wanglab/gogpt-training-data huggingface dataset:
Protein: WD repeat-containing protein 19 (Intraflagellar transport 144 homolog) (Q3UGF1)
Organism: Mus musculus (Mouse)
Function: As component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in cilia function and/or assembly (Probable). Essential for functional IFT-A assembly and ciliary entry of GPCRs (By similarity). Associates with the BBSome complex to mediate ciliary transport.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:16957054}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16957054}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19208653}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q8NEZ3}. Note=Localizes to photoreceptor connecting cilia, to the base of motile cilia in brain ependymal cells and to the base of and along primary cilia in cultured kidney inner mnedullary collecting duct (IMCD) cells. Localizes at the sperm neck and flagellum (By similarity). {ECO:0000250|UniProtKB:Q8NEZ3, ECO:0000269|PubMed:16957054, ECO:0000269|PubMed:19208653}.
Interaction partners:
- Tetratricopeptide repeat protein 21B
- Intraflagellar transport protein 43 homolog
- Intraflagellar transport protein 140 homolog
- Intraflagellar transport protein 122 homolog
- WD repeat-containing protein 35
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 56
Sequence:
MKRVFSLLEKSWLGAPIQFAWQKSSGNYLAVTGADYIVKIFDRHGQKRSEISLPGNCVTMDWDKDGDILAVIAEKSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKIGSFLAVGTIKGNLLIYNHQTSRKIPVLGKHTKKITCGCWNSENLLALGGEDKMITVSNQEGDTIRQTPVKSEPSDIKFSMSKTDERISSAENTISAVVGKKMLFLFHLNEPDNPVDLEFQQAYGNIVCYSWYGDGYIMIGFSRGTFLAISTHFPEVGQEIFKARDHKDNLTSVALSQTLNKAATCGDNCIKIHDLTELRDMYAIINLDDENKGLGTLSWTDDGQLLALSTQRGSLHVFLTKLPILGDACHTRIAYLTSLLEVTVANLIEGEPPITVSVDVEPTFVAVGLYHLAVGMNNRAWFYVLGENVVKKLKDVEYLGTVASICLHSDYAAALFEGKIQLHLIENEMLDAQEERETRLFPAVDDKCRILCHALTSDFLIYGTDTGIIHYFFIEDWQFVNDYRHPVGVKKLFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWENWPMDKGVFIAYDDDKVYTYAFHKDTIQGSKVILAGSTKLPFSHKPLLLYNGELTCQTQSGKINSIYLSTHSFLGSMKDTEPTDLRQMLTQTLLLKRFSDAWDICKMLNDRTSWSELAKACLHHMEVEFAIRVSRTMGDVGTVMSLEQIKGIEDYNLLAGHLAMFTNDFNLAQDLYLASNCPVAALEMRRDLQHWDSALQLAKRLAPDQIPFISKEYAIQLEFTGDYVNALAHYEKGITGDNKEHDEVCLAGVAQMSIRMGDIRRGANQALKHPSRVLKRDCGAILENMKQFSEAAQLYEKGQYYDRAASVYIRCKNWAKVGELLPHVSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWNSVIRIYLDHLNNPEKAVSIVRETQSLDGAKMVARFFLQLGDYGSAIQFLVLSKCNNEAFTLAQQHNKMEIYADIIGAEDTTNEDYQSIALYFEGEKRHFQAGKFFLLCGQYSRALKHFLKCPSSEDNVAIEMAIETVGQAKDELLTNQLIDHLMGESDGMPKDAKYLFRLYMALKQYREAARTAIIIAREEQSAGNYRNAHDVLFSMYAELKAQKIKIPSEMATNLMILHSYILVKIHVKSGDHMKGARMLIRVANNISKFPSHIVPILTSTVIECHRAGLKNSAFSFAAMLMRPEYRNKIDAKYKKKIEAMVRRPDTSETEEATTPCPFCQFLLPECELLCPGCKNNIPYCIATGRHMLKDDWTMCPHCGFPALYSEFKILLNSESTCPMCSERLNSSQLKKITDCSQYLRTEME
