wanglab/gogpt-training-data huggingface dataset:
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type IV) (3-beta-HSD IV) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] (Q62878)
Organism: Rattus norvegicus (Rat)
Function: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- Aromatase
- Cytochrome P450 11B3, mitochondrial
- Steroid 21-hydroxylase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Aldo-keto reductase family 1 member C18
- 25-hydroxycholesterol 7-alpha-hydroxylase
- Estradiol 17-beta-dehydrogenase 2
Sequence:
MPGWSCLVTGAGGFLGQRIVQLLVQEKDLKEVRVLDKVFRPETREEFFNLGTSIKVTVLEGDILDTQCLRRACQGISVVIHTAALIDVTGVNPRQTILDVNLKGTQNLLEACVQASVPAFIYCSTVDVAGPNSYKKIILNGHEEEHHESTWSNPYPYSKKMAEKAVLAANGSILKNGGTLHTCALRPMYIYGERSPFLSVMILAALKSKGILNVTGKFSIANPVYVGNVAWAHILAARGLRDPKKSQNVQGQFYYISDDTPHQSYDDLNYTLSKEWGLHLDSSWSLPLPLLYWLAFLLEIVSFFLHPVYNYRPSFNRHLVTLSNSKFTFSYKKAQRDLGYKPLVSWEEAKQKTSEWIGTLVEQHRETLDTKSQ
Protein: Ubiquitin carboxyl-terminal hydrolase ubh-4 (EC 3.4.19.12) (Ubiquitin C-terminal hydrolase family 1 member 4) (Ubiquitin thioesterase 4) (Q09444)
Organism: Caenorhabditis elegans
Function: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin.
Interaction partners:
- Proteasomal ubiquitin receptor ADRM1 homolog
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit alpha type-1
- PCI domain-containing protein
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 13
Sequence:
MTDAGSWCLIESDPGVFTEMLRGFGVDGLQVEELYSLDDDKAMTRPTYGLIFLFKWRQGDETTGIPSDKQNIFFAHQTIQNACATQALINLLMNVEDTDVKLGNILNQYKEFAIDLDPNTRGHCLSNSEEIRTVHNSFSRQTLFELDIKGGESEDNYHFVTYVPIGNKVYELDGLRELPLEVAEFQKEQDWIEAIKPVIQQRMQKYSEGEITFNLMALVPNRKQKLQEMMENLIQANENNELEEQIADLNKAIADEDYKMEMYRKENNRRRHNYTPFVIELMKILAKEGKLVGLVDNAYQAAKEKSKLNTDITKLELKRKQ
Protein: NADH-cytochrome b5 reductase (EC 1.6.2.2) (Q381N0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytochrome b5, putative
- Cytochrome b5, putative
- Dihydroorotate dehydrogenase
Sequence:
MKFLTFTAASILGAAFKARVSSQQHTAECRTNAVLDTKFKPLALGEVINLAEDVAIFRFLLPRVDDTFDLVPCSTLQACLKEGANIVDQPMRSYTPITPNGTMGYFDLLVKKQPRGRFTEHLFSMNVGDTLLFRVVQYKLQYKKNRWAEVGLIGGGTGICPLLQFMNASLDTPGDKTKLSLLFANRSENKILLKGMLDGTAKKHADRLSVHYTVDMLENPQSDYNGYIGYITPQMIKETMPEPADNNLVLVCGPDPMMTKVVGSSPNVLKAMSGGLAYQPTGTVLNNAPDVGGILGDMGYTKDHVYRF
Protein: PAN2-PAN3 deadenylation complex catalytic subunit pan2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) (Q09798)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:16823372}.
