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Protein

EH domain-containing protein 3

Gene

Ehd3

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

Functioni

ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes tubulation of endocytic membranes (By similarity). Binding to phosphatidic acid induces its membrane tubulation activity (PubMed:26896729). Plays a role in endocytic transport. Involved in early endosome to recycling endosome compartment (ERC), retrograde early endosome to Golgi, and endosome to plasma membrane (rapid recycling) protein transport. Involved in the regulation of Golgi maintenance and morphology (By similarity). Involved in the recycling of internalized D1 dopamine receptor (By similarity). Plays a role in cardiac protein trafficking probably implicating ANK2. Involved in the ventricular membrane targeting of SLC8A1 and CACNA1C and probably the atrial membrane localization of CACNA1GG and CACNA1H implicated in the regulation of atrial myocyte exitability and cardiac conduction (PubMed:20489164, PubMed:24759929, PubMed:25825486). In conjunction with EHD4 may be involved in endocytic trafficking of KDR/VEGFR2 implicated in control of glomerular function (PubMed:21408024). Involved in the rapid recycling of integrin beta-3 implicated in cell adhesion maintenance (By similarity). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing. Plays a role in the formation of the ciliary vesicle, an early step in cilium biogenesis; possibly sharing redundant functions with Ehd1 (PubMed:25686250).By similarity7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei220 – 2201ATPBy similarity
Binding sitei258 – 2581ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 728ATPBy similarity
Calcium bindingi489 – 50012PROSITE-ProRule annotationBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cilium assembly Source: UniProtKB
  • endocytic recycling Source: UniProtKB
  • positive regulation of voltage-gated calcium channel activity Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein targeting to plasma membrane Source: MGI
  • regulation of cardiac conduction Source: UniProtKB
  • regulation of cardiac muscle cell membrane potential Source: MGI
  • regulation of cardiac muscle contraction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Lipid-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
EH domain-containing protein 3Curated
Gene namesi
Name:Ehd3Imported
Synonyms:Ehd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1928900. Ehd3.

Subcellular locationi

GO - Cellular componenti

  • ciliary pocket membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • endocytic vesicle Source: MGI
  • focal adhesion Source: MGI
  • myelin sheath Source: UniProtKB
  • perinuclear region of cytoplasm Source: MGI
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi327 – 3271K → D: Loss of localization to membranes, reduced binding to phosphatidic acid. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 535535EH domain-containing protein 3PRO_0000146113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Cross-linki315 – 315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei456 – 4561PhosphoserineCombined sources
Cross-linki511 – 511Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9QXY6.
MaxQBiQ9QXY6.
PaxDbiQ9QXY6.
PRIDEiQ9QXY6.

PTM databases

iPTMnetiQ9QXY6.
PhosphoSiteiQ9QXY6.

Expressioni

Tissue specificityi

Strong expression seen in the kidney, brain and liver. In the kidney, expressed exclusively by glomerular endothelial cells; at protein level. Expressed in skeletal muscle neuromuscular junction perisynaptic region; at protein level.3 Publications

Gene expression databases

BgeeiQ9QXY6.
CleanExiMM_EHD2.
MM_EHD3.
GenevisibleiQ9QXY6. MM.

Interactioni

Subunit structurei

Homooligomer. Heterooligomer with EHD1 (PubMed:12121420). Heterooligomer with EHD2 and EHD4; ATP-binding is required for heterooligomerization (By similarity). Interacts with PACSIN1 (PubMed:15930129). Interacts with PACSIN2 (PubMed:15930129). Interacts (via EH domain) with MICALL1 (By similarity). Interacts (via EH domain) with RAB11FIP2 (By similarity). Interacts with ANK2 (By similarity). Interacts with CACNA1GG and CACNA1H (PubMed:25825486).By similarity3 Publications

Protein-protein interaction databases

BioGridi208297. 2 interactions.
IntActiQ9QXY6. 5 interactions.
MINTiMINT-1865434.
STRINGi10090.ENSMUSP00000024860.

