wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12) (Deubiquitinating enzyme 11) (Ubiquitin thioesterase 11) (Ubiquitin-specific-processing protease 11) (P36026)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MLLNPDQILNLVRKVYEVDIKQFYSQLRLKNLRGLLDHAAHLFNVYLRDLEINQEMEALTAFIIGCYYLYLIIPQSLQFQTRNNLYSSYAKLKNDYQDEHVMGYVLKVVRDESTVIVDRYLAESNGICRTIKRKRAYSLPLRPLPVHMASLSIHNKFDGSLHEIPNELTKPTNDNSKEDIVRESNQIASSNKLEAGSEVAYYTSKEALSKPSYLKLSTGKDALFKTLSSPATAPPVHSLEVSSQIRDSSQDSSSSLSKVEKPKEEEGKIEAIESSAPKAYNLPVIEDSNDLLSELSITGLQNPCNTCYINSIIQCLFGTTLFRDLFLTKKYRLFLNTNKYPKEVQLSRSIYVLFKKMYLNGGRAIIPNRFLKMCKKLRPDLNIPDDQQDTQEFLLIVLARIHEELSNENVVKYYPDLVSYDANALQVNPSKYEKWYERNVITDGLSPIDHIYRGQLENILKCQRCGNSSYSYSTFYVLSLAIPKLSLYSFTSKSRKIKLEDCINLFTGDEELSGDNAWDCPNCRITDSKSKKEEITSQKKKSTIFGFHSRSRSKSPHHHHHHHHSSDDSTKNAKKRNSKKLTTIKSLDFIVLPPILVIHLSRFYYDLTKKNSTVITYPLILNIILKNGKVIRYKLYGTVNHSGNLINGHYTSVVNKEKSHEIGLNRQVWVTFDDDYIQQHRKDRNNFEAGKTEMSSDEVYVLFYERMDEENYEEEFC
Protein: Uncharacterized WD repeat-containing protein C16H5.13 (O42948)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDWVALSKSCKTHLLDEGLDVSSIHCFDQYLIVGQCSGQVMVFDVSTDNHFTLIQTFIAHKHSVSSIVCLPFEADGIVDLSIITLDESGLLCQWLLKTCDRRATLQLCDGLCLKLFRLNNNFLAVTGTFLKIYLIRISNFQIVATWTGHEDWPILFPFKDEALLIPVAYSDGSVSLWSVDWSALTFKRNSVTKADVKPTFGKVIDVVPADCISSNYALYVYSDAVVLLESHEKFIASYSLAEITSVFVLADGTACIFTLSSSTLLKLHQSPEPHFELISKYSGDFPWKSCTILKSKPVSLCVYPEKITFNWLTEGTVDSCNLCKLSNTAAVSYAYTDSLNLFLGTTSGLVMFSLFDWYLHNDPAPLYSFTRVSGIVTYMKIFETEHSRSILVVATKTGKAYFYQQLQGERWRFLCERALQSSSITKIIHAKKSLSSGSSGLFIFMSLDGSLCALDESYNLLSYLPSDGAQVETLYSFPDLDQIYVAYDNFQLLNWDVVDQKCSEGNYSDIIDSSFISIGTFDKSNLPTLYHGSCALLTDNLVTVFLDAHDLVLNLNFSNENYIEKTYIDEFLDFIQPPFLNSDIEMEHQLLGTVFDQSSLHLGVGKPDGNAILRFDTEMKSIINTAPNCSALLLYLYFSLMVPLCKYDGLSDTKLTEGILLKLKDLKTVDYSISVLSYVWNNSGKVMQGIIKSMLSRTLELISPEELQRLIYYYFEFFTTTGGEYYLKKEVQHSLYILSLIVSLRPSAFDVSQLKFLSSYLLQKSESMDYDLTAIRLLSNGFSVFSKHIDPAKFIYNLVLSSLENTKDLDDKNSILYRSIVDVSVSNAVLLLTCLCDEVYEQMKSNLRSVILKVVSLAIENTQSEFSLFNQLITEKLLPILYSSRSVEEVHDVTNAIATQFPFACFDSKVEKYSYIDDGDLVVYEIAKRRKVVSKENAECDIQVLSASPSGDYFVGVSATQKECIIWKYSQDFVKFLNLSTPSLTIRKRILLQTNKTNEVEIPEVLWISQSSAEVHIGSTFAIIDL
Protein: Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Q583T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03133}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03133}.