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit pan3
- PAB-dependent poly
- Polyadenylate-binding protein, cytoplasmic and nuclear
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Probable mRNA-splicing protein ubp10
- 5'-3' exoribonuclease 1
- Poly
- Probable citrate synthase, mitochondrial
Sequence:
MDAWKEITKTTENDGVSTCSLSSIAFDPYSELVWTGHKNGQIKSSFGPSLTSYTQFIGHEGPVHQVLPQERGVFSLSSKSLRLSNRKGTIRWRYQDSDCIDYRAMFYQSRNNPEVVIGGYHQKLTVVNAERGISIHKDKNVSDIFIMRRNRLLCCGSTNGEIILRDPNSFQPVNKVVAHTGTISDIDTSGNLLLSCGYSLRHGTYMLDPFVKVWDLRNLSSLVPIPFPAGPTIIRMHPKLSTTAVVCSCSGQFHIVDTGNPLDAKLMQIPLTSYLTGMDIASTGDAMVFTDVEDNIHLWSPLENPSFSDLKLPIQLPNTSTETVQLENNDPLNSIGLPYYKDELLSSWSKYLIFDVGKPILDSNLLIAKQISENSHPVPQEIKSFHRNQIIEVPWLNRKLISEGATPKFHSERQKDIMSGNDIEGSASYFEEIEDTISGPDSIPKFYQRPVIKYSKFGIEDFDFGFYNKTKYAGLETDITNSYCNSVLQLLSYVPSFSKAAISHSLGPCDLMECLLCELGFLFAMLKESTGRNCQATNFLRAFSNSSFAQSLGIVFDDYSDGTFPDSFVIQKFTKFMLTEISRIADYEDKKDGTSFPVSFLLKSFCIPEMQTYRCGICGITSQKIKSSLYIIDLHYPSQQLESILSFEWLFKMSLDRRVDLPPGWCEYCLAHQPFLLRSFIRSLPDCLFINTQVKHHEHWKLWARKNWLPKKLHLRRVNDTMQCVSQKISNLDKDQQSLSVYVLRGIIYEIRQNGEEPHFVSTIRVSDNTSSDNPDDNRWYIFNDFLVKEVTEEEALTVHGPWKIPIIVYYEKLDTKIPQWDEVSDYTLLYQPYSLNKNPPINKIQPLTTDEMLYPKMLVGIDSEFVALQQEETEVRSDGTKSTIKPSKLSLARVSVLRGEGPNKGLPFIDDYVATDDKVTDYLTEYSGIHPGDLDPDRSPYNVVPLKVAYKKLRLLVNAGCIFVGHGLQKDFRIINLLVPPEQVVDTVDLFFLSSRQRKLSLKFLAWYLLDEEIQLTEHDSIEDALTALKLYDCYDKLKSQGKLEETLDNIYEVGRRFKFRPPSVASMSLEDRNSYGDESVISNQTN
Protein: Expansin (Q8LKK3)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted, cell wall {ECO:0000256|RuleBase:RU365023}. Membrane {ECO:0000256|RuleBase:RU365023}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365023}.
Interaction partners:
Sequence:
MATKTMMLQIFPLFFFLFSVCNSIFLGANGDDNGGWQTAHATFYGGADATGTMGGACGYGNLYSQGYGTSTAALSTALFNNGLSCGACYELRCNNDPQWCISRTITVTATNFCPPNYALSSDNGGWCNPPREHFDLAEPAFLRIAEYRAGIVPVMFRRVSCVKKGGIRYTMNGHSYFNMVLITNVGGAGDITSESIKGSRTGWLPMSRNWGQNWQSNAYLNGQSLSFKVTASDGRTITAYNVVPAGWQFGQTFEGGQF
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I519)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGPPSTAPDYSSAKDAKELLDKIGQQVHDKVKSESNGFKDELEGSLSLAKVSGVELADTLDPCKLIKEKHENLIGARGDPCGKDGTGKEDDSKRFSKESGAECDEKKIKDNKSKGGNNEGACAPYRRLSLCNKNMEKMGRTSTTKHDLLLDVCMAANYEAESLIPYHDQYEATYKDYGSTMCTMLARSFADIGDIIRGRDLYSGNKVKKKKLDDSLKTIFGKIYEGLTGGVKERYTNDGGDFFQLREDWWTANRETVWKAMTCSEHLKNSAYFRVTCSDKQGESIANHKCRCPMTSDGKPNDQVPTYFDYVPQYLRWFEEWAEDFCRKKKIYVGIVKKYCLDETEEKYCSLNGCDCTQTVRAKGKLRYGNRCTDCLFACHRYEKWIDNQRKQFLKQRNKYADEIKKYINEASSSSGSGRQRRGARNENYDGYESKFYDILKNKRYENVDAFLGLLNNEKACQAVTDDKGGRINFKNVNSGKNSGGGESGDRGKGASSTSDTSGTNDETKGTFYRSKYCQPCPICGMKKKGGKWEAKNDDKCKRGKLYEPTSSAKPTEIKILKSGENHDDIEKKLEAFCETQNRSDGSSSVHVGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGGGGGSGSKSDSQKLYEEWKCYKHDEVQKVQGQGEEEDEDEVEEEDDLKSAGGLCILPNPKKKEESEAKSQNEPEQFQKTFYDFFTYWVAHMLKDSIHWRTEKLDKCINNTNGKQTKCRKGCKGDCDCFLKWVNEKKTEWGKIKDHFKTQEGLDNEGENGIPESTRFGFTHDVVLGEFLELQFLNENNEENSKNSLDSEEIKHLKNLRDIIKKKNQQAGAGATGKRTIMDELIDYEEGIAKDCQQKCQETQKPQQVDRDLARSATGPRDPSSPAAPTAGPVESAAVDDEDDDNEEEEEEEEEEDEKEEVGGSDVVEEKEEKEEEKEPEEQVEPQPAATTTQNDVKVCDTVDKLFKDTTALQDACNLKYVKGKNYGWRCVAPSHTTSETTGKSESATSSSGATTAPAPSLTSPQATASANSANSVSSAVCIPPRRRRLYVGKLEQWASGGNTQGGGGNTQVTPQAGGSEAQTQPQGKDAASTSPQVALLRDAFIQSAAIETFFLWHKYKMEKKKEKEETQGQVYKQTDDEDKTPQELLNSGKIPDGFLRQMFYTLADYKDILFSGDKDKKNGYSDIINGDKEMKAKEEKIKEAIQKFFEQTRGAIPPPPSGTTPSSWWEQHAESIWNGMICALTYTDNSDTVAKGKASITQDTDLKDALWDENGATNEPIKYKYTEATASGDNTPLTQFVLRPPYFRYLEEWGETFCRQRTRMLAKIRGECVKSGSERCSGDGEDCNDQLDADPTIVRDFLCSTCGRHCSFYKKWIQRKKEEFTEQYNAYGGQKTKCQTESETAKEFCGTLNTFNDAAKFLERLKSGPCKNNENVEDNGKDKLDFSKPNETFVPATNCKPCSSFKIDCKKAKCSNRDDTNVGFNCKKNGNGYITSDHIKNEDNFTDTIDMLVSDDNKNKSETVLEACEGADIFEGIKENKWKCGNVCGYVVCKPENGNGKIVNGKPNGENQIIIIRALFKRWLEYFLEDYNKIRKKLKPCMNNSDGSPCIDNYKKKYQCVLQWISRKEEEWKKIKEHYEKQKPKNGDNNMKSLVTDILSGLYPQTDVNKAIKPCKGLTKFESFCGLNRTESSKIKDGTPKDVVECLFQKIQKKIEECKQKHPQPSANNCTTSPTSDTPPDDEEDLLHEEEENQVKAPEICPTPQQEPEAEDEGECKAASPATSEEQTNQTSNPHETPVLKPEEEATAPTSPPRPPLVTSTLAWSVGIGFAAFTYFYLKKKTKSSVGNLFQILQIPKGDYDIPTLKSTNRYIPYASDRHKGKTYIYMEGDTSGDEDKYAFMSDTTDVTSSESEYEELDINDIYVPGSPKYKTLIEVVLEPSKRDTQNDMPSDDIPSDIPNSDTPPPITDDEWNQLKKDFISNMLQNTQNTEPNILRDNVDNNTHPTPSRHTLDQKPFIMSIHDRNLLNGEEYNYDMSTNSGENNVYSGIDPTSDNRDPYSDKKDPISGTKDPISDNHHPYSGIDLINAALNGDYDLYDEILKRKENELFGTNHVKQTSTHSVAKNTNSDPVMNQLDLFHKWLDRHRDMCEKWDTNNKKEELLDKLKEEWNKDNNKHNGENTINKTLNTDVSIHIHMDDPKPTNEFSNMDTYPNNSSMDNILDDLEKYNEPYYDVQDDIYYDVNDHDASTVDSNNMDVPSKVKLEMSVKNTQMMEEKYPIGDVWDI
Protein: F-box domain-containing protein (Q4GYB8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFLKEGNSEMRLSGAAFLKGAVDDINACESPVLSSGSSLVLTSPALSTSDTCRSAMRETIPSVCAGAGLSSRCSTDCTVLKCVNPLHVKFQEPSGLSGADSVDSFDSLGDLSELHEEHQHVSSVASEKPLTLHDVPESVLYGAIPYLSLPDVIALSRTCKKFHKLVQGYFAVNEHGVMSIPAFDTRSFMQYRPERKPPVTKASSMEPATKASDVKPIRLFFGQQRRDPHPSALRRLLRFIAPDLVIAHMEAHTNPVNGRGKGCAWVFALSQLDAERLLRLSGRIFLDINSNGEEVYLFAPPNCREWLNEHAECAVASAVRPSHLPRQPMVVEAPRKSSAKVEKGLEQCVRPHPQHRGVTEQQAPVAAAQQMPDSVEPLVRVGSPQDEGLQQQERPSEAWTTSNHLQGDSTHGRRRSGEALQSGESTPERLQARRRPWLVAADASATQRARELRFCSNSSTSLHHEMWGFHPGARLGSGVGGDRFIACPETTTRTVPHNVYTSTIWTGPRRFRHDPYVYGPLCVLAAS
