Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15075

- EEA1_HUMAN

UniProt

Q15075 - EEA1_HUMAN

Protein

Early endosome antigen 1

Gene

EEA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 6424C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1352 – 141059FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 1-phosphatidylinositol binding Source: UniProtKB
    2. calmodulin binding Source: UniProtKB
    3. GTP-dependent protein binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. early endosome to late endosome transport Source: UniProtKB
    2. endocytosis Source: UniProtKB
    3. synaptic vesicle to endosome fusion Source: UniProtKB
    4. vesicle fusion Source: UniProtKB

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_9047. Toll Like Receptor 9 (TLR9) Cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Early endosome antigen 1
    Alternative name(s):
    Endosome-associated protein p162
    Zinc finger FYVE domain-containing protein 2
    Gene namesi
    Name:EEA1
    Synonyms:ZFYVE2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3185. EEA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytoplasmic vesicle Source: Ensembl
    3. cytosol Source: UniProtKB
    4. early endosome Source: UniProtKB
    5. early endosome membrane Source: UniProtKB-SubCell
    6. extracellular vesicular exosome Source: UniProt
    7. extrinsic component of plasma membrane Source: UniProtKB
    8. membrane Source: ProtInc
    9. recycling endosome Source: Ensembl
    10. serine-pyruvate aminotransferase complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391E → A: Strongly reduces interaction with RAB5C. 1 Publication
    Mutagenesisi41 – 411F → A: Strongly reduces interaction with RAB5C. 1 Publication
    Mutagenesisi42 – 421I → A: Strongly reduces interaction with RAB5C. 1 Publication
    Mutagenesisi44 – 441P → A: Strongly reduces interaction with RAB5C. 1 Publication
    Mutagenesisi47 – 471M → A: Strongly reduces interaction with RAB5C. 1 Publication
    Mutagenesisi60 – 601Y → A: Strongly reduces interaction with RAB5C. 1 Publication
    Mutagenesisi1349 – 13491W → A: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1352 – 13521D → V: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1357 – 13571N → D: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1358 – 13581C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1365 – 13651F → A: Strongly reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1367 – 13682VT → EE or GG: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location.
    Mutagenesisi1370 – 13701R → A: Abolishes endosomal location. 1 Publication
    Mutagenesisi1371 – 13711R → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1372 – 13721H → A: Abolishes endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1373. 2 Publications
    Mutagenesisi1373 – 13731H → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1372. 2 Publications
    Mutagenesisi1374 – 13741C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1375 – 13751R → G: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 2 Publications
    Mutagenesisi1377 – 13771C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1378 – 13781G → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1385 – 13851C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication
    Mutagenesisi1400 – 14001R → G: Strongly reduces phosphatidylinositol 3-phosphate binding and abolishes endosomal location. 2 Publications
    Mutagenesisi1405 – 14051C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication

    Organism-specific databases

    PharmGKBiPA27621.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14111411Early endosome antigen 1PRO_0000098706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ15075.
    PaxDbiQ15075.
    PRIDEiQ15075.

    PTM databases

    PhosphoSiteiQ15075.

    Miscellaneous databases

    PMAP-CutDBQ15075.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15075.
    BgeeiQ15075.
    CleanExiHS_EEA1.
    GenevestigatoriQ15075.

    Organism-specific databases

    HPAiCAB005861.
    CAB018782.
    HPA038158.
    HPA038159.

    Interactioni

    Subunit structurei

    Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and RAB22A that have been activated by GTP-binding. Interacts with RAB31. Interacts with ERBB2. May interact with PLEKHF2.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB2P046265EBI-298113,EBI-641062
    RAB22AQ9UL263EBI-298113,EBI-399456
    RAB5AP203394EBI-298113,EBI-399437
    RAB5BP610203EBI-298113,EBI-399401
    SAMD9Q5K6512EBI-298113,EBI-2814750
    Samd9lQ69Z372EBI-298113,EBI-8784283From a different organism.
    Stx6Q636354EBI-298113,EBI-398854From a different organism.

