FHI1B_HUMAN
ID FHI1B_HUMAN Reviewed; 972 AA.
AC Q8N612; Q9C0A4; Q9H0N3; Q9H624;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=FHF complex subunit HOOK interacting protein 1B {ECO:0000305};
DE Short=FHIP1B {ECO:0000305};
DE AltName: Full=FTS and Hook-interacting protein {ECO:0000303|PubMed:32073997};
DE Short=FHIP {ECO:0000303|PubMed:32073997};
GN Name=FHIP1B {ECO:0000312|HGNC:HGNC:25378};
GN Synonyms=C11orf56, FAM160A2, KIAA1759;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-491.
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT MET-491.
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF COMPLEX,
RP FUNCTION, AND ASSOCIATION WITH THE HOPS COMPLEX.
RX PubMed=18799622; DOI=10.1091/mbc.e08-05-0473;
RA Xu L., Sowa M.E., Chen J., Li X., Gygi S.P., Harper J.W.;
RT "An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal
RT clustering by the homotypic vacuolar protein sorting complex.";
RL Mol. Biol. Cell 19:5059-5071(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-897, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-897, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, AND INTERACTION WITH AKTIP.
RX PubMed=32073997; DOI=10.1091/mbc.e19-11-0658;
RA Mattera R., Williamson C.D., Ren X., Bonifacino J.S.;
RT "The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear
RT distribution of AP-4 and its cargo ATG9A.";
RL Mol. Biol. Cell 31:963-979(2020).
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 (PubMed:32073997). {ECO:0000269|PubMed:18799622,
CC ECO:0000269|PubMed:32073997}.
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 (PubMed:32073997). The FHF complex
CC associates with the homotypic vesicular sorting complex (the HOPS
CC complex). {ECO:0000269|PubMed:18799622, ECO:0000269|PubMed:32073997}.
CC -!- INTERACTION:
CC Q8N612; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-742137, EBI-741181;
CC Q8N612; Q96HR9: REEP6; NbExp=4; IntAct=EBI-742137, EBI-750345;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N612-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N612-2; Sequence=VSP_021129;
CC Name=3;
CC IsoId=Q8N612-3; Sequence=VSP_021128, VSP_021130, VSP_021131;
CC -!- SIMILARITY: Belongs to the FHIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21850.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AB051546; BAB21850.1; ALT_INIT; mRNA.
DR EMBL; AK026318; BAB15443.1; -; mRNA.
DR EMBL; AL136723; CAB66657.1; -; mRNA.
DR EMBL; BC030825; AAH30825.1; -; mRNA.
DR CCDS; CCDS44530.1; -. [Q8N612-1]
DR CCDS; CCDS7760.1; -. [Q8N612-2]
DR RefSeq; NP_001092264.1; NM_001098794.1. [Q8N612-1]
DR RefSeq; NP_115503.2; NM_032127.3. [Q8N612-2]
DR RefSeq; XP_006718406.1; XM_006718343.2. [Q8N612-2]
DR RefSeq; XP_011518699.1; XM_011520397.2. [Q8N612-2]
DR AlphaFoldDB; Q8N612; -.
DR BioGRID; 123862; 21.
DR CORUM; Q8N612; -.
DR IntAct; Q8N612; 10.
DR STRING; 9606.ENSP00000265978; -.
DR iPTMnet; Q8N612; -.
DR PhosphoSitePlus; Q8N612; -.
DR BioMuta; FAM160A2; -.
DR DMDM; 251757473; -.
DR EPD; Q8N612; -.
DR jPOST; Q8N612; -.
DR MassIVE; Q8N612; -.
DR MaxQB; Q8N612; -.
DR PaxDb; Q8N612; -.
DR PeptideAtlas; Q8N612; -.
DR PRIDE; Q8N612; -.
DR ProteomicsDB; 72122; -. [Q8N612-1]
DR ProteomicsDB; 72123; -. [Q8N612-2]
DR ProteomicsDB; 72124; -. [Q8N612-3]
DR Antibodypedia; 67203; 50 antibodies from 12 providers.
DR DNASU; 84067; -.
DR Ensembl; ENST00000265978.8; ENSP00000265978.4; ENSG00000051009.11. [Q8N612-2]
DR Ensembl; ENST00000449352.7; ENSP00000416918.3; ENSG00000051009.11. [Q8N612-1]
DR GeneID; 84067; -.
DR KEGG; hsa:84067; -.
DR MANE-Select; ENST00000449352.7; ENSP00000416918.3; NM_001098794.2; NP_001092264.1.
DR UCSC; uc001mck.5; human. [Q8N612-1]
DR CTD; 84067; -.
DR DisGeNET; 84067; -.
DR GeneCards; FHIP1B; -.
DR HGNC; HGNC:25378; FHIP1B.
DR HPA; ENSG00000051009; Low tissue specificity.