Structurei

3D structure databases

ProteinModelPortaliQ9QXY6.
SMRiQ9QXY6. Positions 1-532.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 286232Dynamin-type GAdd
BLAST
Domaini444 – 53289EHPROSITE-ProRule annotationAdd
BLAST
Domaini476 – 51136EF-handPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili198 – 22730Sequence analysisAdd
BLAST

Domaini

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.By similarity

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 1 EH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ9QXY6.
KOiK12476.
OMAiCSTVASP.
OrthoDBiEOG757CX9.
PhylomeDBiQ9QXY6.
TreeFamiTF314429.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR022812. Dynamin_SF.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR029951. EHD1/EHD3.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF67. PTHR11216:SF67. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF12763. EF-hand_4. 1 hit.
PF16880. EHD_N. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSWLGNDDR RKKDPEVFQT VSDGLKKLYK TKLLPLEEYY RFHEFHSPAL
60 70 80 90 100
EDADFDNKPM VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV
110 120 130 140 150
MQGDVEGIIP GNALVVDPKK PFRKLNAFGN AFLNRFVCAQ LPNAVLESIS
160 170 180 190 200
VIDTPGILSG EKQRISRGYD FAAVLEWFAE RVDRIILLFD AHKLDISDEF
210 220 230 240 250
SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL GKIVNTPEVI
260 270 280 290 300
RVYIGSFWSH PLLIPDNRKL FEAEEQDLFR DIQSLPRNAA LRKLNDLIKR
310 320 330 340 350
ARLAKVHAYI ISSLKKEMPS VFGKDTKKKE LVNNLAEIYG RIEREHQISP
360 370 380 390 400
GDFPNLKRMQ DQLQAQDFSK FQPLKSKLLE VVDDMLAHDI AQLMVLVRQE
410 420 430 440 450
ETQRPVQMVK GGAFEGTLQG PFGHGYGEGA GEGIDDAEWV VARDKPMYDE
460 470 480 490 500
IFYTLSPVDG KITGANAKKE MVRSKLPNSV LGKIWKLADI DKDGMLDDEE
510 520 530
FALANHLIKV KLEGHELPSE LPAHLLPPSK RKVSE
Length:535
Mass (Da):60,821
Last modified:March 18, 2008 - v2
Checksum:i80BF1F3B45CB87DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581R → K in AAF19020 (PubMed:12121420).Curated
Sequence conflicti529 – 5291S → Y in AAF19020 (PubMed:12121420).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155883 mRNA. Translation: AAF19020.1.
AF506002 mRNA. Translation: AAM28633.1.
AK141265 mRNA. Translation: BAE24623.1.
BC046596 mRNA. Translation: AAH46596.1.
CCDSiCCDS28966.1.
RefSeqiNP_065603.2. NM_020578.3.
UniGeneiMm.18526.

Genome annotation databases

EnsembliENSMUST00000024860; ENSMUSP00000024860; ENSMUSG00000024065.
GeneIDi57440.
KEGGimmu:57440.
UCSCiuc008dnn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF155883 mRNA. Translation: AAF19020.1.
AF506002 mRNA. Translation: AAM28633.1.
AK141265 mRNA. Translation: BAE24623.1.
BC046596 mRNA. Translation: AAH46596.1.
CCDSiCCDS28966.1.
RefSeqiNP_065603.2. NM_020578.3.
UniGeneiMm.18526.

3D structure databases

ProteinModelPortaliQ9QXY6.
SMRiQ9QXY6. Positions 1-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208297. 2 interactions.
IntActiQ9QXY6. 5 interactions.
MINTiMINT-1865434.
STRINGi10090.ENSMUSP00000024860.

PTM databases

iPTMnetiQ9QXY6.
PhosphoSiteiQ9QXY6.

Proteomic databases

EPDiQ9QXY6.
MaxQBiQ9QXY6.
PaxDbiQ9QXY6.
PRIDEiQ9QXY6.

Protocols and materials databases

DNASUi57440.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024860; ENSMUSP00000024860; ENSMUSG00000024065.
GeneIDi57440.
KEGGimmu:57440.
UCSCiuc008dnn.2. mouse.

Organism-specific databases

CTDi30845.
MGIiMGI:1928900. Ehd3.