Protein: 2-hydroxyacid dehydrogenase homolog 2 (EC 1.1.1.-) (Q9P7Q1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Probable L-lactate dehydrogenase
- Pyruvate kinase
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Putative D-lactate dehydrogenase C713.03, mitochondrial
- Probable hydroxyacylglutathione hydrolase SPCC13B11.03c
- Probable hydroxyacylglutathione hydrolase glo2
- Pyruvate carboxylase
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- NAD-dependent malic enzyme
- Putative glutathione-independent glyoxalase hsp3105
Sequence:
MRVVLFSSQSYDRGPFEEANKTFNHEIIYHNFSLNKDTVSLAGKAQVVCVFVNDQVDADTLKALAENGVKLVALRCGGYNNVNLKAASEYKITVVHVPSYSPFAVSEFTVGLLLSLNRKIHRAYVRVREDDFNIVGLLGCDIHGKTVGVIGTGKIGSNVAKCFKMGFGCDVLAYDINPDKKLENYGVQFVEQNEVLKKADFLCLHCPLTPSTTHIVNSDSLALMKKGVTIVNTSRGGLIDTKALVDAIDSGQVGGCAIDVYEGERNLFYKDLSNEVIKDSTFQRLVNFPNVLVTSHQAFFTTEALCSIAHTTLKSASDFYTNSLDESVIANK
Protein: Probable acetyl-coenzyme A synthetase (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme) (P78773)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable citrate synthase, mitochondrial
- Acetyl-CoA acetyltransferase
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Putative aldehyde dehydrogenase-like protein C922.07c
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- Acetyl-CoA hydrolase
- 2-isopropylmalate synthase
- Homocitrate synthase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MTKNPVDHTLIIEPPVRLHGDPTVPKPNIASLDEYKRMYEESINDPSTFWGNMARDMMTWDKQFSTVVQGSIDKADSAWFADGAISPCYNLVDRHAIARPDAVALIYEADEPNQGRYITYRELLASVSQCAGALQSMGVGMGDRVAIYMPMIPETIIAMLAIVRLGAIHSVIFAGFSAESVADRVNDSECKVIITADESHRGGKRIPLKGVVNKALTECPTIKKVLVFQRSAEPTASMVEGRDVWWHDIIPKFPRYCPPAVVNPEHPLFLLYTSGSTGKPKGVVHCTGGYLLGAAATCKYVFDLHPTDRMGCAGDVGWITGHTYIVYGPLMLGAATLVFESTPAYPDYSRYWSVVERHRLTQWYIAPTAIRLLQRAGNEFVKHDRSSLRVLGSVGEPIAPESFMWYYEVVGEKRCAVADTYWQTETGSHIVTSLGPVTPMKPGSATLPFFGIDAVIIDPLTGKIIEGNDVEGVLAIRSPWPSAARTVWRGHDRYIDTYLKPYPGFYFTGDGATRDKDGYIWIRGRVDDVVNISGHRLSTAEIEAALLSHDAVAESAVVGVHDELTGQAVNAFILLKPGYEATVELEKELIMAVRSTIGPFASPRKLIFSDLPKTRSGKIMRRILRKILAGEVDQIGDLSTLADPKVVEHIIHAVHYAHQKKP
Protein: Protein S40-1 (AtS40-1) (Q9C7N7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20238146}.
Interaction partners:
Sequence:
MSEEFDESEIIFSDNYFPIRRREDGNEKENNRPVDFRENSERVWNKSSRRSKTTPLPSAVTAFSSSLPVNIPMRRYSTEEEYSDDDGGRKMIPPHLIVGRRMEGGQMAFSVCTGNGRTLKGRDLSRVRNSVLKLTGFLEA
Protein: Alpha-galactosidase A (EC 3.2.1.22) (Alpha-D-galactosidase A) (Alpha-D-galactoside galactohydrolase) (Galactosylgalactosylglucosylceramidase GLA) (Melibiase) (Agalsidase) (P06280)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of glycosphingolipids and participates in their degradation in the lysosome.
Subcellular location: Lysosome.