Protein: AP-1 complex subunit gamma-1 (Adaptor protein complex AP-1 subunit gamma-1) (Adaptor-related protein complex 1 subunit gamma-1) (Clathrin assembly protein complex 1 gamma-1 large chain) (Gamma-adaptin) (Gamma1-adaptin) (Golgi adaptor HA1/AP1 adaptin subunit gamma-1) (P22892)
Organism: Mus musculus (Mouse)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:O43747}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43747}; Cytoplasmic side {ECO:0000250|UniProtKB:O43747}. Cytoplasm {ECO:0000250|UniProtKB:O43747}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43747}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O43747}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:O43747}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (By similarity). Co-localizes with AFTPH/aftiphilin in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:O43747}.
Interaction partners:
- AP-1 complex subunit beta-1
- AP-1 complex subunit mu-1
- AP-1 complex subunit sigma-1A
- AP-1 complex subunit sigma-3
- AP-1 complex subunit mu-2
- AP-1 complex subunit sigma-2
- Clathrin heavy chain 1
- AP-2 complex subunit beta
- AP-2 complex subunit mu
- AP-3 complex subunit beta-1
Sequence:
MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPSEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPASAGGELLDLLGDITLTGAPAAAPTPASVPQISQPPFLLDGLSSQPLFNDIAPGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSVVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ
Protein: Small ribosomal subunit protein uS7 (40S ribosomal protein S5) [Cleaved into: Small ribosomal subunit protein uS7, N-terminally processed] (P97461)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P46782}.
Interaction partners:
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein eS26
Sequence:
MTEWEAATPAVAETPDIKLFGKWSTDDVQINDISLQDYIAVKEKYAKYLPHSAGRYAAKRFRKAQCPIVERLTNSMMMHGRNNGKKLMTVRIVKHAFEIIHLLTGENPLQVLVNAIINSGPREDSTRIGRAGTVRRQAVDVSPLRRVNQAIWLLCTGAREAAFRNIKTIAECLADELINAAKGSSNSYAIKKKDELERVAKSNR
Protein: Peroxisome biogenesis protein 19-2 (Peroxin-19-2) (AtPEX19-2) (Peroxisomal membrane protein import receptor PEX19-2) (Q94EI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to morphology determination of peroxisomes, but not to import of peroxisomal matrix proteins. Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16923726}. Peroxisome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Predominantly cytoplasmic.
