wanglab/gogpt-training-data huggingface dataset:
Protein: Type 2 DNA topoisomerase 6 subunit B-like (Meiotic topoisomerase VIB-like) (AtMTOPVIB) (Q5Q0E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11 (SPO11-1 and SPO11-2), mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.
Subcellular location: Chromosome {ECO:0000269|PubMed:26917763}. Nucleus {ECO:0000269|PubMed:28855712}. Cytoplasm {ECO:0000269|PubMed:28855712}. Note=Localizes to meiotic chromosomes from leptotene to pachytene (PubMed:26917763). Mostly present in the nucleus, but also present in the cytoplasm (PubMed:28855712). {ECO:0000269|PubMed:26917763, ECO:0000269|PubMed:28855712}.
Interaction partners:
- Meiotic recombination protein SPO11-2
- Meiotic recombination protein SPO11-1
- Putative recombination initiation defects 3
- Protein PUTATIVE RECOMBINATION INITIATION DEFECT 1
- Protein MULTIPOLAR SPINDLE 1
- Protein DOUBLE-STRAND BREAK FORMATION
- DNA topoisomerase 6 subunit A
- Meiotic recombination protein DMC1 homolog
- Meiosis-specific protein ASY1
- Pachytene checkpoint protein 2 homolog
Sequence:
MENNAPVPKLLLQLISSAFQRCRLAEDLCRLSVLLDQSTERDPPITCISIADTGIGCNLEEFQNLRCPREFNGAKIWDGLLSVKTTCFTDDEVYYYHINLDEYIANKRLKRQPSQAKNGAKFSGTEVSLSVFGSMDVLVAPIIGFFQKIIVLQILNVTLDLMVKQGTSPGNQTQYVFAVNADKTPCFTASNLERLKSGLEDYVLRHANCLDTMCDYCFSDREHLKVGSGTVCQEDKHKRVGGTMEVVIVISDLLESTQHCSRSCNGKTEVLYFDNFLPSPVPHLALSALKKIDWKKYGLILANVNDQDGHVFLEWDNFPSYVQIQIALHWYHNQYPTRQKNGPGISLLKKGIKNALDNLKAKHEGFLLSSHSRKICSYVPDLARSIAGLIFSSTDLDFQGDCLSVLGFQTQEVERDTVENYIQRKIVTVIGMNERKPQKDQEAAPFLFFDGESETSFFEDEEVEGEYYSSSLE
Protein: Nuclear receptor subfamily 2, group F, member 1 (F2Z3S9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- BCL11 transcription factor B
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
Sequence:
MAMVVSSWRDPQDDVAGGNPGGPNPAAQAARGGGGGEQQQAGSGAPHTPQTPGQPGAPATPGTAGDKGQGPPGSGQSQQHIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYTCRANRNCPIDQHHRNQCQYCRLKKCLKVGMRREAVQRGRMPPTQPNPGQYALTNGDPLNGHCYLSGYISLLLRAEPYPTSRYGSQCMQPNNIMGIENICELAARLLFSAVEWARNIPFFPDLQITDQVSLLRLTWSELFVLNAAQCSMPLHVAPLLAAAGLHASPMSADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTSDACGLSDAAHIESLQEKSQCALEEYVRSQYPNQPSRFGKLLLRLPSLRTVSSSVIEQLFFVRLVGKTPIETLIRDMLLSGSSFNWPYMSIQCS
Protein: Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Homocitrate dehydratase) (EC 4.2.1.-) (C8VG90)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Also catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Citrate synthase, mitochondrial
