HAP1_RAT
ID HAP1_RAT Reviewed; 629 AA.
AC P54256;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Huntingtin-associated protein 1;
DE Short=HAP-1;
GN Name=Hap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Brain;
RX PubMed=7477378; DOI=10.1038/378398a0;
RA Li X.-J., Li S.-H., Sharp A.H., Nucifora F.C. Jr., Schilling G.,
RA Lanahan A., Worley P., Snyder S.H., Ross C.A.;
RT "A huntingtin-associated protein enriched in brain with implications for
RT pathology.";
RL Nature 378:398-402(1995).
RN [2]
RP INTERACTION WITH KALRN.
RX PubMed=9285789; DOI=10.1093/hmg/6.9.1519;
RA Colomer V., Engelender S., Sharp A.H., Duan K., Cooper J.K., Lanahan A.,
RA Lyford G., Worley P., Ross C.A.;
RT "Huntingtin-associated protein 1 (HAP1) binds to a Trio-like polypeptide,
RT with a rac1 guanine nucleotide exchange factor domain.";
RL Hum. Mol. Genet. 6:1519-1525(1997).
RN [3]
RP INTERACTION WITH DCTN1.
RX PubMed=9361024; DOI=10.1093/hmg/6.13.2205;
RA Engelender S., Sharp A.H., Colomer V., Tokito M.K., Lanahan A., Worley P.,
RA Holzbaur E.L.F., Ross C.A.;
RT "Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued
RT subunit of dynactin.";
RL Hum. Mol. Genet. 6:2205-2212(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND SELF-ASSOCIATION.
RX PubMed=9798945; DOI=10.1046/j.1471-4159.1998.71052178.x;
RA Li S.H., Gutekunst C.A., Hersch S.M., Li X.J.;
RT "Association of HAP1 isoforms with a unique cytoplasmic structure.";
RL J. Neurochem. 71:2178-2185(1998).
RN [5]
RP INTERACTION WITH DCTN1 AND HTT, AND SUBCELLULAR LOCATION.
RX PubMed=9454836; DOI=10.1523/jneurosci.18-04-01261.1998;
RA Li S.H., Gutekunst C.A., Hersch S.M., Li X.J.;
RT "Interaction of huntingtin-associated protein with dynactin P150Glued.";
RL J. Neurosci. 18:1261-1269(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9742138; DOI=10.1523/jneurosci.18-19-07674.1998;
RA Gutekunst C.A., Li S.H., Yi H., Ferrante R.J., Li X.J., Hersch S.M.;
RT "The cellular and subcellular localization of huntingtin-associated protein
RT 1 (HAP1): comparison with huntingtin in rat and human.";
RL J. Neurosci. 18:7674-7686(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10924259; DOI=10.1006/mcne.2000.0858;
RA Li S.H., Li H., Torre E.R., Li X.J.;
RT "Expression of huntingtin-associated protein-1 in neuronal cells implicates
RT a role in neuritic growth.";
RL Mol. Cell. Neurosci. 16:168-183(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HGS.
RX PubMed=12021262; DOI=10.1074/jbc.m111612200;
RA Li Y., Chin L.S., Levey A.I., Li L.;
RT "Huntingtin-associated protein 1 interacts with hepatocyte growth factor-
RT regulated tyrosine kinase substrate and functions in endosomal
RT trafficking.";
RL J. Biol. Chem. 277:28212-28221(2002).
RN [9]
RP FUNCTION.
RX PubMed=12890790; DOI=10.1523/jneurosci.23-17-06956.2003;
RA Li S.H., Yu Z.X., Li C.L., Nguyen H.P., Zhou Y.X., Deng C., Li X.J.;
RT "Lack of huntingtin-associated protein-1 causes neuronal death resembling
RT hypothalamic degeneration in Huntington's disease.";
RL J. Neurosci. 23:6956-6964(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH ITPR1.
RX PubMed=12873381; DOI=10.1016/s0896-6273(03)00366-0;
RA Tang T.S., Tu H., Chan E.Y., Maximov A., Wang Z., Wellington C.L.,
RA Hayden M.R., Bezprozvanny I.;
RT "Huntingtin and huntingtin-associated protein 1 influence neuronal calcium
RT signaling mediated by inositol-(1,4,5) triphosphate receptor type 1.";
RL Neuron 39:227-239(2003).
RN [11]
RP FUNCTION.