Interaction partners:
- Beta-galactosidase
- Galactocerebrosidase
- Arylsulfatase A
- Maltase-glucoamylase
- Sucrase-isomaltase, intestinal
- Lactosylceramide 4-alpha-galactosyltransferase
- Lysosomal alpha-glucosidase
- Beta-hexosaminidase subunit beta
- Beta-hexosaminidase subunit alpha
- Probable maltase-glucoamylase 2 pseudogene)
Sequence:
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERFMCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQRDSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFGYYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVYSCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDLRHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWAVAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWTSRLRSHINPTGTVLLQLENTMQMSLKDLL
Protein: Protein CARMIL (dDcarmil) (Capping protein, arp2/3 and myosin I linker) (Leucine-rich repeat-containing protein p116) (p116) (Q95VZ3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Serves as the scaffold for the assembly of a complex that links key players in the nucleation and termination of actin filament assembly with a ubiquitous barbed end-directed motor. This complex is composed of at least capping proteins (acpA and acpB), the Arp2/3 complex, type I myosins (myoB and myoC) and carmil. It has at least a modest ability to activate Arp2/3-dependent actin nucleation. CARMIL localizes along with the Arp2/3 complex, myoB, and myoC in the leading edge of cells and it plays a significant role in the structure and function of these actin-rich cellular extensions.
Subcellular location: Cell projection, pseudopodium {ECO:0000269|PubMed:11425877}. Note=Found in dynamic actin-rich cellular extensions, including the leading edge of cells undergoing chemotactic migration, and dorsal, cup-like, macropinocytic extensions.
Interaction partners:
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
- Myosin IB heavy chain
Sequence:
MSEEISPNDRKFITNLLTQKNQESLLLSIGDKISKKKNKKPSKRIILITKNRIFFLKPSQNKVKKDIHLLDIQEIKSSTSNEFTIVAKVDNKQFSYGLITNKTDEIINQIRVTFNHQFFGCPEESTFKCTDIKDSRLVEIEQKDLPCGGFVETYQSICDHLGVPPRDDICWDMTNIISSKNIRSFNIGEIELPTSAGDTIRCLLGALKYNNYFKSFNFNNYTFNKEQFGYLAEVLKCNSTVEDLSLNNVGLKHDTMPIIATALSSNKNLALTAIDISNNQIEDKGMTAFSSYVASSLRGIASLDVSNTNCNKAGISVLTNALKKNIKMSSTLSYLNLSGNKMEADGSAGLSSFLASPNTLKTLNISNTTPSMETIVGALVIGCAELKTIDISDNKLTKKEVPHLVRFIGASSTLKHFNLSGTKVPVENLKELVVAITSNIYLQDVVLDLKNNDLGIAGARMLASLATDKLSNVIYLDVSENDFGDEGVSVICDGFVGNSTIKKLILNGNFKQSKTKSRPSAIESVISLLESECPLETLHMTVGNSKSPLKADILSLIYSLATNSSLLELDISGHQMGPKGAIGLGKALQTNKTLHTLIWDDNLTTAIGFAGFQVGLERNLTLKNMPTPLNDIIQCHREPKFQQIWKEIDSCINRNQSPTRAFEGNGGNSIGATNLSFLASGQQQGVEKLLNKIKSIGRKVTDPNNILIVKDAESTEKVIGGIHLIKESIHASLEMELNQKLKDFVQVVNDVINAKKNEMTQQILESMQNTFQSMDGPTIKRLATTIQYGSKDVDEQQIHSTLVKGAGAELSSRAHECFISALDIASDYTYEKITIGLDSVFKDLILEESQAQNEASGATPIPDSPVPTRSPQPTSPPITPQPTPTTNVPPVTAPRTGAAAPLKPANPPPVSTTTTPPVSTTPKPTQPVSKFGAKLSANSAVAEAIARNMGGGAPPIRKPVAPEPEPEPVTPTKDVTPLKSKPVVAPRSTPTTSTPTKTPVKKPSGPSVPGSLSDAPESDSAELTHVTASRPHIASKRKPPTRRPRPPTEN
Protein: Probable NAD(P)H dehydrogenase (quinone) FQR1-like 3 (EC 1.6.5.2) (Q9LUX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of electrons from NADH and NADPH to reduce quinone to the hydroquinone state.