- 2-methylcitrate synthase, mitochondrial
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Methylisocitrate lyase, mitochondrial
- Isocitrate lyase
- ATP citrate synthase
- ATP citrate synthase
- Aconitate hydratase, mitochondrial
- Malate dehydrogenase
Sequence:
MITTRLARMGALAPKSRLLFGTRGMATVADLDKKVEMCNLEKGNYINYKKMSENLDVVRRRLTRPLTYAEKILYSHLDDPQNQDIERGKSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTVHCDHLIEAQLGGEKDLARANEINKEVYDFLASSTAKYNIGFWKPGSGIIHQIILENYAFPGGLMIGTDSHTPNAGGLAIAAIGVGGADAVDVMAGLPWELKAPKVIGVRLTGEMSGWTAPKDIILKVAGLLTVKGGTGAIIEYHGPGVNSLSATGMATICNMGAEIGATTSLFPFNDRMYDYLKATKRQQIGDFARSYAKDLREDEGAEYDQLIEINLSELEPHINGPFTPDLATPISQFKEAVKANGWPEELKVGLIGSCTNSSYEDMSRAASIAQDALDHGLKAKSIFTVTPGSEQIRATIERDGQLKTLEEFGGVILANACGPCIGQWDRKDVKKGTPNSIVSSYNRNFTGRNDANPATHAFVTSPDLVVALSIAGTLNFNPLTDTLKDKDGKEFKLKAPTGDGLPSRGYDPGRDTYQAPPTDRSSVDVAVSPSSDRLQLLAGFQPWDGKDATGIPILIKCQGKTTTDHISMAGPWLKYRGHLDNISNNMLIGAVNAENGEANKIKNVFTGEYGAVPATARDYKARGVKWVVIGDWNYGEGSSREHAALEPRHLGGLAIITRSFARIHETNLKKQGMLPLTFSDPADYDRIPPDATVDLLCTELAVDKPMTLRVHPKDGASFDVKLSHTFNESQIEWFKDGSALNTMARKSGN
Protein: E3 ubiquitin-protein ligase PUB22 (EC 2.3.2.27) (Plant U-box protein 22) (RING-type E3 ubiquitin transferase PUB22) (U-box domain-containing protein 22) (Q9SVC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that negatively regulates water stress response. May control in coordination with PUB23 a drought signaling pathway by ubiquitinating cytosolic RPN12a. Acts as negative regulator of the immunity triggered by the pathogen-associated molecular patterns (PAMPs), in association with PUB23 and PUB24. Regulates EXO70B2 ubiquitination and degradation via the 26S proteasome to attenuate PAMP-induced signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18664614}.
Interaction partners:
- Exocyst complex component EXO70B2
- 26S proteasome non-ATPase regulatory subunit 8 homolog A
- Exocyst complex component EXO70H1
- Exocyst complex component EXO70B1
- Squamosa promoter-binding-like protein 11
Sequence:
MDQEIEIPSFFLCPISLDIMKDPVIVSTGITYDRESIEKWLFSGKKNSCPVTKQVITETDLTPNHTLRRLIQSWCTLNASYGIERIPTPKPPICKSEIEKLIKESSSSHLNQVKCLKRLRQIVSENTTNKRCLEAAEVPEFLANIVSNSVDTYNSPSSSLSSSNLNDMCQSNMLENRFDSSRSLMDEALSVLYHLDTSETALKSLLNNKKGTNLVKTLTKIMQRGIYESRAYAALLLKKLLEVADPMQIILLERELFGEVIQILHDQISHKATRSAMQILVITCPWGRNRHKAVEGGTISMIIELLMDDTFSSERRNSEMAMVVLDMLCQCAEGRAEFLNHGAAIAVVSKKILRVSQITSERAVRVLLSVGRFCATPSLLQEMLQLGVVAKLCLVLQVSCGNKTKEKAKELLKLHARVWRESPCVPRNLYDSYPA