Interaction partners:
- Peroxisomal membrane protein PEX14
- Peroxisome biogenesis protein 12
- Peroxisome biogenesis protein 16
- Peroxisome biogenesis factor 10
- Peroxisome biogenesis protein 3-2
- Peroxisome biogenesis protein 3-1
- T-complex protein 1 subunit delta
- Patatin-like protein 6
- Peroxisome biogenesis protein 19-1
- ABC transporter D family member 1
Sequence:
MANDTHTDDLDELLDSALDDFKDLNLTQRNGGVKKEEGDKKETESLPSGVQGLGMGLPDMRSKKKGKKKIAKEDHVTEALDKLREQTRETVKGLESLSSKQQPTGSDDAMVEDWIKQFENLTGSNDLESIVDTMMQQLLSKDILHEPMKEIGARYPKWLEEHESSLNKEEFDRYSRQYELIKELNLVYENEPNNSTKIMEIMQKMQECGQPPSDIVQEMDPGFDFASLGQMSPDMLESSPNCCVM
Protein: ATP-citrate synthase (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase) (Citrate cleavage enzyme) (P16638)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53396}.
Interaction partners:
- Citrate synthase, mitochondrial
- Fatty acid synthase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Aconitate hydratase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Malate dehydrogenase, mitochondrial
- Cytoplasmic aconitate hydratase
- Pyruvate carboxylase, mitochondrial
- Acetyl-CoA carboxylase 1
- Malate dehydrogenase, cytoplasmic
Sequence:
MSAKAISEQTGKELLYKYICTTSAIQNRFKYARVTPDTDWAHLLQDHPWLLSQSLVVKPDQLIKRRGKLGLVGVNLSLDGVKSWLKPRLGHEATVGKAKGFLKNFLIEPFVPHSQAEEFYVCIYATREGDYVLFHHEGGVDVGDVDTKAQKLLVGVDEKLNAEDIKRHLLVHAPEDKKEILASFISGLFNFYEDLYFTYLEINPLVVTKDGVYILDLAAKVDATADYICKVKWGDIEFPPPFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNELANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRAIRDYQGSLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMAWAPAIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVPSPRSLQGKSATLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQKFYWGHKEILIPVFKNMADAMKKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEGIPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYVSRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIGGTEEYKICRGIKEGRLTKPVVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALKEAGVFVPRSFDELGEIIQSVYEDLVAKGAIVPAQEVPPPTVPMDYSWARELGLIRKPASFMTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQRRLPKYSCQFIEMCLMVTADHGPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFVNKMKKEGKLIMGIGHRVKSINNPDMRVQILKDFVKQHFPATPLLDYALEVEKITTSKKPNLILNVDGFIGVAFVDMLRNCGSFTREEADEYVDIGALNGVFVLGRSMGFIGHYLDQKRLKQGLYRHPWDDISYVLPEHMSM
Protein: Meiotic driver cw9 (A0A1X9Q9F0)
Organism: Schizosaccharomyces pombe (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
Sequence:
MKNKYYPLRSSMDEMSAKNDNEIDLEKGPLPEYNSEDGSTLPPYSDLNNPKQMGQNITKLFNWNKSTTPPDYDENRLPITDEGNNPPNTHRENHSSGTTDNSSPFLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALLFLTYFYETWSKAVKVTIIFLAQCIKVTAVFLAQCVKVTAISLAKCVKVTAVGLYNSREKWVVIIWLLWVVICYTLFLRSKFGNLNLNKALICSTCSISAALLLFLLYVRLPFWTLKHMFSGLFQVLGVQSCVVIVTKGLMHLFDKHIDATGYEIEVSSLFVIGNFLFFYEMECPGALRRMPKSIRNGIASFLEGTGRAIRGANDNNNSIPLEETEAESEV
Protein: SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3) (Q61120)
Organism: Mus musculus (Mouse)
Function: Signaling adapter that couples activated growth factor receptors to signaling pathway in neurons. Involved in the signal transduction pathways of neurotrophin-activated Trk receptors in cortical neurons (By similarity).