Interaction partners:
- Cell division cycle protein 16, putative
- Cyclosome subunit 1, putative
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 11
- Rev7, putative
- 40S ribosomal protein S18, putative
- Anaphase-promoting complex subunit 10
- Uncharacterized protein
- Ankyrin repeat protein
- Tyrosyl/methionyl-tRNA synthetase, putative
Sequence:
MTKAVTEWPVNRVRQEFVSFFEQRGHTFVPSSAVVPHNDPTLLFTNAGMNQFKNLFLGTADPNTDFGRLTRAVNSQLCIRAGGKHNDLDDVGRDTYHHTFFEMLGSWSFGDYFKREAILWSWELLTEVYKLPKDRLYATYFEGDPANGIEADEESKQLWLQLLPASRVIAGNAKDNFWEMGDVGPCGPCSEIHFDRIGGRDAADLVNKDDPMVLEVWNLVFMQFERRAGGVIVPLPKMHVDTGMGLERLTSILQGADSNYDTDAWTPLFDTIQKVTGFEKSYAEVRHDTCDATVAYRAVADHIRCLTVALADGAMPDSVGRGFVLRRIIRRAVRYGVQFLGAKVGFFHQLVDSVVSSLGPFFKHIQEPRTVQRIKGVLADEETSFARTWETGLKHFNKAVAEAVNNVISGENAFILHDRYGFPVDLTSLLAEKANMSVDLEGFHATMKASQLSSGRVAAAKTFIDVHQLEELKAGGVSPTDDSAKYTWKKHVAEVKAIFDKKSGSFVDVLLPDSEMGPEDIGIILDVTNFYAEAGGQIYDTGCIVAAPDAIFDVRKVYNVGGYIVHVGGMRSVEDGAAAPIPVTASVELQVDYERRLPIAANHTSTHILNWCLRRVLEEEAKDNFMEVNQKGSLVTPEMLRFDFSYNNKVSLEDLIKVEKLINQIIQQGLEVYRKEIALDAASRIAGLRHMFGEKYPDPVSVISVGVPVEKLIAEPESEEWRAYSTEFCGGTHLSNTQDAQLAVILSEESLMKGIRRMVVATRDAARKAQEGGKALQQEYREIMSRPASDAVAKSLSVLNKKVGDSAIPLVVKNTLREEIDGSIKNVLGALKAQAAQMKEKATEAGRAAAEAYDASAGPLLVRHLTDTGADREALQAYADGFSKAVSGDVGLFLVGSDESKALALVSLPPAFVAKKLDAVSWAKTAVGKGGGKPSAAQSGFPAANTTQVLQKAEVEAAKMMAVLLN
Protein: Mitochondrial import protein 1 (Mitochondrial 13 kDa outer membrane protein) (Q08176)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the MIM complex required for mitochondrial outer membrane protein import. The MIM complex cooperates with the receptor TOM70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. Involved in import of the subset of proteins with multiple alpha-helical transmembrane segments, including UGO1. Required for the assembly of the TOM (translocase of outer membrane) receptor complex, which is responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Required specifically for assembly of TOM40, TOM20, and TOM70, but not TOM22.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:15326197, ECO:0000269|PubMed:15608614}.