Protein: UPF0184 protein CG14818 (O97420)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein CDV3 homolog
- GM14292p
- V-type proton ATPase subunit
- LD45254p
- Putative SERF-like protein
- GEO09647p1
- Hemotin
- V-type proton ATPase subunit D 1
- GEO10215p1
- RH19679p
Sequence:
MSPKNNHDPSSSGDSGNTNVQEADLQEMEDVNNSLDALSCALDAVEQRTDDIMSQLRELLNSNREIRRLIAEENDNAPESGDDNMDGQAGSEAAPK
Protein: GDSL esterase/lipase At2g36325 (EC 3.1.1.-) (Extracellular lipase At2g36325) (Q8RWJ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MNITKLTPWFLFSCLILLSDYIKVNSSISPSSEQTQEDGFFGFKPTKLFVFGDSYADTGNTPFLIVPSWRFPNGITFPGIPTGRFSDGRVSTDYLAKYIGVRTPITYKWGKYGRPRLAVKRGMNFAYGGAGAFETMFKLVPTASVQIDSFEQLLMRNVYSPADLNSSVAFFSIIGNDYLTYDRRNGSEEGRSALTRKVVKQILLDVKRIKDLGVRKVLVALSPPQKCLPKLVTPKGCDTNDTSTYLHNSLLRKGLIKLNDKEINNNDKSFMTLDLYNAFVTIFKNKGVSGVSTFPDPFKACCATKRGTFCGDRSLSGKKLYTLCDDPKSFFFWDNVHISDQGWRSVFSLLLPDSQF
Protein: Chloride channel CLIC-like protein 1 (ER anion channel 1) (ERAC1) (Mid-1-related chloride channel protein) (Q96S66)
Organism: Homo sapiens (Human)
Function: Seems to act as a chloride ion channel. Plays a role in retina development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25698737, ECO:0000269|PubMed:30157172, ECO:0000269|PubMed:31653868, ECO:0000269|PubMed:37142673}; Multi-pass membrane protein {ECO:0000255}. Note=Within the endoplasmic reticulum (ER), localizes to the mitochondria-associated ER membrane, a zone of contact between the ER and mitochondrial membranes. Enriched in the rough ER. {ECO:0000250|UniProtKB:Q99LI2, ECO:0000269|PubMed:31653868}.
Interaction partners:
- Cytochrome c oxidase assembly protein COX11
- Heme A synthase COX15
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MLCSLLLCECLLLVAGYAHDDDWIDPTDMLNYDAASGTMRKSQAKYGISGEKDVSPDLSCADEISECYHKLDSLTYKIDECEKKKREDYESQSNPVFRRYLNKILIEAGKLGLPDENKGDMHYDAEIILKRETLLEIQKFLNGEDWKPGALDDALSDILINFKFHDFETWKWRFEDSFGVDPYNVLMVLLCLLCIVVLVATELWTYVRWYTQLRRVLIISFLFSLGWNWMYLYKLAFAQHQAEVAKMEPLNNVCAKKMDWTGSIWEWFRSSWTYKDDPCQKYYELLLVNPIWLVPPTKALAVTFTTFVTEPLKHIGKGTGEFIKALMKEIPALLHLPVLIIMALAILSFCYGAGKSVHVLRHIGGPESEPPQALRPRDRRRQEEIDYRPDGGAGDADFHYRGQMGPTEQGPYAKTYEGRREILRERDVDLRFQTGNKSPEVLRAFDVPDAEAREHPTVVPSHKSPVLDTKPKETGGILGEGTPKESSTESSQSAKPVSGQDTSGNTEGSPAAEKAQLKSEAAGSPDQGSTYSPARGVAGPRGQDPVSSPCG
Protein: HTH-type transcriptional regulator EthR (Q7TVI1)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Involved in the repression of the monooxygenase EthA which is responsible of the formation of the active metabolite of ethionamide (ETH).