Interaction partners:
- High affinity nerve growth factor receptor
- Proto-oncogene tyrosine-protein kinase Src
- Growth factor receptor-bound protein 2
- BDNF/NT-3 growth factors receptor
- Insulin-like growth factor 1 receptor
- Epidermal growth factor receptor
- Son of sevenless homolog 1
- Receptor tyrosine-protein kinase erbB-4
- Receptor tyrosine-protein kinase erbB-2
- Vascular endothelial growth factor receptor 2
Sequence:
MSATRKSRAGDEPLPRPPRGAPHTSDQVLGPGVTYVVKYLGCIEVLRSMRSLDFSTRTQVTREAISRVCEAVPGAKGALKKRKPPSKMLSSILGKSNLQFAGMSISLTISTASLNLRTPDSKQIIANHHMRSISFASGGDPDTTDYVAYVAKDPVNRRACHILECCDGLAQDVIGSIGQAFELRFKQYLQCPSKVPALQDRMQSLDEPWTEEEGDGPDHPYYNSVPTKMPPPGGFLDARLKGRPHAPEAAQFAGKEQTYYQGRHLGDTFGEDWQRAPTRQGSLDIYSTAEGKTHMVPVGETPTYVNTQPVPPQVWPAATSSTESSPRKDLFDMKPFEDALRNQPLGPMLSKAASVECISPVTPRAPDARMLEELNAEPWYQGEMSRKEAEALLREDGDFLVRKSTTNPGSFVLTGMHNGQAKHLLLVDPEGTIRTKDRVFDSISHLINYHLESSLPIVSAGSELCLQQPVERKP
Protein: A disintegrin-like and metallopeptidase (Reprolysin type) with thrombospondin type 1 motif, 3 (B2RY57)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MVFLSLWLIAASLVEVRTSADGQAGTDEMVQIDLPTKRYREYELVTPVSTNLKGHYLSHILSANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHETAPRPGNTTDPRDSHLHGSASEGSWRSEPLQTSCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLERGKQMDEENGRIHVVYKRSAVEQPPRDVSEDVYHRESDLEGLDDLGTVYSNIGQQLNKTMRRRRHTGENDYNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIERGNPSRSLENVCRWACQQQKTDPNHAEHHDHAIFLTRQDFGPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDETAMGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSYDCLLDDPFEHDWPKLPELPGINYSMDEQCRFDFGVGYKMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTECAAGKWCYKGHCMWKNANQQKQDGNWGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEECQKHFEDFRAQQCQQRNSHFDYQNTKHHWLPHEHPDSKKRCHLYCQSKETGDVAYMKQLVHDGTRCSYKDPYSICVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHCRTVKGTFTRTPRKLGYLKMFDIPPGARHVLIQEDEASPHVLAIKNQATGHYILNGKGEEAKSRTFIDLGVEWDYNIEDDIETLHTDGPLHDPVIVLIIPQENDTRSSLTYKYIIHEDSVPTINSNNVIQEELDTFEWALKSWSQCSEPCGGGFQYTKYGCRRKSDSKMVHRSFCEVNKKPKPIRRMCNIQECTHPVWAADEWEHCSRSCGSSGNQLRTVRCLQPLQDGTNRSVHSKYCLGDRPESRRPCNRVPCPAQWKTGSWNECSVTCGEGTEVRQVLCRTGDHCDGEKPESVRPCQLPPCNDEPCLGDKSIFCQMEVLARYCSIPGYNKLCCESCSKRSGTLPPPYLQEAAEIHSDAIFGPSDLPRSLVMPTPFLPSSSGTRAEKKSLSSFSSMANPNADAAFRASSRASADFPRKRAHQAGRKTLESVPSSSSIKTDHLRPASPVAAAPSPAISDSIGASPQTRTPKKDDAKSVSRRHPTRSTASER
Protein: Matrix metallopeptidase-21 (MMP-21) (EC 3.4.24.-) (A0A0N9E2K8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway.