Phylogenomic databases

eggNOGiKOG1954. Eukaryota.
ENOG410XYGB. LUCA.
GeneTreeiENSGT00760000118985.
HOGENOMiHOG000242040.
HOVERGENiHBG018183.
InParanoidiQ9QXY6.
KOiK12476.
OMAiCSTVASP.
OrthoDBiEOG757CX9.
PhylomeDBiQ9QXY6.
TreeFamiTF314429.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiEhd3. mouse.
PROiQ9QXY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXY6.
CleanExiMM_EHD2.
MM_EHD3.
GenevisibleiQ9QXY6. MM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR022812. Dynamin_SF.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EH_dom.
IPR029951. EHD1/EHD3.
IPR031692. EHD_N.
IPR030381. G_DYNAMIN_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11216:SF67. PTHR11216:SF67. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
PF12763. EF-hand_4. 1 hit.
PF16880. EHD_N. 1 hit.
[Graphical view]
SMARTiSM00027. EH. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EHD3: a protein that resides in recycling tubular and vesicular membrane structures and interacts with EHD1."
    Galperin E., Benjamin S., Rapaport D., Rotem-Yehudar R., Tolchinsky S., Horowitz M.
    Traffic 3:575-589(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH EHD1.
  2. Park S.Y., Lee W.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Strain: C57BL/6J.
  4. "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].
    Tissue: Olfactory epithelium.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 33-41; 125-162; 252-268; 270-280 AND 359-370, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling."
    Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D., Kessels M.M., Qualmann B.
    Mol. Biol. Cell 16:3642-3658(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACSIN1 AND PACSIN2.
  7. "Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3."
    Roland J.T., Kenworthy A.K., Peranen J., Caplan S., Goldenring J.R.
    Mol. Biol. Cell 18:2828-2837(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Expression and subcellular distribution of novel glomerulus-associated proteins Dendrin, Ehd3, Sh2d4a, Plekhh2, and 2310066E14Rik."
    Patrakka J., Xiao Z., Nukui M., Takemoto M., He L., Oddsson A., Perisic L., Kaukinen A., Szigyarto C.A.-K., Uhlen M., Jalanko H., Betsholtz C., Tryggvason K.
    J. Am. Soc. Nephrol. 18:689-697(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen and Testis.
  10. Cited for: FUNCTION.
  11. "Renal thrombotic microangiopathy in mice with combined deletion of endocytic recycling regulators EHD3 and EHD4."
    George M., Rainey M.A., Naramura M., Foster K.W., Holzapfel M.S., Willoughby L.L., Ying G., Goswami R.M., Gurumurthy C.B., Band V., Satchell S.C., Band H.
    PLoS ONE 6:E17838-E17838(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  12. "Eps homology domain endosomal transport proteins differentially localize to the neuromuscular junction."
    Mate S.E., Van Der Meulen J.H., Arya P., Bhattacharyya S., Band H., Hoffman E.P.
    Skelet. Muscle 2:19-19(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "A function for EHD family proteins in unidirectional retrograde dendritic transport of BACE1 and Alzheimer's disease Abeta production."
    Buggia-Prevot V., Fernandez C.G., Udayar V., Vetrivel K.S., Elie A., Roseman J., Sasse V.A., Lefkow M., Meckler X., Bhattacharyya S., George M., Kar S., Bindokas V.P., Parent A.T., Rajendran L., Band H., Vassar R., Thinakaran G.
    Cell Rep. 5:1552-1563(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. Cited for: FUNCTION.
  15. "Eps15 homology domain-containing protein 3 regulates cardiac T-type Ca2+ channel targeting and function in the atria."
    Curran J., Musa H., Kline C.F., Makara M.A., Little S.C., Higgins J.D., Hund T.J., Band H., Mohler P.J.
    J. Biol. Chem. 290:12210-12221(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CACNA1GG AND CACNA1H, SUBCELLULAR LOCATION.
  16. Cited for: FUNCTION.
  17. "Phosphatidic acid induces EHD3-containing membrane tubulation and is required for receptor recycling."
    Henmi Y., Oe N., Kono N., Taguchi T., Takei K., Tanabe K.
    Exp. Cell Res. 342:1-10(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-327.

Entry informationi

Entry nameiEHD3_MOUSE
AccessioniPrimary (citable) accession number: Q9QXY6
Secondary accession number(s): Q8K590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 18, 2008
Last modified: June 8, 2016
This is version 119 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, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.