Interaction partners:
Sequence:
MTTSAASQASLPRGRRTARPSGDDRELAILATAENLLEDRPLADISVDDLAKGAGISRPTFYFYFPSKEAVLLTLLDRVVNQADMALQTLAENPADTDRENMWRTGINVFFETFGSHKAVTRAGQAARATSVEVAELWSTFMQKWIAYTAAVIDAERDRGAAPRTLPAHELATALNLMNERTLFASFAGEQPSVPEARVLDTLVHIWVTSIYGENR
Protein: Preterminal protein (pTP) (Bellett protein) (Precursor terminal protein) [Cleaved into: Intermediate terminal protein (iTP); Terminal protein (TP)] (P04499)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Protein covalently bound to the viral DNA that acts as a primer for viral genomic replication by DNA strand displacement. Assembles on the viral origin of replication in an initiation complex with viral polymerase, DBP, host NFIA and host POU2F1/OCT1. During initiation, the polymerase covalently couples the first dCTP with Ser-580 of pTP. The terminal protein stimulates the template activity over 20 fold compared to protein-free templates. Neo-synthesized viral genomes are linked to two preterminal proteins, one for each 5' end. These new genomes are encapsidated in the nucleus, and during capsid maturation by viral protease, preterminal protein is first cleaved into intermediary (iTP), then into mature TP. May play a role in host nuclear matrix localization of genomic DNA.
Subcellular location: Host nucleus matrix {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:8416372, ECO:0000269|PubMed:8497057}.
Interaction partners:
Sequence:
MALSVNDCARLTGQSVPTMEHFLPLRNIWNRVRDFPRASTTAAGITWMSRYIYGYHRLMLEDLAPGAPATLRWPLYRQPPPHFLVGYQYLVRTCNDYVFDSRAYSRLRYTELSQPGHQTVNWSVMANCTYTINTGAYHRFVDMDDFQSTLTQVQQAILAERVVADLALLQPMRGFGVTRMGGRGRHLRPNSAAAAAIDARDAGQEEGEEEVPVERLMQDYYKDLRRCQNEAWGMADRLRIQQAGPKDMVLLSTIRRLKTAYFNYIISSTSARNNPDRRPLPPATVLSLPCDCDWLDAFLERFSDPVDADSLRSLGGGVPTQQLLRCIVSAVSLPHGSPPPTHNRDMTGGVFQLRPRENGRAVTETMRRRRGEMIERFVDRLPVRRRRRRVPPPPPPPEEEEGEALMEEEIEEEEEAPVAFEREVRDTVAELIRLLEEELTVSARNSQFFNFAVDFYEAMERLEALGDINESTLRRWVMYFFVAEHTATTLNYLFQRLRNYAVFARHVELNLAQVVMRARDAEGGVVYSRVWNEGGLNAFSQLMARISNDLAATVERAGRGDLQEEEIEQFMAEIAYQDNSGDVQEILRQAAVNDTEIDSVELSFRLKLTGPVVFTQRRQIQEINRRVVAFASNLRAQHQLLPARGADVPLPPLPAGPEPPLPPGARPRHRF
Protein: Mitochondrial dynamics protein MID49 (Mitochondrial dynamics protein of 49 kDa) (Mitochondrial elongation factor 2) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein) (Q96C03)
Organism: Homo sapiens (Human)
Function: Mitochondrial outer membrane protein involved in the regulation of mitochondrial organization. It is required for mitochondrial fission and promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface independently of the mitochondrial fission FIS1 and MFF proteins. Regulates DNM1L GTPase activity.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:21508961}; Single-pass membrane protein {ECO:0000269|PubMed:21508961}. Note=Colocalizes with DNM1L at mitochondrial membrane. Forms foci and rings around mitochondria.