RX PubMed=15242649; DOI=10.1016/j.cell.2004.06.018;
RA Gauthier L.R., Charrin B.C., Borrell-Pages M., Dompierre J.P., Rangone H.,
RA Cordelieres F.P., De Mey J., MacDonald M.E., Lessmann V., Humbert S.,
RA Saudou F.;
RT "Huntingtin controls neurotrophic support and survival of neurons by
RT enhancing BDNF vesicular transport along microtubules.";
RL Cell 118:127-138(2004).
RN [12]
RP INTERACTION WITH AR.
RX PubMed=16782802; DOI=10.1093/hmg/ddl156;
RA Takeshita Y., Fujinaga R., Zhao C., Yanai A., Shinoda K.;
RT "Huntingtin-associated protein 1 (HAP1) interacts with androgen receptor
RT (AR) and suppresses SBMA-mutant-AR-induced apoptosis.";
RL Hum. Mol. Genet. 15:2298-2312(2006).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KLC2.
RX PubMed=16339760; DOI=10.1074/jbc.m509806200;
RA McGuire J.R., Rong J., Li S.H., Li X.J.;
RT "Interaction of Huntingtin-associated protein-1 with kinesin light chain:
RT implications in intracellular trafficking in neurons.";
RL J. Biol. Chem. 281:3552-3559(2006).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT THR-598 (ISOFORM A), AND INTERACTION WITH KLC2
RP AND DCTN1.
RX PubMed=16738245; DOI=10.1523/jneurosci.1251-06.2006;
RA Rong J., McGuire J.R., Fang Z.H., Sheng G., Shin J.Y., Li S.H., Li X.J.;
RT "Regulation of intracellular trafficking of huntingtin-associated protein-1
RT is critical for TrkA protein levels and neurite outgrowth.";
RL J. Neurosci. 26:6019-6030(2006).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YWHAZ; KLC2 AND DCTN1, AND
RP PHOSPHORYLATION (ISOFORM A).
RX PubMed=17166838; DOI=10.1074/jbc.m609057200;
RA Rong J., Li S., Sheng G., Wu M., Coblitz B., Li M., Fu H., Li X.J.;
RT "14-3-3 protein interacts with Huntingtin-associated protein 1 and
RT regulates its trafficking.";
RL J. Biol. Chem. 282:4748-4756(2007).
RN [16]
RP FUNCTION, AND INTERACTION WITH BDNF.
RX PubMed=19996106; DOI=10.1074/jbc.m109.073197;
RA Wu L.L., Fan Y., Li S., Li X.J., Zhou X.F.;
RT "Huntingtin-associated protein-1 interacts with pro-brain-derived
RT neurotrophic factor and mediates its transport and release.";
RL J. Biol. Chem. 285:5614-5623(2010).
RN [17]
RP FUNCTION, AND INTERACTION WITH KIF5A; KIF5B; KIF5C AND GABRB3.
RX PubMed=20152113; DOI=10.1016/j.neuron.2009.12.007;
RA Twelvetrees A.E., Yuen E.Y., Arancibia-Carcamo I.L., MacAskill A.F.,
RA Rostaing P., Lumb M.J., Humbert S., Triller A., Saudou F., Yan Z.,
RA Kittler J.T.;
RT "Delivery of GABAARs to synapses is mediated by HAP1-KIF5 and disrupted by
RT mutant huntingtin.";
RL Neuron 65:53-65(2010).
RN [18]
RP FUNCTION, AND INTERACTION WITH BDNF AND SORT1.
RX PubMed=21357693; DOI=10.1074/jbc.m110.195347;
RA Yang M., Lim Y., Li X., Zhong J.H., Zhou X.F.;
RT "Precursor of brain-derived neurotrophic factor (proBDNF) forms a complex
RT with Huntingtin-associated protein-1 (HAP1) and sortilin that modulates
RT proBDNF trafficking, degradation, and processing.";
RL J. Biol. Chem. 286:16272-16284(2011).
RN [19]
RP FUNCTION, AND INTERACTION WITH APP.
RX PubMed=22731248; DOI=10.1111/j.1471-4159.2012.07845.x;
RA Yang G.Z., Yang M., Lim Y., Lu J.J., Wang T.H., Qi J.G., Zhong J.H.,
RA Zhou X.F.;
RT "Huntingtin associated protein 1 regulates trafficking of the amyloid
RT precursor protein and modulates amyloid beta levels in neurons.";
RL J. Neurochem. 122:1010-1022(2012).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [21]
RP FUNCTION, AND INTERACTION WITH BDNF.
RX PubMed=23532844; DOI=10.1074/jbc.m112.420786;
RA Tuz K., Hsiao Y.C., Juarez O., Shi B., Harmon E.Y., Phelps I.G.,
RA Lennartz M.R., Glass I.A., Doherty D., Ferland R.J.;
RT "The Joubert syndrome-associated missense mutation (V443D) in the Abelson-
RT helper integration site 1 (AHI1) protein alters its localization and
RT protein-protein interactions.";
RL J. Biol. Chem. 288:13676-13694(2013).
CC -!- FUNCTION: Originally identified as neuronal protein that specifically
CC associates with HTT/huntingtin and the binding is enhanced by an
CC expanded polyglutamine repeat within HTT possibly affecting HAP1
CC interaction properties. Both HTT and HAP1 are involved in intracellular
CC trafficking and HAP1 is proposed to link HTT to motor proteins and/or
CC transport cargos. Seems to play a role in vesicular transport within
CC neurons and axons such as from early endosomes to late endocytic
CC compartments and to promote neurite outgrowth. The vesicular transport
CC function via association with microtubule-dependent transporters can be
CC attenuated by association with mutant HTT. Involved in the axonal
CC transport of BDNF and its activity-dependent secretion; the function
CC seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP
CC trafficking and seems to facilitate APP anterograde transport and
CC membrane insertion thereby possibly reducing processing into amyloid
CC beta. Involved in delivery of gamma-aminobutyric acid (GABA(A))
CC receptors to synapses; the function is dependent on kinesin motor
CC protein KIF5 and is disrupted by HTT with expanded polyglutamine
CC repeat. Involved in regulation of autophagosome motility by promoting
CC efficient retrograde axonal transport. Seems to be involved in
CC regulation of membrane receptor recycling and degradation, and
CC respective signal transduction, including GABA(A) receptors, tyrosine
CC kinase receptors, EGFR, IP3 receptor and androgen receptor. Among
CC others suggested to be involved in control of feeding behavior
CC (involving hypothalamic GABA(A) receptors), cerebellar and brainstem
CC development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis
CC (involving hypothalamic NTRK2/TrkB), and ITPR1/InsP3R1-mediated Ca(2+)
CC release (involving HTT and possibly the effect of mutant HTT). Via
CC association with DCTN1/dynactin p150-glued and HTT/huntingtin involved
CC in cytoplasmic retention of REST in neurons. May be involved in
CC ciliogenesis. Involved in regulation of exocytosis. Isoform A but not
CC isoform B seems to be involved in formation of cytoplasmic inclusion
CC bodies (STBs). In case of anomalous expression of TBP, can sequester a
CC subset of TBP into STBs; sequestration is enhanced by an expanded
CC polyglutamine repeat within TBP. {ECO:0000269|PubMed:10924259,
CC ECO:0000269|PubMed:12021262, ECO:0000269|PubMed:12873381,
CC ECO:0000269|PubMed:12890790, ECO:0000269|PubMed:15242649,
CC ECO:0000269|PubMed:16339760, ECO:0000269|PubMed:16738245,
CC ECO:0000269|PubMed:17166838, ECO:0000269|PubMed:19996106,
CC ECO:0000269|PubMed:20152113, ECO:0000269|PubMed:21357693,
CC ECO:0000269|PubMed:22731248, ECO:0000269|PubMed:23532844}.
CC -!- SUBUNIT: Self-associates. Interacts with HTT/huntingtin; enhanced by an
CC expanded polyglutamine repeat within HTT. Isoform A interacts with
CC DCTN1; decreased in presence of HTT with expanded polyglutamine repeat;
CC decreased by phosphorylation of Hap1 isoform A at Thr-598. Isoform A
CC interacts with KLC2; decreased by phosphorylation of Hap1 isoform A at
CC Thr-598. Isoform A interacts with ITPR1 and APP. Isoform A interacts
CC with AR; decreased by an expanded polyglutamine repeat within AR.
CC Isoform A interacts with YWHAZ; enhanced by phosphorylation of Hap1
CC isoform A at Thr-598. Isoform A interacts with BDNF and SORT1; probably
CC forming a complex involved in proBDNF trafficking, degradation and
CC processing. Interacts with TBP, AHI1, HGS and KALRN. Interacts with
CC KIF5A, KIF5B, KIF5C and GABRB3; indicative for an HAP1:KIF5 complex
CC transporting a GABA(A) receptor as cargo. Interacts with ATXN3; in
CC STBs. Interacts with NTRK2; HAP1 stabilizes association of NTRK2 with
CC SORT1 preventing NTRK2 degradation. Interacts with CCDC113.
CC {ECO:0000250|UniProtKB:P54257, ECO:0000269|PubMed:12021262,
CC ECO:0000269|PubMed:12873381, ECO:0000269|PubMed:16339760,
CC ECO:0000269|PubMed:16738245, ECO:0000269|PubMed:16782802,
CC ECO:0000269|PubMed:17166838, ECO:0000269|PubMed:19996106,
CC ECO:0000269|PubMed:20152113, ECO:0000269|PubMed:21357693,
CC ECO:0000269|PubMed:22731248, ECO:0000269|PubMed:23532844,
CC ECO:0000269|PubMed:9285789, ECO:0000269|PubMed:9361024,
CC ECO:0000269|PubMed:9454836}.
CC -!- INTERACTION:
CC P54256; P54256: Hap1; NbExp=3; IntAct=EBI-994539, EBI-994539;
CC P54256; Q9JJ50: Hgs; NbExp=5; IntAct=EBI-994539, EBI-7092491;
CC P54256; P97924: Kalrn; NbExp=3; IntAct=EBI-994539, EBI-1397166;
CC P54256; Q14203: DCTN1; Xeno; NbExp=4; IntAct=EBI-994539, EBI-724352;
CC P54256; P42858: HTT; Xeno; NbExp=3; IntAct=EBI-994539, EBI-466029;
CC P54256; Q15154: PCM1; Xeno; NbExp=3; IntAct=EBI-994539, EBI-741421;
CC P54256-1; P54256-1: Hap1; NbExp=2; IntAct=EBI-994549, EBI-994549;
CC P54256-1; P29994: Itpr1; NbExp=2; IntAct=EBI-994549, EBI-8614640;
CC P54256-2; P54256-2: Hap1; NbExp=2; IntAct=EBI-994554, EBI-994554;
CC P54256-2; Q9JJ50: Hgs; NbExp=5; IntAct=EBI-994554, EBI-7092491;
CC P54256-2; P29994: Itpr1; NbExp=4; IntAct=EBI-994554, EBI-8614640;
CC P54256-2; P63104: YWHAZ; Xeno; NbExp=4; IntAct=EBI-994554, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9742138,
CC ECO:0000269|PubMed:9798945}. Presynapse {ECO:0000269|PubMed:9742138}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9454836,
CC ECO:0000269|PubMed:9742138}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:9742138}. Cell projection, dendrite
CC {ECO:0000269|PubMed:9742138}. Cell projection, axon
CC {ECO:0000269|PubMed:9742138}. Lysosome. Endoplasmic reticulum
CC {ECO:0000269|PubMed:9742138}. Mitochondrion
CC {ECO:0000269|PubMed:9742138}. Nucleus {ECO:0000269|PubMed:9742138}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:O35668}.
CC Early endosome {ECO:0000269|PubMed:12021262}. Cell projection, growth
CC cone {ECO:0000269|PubMed:16339760}. Note=Localizes to large
CC nonmembrane-bound cytoplasmic bodies found in various types of neurons,
CC called stigmoid bodies (STBs); STB formation is regulated by the ratio
CC of isoform A to isoform B (PubMed:9798945). In the nucleus localizes to
CC nuclear rods. {ECO:0000269|PubMed:9798945}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm
CC {ECO:0000269|PubMed:10924259}. Note=In NGF-stimulated PC2 cells isoform
CC A can move anterogradely fom neurite cell body to neurite terminal and
CC is localized to growth cone tips whereas isoform B stays in the cell
CC body. {ECO:0000269|PubMed:10924259}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cell projection, growth cone
CC {ECO:0000269|PubMed:10924259}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:10924259, ECO:0000269|PubMed:17166838}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000269|PubMed:10924259}. Presynapse
CC {ECO:0000269|PubMed:10924259}. Note=In NGF-stimulated PC2 cells isoform
CC A can move anterogradely fom neurite cell body to neurite terminal and
CC is localized to growth cone tips whereas isoform B stays in the cell
CC body (PubMed:10924259). Localization to neuronal processes and neurite
CC tips is decreased by YWHAZ (PubMed:17166838).
CC {ECO:0000269|PubMed:10924259, ECO:0000269|PubMed:17166838}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Long;
CC IsoId=P54256-1; Sequence=Displayed;
CC Name=A; Synonyms=Short;
CC IsoId=P54256-2; Sequence=VSP_004280;
CC -!- TISSUE SPECIFICITY: In the brain, especially in the olfactory bulb and
CC in the brain stem. No detectable expression in peripheral tissues such
CC as lung, testis, spleen, and small intestine.
CC -!- PTM: Isoform A is phosphorylated on Thr-598.
CC {ECO:0000269|PubMed:16738245}.
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DR EMBL; U38370; AAC52326.1; -; mRNA.
DR EMBL; U38373; AAC52327.1; -; mRNA.
DR PIR; S67492; S67492.
DR PIR; S67495; S67495.
DR RefSeq; NP_077047.1; NM_024133.2. [P54256-2]
DR RefSeq; NP_817091.1; NM_177982.1. [P54256-1]
DR AlphaFoldDB; P54256; -.
DR SMR; P54256; -.
DR BioGRID; 248077; 21.
DR CORUM; P54256; -.
DR IntAct; P54256; 26.
DR MINT; P54256; -.
DR STRING; 10116.ENSRNOP00000020603; -.
DR jPOST; P54256; -.
DR PaxDb; P54256; -.
DR PRIDE; P54256; -.
DR GeneID; 29430; -.
DR KEGG; rno:29430; -.
DR UCSC; RGD:68327; rat. [P54256-1]
DR CTD; 9001; -.
DR RGD; 68327; Hap1.
DR eggNOG; KOG4360; Eukaryota.
DR InParanoid; P54256; -.
DR OrthoDB; 592923at2759; -.
DR PhylomeDB; P54256; -.
DR PRO; PR:P54256; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; TAS:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0016234; C:inclusion body; ISO:RGD.
DR GO; GO:0005770; C:late endosome; TAS:RGD.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0048403; F:brain-derived neurotrophic factor binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0045022; P:early endosome to late endosome transport; TAS:RGD.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0021979; P:hypothalamus cell differentiation; ISO:RGD.
DR GO; GO:0048311; P:mitochondrion distribution; IBA:GO_Central.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0090261; P:positive regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0032901; P:positive regulation of neurotrophin production; IDA:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; ISS:UniProtKB.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; ISS:UniProtKB.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISO:RGD.
DR InterPro; IPR006933; HAP1_N.
DR Pfam; PF04849; HAP1_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endoplasmic reticulum; Endosome; Exocytosis; Lysosome;
KW Mitochondrion; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..629
FT /note="Huntingtin-associated protein 1"
FT /id="PRO_0000083896"
FT DOMAIN 80..404
FT /note="HAP1 N-terminal"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..320
FT /note="Sufficient for interaction with KIF5B"
FT /evidence="ECO:0000269|PubMed:20152113"
FT REGION 158..262
FT /note="Interaction with TBP"
FT /evidence="ECO:0000250"
FT REGION 213..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..445
FT /note="Sufficient for self-association and interaction with
FT HD"
FT REGION 363..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..583
FT /note="Interaction with TBP"
FT /evidence="ECO:0000250"
FT REGION 563..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..300
FT /evidence="ECO:0000255"
FT COILED 328..369
FT /evidence="ECO:0000255"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 579..629
FT /note="DSPAPQQQTNMGGGIVEQQPIVPTQDSQRLEEDRATHSPSAREEEGPSGAT
FT -> GECSRRGHPPASGTSYRSSTL (in isoform A)"
FT /evidence="ECO:0000303|PubMed:7477378"
FT /id="VSP_004280"
FT MOD_RES P54256-2:598
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16738245"
SQ SEQUENCE 629 AA; 70213 MW; C23C5CB57520B574 CRC64;
MRPKDQVQSS AGDGTGSGDP ATGTPTTQPA ADPAPEPSAE PKPAPAQGTG SGQKSGSRTK
TGGSFCRSRI RGDSDAPWTR YIFQGPYGPR ATGLGTGRAE GIWKTPAAYI GRRPGVSGPE
RAAFIRELQE ALCPNPLPRK KITEDDIKVM LYLLEEKERD LNTAARIGQS LVKQNSVLME
ENNKLETMLG SAREEILHLR KQVNLRDDLL QLYSDSDDDE EDEEDEEEEE GEEEEREGQR
DQDQQHDHPY GAPKPPPKAE TLHHCPQLEA LKQKLKLLEE ENDHLREEAS HLDNLEDKEQ
MLILECVEQF SEASQQMAEL SEVLVLRLEG YERQQKEITQ LQAEITKLQQ RCQSYGAQTE
KLQQQLASEK GVHPESLRAG SHMQDYGSRP RERQEDGKSH RQRSSMPAGS VTHYGYSVPL
DALPSFPETL AEELRTSLRK FITDPAYFME RCDTRCREER KKEQGTMPPP PVQDLKPPED
FEAPEELVPE EELGAIEEVG TAEDGPAEET EQASEETEAW EEVEPEVDEA TRMNVVVSAL
EASGLGPSHL DMKYVLQQLS NWQDAHSKRQ QKQKVVPKDS PAPQQQTNMG GGIVEQQPIV
PTQDSQRLEE DRATHSPSAR EEEGPSGAT
