wanglab/gogpt-training-data huggingface dataset:
Protein: Cholinergic receptor, nicotinic, alpha 4b (Neuronal acetylcholine receptor subunit alpha-4b precursor) (Neuronal nicotinic acetylcholine receptor alpha 4 subunit) (Q0PJT8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Neuronal acetylcholine receptor subunit beta-2
- Cholinergic receptor, nicotinic, alpha 6.
- Acetylcholine receptor subunit alpha
- Cholinergic receptor nicotinic beta 3 subunit b
- Cholinergic receptor, nicotinic, alpha 2a
- Cholinergic receptor, nicotinic, beta 4
- Acetylcholine receptor subunit epsilon precursor
- Acetylcholine receptor subunit gamma precursor
- Cholinergic receptor, nicotinic, alpha 7
- Cholinergic receptor, nicotinic, beta 1
Sequence:
MRAAWRVFFLLCVHLQLAYVFSMSPAHAHAEERLLQSLFINYNKLSRPVANISDVVLVHFGLSIAQLIDVDEKNQMMTTNVWVKQEWNDYKLRWNPEEYENVTSIRIPSEIIWRPDIVLYNNADGDFAVTHLTKAQVFYNGRIKWKPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDRAKIDLISMASDVDQMDYWESGEWVIINAVGTYNIKKYECCTEIYPDITYSFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECAEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIIITVFVLNVHHRSSRTHSMPHWVRQLFLHLVPRYLFMKRPPASGKRNCGKLIEMMHKQANSQSMFLRNNILDISPQSPIPHLGPTSAAQQDQVQQDSTSPKPLFFCSSPSSQYSILQEENSQTPQTPVLSYTCAYTNSIFASSTTSFPDTLLGTLLHTIPQDGAKSTECDFQGHSAESVFMEAKESVLGAGSCQHCLTSEGTSLQKLDLDEAGRCTRHNMPSAQIFSPSSDGSTDLNAAEPVSNLSQSLLKALEGVQYIADHLRAEDSDFSVREDWKYVAMVIDRIFLWMFVLVCILGTVGLFLPPWLAGMI
Protein: Ceramide transfer protein (Collagen type IV alpha-3-binding protein) (A0A2R8Y7Q9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
Protein: Outer membrane channel OmpJ (Q747G2)
Organism: Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Interaction partners:
- Uncharacterized protein
- VCBS repeat-containing protein
- Laccase family multicopper oxidase
- IPT/TIG domain protein
- Zinc finger/thioredoxin putative domain-containing protein
Sequence:
MKKKIFAVAAAGALTAATAVPALALENEFHGMFRVNGFISNFADGASGATKITAQDPKTRNFLEQRARLLYMAKANDDLKLITHFEIDSTWGKSSYVVGRSNDGGALGADSVNIETKNVYLDFNIPSTPLNVKVGIQPISDSYKGVFINADAAAVLAAAKMGDATVALGFARLDDADTFTIGSAANRSATTPGKATRDLYIVDGKYNISKDLKVGGSYYALLADQNDTTLNFALHTIGVNAEYKFDPVTIDGFLLYQRGRTSGTAKVDFGGWAANATAKMKVGPGTLKTSFLYASGEQNANPDNSSYMGVTNETSGANGEHSFYESEMMIMFRNKYNIGDRALVYNVQNVIGGFVGYNANITSKAFAIANVGFVAADKDNTTYGNARVTGEAGHKSKYLGTELNAEVGYKVFDNLTASVQGAYVILGDYFKDTAGTAANPEDPRNPYLTRVMLNYAF
Protein: L-lactate dehydrogenase (EC 1.1.-.-) (P33232)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of L-lactate to pyruvate. Seems to be a primary dehydrogenase in the respiratory chain. To a lesser extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01559, ECO:0000269|PubMed:18473}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01559, ECO:0000269|PubMed:18473}.
