位置:首页 > 蛋白库 > EHD1_MOUSE
EHD1_MOUSE
ID   EHD1_MOUSE              Reviewed;         534 AA.
AC   Q9WVK4;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=EH domain-containing protein 1 {ECO:0000305};
DE   AltName: Full=PAST homolog 1 {ECO:0000305};
DE            Short=mPAST1 {ECO:0000312|EMBL:AAF24223.1};
GN   Name=Ehd1 {ECO:0000312|MGI:MGI:1341878};
GN   Synonyms=Past1 {ECO:0000312|EMBL:AAF24223.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=ICR;
RX   PubMed=10395801; DOI=10.1006/geno.1999.5800;
RA   Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y.,
RA   Kozak C.A., Joyner A., Fein A., Horowitz M.;
RT   "EHD1 -- an EH-domain-containing protein with a specific expression
RT   pattern.";
RL   Genomics 59:66-76(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Plomann M., Behrendt D., Ritter B., Modregger J., Halback A., Paulsson M.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, DOMAIN, MUTAGENESIS OF GLY-65 AND TRP-485, AND INTERACTION WITH
RP   PACSIN1 AND PACSIN2.
RX   PubMed=15930129; DOI=10.1091/mbc.e05-01-0076;
RA   Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D.,
RA   Kessels M.M., Qualmann B.;
RT   "EHD proteins associate with syndapin I and II and such interactions play a
RT   crucial role in endosomal recycling.";
RL   Mol. Biol. Cell 16:3642-3658(2005).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-456, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   FUNCTION.
RX   PubMed=20159556; DOI=10.1016/j.molcel.2009.12.037;
RA   Allaire P.D., Marat A.L., Dall'Armi C., Di Paolo G., McPherson P.S.,
RA   Ritter B.;
RT   "The Connecdenn DENN domain: a GEF for Rab35 mediating cargo-specific exit
RT   from early endosomes.";
RL   Mol. Cell 37:370-382(2010).
RN   [8]
RP   FUNCTION, INTERACTION WITH FER1L5 AND MYOF, AND SUBCELLULAR LOCATION.
RX   PubMed=21177873; DOI=10.1074/jbc.m110.157222;
RA   Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M.,
RA   George M., Band H., McNally E.M.;
RT   "Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5
RT   (Fer1L5) and mediate myoblast fusion.";
RL   J. Biol. Chem. 286:7379-7388(2011).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=24373286; DOI=10.1016/j.celrep.2013.12.006;
RA   Buggia-Prevot V., Fernandez C.G., Udayar V., Vetrivel K.S., Elie A.,
RA   Roseman J., Sasse V.A., Lefkow M., Meckler X., Bhattacharyya S., George M.,
RA   Kar S., Bindokas V.P., Parent A.T., Rajendran L., Band H., Vassar R.,
RA   Thinakaran G.;
RT   "A function for EHD family proteins in unidirectional retrograde dendritic
RT   transport of BACE1 and Alzheimer's disease Abeta production.";
RL   Cell Rep. 5:1552-1563(2013).
RN   [10]
RP   INTERACTION WITH MICALL1 AND RAB35.
RX   PubMed=23572513; DOI=10.1242/jcs.117846;
RA   Kobayashi H., Fukuda M.;
RT   "Rab35 establishes the EHD1-association site by coordinating two distinct
RT   effectors during neurite outgrowth.";
RL   J. Cell Sci. 126:2424-2435(2013).
CC   -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC       reorganization/tubulation upon ATP hydrolysis. In vitro causes
CC       vesiculation of endocytic membranes (By similarity). Acts in early
CC       endocytic membrane fusion and membrane trafficking of recycling
CC       endosomes (PubMed:15930129, PubMed:20159556). Recruited to endosomal
CC       membranes upon nerve growth factor stimulation, indirectly regulates
CC       neurite outgrowth (By similarity). Plays a role in myoblast fusion
CC       (PubMed:21177873). Involved in the unidirectional retrograde dendritic
CC       transport of endocytosed BACE1 and in efficient sorting of BACE1 to
CC       axons implicating a function in neuronal APP processing
CC       (PubMed:24373286). Plays a role in the formation of the ciliary vesicle
CC       (CV), an early step in cilium biogenesis. Proposed to be required for
CC       the fusion of distal appendage vesicles (DAVs) to form the CV by
CC       recruiting SNARE complex component SNAP29. Is required for recruitment
CC       of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of
CC       IFT20 following DAV reorganization before Rab8-dependent ciliary
CC       membrane extension. Required for the loss of CCP110 form the mother
CC       centriole essential for the maturation of the basal body during
CC       ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q641Z6,
CC       ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:15930129,
CC       ECO:0000269|PubMed:20159556, ECO:0000269|PubMed:21177873,
CC       ECO:0000269|PubMed:24373286}.
CC   -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4,
CC       ATP-binding is required for heterooligomerization (By similarity).
CC       Interacts (via EH domain) with MICALL1 (via NPF1 motif); the
CC       interaction is direct and recruits EHD1 to membranes (PubMed:23572513).
CC       Interacts with RAB35; the interaction is indirect through MICALL1 and
CC       recruits EHD1 to membranes (PubMed:23572513). Interacts (via EH domain)
CC       with PACSIN2 (via NPF motifs); regulates localization to tubular
CC       recycling endosome membranes (PubMed:15930129). Interacts with PACSIN1
CC       (PubMed:15930129). Interacts with RAB8A (By similarity). Interacts with
CC       FER1L5 (via second C2 domain) (PubMed:21177873). Interacts with MYOF
CC       (PubMed:21177873). Interacts with ZFYVE20 (By similarity). Interacts
CC       (via EH domain) with RAB11FIP2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:15930129,
CC       ECO:0000269|PubMed:21177873, ECO:0000269|PubMed:23572513}.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC       {ECO:0000269|PubMed:21177873}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:24373286}. Cell projection, cilium membrane
CC       {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially
CC       associates with tubular recycling endosomes (By similarity).