Interaction partners:
- 2-phytyl-1,4-beta-naphthoquinone methyltransferase, chloroplastic
- Nitroreductase family protein
Sequence:
MAVTKIYIVYYSLHGHVETMAREVLRGVNSVPDVEATLWQVPETLPEKILEKVKAVPRPDDVPDIRPEQLAEADGFMFGFPSRFGVMASQVMTFFDNTNDLWTTQALAGKPAGIFWSTGFHGGGQELTALTAVTKLAHHGMIFVPVGYTFGKSMYEMGEVKGGSPYGSGTYAADGSREPTELEIQQANYHGKYFAGIAKKLKKRSPV
Protein: Noncompact myelin-associated protein (Myelin protein of 11 kDa) (MP11) (F1M2Z5)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in myelin formation.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Localized mainly in the Schmidt-Lanterman incisures and paranodes of noncompact peripheral nerve myelin. {ECO:0000269|PubMed:18650334}.
Interaction partners:
Sequence:
MTTATTLGDAVFSLNMTRGEDILYKSSGAIVAAIVVVVVIIVTLVLILLKMYNRRMRTRRELEPKSPKPPVPPALDPNSNGSQQPAAVTSDPADVPVETR
Protein: 3'-phosphate/5'-hydroxy nucleic acid ligase (EC 6.5.1.8) (Q9HT99)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable peptide chain release factor
- Amino acid abc transporter substrate-binding paat family protein
- Large ribosomal subunit protein bL25
- Outer membrane protein OprM
- RNA 3'-terminal phosphate cyclase
- Transcriptional regulator RtcR
- Probable citrate transporter
- Methionyl-tRNA formyltransferase
Sequence:
MGNYIKPLSAGVALIASDSTWIEGKAIQQLQTTAELDGMCRVVGLPDLHPGRGYPVGAAFFSVGRFYPALVGNDIGCGMALWETGLALGKLSADKLEKRLGNLDLPLDETWSDCIEALDLPAREHWRALGTIGGGNHFAELQQVETVFDQAALHALGLDADRLQLLVHSGSRGLGQAILQEHVSLHGHAGLLDGSLEASAYLARHADALRFAEGNRQLIARRILERLRCDGLELLDINHNLVVPAQVDGVDGWLHRKGATPADQGVLVIPGSRGDYSYLVEPVPSAQSLFSLAHGAGRKWQRGECRERLAARFSVDQLGRTRLGSRVICGDRQLIYEEAPEAYKGIDSVVGALLEAGLLRLVARLKPVLTYKTRGECCR
Protein: Golgi phosphoprotein 3 (Coat protein GPP34) (Trans-Golgi protein GMx33) (Q9ERE4)
Organism: Rattus norvegicus (Rat)
Function: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Mitochondrion intermembrane space. Cell membrane {ECO:0000250}. Endosome {ECO:0000250}. Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. {ECO:0000305}.
Interaction partners:
- Unconventional myosin-XVIIIa
- Phosphatidylinositol-3-phosphatase SAC1
- Proprotein convertase subtilisin/kexin type 9
Sequence:
MTSLTQRSSGLVQRRTEASRNAADKERAAGGGGGNGEDEAQSRRDEQDDDDKGDSKETRLTLMEEVLLLGLKDREGYTSFWNDCISSGLRGCMLIELALRGRLQLEACGMRRKSLLTRKVICKSDAPTGDVLLDEALKHVKETQPPETVQNWIELLSGETWNPLKLHYQLRNVRERLAKNLVEKGVLTTEKQNFLLFDMTTHPLTNNNIKQRLIKKVQEAVLDKWVNDPHRMDKRLLALIYLAHASDVLENAFAPLLDEQYDLATKRVRQLLDLDPEVECLKANTNEVLWAVVAAFTK
Protein: Transcriptional regulator (Q9CG39)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Interaction partners:
Sequence:
MNFGQNLKKLRKNAKLTQSQLAEKLGMKQNAYVLWEQKSTNPTLEILEKLADIYDLPIQELIKETDNNAEKQLIDNYRSLTGEQQESVINFTDFLIEQNKTEIINLKTYRRSSLDYAIVEDEELSAGFGQSQSNTGGHYKAYTSETLGRYDGAARVKGESMEPEFPNFSIATFLHTGFGRSGDIYAIAEGDLGEERLYIKQVFEEEDGQFRIHSLNPDPQYKDFYLGQEDNFRIIGPVVDNFEEIEESQIID
Protein: Coiled-coil domain containing 90B (E9PKQ5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MNSRQAWRLFLSQGRGDRWVSRPRGHFSPALRREFFTTTTKEGYDRRPVDITPLEQRKLTFDTHALVQDLETHGFDKTQAETIVSALTALSNVSLDTIYKEMVTQAQQEITVQQLMAHLDAIRKDMVILEKSEFANLRAENEKMKIELDQVKQQLMTFFLTSCCFISYSLQIKKSNLWKQLQNLQKRILKPKVLFQRPVIKLTLKLLP
Protein: DNA-binding protein Rfx5 (Regulatory factor X 5) (Q9JL61)
Organism: Mus musculus (Mouse)
Function: Activates transcription from class II MHC promoters. Recognizes X-boxes. Mediates cooperative binding between RFX and NF-Y. RFX binds the X1 box of MHC-II promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858, ECO:0000269|PubMed:10779326}.
