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 02-SEP-2026, entry version 158. 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 CFAP263. 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}. 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; U38370; AAC52326.1; -; mRNA. DR EMBL; U38373; AAC52327.1; -; mRNA. DR PIR; S67492; S67492. DR PIR; S67495; S67495. DR RefSeq; NP_077047.2; NM_024133.4. DR RefSeq; NP_817091.2; NM_177982.3. DR AlphaFoldDB; P54256; -. DR SMR; P54256; -. DR BioGRID; 248077; 21. DR CORUM; P54256; -. DR FunCoup; P54256; 202. DR IntAct; P54256; 26. DR MINT; P54256; -. DR STRING; 10116.ENSRNOP00000020603; -. DR iPTMnet; P54256; -. DR PhosphoSitePlus; P54256; -. DR jPOST; P54256; -. DR PaxDb; 10116-ENSRNOP00000020603; -. DR GeneID; 29430; -. DR KEGG; rno:29430; -. DR UCSC; RGD:68327; rat. [P54256-1] DR AGR; RGD:68327; -. DR CTD; 9001; -. DR RGD; 68327; Hap1. DR eggNOG; KOG4360; Eukaryota. DR InParanoid; P54256; -. DR PhylomeDB; P54256; -. DR PRO; PR:P54256; -. DR Proteomes; UP000002494; Unplaced. 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:0005829; C:cytosol; 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; EXP:UniProtKB. 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; EXP:UniProtKB. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD. DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO. DR GO; GO:0098793; C:presynapse; EXP:UniProtKB. 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: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:0021979; P:hypothalamus cell differentiation; ISO:RGD. DR GO; GO:0008104; P:intracellular protein localization; 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:0050850; P:positive regulation of calcium-mediated signaling; IDA: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: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: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 InterPro; IPR051946; Intracell_Traff-Reg. DR PANTHER; PTHR15751:SF14; HUNTINGTIN-ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR15751; TRAFFICKING KINESIN-BINDING PROTEIN; 1. DR Pfam; PF04849; HAP1_N; 1. DR SMART; SM01424; 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 1..12 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..31 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..44 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 52..62 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 215..236 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 237..249 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 388..399 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 480..495 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 505..528 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 606..623 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 //