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FHI1A_MOUSE
ID   FHI1A_MOUSE             Reviewed;        1081 AA.
AC   Q505K2; Q8BZ23;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=FHF complex subunit HOOK interacting protein 1A {ECO:0000305};
DE            Short=FHIP1A {ECO:0000305};
GN   Name=Fhip1a; Synonyms=Fam160a1;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-1081.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-1081.
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
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: Probable component of the FTS/Hook/FHIP complex (FHF
CC       complex). FHF complex promotes the distribution of AP-4 complex to the
CC       perinuclear area of the cell. {ECO:0000250|UniProtKB:Q05DH4}.
CC   -!- SUBUNIT: May be a component of the FTS/Hook/FHIP complex (FHF complex),
CC       composed of AKTIP/FTS, FHIP1B, and one or more members of the Hook
CC       family of proteins HOOK1, HOOK2, and HOOK3. May interact directly with
CC       AKTIP/FTS. {ECO:0000250|UniProtKB:Q05DH4}.
CC   -!- SIMILARITY: Belongs to the FHIP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29618.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC102338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC094511; AAH94511.1; -; mRNA.
DR   EMBL; AK036881; BAC29618.1; ALT_INIT; mRNA.
DR   CCDS; CCDS17442.2; -.
DR   RefSeq; NP_766270.2; NM_172682.3.
DR   RefSeq; XP_006501396.1; XM_006501333.3.
DR   RefSeq; XP_011238384.1; XM_011240082.2.
DR   AlphaFoldDB; Q505K2; -.
DR   STRING; 10090.ENSMUSP00000113235; -.
DR   iPTMnet; Q505K2; -.
DR   PhosphoSitePlus; Q505K2; -.
DR   MaxQB; Q505K2; -.
DR   PaxDb; Q505K2; -.
DR   PeptideAtlas; Q505K2; -.
DR   PRIDE; Q505K2; -.
DR   ProteomicsDB; 275973; -.
DR   Antibodypedia; 48311; 12 antibodies from 7 providers.
DR   DNASU; 229488; -.
DR   Ensembl; ENSMUST00000094148; ENSMUSP00000091700; ENSMUSG00000051000.
DR   Ensembl; ENSMUST00000118408; ENSMUSP00000113235; ENSMUSG00000051000.
DR   GeneID; 229488; -.
DR   KEGG; mmu:229488; -.
DR   UCSC; uc008pqu.2; mouse.
DR   CTD; 729830; -.
DR   MGI; MGI:2444746; Fam160a1.
DR   VEuPathDB; HostDB:ENSMUSG00000051000; -.
DR   eggNOG; KOG3695; Eukaryota.
DR   GeneTree; ENSGT00950000182936; -.
DR   HOGENOM; CLU_007807_0_0_1; -.
DR   InParanoid; Q505K2; -.
DR   OMA; RMPSLVQ; -.
DR   OrthoDB; 141539at2759; -.
DR   PhylomeDB; Q505K2; -.
DR   TreeFam; TF313941; -.
DR   BioGRID-ORCS; 229488; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Fam160a1; mouse.
DR   PRO; PR:Q505K2; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q505K2; protein.
DR   Bgee; ENSMUSG00000051000; Expressed in animal zygote and 122 other tissues.
DR   ExpressionAtlas; Q505K2; baseline and differential.
DR   Genevisible; Q505K2; MM.
DR   GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISO:MGI.
DR   InterPro; IPR019384; FHIP.
DR   InterPro; IPR045669; FHIP_C.
DR   InterPro; IPR045668; FHIP_KELAA_motif.
DR   PANTHER; PTHR21705; PTHR21705; 1.
DR   Pfam; PF19314; DUF5917; 1.
DR   Pfam; PF19311; KELAA; 1.
DR   Pfam; PF10257; RAI16-like; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..1081
FT                   /note="FHF complex subunit HOOK interacting protein 1A"
FT                   /id="PRO_0000319579"
FT   REGION          474..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..705
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  120219 MW;  2D8528C959F7B499 CRC64;
     MMSSVSTESK LQQAVSLKGV DPETCMIVFK NHWAQVVKIL EKHDPLKNTQ AKYGSIPPDE
     ASAVQNYVEH MLFLLIEEQA KDAAMGPILE FVVCENIMEK LFLWSLRREF TDETKLEQLK
     MYEMLVTQSY QPLLHHKPIL KPLMMLLSSC SGTATPAVEG KLVVLLNQLC SILAKDPSIL
     ELFFHTSEDQ GAANFLIFSL LIPFIHREGT VGQQARDALL FIMSLSAENS MVANHIVENT
     YFCPVLATGL SGLYSSLPTK LEEKGEDWHC ILKDDWLLLP ALVQFMNSLE FCNAVIQVAH
     PLIRTQLVSY IYNGFLVPVL APALHKVTVE EVMTTTAYLD LFLRSISEPA LLEIFLRFIL
     LHRHENVHIL DTLTSRINTP FRLCVVSLAL FRTLIGLHCE DVMLQLVLRY LVPCNHMMLS
     QRWAVKERDC YSVSAAKLLA LTPVCCASGI TLTLGNQERD YILWSKCMHD GSGSEEQLLP
     ETPCSPSSPS PPPPPAPAAC IVEYGKALDI SYLQYLWEAH TNILHCMRDC RVWSALYDGD
     SPDPETFLQS LSEESRENSG HPEARLPQQS VRTSGQTKDK SQSELEWDDS YDTGISSGAD
     VGSPGPDDEV ETPAPPAPID PPKHIQEMKK NAILLFKGSY IEESDFQDDV MVYRLCAEKD
     TEDTTEPQKD TSEPQGDTLE PLEDTSEQQE DTSEQLEDTS ELQEDTAEPQ GDTADPTAEA
     QPKLQPEAQS LPTSNGPLSS PDPETESQPS RESSDLCQNT FSEAKPENEP GVALALDSEL
     IATTFEAEPQ SELAVVSTES EDFIAQYDQI IQELDSGTEG LTEQSIPISE PSLLTQQEER
     REECKEEEDD DFDSLMAATP AVEAGSSPFG VGEDTAFSSR HPVRTQSTPF TGPFISVVLS
     KLENMLENSL HVNLLLIGII TQLASYPQPL LRSFLLNTNM VFQPSVRSLY QVLASVKNKI
     EQFASVERDF PGLLIQAQQY LLFRVDMSDM APAALTKDPI QEISRPESDK TLLDGPPRVL
     QPFLGNRAKV TRAPPNLPLP VKNTMLAAAL FPEFLKELAA LAQEHSILCY KILGDFEDSC
     C
 
 
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