Interaction partners:
- L-lactate permease
- Putative L-lactate dehydrogenase operon regulatory protein
- Quinone-dependent D-lactate dehydrogenase
- D-lactate dehydrogenase
- Lactaldehyde dehydrogenase
- Probable pyruvate-flavodoxin oxidoreductase
- Pyruvate dehydrogenase
- NADP-dependent malic enzyme
- Pyruvate kinase I
- Formate acetyltransferase 1
Sequence:
MIISAASDYRAAAQRILPPFLFHYMDGGAYSEYTLRRNVEDLSEVALRQRILKNMSDLSLETTLFNEKLSMPVALAPVGLCGMYARRGEVQAAKAADAHGIPFTLSTVSVCPIEEVAPAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPTPGARYRDAHSGMSGPNAAMRRYLQAVTHPQWAWDVGLNGRPHDLGNISAYLGKPTGLEDYIGWLGNNFDPSISWKDLEWIRDFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDIAILADSGIRNGLDVVRMIALGADTVLLGRAFLYALATAGQAGVANLLNLIEKEMKVAMTLTGAKSISEITQDSLVQGLGKELPAALAPMAKGNAA
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (A0A0G2K0J7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- General transcription factor IIF subunit 1
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase subunit beta
- General transcription factor IIF subunit 2
- DNA-directed RNA polymerase II subunit RPB4
- Transcription elongation factor spt6
- RNA polymerase II subunit J
- MLLT1, super elongation complex subunit
Sequence:
MTQHAPRKWVRSERRVKPVSEREQQCRRRPRWAPRPERPVFSFLTSVVTVRAARWVTMEAPPLAGVPTECTPAVAGAEVRCPGPAPLRLLEWKVTAGATVRIGSVLAVYEAAVSAQPAGPAPARAASGGCVRASRTERRLRSERAGVVRELCAQPGQVVAPGALLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEKLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCPQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFPGTGDVNAPPGARESQTRKKVNHSSKGADILEQALPVKDPEEGKPPGVEQSNGLGKASRELNGGEAVPGVFSSKTDEKETWSLTRASPASSSGGRELTEAPELPVSCEWDSRTAPGAHPTQGDATQGLDFDLSSDSESSESSRSEGQKSFSSASDGENEERRRRKKSPATQDRTKVPQHSGPHDTSGGRSAASPSGESGPLHPHDKVSDPDTQEEGERDSLCGLGNGSVDRKEAETESQNSEQSGVTAGESLDQSVGEEEEEDTDDDDHLIHLEEILVRVHTDYYTKYDRYLNKELEEAPDIRKIVPELKSKVLADVAVIFSGLHPTNFPVEKTREHYHATALGAKVLTQLVLSPDAPDRATHLIAARAGTEKVRQAQECKHLHVVSPEWLWSCLERWDKVEEQLFPLMDEDTRTHRDNSPAVFPDRHSMLPTALFHPTPIHSKAHPGPEVRIYDSNTGKLIRMGTQGPAPALSSAPLIHGEPSSFRAVQPHQQQMFGEELPESQDGEQPGPARRKRQPSMSETMPLYTLCKEDLESMDKEVDDILGEGSDDSESEKKKAEDQDSEQERARKPRKPRAPGTRREQPAGLPSPGERSAAGTRAPRGHKRKLNEEDAASESSGESSNDDEEGSSSEADEMAAALEAELNDLM
Protein: Growth-regulating factor 4 (OsGRF4) (Protein GRAIN LENGTH AND WIDTH 2) (Protein GRAIN SIZE ON CHROMOSOME 2) (Protein PANICLE TRAITS 2) (Transcription activator GRF4) (Q6ZIK5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that plays a role in the regulation of meristematic function in leaves, stems and inflorescences. Transcription activator that plays a regulatory role in grain development. Positively regulates grain size by promoting cell division and expansion, leading to increased grain length and width. Positively regulates the expression of genes promoting cell proliferation. Activates the expression of expansin genes to promote cell expansion and grain size. May promote grain size by activating brassinosteroid responses. Component of a network formed by the microRNA396 (miRNA396), the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (Probable). Component of the miRNA396c-GRF4-GIF1 regulatory module that plays an important role in grain size determination (Probable).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU01002, ECO:0000269|PubMed:26187814, ECO:0000269|PubMed:26936408, ECO:0000269|PubMed:27107174, ECO:0000269|PubMed:27250747, ECO:0000269|PubMed:27250749}.
