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FHOD1_MOUSE
ID   FHOD1_MOUSE             Reviewed;        1197 AA.
AC   Q6P9Q4; Q8BMK2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=FH1/FH2 domain-containing protein 1;
DE   AltName: Full=Formin homolog overexpressed in spleen 1;
DE            Short=FHOS;
DE   AltName: Full=Formin homology 2 domain-containing protein 1;
GN   Name=Fhod1; Synonyms=Fhos1;
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].
RC   TISSUE=B-cell, and Spleen;
RX   PubMed=15966898; DOI=10.1111/j.1365-2443.2005.00867.x;
RA   Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.;
RT   "Fhos2, a novel formin-related actin-organizing protein, probably
RT   associates with the nestin intermediate filament.";
RL   Genes Cells 10:665-678(2005).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-524 AND SER-527, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC   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).
CC   -!- FUNCTION: Required for the assembly of F-actin structures, such as
CC       stress fibers. Depends on the Rho-ROCK cascade for its activity.
CC       Contributes to the coordination of microtubules with actin fibers and
CC       plays a role in cell elongation. Acts synergistically with ROCK1 to
CC       promote SRC-dependent non-apoptotic plasma membrane blebbing (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates via the FH2 domain. Binds to F-actin via its
CC       N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus
CC       (By similarity). Interacts with ROCK1 in a Src-dependent manner (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection,
CC       bleb {ECO:0000250}. Note=Predominantly cytoplasmic. {ECO:0000250}.
CC   -!- DOMAIN: Regulated by intramolecular binding to a C-terminal auto-
CC       inhibitory domain. Effector binding abolishes this interaction and
CC       activates the protein (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC       interaction with the GBD/FH3 domain. This autoinhibition is released
CC       upon competitive binding of an activated GTPase. The release of DAD
CC       allows the FH2 domain to then nucleate and elongate nonbranched actin
CC       filaments (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by ROCK1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR   EMBL; AB041045; BAE06182.1; -; mRNA.
DR   EMBL; AK030737; BAC27106.1; -; mRNA.
DR   EMBL; BC060654; AAH60654.1; -; mRNA.
DR   CCDS; CCDS22600.1; -.
DR   RefSeq; NP_808367.2; NM_177699.4.
DR   AlphaFoldDB; Q6P9Q4; -.
DR   SMR; Q6P9Q4; -.
DR   BioGRID; 231560; 1.
DR   IntAct; Q6P9Q4; 2.
DR   MINT; Q6P9Q4; -.
DR   STRING; 10090.ENSMUSP00000014922; -.
DR   iPTMnet; Q6P9Q4; -.
DR   PhosphoSitePlus; Q6P9Q4; -.
DR   EPD; Q6P9Q4; -.
DR   jPOST; Q6P9Q4; -.
DR   MaxQB; Q6P9Q4; -.
DR   PaxDb; Q6P9Q4; -.
DR   PeptideAtlas; Q6P9Q4; -.
DR   PRIDE; Q6P9Q4; -.
DR   ProteomicsDB; 267469; -.
DR   Antibodypedia; 15694; 163 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000014922; ENSMUSP00000014922; ENSMUSG00000014778.
DR   GeneID; 234686; -.
DR   KEGG; mmu:234686; -.
DR   UCSC; uc009nct.2; mouse.
DR   CTD; 29109; -.
DR   MGI; MGI:2679008; Fhod1.
DR   VEuPathDB; HostDB:ENSMUSG00000014778; -.
DR   eggNOG; KOG1925; Eukaryota.
DR   GeneTree; ENSGT00940000160212; -.
DR   HOGENOM; CLU_000814_0_0_1; -.
DR   InParanoid; Q6P9Q4; -.
DR   OMA; TSPNCSC; -.
DR   OrthoDB; 148001at2759; -.
DR   PhylomeDB; Q6P9Q4; -.
DR   TreeFam; TF316268; -.
DR   BioGRID-ORCS; 234686; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Fhod1; mouse.
DR   PRO; PR:Q6P9Q4; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q6P9Q4; protein.
DR   Bgee; ENSMUSG00000014778; Expressed in granulocyte and 166 other tissues.
DR   Genevisible; Q6P9Q4; MM.
DR   GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0001725; C:stress fiber; ISO:MGI.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0043621; F:protein self-association; ISO:MGI.
