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Protein

Early endosome antigen 1

Gene

EEA1

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

Functioni

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

Miscellaneous

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 64C2H2-typePROSITE-ProRule annotationAdd BLAST24
Zinc fingeri1352 – 1410FYVE-typePROSITE-ProRule annotationAdd BLAST59

GO - Molecular functioni

  • 1-phosphatidylinositol binding Source: UniProtKB
  • calmodulin binding Source: UniProtKB
  • GTP-dependent protein binding Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • protein homodimerization activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • early endosome to late endosome transport Source: UniProtKB
  • endocytosis Source: UniProtKB
  • synaptic vesicle to endosome fusion Source: UniProtKB
  • vesicle fusion Source: UniProtKB
  • viral RNA genome replication Source: ParkinsonsUK-UCL

Keywordsi

LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-168138 Toll Like Receptor 9 (TLR9) Cascade
SIGNORiQ15075

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000102189.16
HGNCiHGNC:3185 EEA1
MIMi605070 gene
neXtProtiNX_Q15075

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39E → A: Strongly reduces interaction with RAB5C. 1 Publication1
Mutagenesisi41F → A: Strongly reduces interaction with RAB5C. 1 Publication1
Mutagenesisi42I → A: Strongly reduces interaction with RAB5C. 1 Publication1
Mutagenesisi44P → A: Strongly reduces interaction with RAB5C. 1 Publication1
Mutagenesisi47M → A: Strongly reduces interaction with RAB5C. 1 Publication1
Mutagenesisi60Y → A: Strongly reduces interaction with RAB5C. 1 Publication1
Mutagenesisi1349W → A: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1352D → V: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1357N → D: Reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1358C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1365F → A: Strongly reduces phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1367 – 1368VT → EE or GG: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication2
Mutagenesisi1370R → A: Abolishes endosomal location. 1 Publication1
Mutagenesisi1371R → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1372H → A: Abolishes endosomal location. Abolishes pH sensitivity of the FYVE-type zinc finger domain; when associated with A-1373. 2 Publications1
Mutagenesisi1373H → 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 Publications1
Mutagenesisi1374C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1375R → G: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 2 Publications1
Mutagenesisi1377C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1378G → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1385C → A: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1
Mutagenesisi1400R → G: Strongly reduces phosphatidylinositol 3-phosphate binding and abolishes endosomal location. 2 Publications1
Mutagenesisi1405C → S: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location. 1 Publication1

Organism-specific databases

DisGeNETi8411
OpenTargetsiENSG00000102189
PharmGKBiPA27621

Polymorphism and mutation databases

BioMutaiEEA1
DMDMi229462866

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000987061 – 1411Early endosome antigen 1Add BLAST1411

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei52PhosphoserineCombined sources1
Modified residuei70PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15075
MaxQBiQ15075
PaxDbiQ15075
PeptideAtlasiQ15075
PRIDEiQ15075

PTM databases

iPTMnetiQ15075
PhosphoSitePlusiQ15075
SwissPalmiQ15075

Miscellaneous databases

PMAP-CutDBiQ15075

Expressioni

Gene expression databases

BgeeiENSG00000102189
CleanExiHS_EEA1
ExpressionAtlasiQ15075 baseline and differential
GenevisibleiQ15075 HS

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. Interacts with SAMD9 AND SAMD9L (PubMed:24029230). May interact with PLEKHF2.13 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • GTP-dependent protein binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi113999, 44 interactors
CORUMiQ15075
IntActiQ15075, 89 interactors
MINTiQ15075
STRINGi9606.ENSP00000317955

Structurei

Secondary structure

11411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 42Combined sources5
Turni44 – 46Combined sources3
Beta strandi49 – 52Combined sources4
Helixi53 – 63Combined sources11
Beta strandi65 – 67Combined sources3
Helixi1290 – 1324Combined sources35
Helixi1326 – 1346Combined sources21
Helixi1352 – 1354Combined sources3
Turni1359 – 1361Combined sources3
Beta strandi1367 – 1369Combined sources3
Beta strandi1371 – 1373Combined sources3
Turni1375 – 1377Combined sources3
Beta strandi1380 – 1382Combined sources3
Helixi1383 – 1385Combined sources3
Beta strandi1388 – 1390Combined sources3
Turni1393 – 1396Combined sources4
Beta strandi1399 – 1401Combined sources3
Helixi1403 – 1408Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HYINMR-A1347-1411[»]
1HYJNMR-A1347-1411[»]
1JOCX-ray2.20A/B1287-1324[»]
A/B1326-1411[»]
3MJHX-ray2.03B/D36-69[»]
ProteinModelPortaliQ15075
SMRiQ15075
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15075

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili74 – 1348Sequence analysisAdd BLAST1275

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi397 – 758Gln/Glu/Lys-richAdd BLAST362
Compositional biasi937 – 1032Gln/Glu/Lys-richAdd BLAST96
Compositional biasi1093 – 1231Glu/Lys-richAdd BLAST139

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 64C2H2-typePROSITE-ProRule annotationAdd BLAST24
Zinc fingeri1352 – 1410FYVE-typePROSITE-ProRule annotationAdd BLAST59

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFA7 Eukaryota
ENOG4111F3Q LUCA
GeneTreeiENSGT00910000144126
HOGENOMiHOG000112329
HOVERGENiHBG039440
InParanoidiQ15075
KOiK12478
OMAiLEDCPED
OrthoDBiEOG091G01M6
PhylomeDBiQ15075
TreeFamiTF329698

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR013087 Znf_C2H2_type
IPR000306 Znf_FYVE
IPR017455 Znf_FYVE-rel
IPR011011 Znf_FYVE_PHD
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF01363 FYVE, 1 hit
SMARTiView protein in SMART
SM00064 FYVE, 1 hit
SUPFAMiSSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50178 ZF_FYVE, 1 hit
PS00028 ZINC_FINGER_C2H2_1, 1 hit
PS50157 ZINC_FINGER_C2H2_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti255C → S in AAA79121 (PubMed:7768953).Curated1
Sequence conflicti258 – 259LQ → FE in AAA79121 (PubMed:7768953).Curated2
Sequence conflicti277A → S in AAA79121 (PubMed:7768953).Curated1
Sequence conflicti284A → R in AAA79121 (PubMed:7768953).Curated1
Sequence conflicti520D → E in AAA79121 (PubMed:7768953).Curated1
Sequence conflicti575 – 576EQ → DE in AAA79121 (PubMed:7768953).Curated2
Sequence conflicti583 – 584KL → NV in AAA79121 (PubMed:7768953).Curated2
Sequence conflicti680Q → H in AAA79121 (PubMed:7768953).Curated1
Sequence conflicti1325Missing in AAA79121 (PubMed:7768953).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052980810K → Q2 PublicationsCorresponds to variant dbSNP:rs10745623Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiEEA1_HUMAN
AccessioniPrimary (citable) accession number: Q15075
Secondary accession number(s): Q14221
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: May 5, 2009
Last modified: May 23, 2018
This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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