Interaction partners:
- Mitochondrial import protein 2
- Mitochondrial import receptor subunit TOM70
- Mitochondrial fusion and transport protein UGO1
- Mitochondrial import receptor subunit TOM20
- Sorting assembly machinery 35 kDa subunit
- Mitochondrial import receptor subunit TOM22
- Sorting assembly machinery 50 kDa subunit
- Sorting assembly machinery 37 kDa subunit
- Mitochondrial distribution and morphology protein 10
- Mitochondrial import receptor subunit TOM5
Sequence:
MTEVVGFWESVSDDESEDKDCMEVQNTVSADESPLVQSLVSFVGSCSINLLLPFLNGMMLGFGELFAHELCWRFNWFNHRNKGYKVYPESRKIAALKEISSPGTRGRVASKFL
Protein: NEDD8-conjugating enzyme UBC12 (EC 2.3.2.34) (RUB1-conjugating enzyme) (Ubiquitin carrier protein 12) (P52491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins. The major substrate is CDC53/Cullin.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- Defective in cullin neddylation protein 1
- RING-box protein HRT1
- NEDD8-activating enzyme E1 regulatory subunit
- NEDD8-like protein RUB1
- Ubiquitin-activating enzyme E1 1
- Cell division control protein 53
- Cullin-3
- Ubiquitin-activating enzyme E1-like
- Chitin synthase 2
Sequence:
MLKLRQLQKKKQKENENSSSIQPNLSAARIRLKRDLDSLDLPPTVTLNVITSPDSADRSQSPKLEVIVRPDEGYYNYGSINFNLDFNEVYPIEPPKVVCLKKIFHPNIDLKGNVCLNILREDWSPALDLQSIITGLLFLFLEPNPNDPLNKDAAKLLCEGEKEFAEAVRLTMSGGSIEHVKYDNIVSP
Protein: Calpain-like protease 1 (EC 3.4.22.-) (Calpain-7) (Cysteine protease RIM13) (Regulator of IME2 protein 13) (Q03792)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the proteolytic cleavage of the transcriptional repressor RIM101 in response to alkaline ambient pH, which is necessary for sporulation and invasive growth. Probably the protease that cleaves RIM101.
Interaction partners:
- pH-response transcription factor pacC/RIM101
- pH-response regulator protein palA/RIM20
- Vacuolar-sorting protein SNF7
- pH-response regulator protein palF/RIM8
- Uncharacterized protein YGR122W
- pH-response regulator protein palH/RIM21
- pH-response regulator protein palI/RIM9
- Protein DFG16
- Peflin
- Transcriptional regulator NRG1
Sequence:
MNDWHEFNAAIKSIYCNAEGDSSSIINRLVGLAMKSEDSTFIEAVLVLKENVSKVDKQLRFLWLTSTINSRFYPPIPISEASPVSWNKTEYCAPGTEELQRRYPGRAKLQNEEDYSGGIEQCRDVPDCSLVASLINLRSKNLNLPLIKQISSTKYHVNLSFNGSNKRLVTVDISQIPTSVDGKQLSLKSNDISDKIGELALLLVSKGTYSTDGSNISIDTYRLSGFLPEITQVNSYPFEKLWKFHKSNLCLMGAGTGNRSNDMIKPLVENHDYSIIDITYDSRLVKLRDPRNSALNVEISYEQYLKNFKQLYLNWNQEKLFKRSQVLHFRYDTSRYNKFSIVADKPLFHLVNNSKVTETVWLLLESHLQDEGSQENRSVSFLNEAPECIICPIEPPVECGGNHIGLQLVKLRLDAETERLLYCYSTTNNNFSIHSFSVVKEICFQRLKDTKSLFAKVLFSFPYEIEGKASFDTCNFFQNPTFELEVHSEQDYQVLMDAACISTSSHDLINIQVYYFNDYELIKPIMFDNHYQPGQGLKQDVPILTNVKYMIVCSTYGPPASTEFELLASIRLSSSWRLISGITLRSVNLIYGTYPYHCRNRFHWKETSDKLKIQMTLPTKKYSTNKLFIRVVPVESSARLRMRCNIFEPESALCVYECQEYRTCPSGGIVIPDLEVSRTNIVVLMIERSVPISSCLPTEGQLDELELFVGSSQKIRIEKYSDDVIPK