    Protein-protein interaction databases

    BioGridi113999. 20 interactions.
    IntActiQ15075. 37 interactions.
    MINTiMINT-5004646.
    STRINGi9606.ENSP00000317955.

    Structurei

    Secondary structure

    1
    1411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 425
    Turni44 – 463
    Beta strandi49 – 524
    Helixi53 – 6311
    Beta strandi65 – 673
    Helixi1290 – 132435
    Helixi1326 – 134621
    Helixi1352 – 13543
    Turni1359 – 13613
    Beta strandi1367 – 13693
    Beta strandi1371 – 13733
    Turni1375 – 13773
    Beta strandi1380 – 13823
    Helixi1383 – 13853
    Beta strandi1388 – 13903
    Turni1393 – 13964
    Beta strandi1399 – 14013
    Helixi1403 – 14086

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HYINMR-A1347-1411[»]
    1HYJNMR-A1347-1411[»]
    1JOCX-ray2.20A/B1287-1324[»]
    A/B1326-1411[»]
    3MJHX-ray2.03B/D36-69[»]
    ProteinModelPortaliQ15075.
    SMRiQ15075. Positions 36-69, 1289-1411.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15075.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili74 – 13481275Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi397 – 758362Gln/Glu/Lys-richAdd
    BLAST
    Compositional biasi937 – 103296Gln/Glu/Lys-richAdd
    BLAST
    Compositional biasi1093 – 1231139Glu/Lys-richAdd
    BLAST

    Domaini

    The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns3P-enriched membranes is substantially increased in acidic conditions.1 Publication

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
    Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 6424C2H2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1352 – 141059FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000112329.
    HOVERGENiHBG039440.
    InParanoidiQ15075.
    KOiK12478.
    OMAiNANSEAT.
    OrthoDBiEOG754HNM.
    PhylomeDBiQ15075.
    TreeFamiTF329698.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01363. FYVE. 1 hit.
    [Graphical view]
    SMARTiSM00064. FYVE. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS50178. ZF_FYVE. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15075-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL     50
    GSADELFKHY EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK 100
    EEKWYSEELK KELEKYQGLQ QQEAKPDGLV TDSSAELQSL EQQLEEAQTE 150
    NFNIKQMKDL FEQKAAQLAT EIADIKSKYD EERSLREAAE QKVTRLTEEL 200
    NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM TLERERESEK 250
    LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL 300
    TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ 350
    SRLSASETSL HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ 400
    QREEKEQHGL QLQSEINQLH SKLLETERQL GEAHGRLKEQ RQLSSEKLMD 450
    KEQQVADLQL KLSRLEEQLK EKVTNSTELQ HQLDKTKQQH QEQQALQQST 500
    TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS LLEKEREDLY 550
    AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD 600
    QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL 650
    LLSAEAAKTA QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK 700
    QEHCSQLESH LKEYKEKYLS LEQKTEELEG QIKKLEADSL EVKASKEQAL 750
    QDLQQQRQLN TDLELRATEL SKQLEMEKEI VSSTRLDLQK KSEALESIKQ 800
    KLTKQEEEKK ILKQDFETLS QETKIQHEEL NNRIQTTVTE LQKVKMEKEA 850
    LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ 900
    LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN 950
    EKEEQQLQGN INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL 1000
    TQAAQELAAE KEKISVLQNN YEKSQETFKQ LQSDFYGRES ELLATRQDLK 1050
    SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL KTAKATLEQD SAKKEQQLQE 1100
    RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI TKLNEELKSH 1150
    KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV 1200
    KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL 1250
    GTVKKEWQSS QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL 1300
    KGEGEIEKLQ TKVLELQRKL DNTTAAVQEL GRENQSLQIK HTQALNRKWA 1350
    EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI FCAECSAKNA LTPSSKKPVR 1400
    VCDACFNDLQ G 1411
    Length:1,411
    Mass (Da):162,466
    Last modified:May 5, 2009 - v2
    Checksum:i51BA418F561E3411
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551C → S in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti258 – 2592LQ → FE in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti277 – 2771A → S in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti284 – 2841A → R in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti520 – 5201D → E in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti575 – 5762EQ → DE in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti583 – 5842KL → NV in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti680 – 6801Q → H in AAA79121. (PubMed:7768953)Curated
    Sequence conflicti1325 – 13251Missing in AAA79121. (PubMed:7768953)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti810 – 8101K → Q.2 Publications
    Corresponds to variant rs10745623 [ dbSNP | Ensembl ].
    VAR_052980