Interaction partners:
- Dynamin-1-like protein
- Density-regulated protein
- Mitochondrial fission factor
- Mitochondrial fission 1 protein
- Ribosome-releasing factor 2, mitochondrial
- Mitofusin-1
- Mitofusin-2
- Elongation factor G, mitochondrial
- Dynamin-like GTPase OPA1, mitochondrial
- Ribosome-recycling factor, mitochondrial
Sequence:
MAEFSQKRGKRRSDEGLGSMVDFLLANARLVLGVGGAAVLGIATLAVKRFIDRATSPRDEDDTKADSWKELSLLKATPHLQPRPPPAALSQPVLPLAPSSSAPEGPAETDPEVTPQLSSPAPLCLTLQERLLAFERDRVTIPAAQVALAKQLAGDIALELQAYFRSKFPELPFGAFVPGGPLYDGLQAGAADHVRLLVPLVLEPGLWSLVPGVDTVARDPRCWAVRRTQLEFCPRGSSPWDRFLVGGYLSSRVLLELLRKALAASVNWPAIGSLLGCLIRPSMASEELLLEVQHERLELTVAVLVAVPGVDADDRLLLAWPLEGLAGNLWLQDLYPVEAARLRALDDHDAGTRRRLLLLLCAVCRGCSALGQLGRGHLTQVVLRLGEDNVDWTEEALGERFLQALELLIGSLEQASLPCHFNPSVNLFSSLREEEIDDIGYALYSGLQEPEGLL
Protein: Vacuolar protein sorting-associated protein 53 homolog (P34561)
Organism: Caenorhabditis elegans
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi. Plays a role in the trafficking of cargo to dense-core vesicles, probably through association with the EARP-interacting protein eipr-1. Important for neuronal function.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Perikaryon {ECO:0000269|PubMed:27191843}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27191843}. Note=Co-localizes with rab-2 to perinuclear puncta in the perikaryon. {ECO:0000269|PubMed:27191843}.
Interaction partners:
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 54
- Vps54_N domain-containing protein
- Putative syntaxin 6
- EARP-interacting protein 1
- Exocyst complex component 3
- t-SNARE coiled-coil homology domain-containing protein
- GRIP and coiled-coil domain-containing protein 2
- Ras-related protein rab-6.2
Sequence:
MEEPTTSELKLSDNVMNEISDMCITEYCKPNMSLMAQINELFPTEQSLTQLDSIIASVEGEIGELDNELAYLVETNANVSERGEEALKHAQDAMIELEKSIGSIRERTKSSDEIVREMTRDIKQLDIAKRNLTASITTLHHLHILLTGVESLGAWVDKKDYSSIARQLPAILNVLQLFDAYKESDQIANLSGQLDKLKASLTIQLAKDLKNAFQTGQLSDRITDMCRVAAALEGNVKENFVKWFIEQQLSEYVIIYADNEEGAWLDKVDDRYKWFVRKLTDFERAGLSNIFPADWHMGRRLTSEFCTVTRDILYRIMTRRRQDLDWKLLGHAIQHTKMFEALLTKRFPEKDGISFEKAIWSVFDTFLDVFINAQEKTLNEFLDTCASKIRSGEEKPSRESSTHAVPFPSSADMFLLLKKVITESSKLSSEPDALIRDVIGVVRVCLRGYATSCLVAFLPSLGSQQSGAANLFSLIREEIAYPRLTPDQQFLVCCILATADWCAETSIQLQEKLSQRIPGVDISQETEAFYSITNQSLQVLVQDVESTCDAALQSISKVNWTAVDCVGDESPFIGSMRAHLRQAVPLIRDMLSDRRKYFAHFCLKLATQLAHKFVGSLFRCRTISTHGAEQLLLDTHSLKTFLLSVPSIDSIINSKPPTAYVTSVNAALTKAEMILKVVMCSLETVDEFVEQYIKLLPASDAAEMQKVLEMKGVKRQEHSAVLNAYRLKIGASGSDPIQQSNSLTSRIGGALPTVGSAASVSEAFNAVVSMAADGLSDQAVTSSIDKLKRFERLVKRQL
Protein: Riboflavin transporter RibU (Riboflavin ECF transporter S component RibU) (Q5M614)
Organism: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Function: Substrate-binding (S) component of an energy-coupling factor (ECF) ABC-transporter complex. Mediates riboflavin uptake, may also transport FMN and roseoflavin. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (Probable). Expression of the complex plus RibU in E.coli allows riboflavin uptake.
Subcellular location: Cell membrane {ECO:0000305|PubMed:23359690}; Multi-pass membrane protein {ECO:0000305|PubMed:23359690}.