DR   GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0051660; P:establishment of centrosome localization; IMP:MGI.
DR   GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
DR   Gene3D; 1.20.58.2220; -; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015425; FH2_Formin.
DR   InterPro; IPR042201; FH2_Formin_sf.
DR   InterPro; IPR027647; FHOD1.
DR   InterPro; IPR041387; FHOD1_GBD_N.
DR   InterPro; IPR014768; GBD/FH3_dom.
DR   PANTHER; PTHR45920:SF2; PTHR45920:SF2; 3.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF18382; Formin_GBD_N; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1197
FT                   /note="FH1/FH2 domain-containing protein 1"
FT                   /id="PRO_0000194906"
FT   DOMAIN          53..462
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT   DOMAIN          491..647
FT                   /note="FH1"
FT   DOMAIN          648..1045
FT                   /note="FH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT   DOMAIN          1085..1166
FT                   /note="DAD"
FT   REGION          344..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..839
FT                   /note="Interaction with ROCK1"
FT                   /evidence="ECO:0000250"
FT   REGION          1055..1135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1150..1170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..535
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..641
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1077..1092
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         370
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         490
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT   MOD_RES         499
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT   MOD_RES         502
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT   MOD_RES         524
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         722
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y613"
FT   CONFLICT        323
FT                   /note="L -> Q (in Ref. 2; BAC27106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        929
FT                   /note="E -> K (in Ref. 2; BAC27106)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1196
FT                   /note="E -> G (in Ref. 2; BAC27106)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1197 AA;  129600 MW;  162634FAB9715F01 CRC64;
     MAGEEERGDG DPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP LSAQIPALHR
     LLGAPLKLED CALQVSPSGY YLDPELSLEE QREMLEGFYE EISKGRKPTL ILRTQLSVRV
     NAILEKLYGS SGPELRRSLF SLKQIFQEDK DLVPEFVHSE GLSCLIRVGA AADHNYQSYI
     LRALGQLMLF VDGMLGVVAH SETVQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF
     IQAVNAVASA TGTLPWANLV SILEEKNGAD AELLVYTVTL INKTLAALPD QDSFYDVTDA
     LEQQGMEALV QRFLGTAGTD VDLRTQLTLY ESALRLEDGD MEEAAAAAAA GGRRERRKPS
     SEEGKRSRRS LEGGGCPVRA PEPGSTGSAS PVGSTPSTGS APPTNPAFSS TGPASGLLRT
     SVNLFPTISV GPSVDSSCER SVYKARFLEN VAAAETEKQA ALAQGRAETL AGATVDDTDG
     SSGTRELWDS PEPASAPRTP QSPVSRILLR TQRSLEPEPK KPVSPPSPKA EPIQEPPTCV
     PKLCIGDLDF SDLGEDEDQD TLNVESVEAG KASPFLSSLS PSLSGGPPPP PPPPPPITGS
     CPPPPPPPLP PPATGSCPPP PPPPPPPIIG SCPPPPPLAA PFTHSALDGP RHPTKRKTVK
     LFWRELKLTG GPGCSRSRFG PCPTLWASLE PVSVDTARLE HLFESRAKDV LPTKKAGEGR
     RTMTVVLDPK RSNAINIGLT TLPPVHVIKA ALLNFDEFAV SKDGIEKLLT MMPTEEERQK
     IEEAQLANPD VPLGPAENFL MTLASIGGLA ARLQLWAFKL DYESMEREIA EPLFDLKVGM
     EQLVHNATFR CILATLLAVG NFLNGSQSSG FELSYLEKVS EVKDTVRRQS LLYHLCSLVL
     QTRPDSSDLY SEIPALTRCA KVDFEQLTEN LGQLECRSQA AEDSLRSLAK HELSPALRAR
     LTHFLAQCTR RVAMLRVVHR RVCNRFHAFL LYLGYTPQAA RDVRIMQFCH TLREFALEYR
     TCRERVLQQQ QKRATYRERN KTRGRMITET EKFSGVAGEA PNNLSVPVAV GSGPGQGDTD
     NHASMKSLLT SRPEDATHSR RSRGMVQSSS PVSHTAVGPS AASPEETAAS GLPTDTSDEI
     MDLLVQSVTK SGPRALAARE RKRSRGNRKS LRRTLKSGLG DDLVQALGLS KAPGLEV
 
 
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