FHI1B_MOUSE
ID FHI1B_MOUSE Reviewed; 975 AA.
AC Q3U2I3; Q3TWF5; Q6P543; Q80T93; Q811J6; Q8BI34; Q8VE55;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=FHF complex subunit HOOK interacting protein 1B;
DE Short=FHIP1B;
DE AltName: Full=FTS and Hook-interacting protein;
DE Short=FHIP;
GN Name=Fhip1b; Synonyms=Fam160a2, Kiaa1759;
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 MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Skin;
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] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N-3; TISSUE=Embryo, and Mammary gland;
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-510 AND SER-523, AND
RP IDENTIFICATION BY 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-510 AND SER-900, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, 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: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF
CC complex may function to promote vesicle trafficking and/or fusion via
CC the homotypic vesicular protein sorting complex (the HOPS complex). FHF
CC complex promotes the distribution of AP-4 complex to the perinuclear
CC area of the cell. {ECO:0000250|UniProtKB:Q8N612}.
CC -!- SUBUNIT: Component of the FTS/Hook/FHIP complex (FHF complex), composed
CC of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of
CC proteins HOOK1, HOOK2, and HOOK3. The FHF complex associates with the
CC homotypic vesicular sorting complex (the HOPS complex).
CC {ECO:0000250|UniProtKB:Q8N612}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U2I3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U2I3-2; Sequence=VSP_021134;
CC Name=3;
CC IsoId=Q3U2I3-3; Sequence=VSP_021132, VSP_021133;
CC -!- SIMILARITY: Belongs to the FHIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65834.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122552; BAC65834.2; ALT_INIT; Transcribed_RNA.
DR EMBL; AK014591; BAC25444.1; -; mRNA.
DR EMBL; AK155273; BAE33157.1; -; mRNA.
DR EMBL; AK159716; BAE35311.1; -; mRNA.
DR EMBL; BC019738; AAH19738.1; -; mRNA.
DR EMBL; BC043717; AAH43717.1; -; mRNA.
DR EMBL; BC063093; AAH63093.1; -; mRNA.
DR CCDS; CCDS21649.1; -. [Q3U2I3-1]
DR CCDS; CCDS57575.1; -. [Q3U2I3-3]
DR RefSeq; NP_001229292.1; NM_001242363.2. [Q3U2I3-1]
DR RefSeq; NP_001229293.1; NM_001242364.2.
DR RefSeq; NP_001229294.1; NM_001242365.2. [Q3U2I3-3]
DR RefSeq; NP_950174.1; NM_199009.3. [Q3U2I3-1]
DR AlphaFoldDB; Q3U2I3; -.
DR BioGRID; 216681; 1.
DR STRING; 10090.ENSMUSP00000112711; -.
DR iPTMnet; Q3U2I3; -.
DR PhosphoSitePlus; Q3U2I3; -.
DR jPOST; Q3U2I3; -.
DR MaxQB; Q3U2I3; -.
DR PaxDb; Q3U2I3; -.
DR PRIDE; Q3U2I3; -.
DR ProteomicsDB; 275506; -. [Q3U2I3-1]
DR ProteomicsDB; 275507; -. [Q3U2I3-2]
DR ProteomicsDB; 275508; -. [Q3U2I3-3]
DR Antibodypedia; 67203; 50 antibodies from 12 providers.
DR DNASU; 74349; -.
DR Ensembl; ENSMUST00000118726; ENSMUSP00000112605; ENSMUSG00000044465. [Q3U2I3-3]
DR Ensembl; ENSMUST00000122327; ENSMUSP00000112711; ENSMUSG00000044465. [Q3U2I3-1]
DR Ensembl; ENSMUST00000179474; ENSMUSP00000137163; ENSMUSG00000044465. [Q3U2I3-1]
DR GeneID; 74349; -.
DR KEGG; mmu:74349; -.
DR UCSC; uc009ixy.2; mouse. [Q3U2I3-1]
DR UCSC; uc012frl.2; mouse. [Q3U2I3-3]
DR CTD; 84067; -.
