF50. 1 hit.
    Pfami PF01417. ENTH. 1 hit.
    [Graphical view ]
    SMARTi SM00273. ENTH. 1 hit.
    SM00726. UIM. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48464. SSF48464. 1 hit.
    PROSITEi PS50942. ENTH. 1 hit.
    PS50330. UIM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module."
      Rosenthal J.A., Chen H., Slepnev V.I., Pellegrini L., Salcini A.E., Di Fiore P.P., De Camilli P.
      J. Biol. Chem. 274:33959-33965(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH AP-2 AND CLATHRIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ALA-401.
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-401.
      Tissue: Brain.
    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 2 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORM 3), VARIANT ALA-401.
      Tissue: Embryo, Fetal brain and Placenta.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-401.
    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], VARIANT ALA-401.
      Tissue: Brain.
    7. "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 SER-192 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-192 AND SER-195 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-156 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiEPN2_HUMAN
    AccessioniPrimary (citable) accession number: O95208
    Secondary accession number(s): A8MTV8
    , B3KRX8, E9PBC2, O95207, Q52LD0, Q9H7Z2, Q9UPT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 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 17
      Human chromosome 17: 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