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Q15075 (EEA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Early endosome antigen 1
Alternative name(s):
Endosome-associated protein p162
Zinc finger FYVE domain-containing protein 2
Gene names
Name:EEA1
Synonyms:ZFYVE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1411 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.17 Ref.18

Subcellular location

Cytoplasm. Early endosome membrane; Peripheral membrane protein Ref.1 Ref.7 Ref.9 Ref.13 Ref.17.

Domain

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. Ref.14

Miscellaneous

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

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 FYVE-type zinc finger.

Ontologies

Keywords
   Cellular componentCytoplasm
Endosome
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processearly endosome to late endosome transport

Non-traceable author statement Ref.1. Source: UniProtKB

endocytosis

Inferred from mutant phenotype PubMed 21081650. Source: UniProtKB

synaptic vesicle to endosome fusion

Traceable author statement Ref.18. Source: UniProtKB

vesicle fusion

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay Ref.1. Source: UniProtKB

early endosome

Inferred from direct assay Ref.18PubMed 15792797PubMed 15880641. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

extrinsic component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

membrane

Traceable author statement Ref.1. Source: ProtInc

recycling endosome

Inferred from electronic annotation. Source: Ensembl

serine-pyruvate aminotransferase complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_function1-phosphatidylinositol binding

Inferred from direct assay PubMed 11256955. Source: UniProtKB

GTP-dependent protein binding

Inferred from direct assay Ref.6. Source: UniProtKB

calmodulin binding

Non-traceable author statement Ref.18. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6Ref.7Ref.10Ref.5. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.18. Source: UniProtKB

zinc ion binding

Traceable author statement Ref.18. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14111411Early endosome antigen 1
PRO_0000098706

Regions

Zinc finger41 – 6424C2H2-type
Zinc finger1352 – 141059FYVE-type
Coiled coil74 – 13481275 Potential
Compositional bias397 – 758362Gln/Glu/Lys-rich
Compositional bias937 – 103296Gln/Glu/Lys-rich
Compositional bias1093 – 1231139Glu/Lys-rich

Amino acid modifications

Modified residue701Phosphoserine Ref.15

Natural variations

Natural variant8101K → Q. Ref.1 Ref.2
Corresponds to variant rs10745623 [ dbSNP | Ensembl ].
VAR_052980

Experimental info

Mutagenesis391E → A: Strongly reduces interaction with RAB5C. Ref.11
Mutagenesis411F → A: Strongly reduces interaction with RAB5C. Ref.11
Mutagenesis421I → A: Strongly reduces interaction with RAB5C. Ref.11
Mutagenesis441P → A: Strongly reduces interaction with RAB5C. Ref.11
Mutagenesis471M → A: Strongly reduces interaction with RAB5C. Ref.11
Mutagenesis601Y → A: Strongly reduces interaction with RAB5C. Ref.11
Mutagenesis13491W → A: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis13521D → V: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.8
Mutagenesis13571N → D: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.8
Mutagenesis13581C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis13651F → A: Strongly reduces phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis1367 – 13682VT → EE or GG: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location.
Mutagenesis13701R → A: Abolishes endosomal location. Ref.9
Mutagenesis13711R → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis13721H → A: Abolishes endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1373. Ref.9 Ref.14
Mutagenesis13731H → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1372. Ref.9 Ref.14
Mutagenesis13741C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis13751R → G: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.8 Ref.9
Mutagenesis13771C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis13781G → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis13851C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Mutagenesis14001R → G: Strongly reduces phosphatidylinositol 3-phosphate binding and abolishes endosomal location. Ref.8 Ref.9
Mutagenesis14051C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. Ref.9
Sequence conflict2551C → S in AAA79121. Ref.1
Sequence conflict258 – 2592LQ → FE in AAA79121. Ref.1
Sequence conflict2771A → S in AAA79121. Ref.1
Sequence conflict2841A → R in AAA79121. Ref.1
Sequence conflict5201D → E in AAA79121. Ref.1
Sequence conflict575 – 5762EQ → DE in AAA79121. Ref.1
Sequence conflict583 – 5842KL → NV in AAA79121. Ref.1
Sequence conflict6801Q → H in AAA79121. Ref.1
Sequence conflict13251Missing in AAA79121. Ref.1

Secondary structure

................................... 1411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15075 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 51BA418F561E3411

FASTA1,411162,466
        10         20         30         40         50         60 
MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY 

        70         80         90        100        110        120 
EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ 

       130        140        150        160        170        180 
QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD 

       190        200        210        220        230        240 
EERSLREAAE QKVTRLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM 

       250        260        270        280        290        300 
TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL 

       310        320        330        340        350        360 
TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ SRLSASETSL 