DR neXtProt; NX_Q8N612; -.
DR OpenTargets; ENSG00000051009; -.
DR VEuPathDB; HostDB:ENSG00000051009; -.
DR eggNOG; KOG3695; Eukaryota.
DR GeneTree; ENSGT00950000182936; -.
DR HOGENOM; CLU_007807_1_0_1; -.
DR InParanoid; Q8N612; -.
DR OMA; CLDWDSG; -.
DR OrthoDB; 141539at2759; -.
DR PhylomeDB; Q8N612; -.
DR TreeFam; TF313941; -.
DR PathwayCommons; Q8N612; -.
DR SignaLink; Q8N612; -.
DR BioGRID-ORCS; 84067; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; FAM160A2; human.
DR GeneWiki; C11orf56; -.
DR GenomeRNAi; 84067; -.
DR Pharos; Q8N612; Tbio.
DR PRO; PR:Q8N612; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N612; protein.
DR Bgee; ENSG00000051009; Expressed in ileal mucosa and 167 other tissues.
DR ExpressionAtlas; Q8N612; baseline and differential.
DR Genevisible; Q8N612; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070695; C:FHF complex; IDA:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; IMP: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..972
FT /note="FHF complex subunit HOOK interacting protein 1B"
FT /id="PRO_0000253859"
FT REGION 465..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2I3"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U2I3"
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 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021128"
FT VAR_SEQ 479
FT /note="G -> GGPSRETGRREDITG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_021129"
FT VAR_SEQ 757..780
FT /note="VYVNFLLTGLVAQLACHPQPLLRS -> ALSCSTPTWSSSPVSSPCCRCWAL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021130"
FT VAR_SEQ 781..972
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021131"
FT VARIANT 462
FT /note="R -> W (in dbSNP:rs35932378)"
FT /id="VAR_057805"
FT VARIANT 491
FT /note="T -> M (in dbSNP:rs3750944)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_028739"
FT VARIANT 619
FT /note="R -> L (in dbSNP:rs3750943)"
FT /id="VAR_028740"
FT VARIANT 754
FT /note="Q -> H (in dbSNP:rs11040808)"
FT /id="VAR_028741"
FT CONFLICT 95
FT /note="P -> S (in Ref. 4; CAB66657)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="M -> V (in Ref. 4; CAB66657)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="C -> Y (in Ref. 3; BAB15443)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="A -> V (in Ref. 4; CAB66657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 972 AA; 105568 MW; F1CC45667E1B6811 CRC64;
MERMNWLSRL ASRGPGHRIP QGANLQTPVM ADPETCLMVF KNHWSQVVRI LERQGPRAAP
GGADDLSAVR NHTYQMLTLL AEDRAVPSAP TGPGPLLEFA LHEDLLTRVL TWQLQWDELG
DGVEERRAEQ LKLFEMLVSE ARQPLLRHGP VREALLTLLD ACGRPVPSSP ALDEGLVLLL
SQLCVCVAQE PSLLEFFLQP PPEPGAAPRL LLFSRLVPFV HREGTLGQQA RDALLLLMAL
SAGSPTVGRY IADHSYFCPV LATGLSALYS SLPRKIEVPG DDWHCLRRED WLGVPALALF
MSSLEFCNAV IQVAHPLVQK QLVDYIHNGF LVPVMGPALH KTSVEEMIAS TAYLELFLRS
ISEPALLRTF LRFLLLHRHD THTILDTLVA RIGSNSRLCM VSLSLFRTLL NLSCEDVLLQ
LVLRYLVPCN HVMLSQKPAV RDVDLYGRAA DKFLSLIPRC CRHHAPSPPR PEHASWARGP
GSPSVDSSSV TTVPRPSTPS RLALFLRQQS LGGSESPGPA PCSPGLSASP ASSPGRRPTP
AEEPGELEDN YLEYLREARR GVDRCVRACR TWSAPYDGER PSPEPSPFGS RTKKRSLLPE
EDRNNVGEGE EEELGRRGRA GGAGEGPGHL PPPQLNGVPG SWPEGAKKVR LVPKEGAGEL
LEGISEGMAG LEGFGQELRE LEVALSNGGT GSESPLEPPL PLEEEEAYES FTCPPEPPGP
FLSSPLRTLN QLPSQPFTGP FMAVLFAKLE NMLQNSVYVN FLLTGLVAQL ACHPQPLLRS
FLLNTNMVFQ PSVKSLLQVL GSVKNKIENF AASQEDFPAL LSKAKKYLIA RGKLDWAEGP
AAGPAPRRSD PLVKSRRPSL GELLLRHAHS PTRARQAAQL VLQPGRDGAG LGLSGGSPGA
STPVLLTRGG APERQGEALR VKNAVYCAVI FPEFLKELAA ISQAHAVTSP FLLETSEEGS
GPLISGCGPL NP