Interaction partners:
- Conserved hypothetical, predicted membrane protein
Sequence:
MRSLFFGIGKSIGNFFQIVKIWRNFFMTNTRKLAYIAILSAVSFLLLYFSFPLIPAADFLKVDFSILPVLIALVIFDFKSAIGVLLLRSLLKLLLNNGGPGSMIGLPMNFVALGVFVWGLSYFWKKNQTSKNYILGSVLGTILLTVAMVVLNYIYAVPLYAKFANFDIAQFIGLYKYLFAMVVPFNLLEGLIFSVAFALIYAPLKSILVKL
Protein: UDP-glucuronosyltransferase 3A1 (UDPGT 3A1) (EC 2.4.1.17) (Q3UP75)
Organism: Mus musculus (Mouse)
Function: UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Complement component C8 alpha chain
- Cytochrome P450 2J5
- UDP-glucuronosyltransferase 3A2
- Exostosin-2
- 2-aminomuconic semialdehyde dehydrogenase
Sequence:
MAAHRSWLLVSFFLLEVLLLEAAKILTISTLSASHYILMNRVSQILQGGGHDVIKLLYEGGDIPDFRKENSSYQVINWRLPEDQQKTFENRWHRLIDEYAYGRSKYHTLLKIHQYFADLCSHLLSRKDIMELLQKENFDLVLLDSMDLCSFLIVEKLGKRFVSFLPFQFSYMDFGLPNAPLSYAPVYGSGLTDQMDFWGRVKNILMFFHFTKKRRDIFSQYGNTVQEHFAEGSQPVLSDLLLKAELWFVNSDFALDFARPLFPNTVYVGGLLDKPVQPIPQDLEDFISQFGDSGFVLVALGSVVSMIQSKEIIKEMNSAFAHLPQGVLWTCKSSHWPKDVSLAPNVKIMDWLPQIDLLAHPSIRLFVTHGGMNSVMEAVHHGVPMVGIPFFGDQPENMVRVEAKNLGVSIQLQTLKAESFLLTMKEVIEDQRYKTAAMASKVIRQSHPLTPAQRLVGWIDHILQTGGAAHLKPYAFQQPWHEQYMLDVFLFLLGLTLGTLWLSVKVLVAVTRYLSISRKVKQA
Protein: Protein Aster-C (GRAM domain-containing protein 1C) (Q8CI52)
Organism: Mus musculus (Mouse)
Function: Cholesterol transporter that mediates non-vesicular transport of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER). Contains unique domains for binding cholesterol and the PM, thereby serving as a molecular bridge for the transfer of cholesterol from the PM to the ER. Plays a crucial role in cholesterol homeostasis and has the unique ability to localize to the PM based on the level of membrane cholesterol. In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS) which is mediated by the GRAM domain. At the EPCS, the sterol-binding VASt/ASTER domain binds to the cholesterol in the PM and facilitates its transfer from the PM to ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30220461}; Single-pass membrane protein {ECO:0000255}. Note=In lipid-poor conditions localizes to the ER membrane and in response to excess cholesterol in the PM is recruited to the endoplasmic reticulum-plasma membrane contact sites (EPCS). {ECO:0000269|PubMed:30220461}.