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (O61444)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase kinase kinase 7
- FI16976p1
- Putative mitogen-activated protein kinase kinase kinase 7-like
- Transcription factor Jra
- Apoptotic signal-regulating kinase 1, isoform C
- GH01161p
Sequence:
MAERPKNLFATGSSRSRNPPDQLSLNNLSIRHPPSSTSSTSSGSTSSGSSSSSQHNHVTRCFGAQQPQQTPPVASSQVPPVPAASSSSAADRHRERIRQQACGKLQFGEGGANTHTFTSDDLEDEGEIGRGAFGAVNKMTFKKLDKVMAVKRIRSTVDEKEQKQLLMDLEVVMKSNECIYIVQFYGALFKEGDCWICMELMDTSLDKFYKYIYEKQQRHIPESILAKITVATVNALNYLKEELKIIHRDVKPSNILLHRRGDIKLCDFGISGQLVDSIAKTKDAGCRPYMAPERIDPERAKGYDVRSDVWSLGITLMEVATGNFPYRKWDSVFEQLCQVVQGEPPRLLTSYNGMEFSKEFVDFVNTCLIKKESDRPKYSRLLEMPFIRRGETSHTDVAVYVADILESMEKDGITQFTANQQAES
Protein: Fucose kinase (A0A0G2JVI4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- GDP-L-fucose synthase
- Galactose mutarotase
- GDP-mannose 4,6 dehydratase
- Bifunctional polynucleotide phosphatase/kinase
- REC114 meiotic recombination protein
- Galactose-1-phosphate uridylyltransferase
Sequence:
MDQPKGVNWTVIILTCQYKDSVQVFQRELEVRQKREQIPAGTMLLAVEDPQTRVGSGGATLNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPQAPVEALVCNLDCLLDIMTHRLGPGSPPGVWVCSTDMLLSVPPNPGISWDGFRGTRVIAFPGSLAYALNHGVYLTDSQGVVLDIYYQGTKAEIQRCVRPDGLVPLVSGVVFFSVETAEHLLATHVSPPLDACTYMGLDSGAQPVQLSLFFDILLCMARNMSRENFVAGRPPEMGQGDPDVARYLKGARAQLWRELRDQPLTMVYVPDGGYSYMTTDATEFLHRLTMPGVAVAQIVHSQVEEPQLLEATCSVVSCLLEGPVHLGPRSVLQHCHLRGPIHIGAGCFVSGLDTAHSEALHGLELHDLILQGHHIRLHGSQSRVFTLAGRLDSWERQGAGMYLNMSWNEFFKKTGIRDWDLWDPDTPLSDRCLLSARLFPVLHPTRALGPQDVLWMLHPHKDRGEALRAWRASWRLSWEQLQPRLDRAATLDFRRDLFFRQALQKARHVLEARQDLCLHPLIRAAVGEGCSGPLLATLDKVAAGAEDPGVAARALACVADVLGCMAEGQGGLRSGPAANPEWIQPFSYLERGDLMRGVEALAQEREKWLTRPALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVDGRRPIGAKARRILEPELWLAVGPRQDEMTVKIVCRSLDDLQDYCQPHAPGALLKAAFICADIVHVNSEVPLHEQLLRSFNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRTVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKVGRSRAQLPLKVEVEEITVPENFVQRINDHLLLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTEKCAEAFRQGNLALLGQYLTSYWEQKKLMAPGCEPLAVHRMMDVLAPYAFGQSLAGAGGGGFLYLLTKEPRQKEVLEAVLAKVEGLGNYSVHLVQVDTQGLSLQLLGHDAHLCGAGPSEVGNT
Protein: Protein disulfide-isomerase A6 (EC 5.3.4.1) (Thioredoxin domain-containing protein 7) (Q922R8)
Organism: Mus musculus (Mouse)
Function: May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (By similarity). May also regulate the UPR via the EIF2AK3 UPR sensor (By similarity). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q15084}. Cell membrane {ECO:0000250|UniProtKB:Q15084}. Melanosome {ECO:0000250|UniProtKB:Q15084}.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- DnaJ homolog subfamily B member 11
- Hypoxia up-regulated protein 1
- Protein disulfide-isomerase A4
- ERO1-like protein beta
- Calreticulin
- ERO1-like protein alpha
- Protein disulfide-isomerase
- Stromal cell-derived factor 2-like protein 1
Sequence:
MARLVLGLVSCTFFLAVSGLYSSSDDVIELTPSNFNREVIQSDGLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVNADKHQSLGGQYGVQGFPTIKIFGANKNKPEDYQGGRTGEAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRGDSSSKKDVVELTDDTFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAATEVKEQTKGKVKLAAVDATVNQVLASRYGIKGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKKTCEEHQLCVVAVLPHILDTGAAGRNSYLEVLLKLADKYKKKMWGWLWTEAGAQYELENALGIGGFGYPAMAAINARKMKFALLKGSFSEQGINEFLRELSFGRGSTAPVGGGSFPTITPREPWDGKDGELPVEDDIDLSDVELDDLEKDEL
Protein: Alpha-glucosidase (EC 3.2.1.20) (Maltase) (P56526)
Organism: Aspergillus niger
Function: Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.
Interaction partners:
Sequence:
MVKLTHLLARAWLVPLAYGASQSLLSTTAPSQPQFTIPASADVGAQLIANIDDPQAADAQSVCPGYKASKVQHNSRGFTASLQLAGRPCNVYGTDVESLTLSVEYQDSDRLNIQILPTHVDSTNASWYFLSENLVPRPKASLNASVSQSDLFVSWSNEPSFNFKVIRKATGDALFSTEGTVLVYENQFIEFVTALPEEYNLYGLGEHITQFRLQRNANLTIYPSDDGTPIDQNLYGQHPFYLDTRYYKGDRQNGSYIPVKSSEADASQDYISLSHGVFLRNSHGLEILLRSQKLIWRTLGGGIDLTFYSGPAPADVTRQYLTSTVGLPAMQQYNTLGFHQCRWGYNNWSDLADVVANFEKFEIPLEYIWTDIDYMHGYRNFDNDQHRFSYSEGDEFLSKLHESGRYYVPIVDAALYIPNPENASDAYATYDRGAADDVFLKNPDGSLYIGAVWPGYTVFPDWHHPKAVDFWANELVIWSKKVAFDGVWYDMSEVSSFCVGSCGTGNLTLNPAHPSFLLPGEPGDIIYDYPEAFNITNATEAASASAGASSQAAATATTTSTSVSYLRTTPTPGVRNVEHPPYVINHDQEGHDLSVHAVSPNATHVDGVEEYDVHGLYGHQGLNATYQGLLEVWSHKRRPFIIGRSTFAGSGKWAGHWGGDNYSKWWSMYYSISQALSFSLFGIPMFGADTCGFNGNSDEELCNRWMQLSAFFPFYRNHNELSTIPQEPYRWASVIEATKSAMRIRYAILPYFYTLFDLAHTTGSTVMRALSWEFPNDPTLAAVETQFMVGPAIMVVPVLEPLVNTVKGVFPGVGHGEVWYDWYTQAAVDAKPGVNTTISAPLGHIPVYVRGGNILPMQEPALTTREARQTPWALLAALGSNGTASGQLYLDDGESIYPNATLHVDFTASRSSLRSSAQGRWKERNPLANVTVLGVNKEPSAVTLNGQAVFPGSVTYNSTSQVLFVGGLQNLTKGGAWAENWVLEW
Protein: Calsequestrin (Q20203)
Organism: Caenorhabditis elegans
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}.