Interaction partners:
- Shaggy-related protein kinase GSK2
- GRF-interacting factor 1
Sequence:
MAMPYASLSPAVADHRSSPAAATASLLPFCRSTPLSAGGGGVAMGEDAPMTARWPPAAAARLPPFTAAQYEELEQQALIYKYLVAGVPVPPDLVLPIRRGLDSLAARFYNHPALGYGPYFGKKLDPEPGRCRRTDGKKWRCSKEAAPDSKYCERHMHRGRNRSRKPVETQLVAQSQPPSSVVGSAAAPLAAASNGSSFQNHSLYPAIAGSNGGGGGRNMPSSFGSALGSQLHMDNAAPYAAVGGGTGKDLRYTAYGTRSLADEQSQLITEAINTSIENPWRLLPSQNSPFPLSSYSQLGALSDLGQNTPSSLSKVQRQPLSFFGNDYAAVDSVKQENQTLRPFFDEWPKGRDSWSDLADENANLSSFSGTQLSISIPMASSDFSAASSRSTNGD
Protein: Exocyst complex component Sec6 (Q386Z3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPVPHQSNVALGELDSSQFYTAEELWPYLSETDRVVLAEEVNTAINHELAHAEDLEAVIPRLLRACTTEAQELRRAIKSMASSQMLEGHRAVQIVKESGERIQDLRELFIKQGSIIAQMNVTSGSYKQLRELHYLRSNVTSVIEWVEVLNELRYTDMYRLVEQRQFAAVYKRLCRLQLIRQTVTEELHSYPKAHQNSFDPYFEKLELVQTMFVEGVYKLFRETSVPAAIQKALKDPPRMGAVVQSIPEFTQLEECVQLCAVEITEDKGFLYSADGEPLITEAKIFEAVAACAKKLWVDDVMAEFTNPVAQGVAYLDRMKKIAPILSALEMTLIPLSSRLSLFPIVVVSLHGEVVKSLEIYADPGLEAKANDLIAASDFVRWYKEMLKDGNYSSHVDIAALDKLSACMTAGAVDGLMMHLVQLCKVCARTVLEDGNKPFRSSSGLPVTTGPKDMFAVLQQTLAGLSTAIEVDVMRQIGRACAAAIESYFSECKLLIDYDRWEEMEQRQKSGGNSGNEEWKMRRLAFLYAFCNDCSVIERNMDTVELVFVSYWNEEEGLEDNSPFIQTQDVLVDHASHYIDEVILHVERMVEGQWPDVFRSKGWYEGEDSPTRIILDTMADFIDEEFSCSFEASQLHTVTHRMMQRYIQKFLTELMEFLGDAVRHPSSKAAKDWNEFVNCFVRDIVITIDMWKARISDSRGKLISKVNKALELVKNLLAVRKPVDFDFIVQKDLLDDFGDCPTFVVRFLLLSRKKEIGEDTCNSMLALWDERIAHQRRDADDKPTTGWKQMPSFFGMLDRSLADIGKKGGLFSSSPTKKRKKAEQKRQKMEKEKRKAEQEKRLADAATAVKSKSPPAPLVPRRDSVEVVTLASVLDT
Protein: Valine N-monooxygenase 1 (EC 1.14.14.38) (Cytochrome P450 79D1) (Isoleucine N-monooxygenase 1) (EC 1.14.14.39) (Q9M7B8)
Organism: Manihot esculenta (Cassava) (Jatropha manihot)
Function: Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Can use L-valine or L-isoleucine as substrate, but not L-leucine, L-phenylalanine, L-tyrosine, D-valine or D-isoleucine.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAMNVSTTIGLLNATSFASSSSINTVKILFVTLFISIVSTIVKLQKSAANKEGSKKLPLPPGPTPWPLIGNIPEMIRYRPTFRWIHQLMKDMNTDICLIRFGRTNFVPISCPVLAREILKKNDAIFSNRPKTLSAKSMSGGYLTTIVVPYNDQWKKMRKILTSEIISPARHKWLHDKRAEEADNLVFYIHNQFKANKNVNLRTATRHYGGNVIRKMVFSKRYFGKGMPDGGPGPEEIEHIDAVFTALKYLYGFCISDFLPFLLGLDLDGQEKFVLDANKTIRDYQNPLIDERIQQWKSGERKEMEDLLDVFITLKDSDGNPLLTPDEIKNQIAEIMIATVDNPSNAIEWAMGEMLNQPEILKKATEELDRVVGKDRLVQESDIPNLDYVKACAREAFRLHPVAHFNVPHVAMEDTVIGDYFIPKGSWAVLSRYGLGRNPKTWSDPLKYDPERHMNEGEVVLTEHELRFVTFSTGRRGCVASLLGSCMTTMLLARMLQCFTWTPPANVSKIDLAETLDELTPATPISAFAKPRLAPHLYPTSP