Interaction partners:
Sequence:
MEGALTARQIVNEGDSSLATELQEEPEESPGPVVDENIVSAKKQGQSTHNWSGDWSFWISSSTYKDRNEEYRQQFTHLPDSEKLIADYACALQKDILVQGRLYLSEKWLCFYSNIFRWETTISIALKNITFMTKEKTARLIPNAIQIITEGEKFFFTSFGARDRSYLIIFRLWQNVLLDKSLTRQEFWQLLQQNYGTELGLNAEEMEHLLSVEENVQPRSPGRSSVDDAGERDEKFSKAVSFTQESVSRASETEPLDGNSPKRGLGKEDSQSERNVRKSPSLASEKRISRAPSKSLDLNKNEYLSLDKSSTSDSVDEENIPEKDLQGRLYINRVFHISAERMFELLFTSSHFMQRFANSRNIIDVVSTPWTVESGGNQLRTMTYTIVLSNPLTGKYTAATEKQTLYKESREAQFYLVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWGLIKSLIEKNSWSSLESYFKKLESDLLMEESVLSQSIEDAGKHSSLRRRRRTLNRTAEPVPKLSSQRSSTDLGFEAKVDVTGKRKTVDSYDTALIVVMSIFLLLLVLLNVTLFLKLSKIEHATQSFYQLHLQGEKSLNLVSDRFSRTENIQKNKDQAHRLKGVLQDSIVMLEQLKSSLIMLQKTFDLLNKNKSGVAVES
Protein: Glycine cleavage system H protein, mitochondrial (Glycine decarboxylase complex subunit H) (P39726)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Glycine dehydrogenase
- Aminomethyltransferase, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Putative lipoate-protein ligase A
- Serine hydroxymethyltransferase, mitochondrial
- Octanoyltransferase, mitochondrial
- DASH complex subunit DAD4
- Lipoyl synthase, mitochondrial
- Alanine--glyoxylate aminotransferase 1
Sequence:
MLRTTRLWTTRMPTVSKLFLRNSSGNALNKNKLPFLYSSQGPQAVRYTSQHEWIAVHQDKTAFVGITKYATDALGDATYVELPEVGTEIAQGESLGSIESVKSASEIYQPADGTVEEINTNLEENPGVVNEDPMGDGWLVKMKLGEGVNVEQVEGLMSLEQYEKTLVHDD
Protein: Probable allantoate deiminase (EC 3.5.3.9) (Allantoate amidohydrolase) (OsAAH) (Q655X8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the catabolism of purine nucleotides. The sequential activity of AAH, UGLYAH and UAH allows a complete purine breakdown without the intermediate generation of urea.
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:C0M0V4}.
Interaction partners:
- Probable
- Probable allantoinase
- Nitrate reductase
- Os03g0243200 protein
- Nitrate reductase 1
- Nitrate reductase
Sequence:
MALLLSYPRRHPSIHLLILSAYALFLLPILDGLELGGDGLYREILRDETVLRLKELGKISDGEGYLERTFLSPASIRASAVIISWMKDAGLTTWIDQMGNIHGRFEPTNSTKEALLIGSHMDTVIDAGMYDGALGIISAISALKVLKVTGRLQRLTRPVEVIAFSDEEGVRFQTTFLGSAAVAGTLPESILQVSDKSGTTVQDVLKLNSLEGTANALGEVRYSPESVGSYVEVHIEQGPVLEALRYPLGVVKGIAGQTRLKVIINGSQGHAGTVPMKLRRDPMVAAAELVLTLETLCKEPNKFLTYDEECGCFTEESLAGLVCTVGELLTWPSASNVIPGQVNFTVDIRAMDDKVRETIVTSFSRLVLQRCDDRLVDCAVEQKHAAAATPCDAELTSRLERATRSTISSMAAGVRRAGGETPVLMSGAGHDAMAMARLTKVGMLFVRCRGGVSHSPEESVMDDDVWAAGLALVNFIDQNAVDAAAATAAES
Protein: Ribosomal protein S3A (D6R9B6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGSSSGKATGDETGAKVERADGYEPPVQESV
Protein: Phosphatidylinositol 3-kinase VPS34 (PI3-kinase VPS34) (PI3K VPS34) (PtdIns-3-kinase VPS34) (EC 2.7.1.137) (Vacuolar protein sorting-associated protein 34) (A0A1D8PDV7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}. Endosome membrane {ECO:0000250|UniProtKB:P22543}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22543}.
