wanglab/gogpt-training-data huggingface dataset:
Protein: Lysophospholipase D GDPD1 (EC 3.1.4.-) (Glycerophosphodiester phosphodiesterase 4) (Glycerophosphodiester phosphodiesterase domain-containing protein 1) (Q8N9F7)
Organism: Homo sapiens (Human)
Function: Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic acid (LPA) and the corresponding amines. Shows a preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine (lyso-PC). May be involved in bioactive N-acylethanolamine biosynthesis from both N-acyl-lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N-acyl-lysophosphatidylethanolamin (N-acyl-lysoPE). In addition, hydrolyzes glycerophospho-N-acylethanolamine to N-acylethanolamine. Does not display glycerophosphodiester phosphodiesterase activity, since it cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18991142}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18991142}. Endoplasmic reticulum {ECO:0000269|PubMed:27637550}. Note=Concentrated at the perinuclear region and the cell periphery (PubMed:18991142). {ECO:0000269|PubMed:18991142}.
Interaction partners:
- Autotaxin
- Glycerophosphocholine cholinephosphodiesterase ENPP6
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Lysophospholipid acyltransferase LPCAT4
- Lysophospholipase D GDPD3
- Lysoplasmalogenase TMEM86B
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Group 10 secretory phospholipase A2
- Lysophosphatidic acid receptor 1
- Cytosolic phospholipase A2
Sequence:
MSSTAAFYLLSTLGGYLVTSFLLLKYPTLLHQRKKQRFLSKHISHRGGAGENLENTMAAFQHAVKIGTDMLELDCHITKDEQVVVSHDENLKRATGVNVNISDLKYCELPPYLGKLDVSFQRACQCEGKDNRIPLLKEVFEAFPNTPINIDIKVNNNVLIKKVSELVKRYNREHLTVWGNANYEIVEKCYKENSDIPILFSLQRVLLILGLFFTGLLPFVPIREQFFEIPMPSIILKLKEPHTMSRSQKFLIWLSDLLLMRKALFDHLTARGIQVYIWVLNEEQEYKRAFDLGATGVMTDYPTKLRDFLHNFSA
Protein: PRA1 family protein B6 (AtPRA1.B6) (Prenylated Rab acceptor 3) (Q9LYQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- Protein YIP
- Protein YIP4a
- Ras-related protein RABD2b
- PRA1 family protein C
- Aspartic proteinase A1
- Ras-related protein RABA3
Sequence:
MASPLLPTSTTPDQLPGGDPQLLSSLRVLLSRVLATVRHASADARPWAELVDRSAFSRPPSLSEATSRVRKNFSYFRANYITLVAILLAASLLTHPFALFLLASLAASWLFLYFFRPADQPLVIGGRTFSDLETLGILCLSTVVVMFMTSVGSLLMSTLAVGIMGVAIHGAFRAPEDLFLEEQEAIGSGLFAFFNNNASNAAAAAIATSAMSRVRV
Protein: DNA repair protein RAD51 homolog 4 (R51H3) (RAD51 homolog D) (RAD51-like protein 3) (TRAD) (O75771)
Organism: Homo sapiens (Human)
Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, telomere.