       370        380        390        400        410        420 
HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ QREEKEQHGL QLQSEINQLH 

       430        440        450        460        470        480 
SKLLETERQL GEAHGRLKEQ RQLSSEKLMD KEQQVADLQL KLSRLEEQLK EKVTNSTELQ 

       490        500        510        520        530        540 
HQLDKTKQQH QEQQALQQST TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS 

       550        560        570        580        590        600 
LLEKEREDLY AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD 

       610        620        630        640        650        660 
QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKTA 

       670        680        690        700        710        720 
QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK QEHCSQLESH LKEYKEKYLS 

       730        740        750        760        770        780 
LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI 

       790        800        810        820        830        840 
VSSTRLDLQK KSEALESIKQ KLTKQEEEKK ILKQDFETLS QETKIQHEEL NNRIQTTVTE 

       850        860        870        880        890        900 
LQKVKMEKEA LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ 

       910        920        930        940        950        960 
LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN EKEEQQLQGN 

       970        980        990       1000       1010       1020 
INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN 

      1030       1040       1050       1060       1070       1080 
YEKSQETFKQ LQSDFYGRES ELLATRQDLK SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL 

      1090       1100       1110       1120       1130       1140 
KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI 

      1150       1160       1170       1180       1190       1200 
TKLNEELKSH KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV 

      1210       1220       1230       1240       1250       1260 
KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL GTVKKEWQSS 

      1270       1280       1290       1300       1310       1320 
QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKVLELQRKL 

      1330       1340       1350       1360       1370       1380 
DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI 

      1390       1400       1410 
FCAECSAKNA LTPSSKKPVR VCDACFNDLQ G 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"EEA1 links PI(3)K function to Rab5 regulation of endosome fusion."
Simonsen A., Lippe R., Christoforidis S., Gaullier J.-M., Brech A., Callaghan J.M., Toh B.-H., Murphy C., Zerial M., Stenmark H.
Nature 394:494-498(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB5A.
[6]"Direct interaction of EEA1 with Rab5b."
Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.
Eur. J. Biochem. 265:361-366(1999) [PubMed] [Europe PMC] [Abstract]
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]"Membrane insertion of the FYVE domain is modulated by pH."
He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G., Kutateladze A.G., Verkhusha V.V., Stahelin R.V., Kutateladze T.G.
Proteins 76:852-860(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Multivalent endosome targeting by homodimeric EEA1."
Dumas J.J., Merithew E., Sudharshan E., Rajamani D., Hayes S., Lawe D., Corvera S., Lambright D.G.
Mol. Cell 8:947-958(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31874.1.
PIRA57013.
RefSeqNP_003557.2. NM_003566.3.
UniGeneHs.567367.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYINMR-A1347-1411[»]
1HYJNMR-A1347-1411[»]
1JOCX-ray2.20A/B1287-1324[»]
A/B1326-1411[»]
3MJHX-ray2.03B/D36-69[»]
ProteinModelPortalQ15075.
SMRQ15075. Positions 36-69, 1289-1411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113999. 20 interactions.
IntActQ15075. 33 interactions.
MINTMINT-5004646.
STRING9606.ENSP00000317955.

PTM databases

PhosphoSiteQ15075.

Polymorphism databases

DMDM229462866.

Proteomic databases

MaxQBQ15075.
PaxDbQ15075.
PRIDEQ15075.

Protocols and materials databases

DNASU8411.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322349; ENSP00000317955; ENSG00000102189.
GeneID8411.
KEGGhsa:8411.
UCSCuc001tck.3. human.

Organism-specific databases

CTD8411.
GeneCardsGC12M093102.
HGNCHGNC:3185. EEA1.
HPACAB005861.
CAB018782.
HPA038158.
HPA038159.
MIM605070. gene.
neXtProtNX_Q15075.
PharmGKBPA27621.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000112329.
HOVERGENHBG039440.
InParanoidQ15075.
KOK12478.
OMANANSEAT.
OrthoDBEOG754HNM.
PhylomeDBQ15075.
TreeFamTF329698.

Gene expression databases

ArrayExpressQ15075.
BgeeQ15075.
CleanExHS_EEA1.
GenevestigatorQ15075.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01363. FYVE. 1 hit.
[Graphical view]
SMARTSM00064. FYVE. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS50178. ZF_FYVE. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEEA1. human.
EvolutionaryTraceQ15075.
GeneWikiEEA1.
GenomeRNAi8411.
NextBio31490.
PMAP-CutDBQ15075.
PROQ15075.
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Entry information

Entry nameEEA1_HUMAN
AccessionPrimary (citable) accession number: Q15075
Secondary accession number(s): Q14221
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM