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Q8BL66

- EEA1_MOUSE

UniProt

Q8BL66 - EEA1_MOUSE

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Protein

Early endosome antigen 1

Gene

Eea1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

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. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. endocytosis Source: UniProtKB
  2. vesicle fusion Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Early endosome antigen 1
Gene namesi
Name:Eea1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:2442192. Eea1.

Subcellular locationi

Cytoplasm By similarity. Early endosome membrane By similarity; Peripheral membrane protein By similarity

GO - Cellular componenti

  1. axonal spine Source: MGI
  2. cytoplasmic vesicle Source: MGI
  3. cytosol Source: UniProtKB
  4. early endosome Source: UniProtKB
  5. endosome Source: MGI
  6. extracellular vesicular exosome Source: Ensembl
  7. extrinsic component of plasma membrane Source: UniProtKB
  8. recycling endosome Source: Ensembl
  9. serine-pyruvate aminotransferase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14111411Early endosome antigen 1PRO_0000098707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8BL66.
PaxDbiQ8BL66.
PRIDEiQ8BL66.

2D gel databases

REPRODUCTION-2DPAGEIPI00453776.

PTM databases

PhosphoSiteiQ8BL66.

Expressioni

Gene expression databases

BgeeiQ8BL66.
CleanExiMM_EEA1.
GenevestigatoriQ8BL66.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi229728. 3 interactions.
IntActiQ8BL66. 11 interactions.
MINTiMINT-1865447.

Structurei

3D structure databases

ProteinModelPortaliQ8BL66.
SMRiQ8BL66. Positions 36-69, 1289-1411.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili78 – 13481271Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi396 – 706311Gln/Glu/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 (By similarity).By similarity

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.
InParanoidiQ8BL66.
KOiK12478.
OMAiKHYEVVH.
OrthoDBiEOG754HNM.
PhylomeDBiQ8BL66.
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.

Q8BL66-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL
60 70 80 90 100
GSADELFKHY QAVHDAGNDS GHGGEAGLAL TRDDITLLRQ EVQDLQASLK
110 120 130 140 150
EEKWYSEELK KELEKYQGLQ QQEAKSDGLV TDSSAELQAL EQQLEEAQTE
160 170 180 190 200
NFNIKQMKDL FEQKAAQLAT EIADIKSKYD EEKSLRAAAE QKVTHLTEDL
210 220 230 240 250
NKQTTVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM TLERERESEK
260 270 280 290 300
LKDECKKLQS EHAHLEATIN QLRSELAKGP QEVAVYVQEI QKLKGSINEL
310 320 330 340 350
TQKNQNLTEK LQKKDLDYTH LEEKHNEESA SRKTLQASLH QRDLDCQQLQ
360 370 380 390 400
ARLTASESSL QRAQGELSEK AEAAQKLREE LREVESTRQH LKVEVKQLQQ
410 420 430 440 450
QREEKEQHGL QLQGEVSQLH CKLLETERQL GEAHGRLKEQ RQLSSEKLME
460 470 480 490 500
KEQQVADLQL KLSRLEEQLK EKVTNSTELQ HQLEKSKQQH QEQQALQQSA
510 520 530 540 550
TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKGKESVS LLEKEREDLY
560 570 580 590 600
AKIQAGEGET AVLNQLQEKN HALQQQLTQL TEKLKNQSES HKQAEENLHD
610 620 630 640 650
QVQEQKAHLR AAQDRVLSLE TSVSELSSQL NESKEKVSQL DIQIKAKTEL
660 670 680 690 700
LLSAEAAKAA QRADLQNHLD TAQHALQDKQ QELNKVSVQL DQLTAKFQEK
710 720 730 740 750
QEHCIQLESH LKDHKEKHLS LEQKVEDLEG HIKKLEADAL EVKASKEQAL
760 770 780 790 800
QSLQQQRQLS TDLELRNAEL SRELQEQEEV VSCTKLDLQN KSEILENIKQ
810 820 830 840 850
TLTKKEEENV VLKQEFEKLS QDSKTQHKEL GDRMQAAVTE LTAVKAQKDA
860 870 880 890 900
LLAELSTTKE KLSKVSDSLK NSKSEFEKEN QKGKAAVLDL EKACKELKHQ
910 920 930 940 950
LQVQAESALK EQEDLKKSLE KEKETSQQLK IELNSVKGEV SQAQNTLKQK
960 970 980 990 1000
EKDEQQLQGT INQLKQSAEQ KKKQIEALQG EVKNAVSQKT VLENKLQQQS
1010 1020 1030 1040 1050
SQAAQELAAE KGKLSALQSN YEKCQADLKQ LQSDLYGKES ELLATRQDLK
1060 1070 1080 1090 1100
SVEEKLTLAQ EDLISNRNQI GNQNKSIQEL QAAKASLEQD SAKKEALLKE
1110 1120 1130 1140 1150
QSKALEDAQR EKSVKEKELV AEKSKLAEME EIKCRQEKEI TKLNEELKSH
1160 1170 1180 1190 1200
KQESIKEITN LKDAKQLLIQ QKLELQGRVD SLKAALEQEK ESQQLMREQV
1210 1220 1230 1240 1250
KKEEEKRKEE FSEKEAKLHS EIKEKEAGMK KHEENEAKLT MQVTTLNENL
1260 1270 1280 1290 1300
GTVKKEWQSS QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL
1310 1320 1330 1340 1350
KGEGEIEKLQ TKALELQRKL DNTTAAVQEL GRENQSLQIK HTQALNRKWA
1360 1370 1380 1390 1400
EDNEVQNCMS CGKCFSVTVR RHHCRQCGNI FCAECSTKNA LTPSSKKPVR
1410
VCDACFNDLQ G
Length:1,411
Mass (Da):160,915
Last modified:September 27, 2005 - v2
Checksum:i2365A51EF92019FD
GO

Sequence cautioni

The sequence BAC32647.1 differs from that shown. Reason: Erroneous termination at position 105. Translated as Tyr.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251V → I in BAC32647. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC075637 mRNA. Translation: AAH75637.1.
AK046231 mRNA. Translation: BAC32647.1. Sequence problems.
CCDSiCCDS36042.1.
RefSeqiNP_001001932.1. NM_001001932.3.
UniGeneiMm.210035.
Mm.490373.

Genome annotation databases

EnsembliENSMUST00000053484; ENSMUSP00000061493; ENSMUSG00000036499.
GeneIDi216238.
KEGGimmu:216238.
UCSCiuc007gwu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC075637 mRNA. Translation: AAH75637.1 .
AK046231 mRNA. Translation: BAC32647.1 . Sequence problems.
CCDSi CCDS36042.1.
RefSeqi NP_001001932.1. NM_001001932.3.
UniGenei Mm.210035.
Mm.490373.

3D structure databases

ProteinModelPortali Q8BL66.
SMRi Q8BL66. Positions 36-69, 1289-1411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229728. 3 interactions.
IntActi Q8BL66. 11 interactions.
MINTi MINT-1865447.

PTM databases

PhosphoSitei Q8BL66.

2D gel databases

REPRODUCTION-2DPAGE IPI00453776.

Proteomic databases

MaxQBi Q8BL66.
PaxDbi Q8BL66.
PRIDEi Q8BL66.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000053484 ; ENSMUSP00000061493 ; ENSMUSG00000036499 .
GeneIDi 216238.
KEGGi mmu:216238.
UCSCi uc007gwu.1. mouse.

Organism-specific databases

CTDi 8411.
MGIi MGI:2442192. Eea1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000110715.
HOGENOMi HOG000112329.
HOVERGENi HBG039440.
InParanoidi Q8BL66.
KOi K12478.
OMAi KHYEVVH.
OrthoDBi EOG754HNM.
PhylomeDBi Q8BL66.
TreeFami TF329698.

Miscellaneous databases

NextBioi 375093.
PROi Q8BL66.
SOURCEi Search...

Gene expression databases

Bgeei Q8BL66.
CleanExi MM_EEA1.
Genevestigatori Q8BL66.

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. "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].
    Strain: C57BL/6.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-946.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RAB31.

Entry informationi

Entry nameiEEA1_MOUSE
AccessioniPrimary (citable) accession number: Q8BL66
Secondary accession number(s): Q6DIC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: September 27, 2005
Last modified: October 29, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3