Interaction partners:
- Cilia and flagella-associated protein 52.
- Cilia- and flagella-associated protein 53
- B-cell CLL/lymphoma 9-like protein
Sequence:
MLTVIRRIFIIQTFIFITAEKIFHSRDHSDVLNNIHQAELITDTDTAQRFLSKYGFIKAAGSEESQLSESSGDLDFSLSLDLHEGGTTSGSSSSDLQFVSALRDFQRLSDLPVTGVFDDATKAAMNKPRCGVMDDDQELKDVTGSNSTRNHIRTSTNTSHNHEHQAPVRKKRHLSALLKNTSLQKRDVSKWTGHMAFSKSVLKWRLIGEGYSSQLSIQEQKYIFRLAFRMWSEISPLQFIEDLHSPLENIDIRLGFGTGRHLGCSQRFDGAGREFAHAWFLGDIHFDDDEHFTVPNTGSGISLLKVAVHEIGHVLGLPHIYRPGSIMQPSYLPQDAGFEIDWMDRKSIQRLYGVCTGRFSTVFDWIRKEQTPYGEVVVRFNTYFMRDGLYWLYENRNNRTRYGDPVAVQVGWHGLPSGGVDAYVHVWNRKTDAVYFFKGMQYWRYDSENDHVFSHAPDGRLYPRLISEDFPGVSGPLDTAYYDRRDAHIYFFKGSQVFRFDVRMRRLASSSPQEMTEVFPAIVSGDHPVRSLDAAYFSYTHNTVFLLKGSLFWRVLSGKERRRRAFLPMNGLLAHRRVHEQWFDICDVHSSSLRTTRRR
Protein: Uncharacterized protein C553.10 (O74947)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}. Note=Localizes at the cell surface.
Interaction partners:
- Uncharacterized protein PB18E9.04c
- Putative cell agglutination protein pfl4
- Uncharacterized protein C4H3.03c
- Putative cell agglutination protein pfl5
- Putative cell agglutination protein pfl9
Sequence:
MLFKISFLALIASALAMSINSPTNGDTWQTNGEEQITWNVVSTDEPSAALYLTNFAVYPTVTQYLDTVDTSTGSYTTNTTNWPTGQGFQINMAYPGRPEQIYAQSQQFNIVEGAASSSSSSSSSSSSLVSSTTSSSSSATPSTTSSSSSSSSSSSSSSSKSSSSSSKSSSRSSSRTTSHRTTSHKSSSYRPTVFPYTTISHYNITNATNGTYCNGTNGTNFTCIVNASNATNSTFWLNGTNSTNGTNSTNSTSTTSHSLTKLPTSSKSLTTSKTTASGHITKGVMEALSTNDTTNTTDDATNTTSDSSSSSSASASSSSSSSSAASLVSQPVGISAVIAFFAVALSLTL
Protein: tRNA N(3)-cytidine methyltransferase METTL2B (EC 2.1.1.-) (Methyltransferase-like protein 2B) (Q6P1Q9)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr)(UGU) and tRNA(Arg)(CCU).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:34268557}.
Interaction partners:
- Presenilin-2
- Presenilin-1
- Probable methyltransferase-like protein 25
Sequence:
MAGSYPEGAPAILADKRQQFGSRFLSDPARVFHHNAWDNVEWSEEQAAAAERKVQENSIQRVCQEKQVDYEINAHKYWNDFYKIHENGFFKDRHWLFTEFPELAPSQNQNHLKDWFLENKSEVCECRNNEDGPGLIMEEQHKCSSKSLEHKTQTPPVEENVTQKISDLEICADEFPGSSATYRILEVGCGVGNTVFPILQTNNDPGLFVYCCDFSSTAIELVQTNSEYDPSRCFAFVHDLCDEEKSYPVPKGSLDIIILIFVLSAVVPDKMQKAINRLSRLLKPGGMVLLRDYGRYDMAQLRFKKGQCLSGNFYVRGDGTRVYFFTQEELDTLFTTAGLEKVQNLVDRRLQVNRGKQLTMYRVWIQCKYCKPLLSSTS