Interaction partners:
- DNA repair protein RAD51 homolog 3
- DNA repair protein XRCC2
- DNA repair protein RAD51 homolog 2
- Breast cancer type 2 susceptibility protein
- Fanconi anemia group M protein
- DNA repair protein XRCC3
- Breast cancer type 1 susceptibility protein
- DNA repair protein SWI5 homolog
- Partner and localizer of BRCA2
- Double-strand break repair protein MRE11
Sequence:
MGVLRVGLCPGLTEEMIQLLRSHRIKTVVDLVSADLEEVAQKCGLSYKALVALRRVLLAQFSAFPVNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCMAANVAHGLQQNVLYVDSNGGLTASRLLQLLQAKTQDEEEQAEALRRIQVVHAFDIFQMLDVLQELRGTVAQQVTGSSGTVKVVVVDSVTAVVSPLLGGQQREGLALMMQLARELKTLARDLGMAVVVTNHITRDRDSGRLKPALGRSWSFVPSTRILLDTIEGAGASGGRRMACLAKSSRQPTGFQEMVDIGTWGTSEQSATLQGDQT
Protein: Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (P38816)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts on mitochondrial thioredoxin 3. Implicated in the defense against oxidative stress.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10037727, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Thioredoxin reductase 1
- Thioredoxin-3
- Glutathione reductase
- Thioredoxin-2
- Thioredoxin-1
- Peroxiredoxin PRX1, mitochondrial
- Cystathionine gamma-lyase
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- Peroxiredoxin TSA2
Sequence:
MIKHIVSPFRTNFVGISKSVLSRMIHHKVTIIGSGPAAHTAAIYLARAEMKPTLYEGMMANGIAAGGQLTTTTDIENFPGFPESLSGSELMERMRKQSAKFGTNIITETVSKVDLSSKPFRLWTEFNEDAEPVTTDAIILATGASAKRMHLPGEETYWQQGISACAVCDGAVPIFRNKPLAVIGGGDSACEEAEFLTKYASKVYILVRKDHFRASVIMQRRIEKNPNIIVLFNTVALEAKGDGKLLNMLRIKNTKSNVENDLEVNGLFYAIGHSPATDIVKGQVDEEETGYIKTVPGSSLTSVPGFFAAGDVQDSRYRQAVTSAGSGCIAALDAERYLSAQE
Protein: NF-kappa-B inhibitor-interacting Ras-like protein 1 (I-kappa-B-interacting Ras-like protein 1) (Kappa B-Ras protein 1) (KappaB-Ras1) (Q9NYS0)
Organism: Homo sapiens (Human)
Function: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15024091}.
Interaction partners:
- NF-kappa-B inhibitor beta
- NF-kappa-B inhibitor alpha
Sequence:
MGKGCKVVVCGLLSVGKTAILEQLLYGNHTIGMEDCETMEDVYMASVETDRGVKEQLHLYDTRGLQEGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKIDLSEQRQVDAEVAQQWAKSEKVRLWEVTVTDRKTLIEPFTLLASKLSQPQSKSSFPLPGRKNKGNSNSEN
Protein: DNA (Cytosine-5)-methyltransferase (EC 2.1.1.37) (Q8IBI4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- S-adenosylmethionine synthase
- Adenosylhomocysteinase
Sequence:
MHKIKVLELYCGIGGLHYSLLQAFNNFVHANKITEKKCDTYKDGIHNHMSNNKSIEIHKYHDCTLTCLNDLFCFISVDLNPVANQTYFHNFKDSTILLTQTRDVHKFFKWKCDSMDKQSNGSTHNEHEKTQKKKNKKKNNDDDEKNNIFNINKNYIIQTDINNIMPEFLNNHHFNILLISNPCQPYTRQNQKFKEINLDLLFCKNNEYKQNVNNNISNDNNSFYSNHNGDENHQFNVDNINIDELNNYIYNDKDERTKSFIHICTLLTKVDFKNLPEYIFIENVKNFELSSSFIYFLYCIKNNYSFQTYLLSPLQFGIPNERLRFYCICKKKNYDFKHANNLSGINYIKDKNLNLYTNSLIPKNYLHKNNIHEQKNNQGDNYNNISCENVIFYTPNLITYLDVNNNFNITNNIWNHINIYNNYLDNYQVQNQVLQKNASYCFDIININKKTTTCCHVANYYHHHHQKKKENVNNISPDEPTKHMNAKGNYAMCFTSNYGRYIKGSGSILYYNRKENSNCAEQKTKNKETNVLTKENNEYVHTSNYTCNSISNSDNDTYETRRKKNCMKKYEQNVRYFTPTEISRLMGFKMKTNNKNINQNEKGKNTYGNVFWNIDHINHTCAYFSNVHYCDVQNKNACLLTYQNVTNLNNNHTYQNCHQKNCLCHEFVFPNFLTDRQKYKLIGNSVNVIVISYIFHVHNIFEHIHI
Protein: tRNA(adenine(34)) deaminase (EC 3.5.4.33) (Q381Q7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Deaminase, putative
- Abnormal spindle-like microcephaly-associated protein ASH domain-containing protein
- NADAR domain-containing protein
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MEEVVVPEEPPKLVSALATYVQQERLCTMFLSIANKLLPLKPHACHLKRIRRSSATRVATAPMDGFAGGVICDKRDSSVATSTISDGCERNSAALGTPAAENSHILELLLSVGGPVDSSALKELESAADTTVAVHRVWVPDRAPRSSAEEWTKWCQIWPFATPKPRAPTQLSECEMGSIQRIFRTVVMPLAKRLRTDETLGIAAVLVDPSDGYRVLVSSGEEHALKRGNSAACLGYVSNSGCRKSNRVVLDHPVTFVLKEVTRKQCKDREVEGDASYLANGMDMFVSHEPCVMCSMALVHSRVRRVFYCFPNPVHGGLGSTVSIHAIQELNHHFRVFRCDSRWLSDPEGVSSDHDNPYWEDLTVP
Protein: Protein spartin (Q9VN45)
Organism: Drosophila melanogaster (Fruit fly)
Function: During postembryonic development, functions with endocytic adapter Eps-15 in neurons to restrain synaptic growth, by inhibiting BMP signaling, and to control synaptic endocytosis. Required presynaptically for neuromuscular junction (NMJ) neurotransmission. Inhibits neuronal BMP signaling by promoting endocytic internalization and subsequent endosomal trafficking of the BMP receptor wit. In this way, regulates the Fmr1 translational regulator controlling Futsch expression to modulate neuronal microtubule stability, which controls both synaptogenesis and neuronal survival.
Subcellular location: Presynaptic cell membrane {ECO:0000269|PubMed:23439121}. Early endosome {ECO:0000269|PubMed:23439121}. Lipid droplet {ECO:0000269|PubMed:23439121}. Note=Colocalizes with Eps-15 at presynaptic cell membrane. {ECO:0000269|PubMed:23439121}.
Interaction partners:
- Spastin
- IST1 homolog
- Seipin
- Atlastin
- Spichthyin, isoform B
- Receptor expression enhancing protein A, isoform I
- Uncharacterized protein, isoform B
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
- E3 ubiquitin-protein ligase Su
Sequence:
MAEEESEFLEAYAGIRTAYKAAMTQVDLAVSHEEQESPGQAIVAYELALRMIEDTFGIPVGLPNKIDTVQAEWNDACALIQKLKSAETELRYRLKVLRSQKQSIDDSAVEATEESRAEMDTKRPPLLAENPSTQYGIANASGAPKTYRELAAGLRELLAVRDAKVLLDELFRAQVKMYRIEASGSVTTISGSSTMSLVMCTVGGKWKYLSGIYFIQCSMPNEGTAGIWLYPLVPSITNCYQTEYGAFIFPDMECQQPGNAFGLMLTKEGQTSRTEDELEDLQQFFLDLLEAVLAGTVVQLKSPTSQRAGLASDTVSGSEQVSRHIVSAADFIASNLVRGAEKTGGFMLRSTPYIISKMTPASMDAQVPSSVQTSVEVAQKVTHAAAGMTGWIAGKVGTASMAVGRYLAPHIQEQGSKLLQKGFGYDTSEANSTMEGAMTIAAGAVEGVSTVFDGLETSAKILGSSLSENSVKIIEHKYGQQTGNLASGTFDTVGNVFVVSQNVNYITPKGIAKKMVKRTGEAVVSDYKRDLRKSESHYINAGSLYPDLRALKE
Protein: Putative NAD(P)-binding protein YbjT (P75822)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- NADH-quinone oxidoreductase subunit C/D
- Low specificity L-threonine aldolase
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit F
- Acyl carrier protein
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit M
- Inner membrane transporter YcaM
Sequence:
MPQRILVLGASGYIGQHLVRTLSQQGHQILAAARHVDRLAKLQLANVSCHKVDLSWPDNLPALLQDIDTVYFLVHSMGEGGDFIAQERQVALNVRDALREVPVKQLIFLSSLQAPPHEQSDHLRARQATADILREANVPVTELRAGIIVGAGSAAFEVMRDMVYNLPVLTPPRWVRSRTTPIALENLLHYLVALLDHPASEHRIFEAAGPEVLSYQQQFEHFMAVSGKRRWLIPIPLPTRWISVWFLNVITSVPPTTARALIQGLKHDLLADDTALRALIPQRLIAFDDAVRSTLKEEEKLVNSSDWGYDAQAFARWRPEYGYFAKQAGFTVKTSASLAALWQVVNQIGGKERYFFGNILWQTRALMDRAIGHKLAKGRPEREYLQTGDAVDSWKVIVVEPEKQLTLLFGMKAPGLGRLCFSLEDKGDYRTIDVRAFWHPHGMPGLFYWLLMIPAHLFIFRGMAKQIARLAEQSTD
Protein: WD-40 family member protein (Q86M30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGTNSGATAGINNKPVGGATGAGVLVGGGVGGANSSIGGVLSNSLGGGGSGGLSISGLNAGGQNANVGGMGNVGGDDGGNGMVGGGVNNQQATTPQYTIPGILHFIQHEWSRFELERSQWDVDRAELQARIAMLLGERKCLESLKSDLTRRIKMLEYALRQERAKFYRLKYGTDPPQLNEFKPSNEDAGLAGEVATDSEVPYSSVSNTTWRQGRQMLRQYLAEIGYTDNIIDVRSNRVRSILGLNNNAEHDGSGGGLGGGLGGGTGGENLSPNINGNESNKRASETEGRHTPAKKVQQSIDEIIVDSEAAVMANFEFLGATEMSDDDEISDDLEMVATDNDDTDVKLAKRAKSGKDMLTEEVDGSLGLGELAQLTVNNESDGAYDANSKDGTGGSAGGAGYRKTWNAKYTLRSHFDGVRSLIFHPEEPVLITASEDHTLKLWNLQKTVQAKKSASLDVEPLYTFRAHTGPVLCLGMSSSGETCYSGGLDGNIECWQLPSPNIDPYDCYDPNVHSGTLEGHTDAVWGLTTMQSNIVSCSADGTVKLWSPYNKEPLLRTYTASEAEGVPSSVDFVRNEVDHIVVAYNSAHCIVYDTETGKQVVRLEAAQEMSGNTGKFINKVVSHPTLPITITAHEDRHIRFWDNTSGTLVHSMVAHLEPVTSLAVDAHGLYLLSGSHDCSIRLWNLDNKTCVQEITAHRKKFDESIFDVAFHATKPYIASAGADGLAKVFV
Protein: Folate synthesis bifunctional protein [Includes: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) (EC 2.7.6.3) (2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (PPPK); Dihydropteroate synthase (DHPS) (EC 2.5.1.15)] (Q1ENB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis. Plays a role in seed stress response and survival.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17289662}.