Protein: Optineurin (FIP-2-like protein) (Q8R5M4)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8. Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation. Negatively regulates the induction of IFNB in response to RNA virus infection. Plays a neuroprotective role in the eye and optic nerve. Probably part of the TNF-alpha signaling pathway that can shift the equilibrium toward induction of cell death. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and hungtingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment. Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy) and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Recycling endosome {ECO:0000250}. Note=Found in the perinuclear region and associates with the Golgi apparatus. Colocalizes with MYO6 and RAB8 at the Golgi complex and in vesicular structures close to the plasma membrane. Localizes to LC3-positive cytoplasmic vesicles upon induction of autophagy. {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- Ras-related protein Rab-8A
- Ras-related protein Rab-8B
- Ubiquilin 2
- Huntingtin
- Sequestosome-1
- Microtubule-associated protein 1 light chain 3 beta
- RB1-inducible coiled-coil protein 1
- Next to BRCA1 gene 1 protein
- Receptor-interacting serine/threonine-protein kinase 1
Sequence:
MSHQPLSCLTEKGDSSCETPGNGPSNMVHPNLDTFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQLFEIQSKEAKERLKALSHENERLKEELGKLKEKSERPFEDITGRCGFPRTDLEQEVEQLKRQVEQEVEHLKIQVRRLQAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGEAEGAMKEMRNSAGPTRTDSISMGKCTEDARTCVEFEELTVSQLLLCLREGNQKVERLEIALREAKERISDFEKKANGHSAIETQTEGSTQKEEEDKDPESVGIEVETLNVQVASLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNRKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHDKLLQEHNKALRTIEELTKQQAEKVDKVQLQELSEKLELAEQALASKQLQMDEMKQTIAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDFEDGGSRQSLMEMQCRHGARTSDSDQQAYLFQRGAEDMSWQHGQQPRSIPIHSCPKCGEVLPDIDTLQIHVMDCII
Protein: GATOR1 complex protein DEPDC5 (DEP domain-containing protein 5) (P61460)
Organism: Mus musculus (Mouse)
Function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. The GATOR1 complex strongly increases GTP hydrolysis by RRAGA and RRAGB within RRAGC-containing heterodimers, thereby deactivating RRAGs, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling. The GATOR1 complex is negatively regulated by GATOR2 the other GATOR subcomplex in this amino acid-sensing branch of the TORC1 pathway.
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:O75140}. Cytoplasm, cytosol {ECO:0000269|PubMed:23542697}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:23542697}. Note=Localization to lysosomes is mediated by the KICSTOR complex and is amino acid-independent. {ECO:0000250|UniProtKB:O75140}.