Interaction partners:
- Regulatory factor X-associated protein
- DNA-binding protein RFXANK
- MHC class II transactivator
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MAEDKPDAKSPKTGARPQGGADAGEPTTLLQRLRGTISKAVQNKVEGILQEVQKFSDNDKLYLYLQLPSGPSVGEKSSEPSLLSNEEYMYAYRWIRNHLEEHMDTCLPKQSVYDAYRKYCESLACCRPLSTANFGKIIREIFPDIKARRLGGRGQSKYCYSGIRRKTLVSMPPLPGLDLKGSESPEMGPEVSPAPRDELVEAACALTCDWAERILKRSFSSIVQVARYLLQQHLISARSAHAHVLKAGGLAEEDERAPRERSLCKSKNVVESLEGGGPKKPERPAQPPKEQEARAGTDLPGRAERKKSVIDSSVPAASKPQVNALVARLPVLLPRAPRSLITPISGTLKVATLPLPTRVGGPQTAVPIINMILPPVPTLSGAGPGPGPGLGPRFGPGPGLGPGPGPGLGAGLGPGLGPGLGAGPGPGLGAGLGAGLGLGPGRVPPRAPILPRGAENREVGISSDPRPHDKGIKRTAEVPLSEASGQDPPVKEMKHETQDTTVSEAKRKRGRPRKKPGGSGERNATPEKSAAIVNSPRSPRLLWETWGSKRENNFIGRPEGPGPGGEAERETVLVQGQQDGAVSKGERSLSSQEAKEAEDKIPPVTSKVSVIKGRIQKEALQLVKGEADAATQGNKGLKGRVLQSSLTPEHKDPKATPP
Protein: Antizyme inhibitor 2 (AzI2) (Arginine decarboxylase) (ADC) (ARGDC) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) (Q96A70)
Organism: Homo sapiens (Human)
Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking.
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region. Membrane {ECO:0000250}. Cytoplasmic vesicle. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Golgi apparatus, cis-Golgi network {ECO:0000250}. Golgi apparatus, trans-Golgi network. Cytoplasmic granule. Cell projection, axon. Cell projection, dendrite. Perikaryon. Note=Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in an antizyme-dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules (By similarity). Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}.
Interaction partners:
- Guanidino acid hydrolase, mitochondrial
- Arginase-2, mitochondrial
- Arginase-1
- Ornithine decarboxylase antizyme 3
- Glycine amidinotransferase, mitochondrial
- Ornithine decarboxylase antizyme 2
- Ornithine decarboxylase antizyme 1
- Nitric oxide synthase 1
- Nitric oxide synthase 3
- Argininosuccinate lyase
Sequence:
MAGYLSESDFVMVEEGFSTRDLLKELTLGASQATTDEVAAFFVADLGAIVRKHFCFLKCLPRVRPFYAVKCNSSPGVLKVLAQLGLGFSCANKAEMELVQHIGIPASKIICANPCKQIAQIKYAAKHGIQLLSFDNEMELAKVVKSHPSAKMVLCIATDDSHSLSCLSLKFGVSLKSCRHLLENAKKHHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFEMGTELGHKMHVLDLGGGFPGTEGAKVRFEEIASVINSALDLYFPEGCGVDIFAELGRYYVTSAFTVAVSIIAKKEVLLDQPGREEENGSTSKTIVYHLDEGVYGIFNSVLFDNICPTPILQKKPSTEQPLYSSSLWGPAVDGCDCVAEGLWLPQLHVGDWLVFDNMGAYTVGMGSPFWGTQACHITYAMSRVAWEALRRQLMAAEQEDDVEGVCKPLSCGWEITDTLCVGPVFTPASIM
Protein: TATA box-binding protein-like 1 (TBP-like factor) (Q7KA83)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQTAGGPSLQRKLANGDTIVLATGSKNMFLTSSENKANLPTVASNGNGLITAKMDLLEEEVMQSITVIDDDDEEKKEVAEDEEESSNNAKPIDLHQPIADNEHELDIVINNVVCSFSVGCHLKLREIALQGSNVEYRRENGMVTMKLRHPYTTASIWSSGRITCTGATSESMAKVAARRYARCLGKLGFPTRFLNFRIVNVLGTCSMPWAIKIVNFSERHRENASYEPELHPGVTYKMRDPDPKATLKIFSTGSVTVTAASVNHVESAIQHIYPLVFDFRKQRSAEELQHLRQKQRLQAGGDPHELEKNVLADNKTASLDNIFVNTTAAHSKSSSNDQTSAPATILSSTVDSMPRLKQMVNYHQMMKQTQEERRHIMFNGEKANPASTSSAAAAPSTSSSSSSSGDNICANARRRATECWATKLQNKRPRYNDPGTTGTINAASSTASAATSSLASQATHLRNPLKTAALANARMLGAKVTTCTRNSIIVQQPQRIQMQQQQQQLQPQQQQTSFSPSEFDVDDLIEEEENNELDMPF