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40157 mRNA. Translation: AAA79121.1.
    X78998 mRNA. Translation: CAA55632.1.
    AC016136 Genomic DNA. No translation available.
    AC021646 Genomic DNA. No translation available.
    AC026111 Genomic DNA. No translation available.
    CCDSiCCDS31874.1.
    PIRiA57013.
    RefSeqiNP_003557.2. NM_003566.3.
    UniGeneiHs.567367.

    Genome annotation databases

    EnsembliENST00000322349; ENSP00000317955; ENSG00000102189.
    GeneIDi8411.
    KEGGihsa:8411.
    UCSCiuc001tck.3. human.

    Polymorphism databases

    DMDMi229462866.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40157 mRNA. Translation: AAA79121.1 .
    X78998 mRNA. Translation: CAA55632.1 .
    AC016136 Genomic DNA. No translation available.
    AC021646 Genomic DNA. No translation available.
    AC026111 Genomic DNA. No translation available.
    CCDSi CCDS31874.1.
    PIRi A57013.
    RefSeqi NP_003557.2. NM_003566.3.
    UniGenei Hs.567367.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HYI NMR - A 1347-1411 [» ]
    1HYJ NMR - A 1347-1411 [» ]
    1JOC X-ray 2.20 A/B 1287-1324 [» ]
    A/B 1326-1411 [» ]
    3MJH X-ray 2.03 B/D 36-69 [» ]
    ProteinModelPortali Q15075.
    SMRi Q15075. Positions 36-69, 1289-1411.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113999. 20 interactions.
    IntActi Q15075. 37 interactions.
    MINTi MINT-5004646.
    STRINGi 9606.ENSP00000317955.

    PTM databases

    PhosphoSitei Q15075.

    Polymorphism databases

    DMDMi 229462866.

    Proteomic databases

    MaxQBi Q15075.
    PaxDbi Q15075.
    PRIDEi Q15075.

    Protocols and materials databases

    DNASUi 8411.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322349 ; ENSP00000317955 ; ENSG00000102189 .
    GeneIDi 8411.
    KEGGi hsa:8411.
    UCSCi uc001tck.3. human.

    Organism-specific databases

    CTDi 8411.
    GeneCardsi GC12M093102.
    HGNCi HGNC:3185. EEA1.
    HPAi CAB005861.
    CAB018782.
    HPA038158.
    HPA038159.
    MIMi 605070. gene.
    neXtProti NX_Q15075.
    PharmGKBi PA27621.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000112329.
    HOVERGENi HBG039440.
    InParanoidi Q15075.
    KOi K12478.
    OMAi NANSEAT.
    OrthoDBi EOG754HNM.
    PhylomeDBi Q15075.
    TreeFami TF329698.

    Enzyme and pathway databases

    Reactomei REACT_9047. Toll Like Receptor 9 (TLR9) Cascade.