Interaction partners:
- GATOR1 complex protein NPRL2
- GATOR1 complex protein NPRL3
- GATOR2 complex protein MIOS
- GATOR2 complex protein WDR59
- GATOR2 complex protein WDR24
- Ras-related GTP-binding protein C
- Nucleoporin SEH1
- KICSTOR complex protein SZT2
- Protein SEC13 homolog
- KICSTOR complex protein ITFG2
Sequence:
MRTTKVYKLVIHKKGFGGSDDELVVNPKVFPHIKLGDIVEIAHPNDEYSPLLLQVKSLKEDLQKETISVDQTVTQVFRLRPYQDVYVNVVDPKDVTLDLVELTFKDQYIGRGDMWRLKKSLVSTCAYITQKVEFAGIRAQAGELWVKNEKVMCGYISEETRVVFRSTSAMVYIFIQMSCEMWDFDIYGDLYFEKAVNGFLADLFTKWKEKNCSHEVTVVLFSRTFYDAKSIDEFPEINRASIQEDHKGRFYEDFYKVVVQNERREEWTSLLVTIKKLFIQYPVLVRLEQAGGFPQGDNSTSAQGNYLEAINLSFNVFDKHYINRNFDRTGQMSVVITPGVGVFEVDRLLMILTKQRMIDNGIGVDLVCMGEQPLHAVPLFKLHNRSVPRDSRLGDDYNIPHWINHSFYTSKSQLFCNSFTPRIKLAGKKSASEKTKNGRDTSLGTPKESENTLPIQVDYDAYDAQVFRLPGPSRAQRLATCRSVREQENHSRKSASSCDVSSSPSLPSRALPTEEVRSQASDDSSLGKSTNILMIPNPHLHQYEVSSSLGYTSTRDVLENMIEPPQRDSSAPGRFHVGSAESMLHVRPGGYTPQRALINPFAPSRMPMKLTSNRRRWMHTFPVGPSGEAIQIHHQTRQNMAELQGSRQRDPTHSSAELLELAYHEAAGRHSTSRQPGDSMSLNFSGTEELSVSLLSNSSTGVNPRTQNKDSLEDSVSTSPDPMPGFCCTVGVDWKSLTTPACLPLTTDYFPDRQGLQNDYTEGCYDLLPEADMDRRDEEGVQMTAQQVFEEFICQRLMQGYQIIVQPKTQKPNTTVPPPLSSSPLYSRGLVSRNRPEEEGQYWLSMGRTFHKVTLKDKMITVTRYLPKYPYESAQIHYTYSLCPSHSDSEFVSCWVDFCHERLEEYKWNYLDQYICSAGSEDFSLIESLKFWRTRFLLLPACVTATKRITEGEVHCDIYGDKPRADEDEWQLLDGFIRFVEGLNRIRRRHRSDRMIRKGTAMKGLQMTGPISAHSLEAAGPPVGKKGTSALSALLEMEASQKSLGEQQTTVHGKSSTQPAENSSVAMTPTYVDSPRKDGAFFMEFVRSPRTASSAFYPQASVDQTAPLVLDSTSLGVSTGQPMDRGNNQTFGNSQNIEQAFPSANSGDYSSQQHVASSLTSSSTLVEILEAMKHPSTGVQLLSEQKGLSPCCFISAEVVHWLMNNVEGVQTQAMGIDIMQKMLEEQLITHASGEAWRTFIYGFYFYKIVMDKEPERVAMQQPSAPWYTAGADDFASFQRKWFEVAFVAEELVHSEIPAFLLPWLPSRPASYASRHSSFSRSFGGRSQAAALLAATVPEQRTVTLDVDVNNRTDRLEWCSCYYHGNFSLNAAFEIKLHWMAVTATVLFEMVQGWHRKATSCGFLLVPVLEGPFALPSYLYGDPLRAQLFIPLNLSCLLKEGSEHLFDSFEPETYWDRMHLFQEAIAHRFGFVQDKYSVSAFNFPAENKPQYIHVTGTVFLQLPYSKRKFSGQQRRRRNSTSSTNQNMFCEERVGYNWAYNTMLTKTWRSSATGDEKFADRLLKDFTDFCINRDNRLVTFWTNCLEKMHASAP
Protein: Suppressor protein MPT5 (Protein HTR1) (Pumilio homology domain family member 5) (P39016)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of HO by binding to the 3'-UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin modifiers and spindle pole body components. Recognizes and binds to 5'-TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor of POP2 mutation. Required for high temperature growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15024427}.