Protein: Mnt, isoform D (Mnt, isoform H) (Q9W4Q7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSGIGGIGVLLEAAQFLEQHEKLPQAGGGGGSALGVGVALPQQQQQTVHCKSNSIINNNNSSQHNRNSSSSSNGIIATPPFTNGNGNGTVGVGNASAIFNVSVNANGNGLSNGHSSPRSQLAAAATAHDYEYSAAGVANGHSEGRPHVSEDDNSSINNNNNNNNTHPPQQQQHSAAGRTTTTRITTTPAILTKLMGNSVTPASNTTSLPTSTPSVTTSPPASTDFMLLAAAATSATSATPATATSAAATAASNPAKRKLSSIAEIPSKFLVVSDAKGVYSAHTHPNGFAADSLGVDNNETMIKKLMQNLQSQRQQQSLQQLRSLRPAEISLTPPPAATRKVDISNSRTRSYSLSNVSAARDQQDHPQHQQHANHMQIQQHYGYMRSNIGGVIYGLHKDSADSAASSACGAGAGAAAVGMSIASSAPAAGSQLSAHHHTGHGGRRRTTSSNSNGAGTREVHNKLEKERRAQLKECYDLLKKVLPMGDEDRKKTSNLTILDTAHKYVNSLSHEVCEQEAKIEKLAKQKIELQKRLKQLSLRRESPPTDQQIIPQADKAVCLATTATTAPPTAASGHNGTTILFDAGNACATGQLTTVINKTNGGATAAASSKHNGNHTGGATTTLTPAMGIMTIKNGNGSNGNMLAISPTGGHNHQLHQHHNGSPAGSPSGIGATTGATITRGSPTPSTPSPSPSSSSSGVSLSTSFMGGSSSSSSSSSSSSSSSSSSSSSSPTQQQQIITPTATARSVGLKFHGGAGAAVPAGGGSVNGFHQADKDRNYTFLRLSAGTTAQ
Protein: Copine 1 (Q5JX61)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSKTLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGKPAGRGTITDFLGKSDPFLEFFRQGDGKWHLVYRSEVIKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAV
Protein: Myosin-8 (Myosin heavy chain 8) (Myosin heavy chain, skeletal muscle, perinatal) (MyHC-perinatal) (P13535)
Organism: Homo sapiens (Human)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-1
- Myosin-13
- Myosin-2
- Myosin regulatory light chain 11
- Myosin-7
- Myosin-9
- Myosin-10
- Myosin-4
- Myosin-14
Sequence:
MSASSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKTSVFVAEPKESYVKSTIQSKEGGKVTVKTEGGATLTVREDQVFPMNPPKYDKIEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSSAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQIITRTQAVCRGFLMRVEYQKMLQRREALFCIQYNVRAFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQSEADSLADAEERCEQLIKNKIQLEAKIKEVTERAEEEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLSKEKKALQETHQQTLDDLQAEEDKVNILTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDMENDKQQLDEKLEKKEFEISNLISKIEDEQAVEIQLQKKIKELQARIEELGEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQVELNKKREAEFQKLRRDLEEATLQHEAMVAALRKKHADSMAELGEQIDNLQRVKQKLEKEKSELKMETDDLSSNAEAISKAKGNLEKMCRSLEDQVSELKTKEEEQQRLINDLTAQRARLQTEAGEYSRQLDEKDALVSQLSRSKQASTQQIEELKHQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERSNAACAALDKKQRNFDKVLSEWKQKYEETQAELEASQKESRSLSTELFKVKNVYEESLDQLETLRRENKNLQQEISDLTEQIAEGGKQIHELEKIKKQVEQEKCEIQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHTRVVETMQSTLDAEIRSRNDALRVKKKMEGDLNEMEIQLNHANRLAAESLRNYRNTQGILKETQLHLDDALRGQEDLKEQLAIVERRANLLQAEIEELWATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLENDVSQLQSEVEEVIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVENEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQAKVKSYKRQAEEAEEQSNANLSKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKISAE
Protein: Activating signal cointegrator 1 complex subunit 3 (EC 3.6.4.13) (B8JLP0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- DEAD
- Something about silencing protein 10
- WD repeat domain 46.
