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Q15075

- EEA1_HUMAN

UniProt

Q15075 - EEA1_HUMAN

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Protein

Early endosome antigen 1

Gene

EEA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 homodimerization activity Source: UniProtKB
  5. 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
Complete GO annotation...

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. axonal spine Source: Ensembl
  2. cytoplasm Source: ProtInc
  3. cytoplasmic vesicle Source: Ensembl
  4. cytosol Source: UniProtKB
  5. early endosome Source: UniProtKB
  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
Complete GO annotation...

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. 1 Publication
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

BgeeiQ15075.
CleanExiHS_EEA1.
ExpressionAtlasiQ15075. baseline and differential.
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. 22 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.
GeneTreeiENSGT00730000110715.
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

        10         20         30         40         50
MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL
60 70 80 90 100
GSADELFKHY EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK
110 120 130 140 150
EEKWYSEELK KELEKYQGLQ QQEAKPDGLV TDSSAELQSL EQQLEEAQTE
160 170 180 190 200
NFNIKQMKDL FEQKAAQLAT EIADIKSKYD EERSLREAAE QKVTRLTEEL
210 220 230 240 250
NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM TLERERESEK
260 270 280 290 300
LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL
310 320 330 340 350
TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ
360 370 380 390 400
SRLSASETSL HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ
410 420 430 440 450
QREEKEQHGL QLQSEINQLH SKLLETERQL GEAHGRLKEQ RQLSSEKLMD
460 470 480 490 500
KEQQVADLQL KLSRLEEQLK EKVTNSTELQ HQLDKTKQQH QEQQALQQST
510 520 530 540 550
TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS LLEKEREDLY
560 570 580 590 600
AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD
610 620 630 640 650
QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL
660 670 680 690 700
LLSAEAAKTA QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK
710 720 730 740 750
QEHCSQLESH LKEYKEKYLS LEQKTEELEG QIKKLEADSL EVKASKEQAL
760 770 780 790 800
QDLQQQRQLN TDLELRATEL SKQLEMEKEI VSSTRLDLQK KSEALESIKQ
810 820 830 840 850
KLTKQEEEKK ILKQDFETLS QETKIQHEEL NNRIQTTVTE LQKVKMEKEA
860 870 880 890 900
LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ
910 920 930 940 950
LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN
960 970 980 990 1000
EKEEQQLQGN INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL
1010 1020 1030 1040 1050
TQAAQELAAE KEKISVLQNN YEKSQETFKQ LQSDFYGRES ELLATRQDLK
1060 1070 1080 1090 1100
SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL KTAKATLEQD SAKKEQQLQE
1110 1120 1130 1140 1150
RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI TKLNEELKSH
1160 1170 1180 1190 1200
KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV
1210 1220 1230 1240 1250
KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL
1260 1270 1280 1290 1300
GTVKKEWQSS QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL
1310 1320 1330 1340 1350
KGEGEIEKLQ TKVLELQRKL DNTTAAVQEL GRENQSLQIK HTQALNRKWA
1360 1370 1380 1390 1400
EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI FCAECSAKNA LTPSSKKPVR
1410
VCDACFNDLQ G
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. 22 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.
GeneTreei ENSGT00730000110715.
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

Bgeei Q15075.
CleanExi HS_EEA1.
ExpressionAtlasi Q15075. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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