Interaction partners:
- Ubiquitin-binding serine/threonine protein kinase
- Beclin 1
- Autophagy-related protein 6
- Serine/threonine-protein kinase ATG1
- Ubiquitin-like protein ATG12
- Autophagy protein 5
- Autophagy-related protein 3
- Autophagy-related protein 9
- Rab family GTPase
- Rab family GTPase
Sequence:
MATLSQPQSALPKTKIATTFGLSKDLKSPISVKVCYLECTRNNVSLVPLSTKFEDPTVFKKLSQIYKNSDLFVEIRVYDGKNNNLISTPVRTSYKAFNNKGRTWNQQLKLNIDYNQISIDAYLKFSICEIIDTKPSVFGVSYLSLFSHDSSTLRSGSHKIPVFMEDDPQYSKNIQYGTLIGLTDLEKRLIDYENGKYPRLNWLDKMVLPKVDATFLKTNNKDHDYYLYIELPQFEFPIVYSDIIYQIPTIEPITETTSKIPPDDTLNSNIIINSIDIPMATSHDPSIMKVYDPDFHITANNHLNPNATTFDPVELKYRKLERNIDNNTILDKELKPTPQLRDELLRIMIKPSNAELTDNEKNLIWKFRYYFSKNNSGNDPSNKSVKSFLPKFLRSINWENDYELDHTFKEIIPFYWNVDKLQIGDALELLGDYFNPYTLGKPTYQDDSMTSKSSKMKSDEKRFIKIYNNVCFLRKLAVERLKLANSEELLLYLLQLVQALKYEALIYEKSPPFCERSDQIEDNASSTLKSPLADFLIERAVENEKLGNFFYWYVKVENEDQLNNPHIDGPIKIYMDILNRYIELLKAHCHENRLPYYKHLKHQIWFIKKLTSLVELLRASFKKNEATAKKVEYLREYLANSGNELLKFPEPFPLPLDPSVMICGCYPEESSVFKSSLAPLKITLKTIEKKKHGHATSQLFGKRSRYGKYPLMFKIGDDLRQDQLVIQIIDLMDQLLKNENLDLKLTPYKILATSPISGLIQFVPNETLDSILSKTYPTSVTYSGGGETSDVPPSVSNNGILNYLRLHSQEQQSEEPISKSILSTNTSQSNTEIPVLPRQPKPTITSDLGVSPILMDNYVKSCAGYCVITYILGVGDRHLDNLLLSPNGKFWHADFGYILGRDPKPFPPLMKLPIQVIDGMGGLHHENYNVFKSYCFITYTTLRKNSNLILNLFQLMLDANIPDIQFDPSRVIEKVQEKFCLQMTEEEAILHFQNLINDSVNAFLPVVIDRLHSLAQYWRA
Protein: Universal stress protein Rv2005c (USP Rv2005c) (P9WLN1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably involved in aminoglycosides resistance and virulence. Overexpression increases resistance to the aminoglycosides amikacin (AK) and kanamycin (KM).
Interaction partners:
- Uncharacterized protein Rv2004c
- Uncharacterized protein Rv2003c
- Uncharacterized glycosyl hydrolase Rv2006
- DNA-binding transcriptional activator DevR/DosR
- Oxygen sensor histidine kinase response regulator DevS/DosS
- Uncharacterized protein Rv2629
- Probable cation-transporting ATPase F
- Acetyltransferase Pat
- Uncharacterized protein Rv0569
- Ribosomal-protein-alanine acetyltransferase RimJ
Sequence:
MSKPRKQHGVVVGVDGSLESDAAACWGATDAAMRNIPLTVVHVVNADVATWPPMPYPETWGVWQEDEGRQIVANAVKLAKEAVGADRKLSVKSELVFSTPVPTMVEISNEAEMVVLGSSGRGALARGLLGSVSSSLVRRAGCPVAVIHSDDAVIPDPQHAPVLVGIDGSPVSELATAVAFDEASRRGVELIAVHAWSDVEVVELPGLDFSAVQQEAELSLAERLAGWQERYPDVPVSRVVVCDRPARKLVQKSASAQLVVVGSHGRGGLTGMLLGSVSNAVLHAARVPVIVARQS