    Miscellaneous databases

    ChiTaRSi EEA1. human.
    EvolutionaryTracei Q15075.
    GeneWikii EEA1.
    GenomeRNAii 8411.
    NextBioi 31490.
    PMAP-CutDB Q15075.
    PROi Q15075.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15075.
    Bgeei Q15075.
    CleanExi HS_EEA1.
    Genevestigatori Q15075.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01363. FYVE. 1 hit.
    [Graphical view ]
    SMARTi SM00064. FYVE. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS50178. ZF_FYVE. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine 'fingers' and contains a calmodulin-binding IQ motif."
      Mu F.-T., Callaghan J.M., Steele-Mortimer O., Stenmark H., Parton R.G., Campbell P.L., McCluskey J., Yeo J.-P., Tock E.P.C., Toh B.-H.
      J. Biol. Chem. 270:13503-13511(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, VARIANT GLN-810.
      Tissue: Cervix carcinoma.
    2. Seelig H.P.
      Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-810.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 996-1011 AND 1319-1332, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    5. Cited for: INTERACTION WITH RAB5A.
    6. Cited for: INTERACTION WITH RAB5A AND RAB5B.
    7. "The Rab5 effector EEA1 interacts directly with syntaxin-6."
      Simonsen A., Gaullier J.-M., D'Arrigo A., Stenmark H.
      J. Biol. Chem. 274:28857-28860(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STX6, SUBCELLULAR LOCATION.
    8. "Phosphatidylinositol 3-phosphate recognition by the FYVE domain."
      Kutateladze T.G., Ogburn K.D., Watson W.T., de Beer T., Emr S.D., Burd C.G., Overduin M.
      Mol. Cell 3:805-811(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-1352; ASN-1357; 1367-VAL-THR-1368; ARG-1375 AND ARG-1400, HOMODIMERIZATION, INTERACTION WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
    9. "Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes. Role of conserved residues."
      Gaullier J.-M., Roenning E., Gillooly D.J., Stenmark H.
      J. Biol. Chem. 275:24595-24600(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-1349; CYS-1358; PHE-1365; ARG-1370; ARG-1371; HIS-1372; HIS-1373; CYS-1374; ARG-1375; CYS-1377; GLY-1378; CYS-1385; ARG-1400 AND CYS-1405, SUBCELLULAR LOCATION, INTERACTION WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
    10. "The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking."
      Kauppi M., Simonsen A., Bremnes B., Vieira A., Callaghan J.M., Stenmark H., Olkkonen V.M.
      J. Cell Sci. 115:899-911(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB22A.
    11. "Determinants of Rab5 interaction with the N-terminus of early endosome antigen 1."
      Merithew E., Stone C., Eathiraj S., Lambright D.G.
      J. Biol. Chem. 278:8494-8500(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-39; PHE-41; ILE-42; PRO-44; MET-47 AND TYR-60, HOMODIMERIZATION, INTERACTION WITH RAB5C.
    12. "Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor."
      Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.
      Mol. Cell. Biol. 25:11005-11018(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB2.
    13. "Rab22B is expressed in the CNS astroglia lineage and plays a role in epidermal growth factor receptor trafficking in A431 cells."
      Ng E.L., Ng J.J., Liang F., Tang B.L.
      J. Cell. Physiol. 221:716-728(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RAB31.
    14. Cited for: DOMAIN FYVE-TYPE ZINC-FINGER, MUTAGENESIS OF HIS-1372 AND HIS-1373.
    15. "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 SER-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The PtdIns3P-binding protein Phafin 2 mediates epidermal growth factor receptor degradation by promoting endosome fusion."
      Pedersen N.M., Raiborg C., Brech A., Skarpen E., Roxrud I., Platta H.W., Liestol K., Stenmark H.
      Traffic 13:1547-1563(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PLEKHF2, SUBCELLULAR LOCATION.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1289-1411 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE, HOMODIMERIZATION.
    19. "Structural mechanism of endosome docking by the FYVE domain."
      Kutateladze T.G., Overduin M.
      Science 291:1793-1796(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1346-1410 ALONE AND IN COMPLEX WITH PHOSPHATIDYLINOSITOL 3-PHOSPHATE.

    Entry informationi

    Entry nameiEEA1_HUMAN
    AccessioniPrimary (citable) accession number: Q15075
    Secondary accession number(s): Q14221
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 126 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

    Miscellaneous

    Antibodies against EEA1 are found in sera from patients with subacute cutaneous lupus erythematosus and other autoimmune diseases.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3