DR MGI; MGI:1921599; Fam160a2.
DR VEuPathDB; HostDB:ENSMUSG00000044465; -.
DR eggNOG; KOG3695; Eukaryota.
DR GeneTree; ENSGT00950000182936; -.
DR HOGENOM; CLU_007807_1_0_1; -.
DR InParanoid; Q3U2I3; -.
DR OMA; CLDWDSG; -.
DR OrthoDB; 141539at2759; -.
DR PhylomeDB; Q3U2I3; -.
DR TreeFam; TF313941; -.
DR BioGRID-ORCS; 74349; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Fam160a2; mouse.
DR PRO; PR:Q3U2I3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3U2I3; protein.
DR Bgee; ENSMUSG00000044465; Expressed in granulocyte and 245 other tissues.
DR ExpressionAtlas; Q3U2I3; baseline and differential.
DR Genevisible; Q3U2I3; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Alternative splicing; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..975
FT /note="FHF complex subunit HOOK interacting protein 1B"
FT /id="PRO_0000253860"
FT REGION 465..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H54"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66H54"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N612"
FT MOD_RES 892
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66H54"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 478
FT /note="R -> RGGPSREAGRREDIT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021132"
FT VAR_SEQ 545..742
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021133"
FT VAR_SEQ 744..809
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_021134"
FT CONFLICT 57
FT /note="R -> W (in Ref. 3; AAH43717)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="S -> G (in Ref. 2; BAE33157 and 3; AAH43717)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="T -> S (in Ref. 2; BAE33157/BAE35311)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="R -> S (in Ref. 2; BAE35311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 975 AA; 106541 MW; C07662ECA31723F9 CRC64;
MEKMNWLSRL ASRVPGHRVP QGASLQTPVM ADPETCLMVF KNHWSQVVRI LERQGPRAAT
GGADDLSAVR NHTYQMLTLL AEDRAVPSAP SGPGPLLEFA LREDLLSRVL TWQLQWDEFG
DGVEERRAEQ LKLFEMLVSE ARQPLLRHGP VREALLALLD ACGRPVPSSP ALDEGLVLLL
SQLCVCVARE PSLLEFFLQP PPEPGAAPRL LLFSRLVPFV HREGTLGQQA RDALLLLMAL
SDGSPTVGRY IADHSYFCPV LATGLSALYS SLPRKIEVPG DDWHCLRRED WIGVPALALF
MSSLEFCNAV IQVAHPLVQK QLVDYIHNGF LVPVMGPALH KTSVEEMIAS TAYLELFLRS
ISEPALLRTF LRFLLLHRHD THTILDTLVA RIGSNSRLCM VSLSLFRTLL NLSCEDVLLQ
LVLRYLVPCN HVMLSQKPAV RDVDLYGRAA DKFLSLIPRC CRHHAPSPPR PEHASWARGP
GSPSVDSSSV VTVPRPSTPS RLALFLRQQS LGGSESPGPV PRSPGLTASP TSSPSRRPSP
AEEPGELEDN YLEYLREARR GVDRCVRACR TWSAPYDGER PPPEPNPLGS RTKKRSLLPE
EDRDNVREGE EENLGSRGLA VGVGDTPGYL LPPQLNGVPG PWPEGAKKVR LVPRLVPQEG
VRELLEGTSE DMAGLESFGQ ELQELEVALS NGGAGSEPPL EPPLPPEEEE AYESFTCPPE
PPGPFLSSPL RTLHQLPSQP FTGPFMAVLF AKLENMLQNS VYVNFLLTGL VAQLACHPQP
LLRSFLLNTN MVFQPSVKSL LQVLGSVKNK IESFAASQED FPALLSKAKK YLIARGKLDW
AEGPTAGPAP RRSDSLVRSR RPSLGELLLR HAHSPTRARQ AVQVLQPGRD GTGLGLGGGS
PGASTPVLLP RGGASERQGE ALRVKNAVYC AVIFPEFLKE LAAISQAHAV TSPFLLDTSE
EVSLPPISGF GPLNP