CC       Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes
CC       (PubMed:21177873). Localizes to the ciliary pocket from where the
CC       cilium protrudes (By similarity). Colocalizes with BACE1 in
CC       tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP
CC       amyloid beta proteins in hippocampal mossy fiber terminals.
CC       {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:21177873,
CC       ECO:0000269|PubMed:24373286}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC       kidney, heart, intestine, and brain. {ECO:0000269|PubMed:10395801}.
CC   -!- DEVELOPMENTAL STAGE: Expression is already noted at day 9.5 in the limb
CC       buds and pharyngeal arches and at day 10.5 in sclerotomes, at various
CC       elements of the branchial apparatus (mandible and hyoid), and in the
CC       occipital region. At day 15.5 expression peaks in cartilage, preceding
CC       hypertrophy and ossification, and at day 17.5 there is no expression in
CC       the bones. {ECO:0000269|PubMed:10395801}.
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC       proteins. {ECO:0000269|PubMed:15930129}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01055}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF099186; AAD45423.1; -; mRNA.
DR   EMBL; AF173156; AAF24223.1; -; mRNA.
DR   EMBL; AK012896; BAB28540.1; -; mRNA.
DR   CCDS; CCDS29501.1; -.
DR   RefSeq; NP_034249.1; NM_010119.5.
DR   AlphaFoldDB; Q9WVK4; -.
DR   BMRB; Q9WVK4; -.
DR   SMR; Q9WVK4; -.
DR   BioGRID; 199408; 15.
DR   DIP; DIP-59491N; -.
DR   IntAct; Q9WVK4; 5.
DR   STRING; 10090.ENSMUSP00000025684; -.
DR   iPTMnet; Q9WVK4; -.
DR   PhosphoSitePlus; Q9WVK4; -.
DR   SwissPalm; Q9WVK4; -.
DR   EPD; Q9WVK4; -.
DR   jPOST; Q9WVK4; -.
DR   MaxQB; Q9WVK4; -.
DR   PaxDb; Q9WVK4; -.
DR   PRIDE; Q9WVK4; -.
DR   ProteomicsDB; 275908; -.
DR   Antibodypedia; 44098; 179 antibodies from 29 providers.
DR   DNASU; 13660; -.
DR   Ensembl; ENSMUST00000025684; ENSMUSP00000025684; ENSMUSG00000024772.
DR   GeneID; 13660; -.
DR   KEGG; mmu:13660; -.
DR   UCSC; uc008ghz.1; mouse.
DR   CTD; 10938; -.
DR   MGI; MGI:1341878; Ehd1.
DR   VEuPathDB; HostDB:ENSMUSG00000024772; -.
DR   eggNOG; KOG1954; Eukaryota.
DR   GeneTree; ENSGT00940000158249; -.
DR   HOGENOM; CLU_017595_1_1_1; -.
DR   InParanoid; Q9WVK4; -.
DR   OMA; WYEETIL; -.
DR   OrthoDB; 377342at2759; -.
DR   PhylomeDB; Q9WVK4; -.
DR   TreeFam; TF314429; -.
DR   Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 13660; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Ehd1; mouse.
DR   PRO; PR:Q9WVK4; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9WVK4; protein.
DR   Bgee; ENSMUSG00000024772; Expressed in granulocyte and 74 other tissues.
DR   ExpressionAtlas; Q9WVK4; baseline and differential.
DR   Genevisible; Q9WVK4; MM.
DR   GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005811; C:lipid droplet; IDA:BHF-UCL.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031095; C:platelet dense tubular network membrane; IDA:BHF-UCL.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   GO; GO:0016197; P:endosomal transport; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
DR   GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:UniProtKB.
DR   GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR   GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR   CDD; cd00052; EH; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR040990; DUF5600.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000261; EH_dom.
DR   InterPro; IPR029951; EHD1/EHD3.
DR   InterPro; IPR031692; EHD_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11216:SF127; PTHR11216:SF127; 1.
DR   Pfam; PF18150; DUF5600; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF12763; EF-hand_4; 1.
DR   Pfam; PF16880; EHD_N; 1.
DR   SMART; SM00027; EH; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasmic vesicle; Endosome;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..534
FT                   /note="EH domain-containing protein 1"
FT                   /id="PRO_0000146110"
FT   DOMAIN          55..286
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   DOMAIN          444..532
FT                   /note="EH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT   DOMAIN          476..511
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          65..72
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          91..92
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          153..156
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          219..222
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          243
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COILED          198..227
FT                   /evidence="ECO:0000255"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4M9"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT   BINDING         258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT   BINDING         489
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         491
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         493
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         500
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4M9"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         65
FT                   /note="G->R: Abolishes interaction with PACSIN2."
FT                   /evidence="ECO:0000269|PubMed:15930129"
FT   MUTAGEN         485
FT                   /note="W->A: Abolishes interaction with PACSIN2."
FT                   /evidence="ECO:0000269|PubMed:15930129"
SQ   SEQUENCE   534 AA;  60603 MW;  35502055BC6164F7 CRC64;
     MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM
     VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR
     PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE
     RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL
     GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
     ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISS GDFPSLRKMQ
     ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQAVK GGAFDGTMNG
     PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
     LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLIPPSK RRHE
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024