Interaction partners:
- Dihydroneopterin aldolase 2
- Probable dihydroneopterin aldolase 3
- Dihydroneopterin aldolase 1
- GTP cyclohydrolase 1
- Dihydrofolate synthetase
- Folylpolyglutamate synthase
- D-amino-acid transaminase, chloroplastic
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Aminodeoxychorismate synthase, chloroplastic
Sequence:
MDFTSLETTTFEEVVIALGSNVGNRMNNFKEALRLMKDYGISVTRHSCLYETEPVHVTDQPRFLNAAIRGVTKLKPHELLNVLKKIEKEMGREENGLRYGPRPLDLDILFYGKHKIISDKLIIPHERIWERPFVLAPLVDLLGTEDIDNDKIVAYWHSLSMHSGGIFQAWERLGGESLLGKDGIIQRVIPIGDHLWDFSKKTYVMGILNLTPDSFSDGGKFQSVDTAVSRVRSMISEGVDIIDIGAQSTRPMASRISSQEEIDRLIPVLKVVRGMAEMKGKLISVDTFNSEVALEAIRNGADILNDVSGGSLDENMHKVVADSDVPYMIMHMRGDPCTMQNKENLEYNEICKDVATELYERVREAELSGIPAWRIMIDPGIGFSKGIDHNLDIVMELPKIREEMAKKSIGLSHAPILIGPSRKRFLGDICGRPEASERDAATVACVTAGILKGANIIRVHNVRDNVDAARLCDAMMTKRFKNVD
Protein: Monosaccharide-sensing protein 1 (Monosaccharide transporter 1) (Sugar transporter MSSP1) (Sugar transporter MT1) (Tonoplast monosaccharide transporter 1) (AtTMT1) (Q96290)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sugar proton-coupled antiporter which contributes to vacuolar sugar import (e.g. monosaccharides including glucose, sucrose and fructose), particularly during stress responses (e.g. in response to cold). Required for cytosolic glucose homeostasis.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17158605, ECO:0000269|PubMed:21838775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sucrose transport protein SUC4
- Sucrose transport protein SUC3
- Bidirectional sugar transporter SWEET16
- Sucrose transport protein SUC2
Sequence:
MKGATLVALAATIGNFLQGWDNATIAGAMVYINKDLNLPTSVQGLVVAMSLIGATVITTCSGPISDWLGRRPMLILSSVMYFVCGLIMLWSPNVYVLCFARLLNGFGAGLAVTLVPVYISETAPPEIRGQLNTLPQFLGSGGMFLSYCMVFTMSLSDSPSWRAMLGVLSIPSLLYLFLTVFYLPESPRWLVSKGRMDEAKRVLQQLCGREDVTDEMALLVEGLDIGGEKTMEDLLVTLEDHEGDDTLETVDEDGQMRLYGTHENQSYLARPVPEQNSSLGLRSRHGSLANQSMILKDPLVNLFGSLHEKMPEAGGNTRSGIFPHFGSMFSTTADAPHGKPAHWEKDIESHYNKDNDDYATDDGAGDDDDSDNDLRSPLMSRQTTSMDKDMIPHPTSGSTLSMRRHSTLMQGNGESSMGIGGGWHMGYRYENDEYKRYYLKEDGAESRRGSIISIPGGPDGGGSYIHASALVSRSVLGPKSVHGSAMVPPEKIAASGPLWSALLEPGVKRALVVGVGIQILQQFSGINGVLYYTPQILERAGVDILLSSLGLSSISASFLISGLTTLLMLPAIVVAMRLMDVSGRRSLLLWTIPVLIVSLVVLVISELIHISKVVNAALSTGCVVLYFCFFVMGYGPIPNILCSEIFPTRVRGLCIAICAMVFWIGDIIVTYSLPVLLSSIGLVGVFSIYAAVCVISWIFVYMKVPETKGMPLEVITDYFAFGAQAQASAPSKDI
Protein: O-antigen polymerase (ORF_10; potential multiple membrane spanning domains) (Wzy) (Q7B782)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MYILARVDRSILLNTVLLFAFFSATVWVNNNYIYHLYDYMGSAKKTVDFGLYPYLMVLALICALLCGGAIRRPGDLLVTLLVVILVPHSLVLNGANQYSPDAQPWAGVPLAIAFGILIIGIVNKIRFHPLGALQRENQGRRMLVLLSVLNIVVLVFIFFKSAGYFSFDFAGQYARRALAREVFAAGSANGYLSSIGTQAFFPVLFAWGVYRRQWFYLVLGIVNALVLWGAFGQKYPFVVLFLIYGLMVYFRRFGQVRVSWVVCALLMLLLLGALEHEVFGYSFLNDYFLRRAFIVPSTLLGAVDQFVSQFGSNYYRDTLLGALLGQGRTEPLSFRLGTEIFNNPDMNANVNFFAIAYMQLGYVGVMAESMLVGGSVVLMNFLFSRYGAFMAIPVALLFTTKILEQSLLTVMLGSGVFLMLLFLALISFPLKMSLGKTL
Protein: Glutathione S-transferase theta-1 (EC 2.5.1.18) (GST 5-5) (GST class-theta-1) (Glutathione S-transferase 5) (Q01579)
Organism: Rattus norvegicus (Rat)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Also binds steroids, bilirubin, carcinogens and numerous organic anions. Has dichloromethane dehalogenase activity.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase Mu 1
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase alpha-3
- Glutathione S-transferase P
- Bifunctional glutamate/proline--tRNA ligase
- Glutathione S-transferase Mu 5
- Glutathione S-transferase Mu 7
- Glutathione S-transferase
- Glutathione S-transferase omega-1
- Glutathione S-transferase alpha-5
Sequence:
MVLELYLDLLSQPCRAIYIFAKKNNIPFQMHTVELRKGEHLSDAFAQVNPMKKVPAMKDGGFTLCESVAILLYLAHKYKVPDHWYPQDLQARARVDEYLAWQHTTLRRSCLRTLWHKVMFPVFLGEQIRPEMLAATLADLDVNVQVLEDQFLQDKDFLVGPHISLADVVAITELMHPVGGGCPVFEGRPRLAAWYRRVEAAVGKDLFLEAHEVILKVRDCPPADPVIKQKLMPRVLTMIQ
Protein: Col5a3 protein (A1A4B3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRSCRRLDQLQAGLCLLLASLQLVSWTLAAEPVDVLEAWGVHRDQAGVAEGPGFCPLRIPQGDRAFRVGKSSLLSVPTWQLFPDGHFPENFSVLLTLRAQPANQSVLLSIYDEKGVRQLGLALGPALGLLGDSFRPLPKQVNIMDGRWHRVAVSISGNKVTLVVDCEPQPPTFGQGPRFISTAGLTVMGTQDTREESFEGDIQELLLIPDPQAAFQACESYLPGCETLDSTTTGAPKDDEPETPAPRRRKGKKKKK
Protein: Gustatory and odorant receptor 24 (Q7PYF4)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. GPRgr22 and GPRgr24 together are sufficient for olfactory carbon dioxide-chemosensation.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MSLYFNADTMRIERSSVHEPKRNRNVFLDVKPIADDANVNVPPRQAARRNATVFNNRVGFPPLTPKEAFVDAVPADQTCMVFESSKPIYLVLRAIGVLPYTRLPSGGTAFVLASPSMTYCVLFFLLLTVYIAFILLNRIEIVRTLEGRFEESVIAYLFIVNILPILIIPLMWYESRKVVSVVNGWVDFETVYRETTGRALELRLRTKAQVIAILLPILCSLSVAITHVTMVDFKLLQVIPYCVLDTITYMMGGYWYMACETLSITAKILAEDFQRALRHVGPAAKVSEYRSLWLRLSKLARDTGFSTCYTFTFICLYLFFIITLSIYGLMSQISDGFGVKDIGLAVTAFCSVGLLFYICDEAHYASFNVRTNFQKKLLMVELSWMNTDAQTEINMFLRATEMNPSSINLGGFFDVNRTLFKSLLATMVTYLVVLLQFQISIPDEPSAMLMHSNSSHS
Protein: Polyadenylate-binding protein (PABP) (A0A087WTT1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Protein: rRNA methyltransferase 1, mitochondrial (EC 2.1.1.-) (16S rRNA (guanosine(1145)-2'-O)-methyltransferase) (16S rRNA [Gm1145] 2'-O-methyltransferase) (Q99J25)
Organism: Mus musculus (Mouse)
Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q6IN84, ECO:0000269|PubMed:24036117}.
Interaction partners:
- Mitochondrial ribosome-associated GTPase 1
- rRNA methyltransferase 2, mitochondrial
- Mitochondrial assembly of ribosomal large subunit protein 1
- Pseudouridylate synthase RPUSD4, mitochondrial
- Large ribosomal subunit protein uL29m
- rRNA methyltransferase 3, mitochondrial
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- GTP-binding protein 8
- Mitochondrial mRNA pseudouridine synthase Rpusd3
- 5-cytosine rRNA methyltransferase NSUN4
Sequence:
MRRLWTVGCFSRLIARHFSSVARRGERPGGEELSRLLLDDLAPAQRLERLFGLSPCLLALRAARRRVARLLLQAGKAGLQGERAELLRVAEARGIPVLRPRRQKLDALCGYQVHQGVCMEVSPLRPRPCDEAADTSSGDDPQQLWLVLEGLQDPRNLGAVMRSAHFLGVDRVITSQRNSCPLTPVVSKASAGAMEVMDVFATPDLPGFLQAKAQQGWLVVGTVGCPGPEISQSSKVPITSCLEFVWDRPTLLVLGSEGSGLSQEVFASCQLLLTILPRRHLPPGLESLNVSVATGILLHSICSQKKGFPVQERGQLLQDS
Protein: HL07962p (Transport and golgi organization 10, isoform A) (Transport and golgi organization 10, isoform B) (Transport and golgi organization 10, isoform C) (Q7K187)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNDNGNGGAAPVSGGVCGVGGAHGAAGGADGAGGAGGGGGCGAGGGGAGAGPGGGPGGGAAAADLAGEAAGGAAGGDAAINNQANANGTSESPAKGLNSSEDLDAKRRKCRETEEGQDEASTMIDANSVLNKIANLYAEQLMSDIVLLVDGKEFPAHRVILCASSDVFQVMLMNPEWNECSKHVIELHEEACCSAVFPQFIKYLYVGQIEVTLQTVMPMLALSDKYNIRDLIDLCVDYMNKHVAKAATSGYLVSWLQYTLSFTPTHNDLTETLKRFLKWNLEMVAESRDFVEMDPAILILLLQQNDLVVTSEYKLFDILQTWLLHRREQMEATGSGGFMELIEQTVSHIRFGMMTPRQLSHLLMDPLVEYHKEFLVERIAIGMSYQSGHEDRVREVRATESGKLQFTPRLYWNDTWSVDIDVHNFTAIEDYKNYVTCFFSQRHIAETEEDDPCMTWEIEFFPRGVRYNKAKMVWGEDVPGCSLNTVRLRVTCKHQNIGEERFKIAVLIVGMQNQIMHIRTVVERTEYFSDTSRVVNLDNLLPYEELEHTSLYLSPHLTGTARNTLTLHVVITPMGSHTCRDTPPFQF
Protein: TIPARP protein (Q05BQ2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEMETTEPEPDCVVQPPSPPDDFSCQMRLSEKITPLKTCFKKKDQKRLGTGTLRSLRPILNTLLESGSLDGVFRSRNQSTDENSLHEPMMKKAMEINSSCPPAENNMSVLIPDRTNVGDQIPEAHPSTEAPERVVPIQDHSFPSETLSGTVADSTPAHFQTDLLHPVSSDVPTSPDCLDKVIDYVPGIFQENSFTIQYILDTSDKLSTELFQDKSEEASLDLVFELVNQLQYHTHQENGIEICMDFLQGTCIYGRDCLKHHTVLPYHWQIKRTTTQKWQSVFNDSQEHLERFYCNPENDRMRMKYGGQEFWADLNAMNVYETTEFDQLRRLSTPPSSNVNSIYHTVWKFFCRDHFGWREYPESVIRLIEEANSRGLKEVRFMMWNNHYILHNSFFRREIKRRPLFRSCFILLPYLQTLGGVPTQAPPPLEATSSSQIICPDGVTSANFYPETWVYMHPSQDFIQVPVSAEDKSYRIIYNLFHKTVPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMFGRDRIINERHLFHGTSQDVVDGICKHNFDPQVCGKHATMFGQGSYFAKKASYSHNFSKKSSKGVHFMFLAKVLTGRYTMGSHGMRRPPPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQYEEVSNTEKKKKK
Protein: Cystinosin precursor (Cystinosis, nephropathic) (Q503T0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MLKQTFFLFLLTLYLCKHTAFGDPEVAVSAPATVNLQEFSSENITITLSSPLNTSVTVYFNITYESNNVSLIIQLPDEVVVPAGNTSVSFAVQAKGVGQVTAYLSSNDTHIKSLDARIRFLIVRSNALFIINQIIGWIYFVAWSVSFYPQAYENWKRRSVVGLNFDFLALNLTGFIAYSVFNVGLFWVTYIQEEFLKKDPNGVIPVDANDVFFSLHALLLTLVYICQCAIYERGGQKVSKVAIGLLAIGWTFAFVSLFVAVAKKISWLDYLYYFSYIKLGVTLVKYIPQAHMNYRRKSTEGWSIGNVLLDFTGGSFSLIQMFLEAYNNDKWRFIFGDPTKFGLGIFSIFFDILFIIQHYCLYRNREPMYQDLDEQNDQHSSVKT
Protein: Cullin-associated NEDD8-dissociated protein 1 homolog (CAND1 homolog) (Longevity-assurance protein 2) (Q92325)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor (By similarity). Involved in the aging process. Longevity-assurance protein.
Interaction partners:
- NEDD8-like protein RUB1
- Cell division control protein 53
- Defective in cullin neddylation protein 1
- Ubiquitin-conjugating enzyme E2-34 kDa
- RING-box protein HRT1
Sequence:
MSLHISKLIEQYRSTKDNDLKYMLLRQNFKINDIEDELAPLVNELLLPVLVEEQDMEILNLVSFQVLPDLVLSMISDPAAAQLGWVISLICDPLLNQSMIHANRSFVLIETLRNVLQKIENSPHLDYHQPVNSSLEFISKFIVEMKRHMCDVDAAQLSHSLSESNMLIYIESLNLLLKFSFFSDAASPSVMVTLPFDILNDVFTIAQDYSATNTNESIDRITEKLLLTSTQLTHPVDLENLCPKMKYNTLAAVSRIWYKFGPIVDKLFTNRLLPVLFPPQMGEECNVEDVLEIVHNFHPYFSIRRLKDNRPLLSDSTISQLREGLFGMLSILNDSLTRTQNENDHGSDNLIDSDDGFGSDNDPEQQAYLDELVSEGYDENMYDGDTDDEDADDINVEKNDEATKDITETNKILLIFSELHYPQEERFSELLVELQTKIAINTSLIDKILSKETTELPTHNGEIADLNEILNEVKGNKPIRKNVIFCTLAHTLSLQSGSELSVLQLSIEVIDHLLVKNHSNNITRGEQFQLIKLILPHLKTNKSFIDTLKAGNFTQKIDEGVTLRTMILSLLLQLFPLDYSMLGEILPTIARYSVRDKDLGVRDLSFQLLDQILRTYYNYLIGIDWEWYKDDFYQVLQETCIKKDINTNLLLQFPPYLPHD