Interaction partners:
- Poly
- ATP-dependent RNA helicase DHH1
- Pumilio homology domain family member 6
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Protein SSD1
- RNA-binding protein VTS1
- Pumilio homology domain family member 4
- Protein CAF40
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- Cap-associated protein CAF20
Sequence:
MINNEPFPSADSASILTTSTSNNSLMSYNHQPQLSINSVQSLLEPVTPPPLGQMNNKRNHQKAHSLDLSGFNQFISSTQSPLALMNNTSTSNSANSFSPNPNAASNSTGLSASMANPPAILPLINEFDLEMDGPRRKSSHDFTVVAPSNSGVNTSSLIMETPSSSVTPAASLRNFSNSNNAASKCGVDNSSFGLSSSTSSSMVEISALPLRDLDYIKLATDQFGCRFLQKKLETPSESNMVRDLMYEQIKPFFLDLILDPFGNYLVQKLCDYLTAEQKTLLIQTIYPNVFQISINQYGTRSLQKIIDTVDNEVQIDLIIKGFSQEFTSIEQVVTLINDLNGNHVIQKCIFKFSPSKFGFIIDAIVEQNNIITISTHKHGCCVLQKLLSVCTLQQIFKISVKIVQFLPGLINDQFGNYIIQFLLDIKELDFYLLAELFNRLSNELCQLSCLKFSSNVVEKFIKKLFRIITGFIVNNNGGASQRTAVASDDVINASMNILLTTIDIFTVNLNVLIRDNFGNYALQTLLDVKNYSPLLAYNKNSNAIGQNSSSTLNYGNFCNDFSLKIGNLIVLTKELLPSIKTTSYAKKIKLKVKAYAEATGIPFTDISPQVTAMSHNNLQTINNENKNPHNKNSHNHNHNHNHNHAHNNNNNNNQKSHTRHFSLPANAYHRRSNSSVTNNFSNQYAQDQKIHSPQQIMNFNQNAYPSMGAPSFNSQTNPPLVSHNSLQNFDNRQFANLMAHPNSAAPIHSFSSSNITNVNPNVSRGFKQPGFMMNETDKINANHFSPYSNANSQNFNESFVPRMQYQTEGANWDSSLSMKSQHIGQGPYNQVNMSRNASISNMPAMNTARTSDELQFTLP
Protein: Transmembrane protein 39A (Q9NV64)
Organism: Homo sapiens (Human)
Function: Regulates autophagy by controlling the spatial distribution and levels of the intracellular phosphatidylinositol 4-phosphate (PtdIns(4)P) pools. Modulates (PtdIns(4)P) levels by regulating the ER-to-Golgi trafficking of the phosphatidylinositide phosphatase SACM1L.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:31806350}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPGGRRGPSRQQLSRSALPSLQTLVGGGCGNGTGLRNRNGSAIGLPVPPITALITPGPVRHCQIPDLPVDGSLLFEFLFFIYLLVALFIQYINIYKTVWWYPYNHPASCTSLNFHLIDYHLAAFITVMLARRLVWALISEATKAGAASMIHYMVLISARLVLLTLCGWVLCWTLVNLFRSHSVLNLLFLGYPFGVYVPLCCFHQDSRAHLLLTDYNYVVQHEAVEESASTVGGLAKSKDFLSLLLESLKEQFNNATPIPTHSCPLSPDLIRNEVECLKADFNHRIKEVLFNSLFSAYYVAFLPLCFVKSTQYYDMRWSCEHLIMVWINAFVMLTTQLLPSKYCDLLHKSAAHLGKWQKLEHGSYSNAPQHIWSENTIWPQGVLVRHSRCLYRAMGPYNVAVPSDVSHARFYFLFHRPLRLLNLLILIEGSVVFYQLYSLLRSEKWNHTLSMALILFCNYYVLFKLLRDRIVLGRAYSYPLNSYELKAN
Protein: Spexin (Liver regeneration-related protein LRRGT00060) (NPQ) (Neuropeptide Q) (Spexin hormone) [Cleaved into: Spexin-1; Spexin-2 (NPQ 53-70)] (M0R8L2)
Organism: Rattus norvegicus (Rat)
Function: Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release.