- U3 small nucleolar RNA-associated protein 25 homolog
- KRR1 small subunit processome component homolog.
- Nucleolar complex protein 4 homolog
- NOP14 nucleolar protein homolog
- rRNA-processing protein FCF1 homolog
- EMG1 N1-specific pseudouridine methyltransferase.
- DDB1- and CUL4-associated factor 13
Sequence:
MGRLRKKHNWKGRQQSTSVQTAAADRQTNVQVEIQDGAVLKGVDDCNALVLPATKTKKQKVERPVTKKKALTKKQRKNLEKVLEQKDKKAHRAEVLSKLAEVQLPEAELKLLYTTAKLGTGGKLYHIKESVNEGQDGGSSSVKISSLSGANRKRRREADEEEEENESEMSESSEDDDDSEESDSSEEEKEKISEEKHTEEQQQQVLKEETKPKEADMKEEKKAETWTKEDCKPAVFIPVERLPEIQEARLRLPVLAEEQIIMEAVKDHECVVLCGETGSGKTTQVPQFLYEAGFASSGGIIGVTEPRRVAAISMSHRVATEMNLSSGVVSYQIRYEGNVTENTKIKVMTDGVLLKEIQRDFLLQKYSVIIIDEAHERSVYTDILIGLLSRIVPLRNKKGLPMKLIIMSATLRVEDFTENKRLFSSPPPVIKVEARQFAVTVHFNKRTPMDDYTGETFRKICKIHRMLPPGGILVFLTGQAEVHSVCRRLRKAFPYKPNREHTDMMETEEDLKKSKRAKKKNVSLPRINLDNYSALPVDEGDEDRQAGIDEDDGEGSDLELELGDHPDTDHEEKADPSIPLYVLPLYSLLAPEQQAKVFRPPPAGSRLCVVATNVAETSLTIPGIKYVVDCGRVKKRFYDRVTGVSSFKVTWISQASANQRAGRAGRTEPGHCYRLYSSAVFGDFSLFSEAEITRRPVEDLVLQMKDLNIEKVVNFPFPTPPSSEALIAAEELLISLGALEKPARHGRLSEMEKARLSCPISPLGRAMAAFPVAPRYAKMLALGRQQGCMQYIITIVSAMTVREIFEDYDRPAGSEEENVKMSGKKARSVQMRRLWAGQGASLLLGDLMVLLGAVGACEFAGLTPQFCEENGLRFKAMLEIRRLRGQLTNAVNAVCADADVYVDNKMAPPTEAQVLCLRQIVLAGLGDHIARRVQAEELLDPKWRNAYKTPLLDDPVFIHPSSALHKTLPEFVVYQEIMETTKMYMRGVCAVQDDWIPKLLPQYCHFSAPEESPAPRFCPLIGRVKCHQQSTFFRVSWKLPAIEMDYPEGLERYKLFAKFFLEGQVCPKIQKFSSCLLSSPSTMLKTWAKLQPRTEVLLTALVSEKADNRTSLEAAWRKNEKYLLSAYCQWIPESLHEEVSKIWPPIGQADPR