Subcellular location: Secreted {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed and amidated peptide. Localized extracellularly surrounding the villous trophoblastic cells. Detected in the serum (By similarity). {ECO:0000250}.
Interaction partners:
- Galanin receptor type 2
- Galanin receptor type 3
- Galanin peptides
- Galectin-2
- Galanin receptor type 1
Sequence:
MKGPSILAVAALALLLVLSVLENSSGAPQRLSEKRNWTPQAMLYLKGAQGHRFISDQSRRKELADRPPPERRNPNLQLLTLPEAAALFLASLEKPQKDEGGDFDKSKLLEDRRFYW
Protein: Corticotropin-releasing factor receptor 1 (CRF-R-1) (CRF-R1) (CRFR-1) (Corticotropin-releasing hormone receptor 1) (CRH-R-1) (CRH-R1) (P35353)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for CRH (corticotropin-releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli.
Subcellular location: Cell membrane; Multi-pass membrane protein. Endosome {ECO:0000250}. Note=Agonist-binding promotes endocytosis. {ECO:0000250}.
Interaction partners:
- Urocortin
- Corticoliberin
- Urocortin-2
- Urocortin 3.
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Corticotropin-releasing factor-binding protein
Sequence:
MGRRPQLRLVKALLLLGLNPVSTSLQDQRCENLSLTSNVSGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLISAFILRNATWFVVQLTVSPEVHQSNVAWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFVCIGWGVPFPIIVAWAIGKLHYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWRRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV
Protein: BBSome complex member BBS5 (Bardet-Biedl syndrome 5 protein) (Q8N3I7)
Organism: Homo sapiens (Human)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly.
Subcellular location: Cell projection, cilium membrane. Cytoplasm. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Note=Localizes to basal bodies. {ECO:0000250}.
Interaction partners:
- Tetratricopeptide repeat protein 8
- Protein PTHB1
- BBSome complex member BBS7
- BBSome complex member BBS1
- BBSome complex member BBS2
- BBSome complex member BBS4
- BBSome complex assembly protein BBS10
- Leucine zipper transcription factor-like protein 1
- Chaperonin-containing T-complex member BBS12
- Rab-3A-interacting protein
Sequence:
MSVLDALWEDRDVRFDLSAQQMKTRPGEVLIDCLDSIEDTKGNNGDRGRLLVTNLRILWHSLALSRVNVSVGYNCILNITTRTANSKLRGQTEALYILTKCNSTRFEFIFTNLVPGSPRLFTSVMAVHRAYETSKMYRDFKLRSALIQNKQLRLLPQEHVYDKINGVWNLSSDQGNLGTFFITNVRIVWHANMNDSFNVSIPYLQIRSIKIRDSKFGLALVIESSQQSGGYVLGFKIDPVEKLQESVKEINSLHKVYSASPIFGVDYEMEEKPQPLEALTVEQIQDDVEIDSDGHTDAFVAYFADGNKQQDREPVFSEELGLAIEKLKDGFTLQGLWEVMS