Interaction partners:
- Ryanodine receptor
- Aspartyl/asparaginy/proline hydroxylase domain-containing protein
- Myosin, essential light chain
- Calreticulin
- EF-hand domain-containing protein
- RRM domain-containing protein
- Junctophilin-1
- Tubulin alpha chain
- Troponin I 2
- peptidylprolyl isomerase
Sequence:
MTWIKLASLALVVVLASAGISKNEDLECMFLGYPDLEYDGFDRTEVLTEKNFNRTVFAEDTKSVVFFNDVEEDDSELDQYECFLQLSAQIMTKRGYNFYTVNTTKEHRLRKQEEVEKGEDTIHVYKDGYKIEYNGVRDPETFVSWLMDIPDDPVTIINDEHDLEEFENMDDECVRIIGYFEPGSVALKEFEEAAEDFMGEIEFFAVVTSKWARKVGLKRVGEVQMRRPFEEDPLFAPTSADTEEEFEDWVEKNKEPVMQKLTLDNYFNLWRDPEEEERMILAFVDEETREGRAMKRLLDKIADENSEHAGTLEIILVDPDEFPLMVDVWEDMFGIDIEEGPQIGLIDISEKEGIWFDMSQVNLDDPKKHSDSNFEALQSWIDQILSGSISLDDDDDDEPEPPAPPPTPKGKKSRKEL
Protein: Leptin receptor (LEP-R) (HuB219) (OB receptor) (OB-R) (CD antigen CD295) (P48357)
Organism: Homo sapiens (Human)
Function: Receptor for hormone LEP/leptin (Probable). On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (By similarity). In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity. Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis. Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T -ells. Leptin increases Th1 and suppresses Th2 cytokine production (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:19159218}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:19159218}.; SUBCELLULAR LOCATION: [Isoform E]: Secreted {ECO:0000250|UniProtKB:P48356}.
Interaction partners:
- Leptin
- Tyrosine-protein kinase JAK2
- Suppressor of cytokine signaling 3
- Signal transducer and activator of transcription 3
- Pro-opiomelanocortin
- Tyrosine-protein phosphatase non-receptor type 11
- Interleukin-6
- Leptin receptor gene-related protein
- Insulin
- Agouti-related protein
Sequence:
MICQKFCVVLLHWEFIYVITAFNLSYPITPWRFKLSCMPPNSTYDYFLLPAGLSKNTSNSNGHYETAVEPKFNSSGTHFSNLSKTTFHCCFRSEQDRNCSLCADNIEGKTFVSTVNSLVFQQIDANWNIQCWLKGDLKLFICYVESLFKNLFRNYNYKVHLLYVLPEVLEDSPLVPQKGSFQMVHCNCSVHECCECLVPVPTAKLNDTLLMCLKITSGGVIFQSPLMSVQPINMVKPDPPLGLHMEITDDGNLKISWSSPPLVPFPLQYQVKYSENSTTVIREADKIVSATSLLVDSILPGSSYEVQVRGKRLDGPGIWSDWSTPRVFTTQDVIYFPPKILTSVGSNVSFHCIYKKENKIVPSKEIVWWMNLAEKIPQSQYDVVSDHVSKVTFFNLNETKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTSTIQSLAESTLQLRYHRSSLYCSDIPSIHPISEPKDCYLQSDGFYECIFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSSVKAEITINIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKMYEVYDAKSKSVSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSNPAYTVVMDIKVPMRGPEFWRIINGDTMKKEKNVTLLWKPLMKNDSLCSVQRYVINHHTSCNGTWSEDVGNHTKFTFLWTEQAHTVTVLAINSIGASVANFNLTFSWPMSKVNIVQSLSAYPLNSSCVIVSWILSPSDYKLMYFIIEWKNLNEDGEIKWLRISSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDDIEKHQSDAGLYVIVPVIISSSILLLGTLLISHQRMKKLFWEDVPNPKNCSWAQGLNFQKPETFEHLFIKHTASVTCGPLLLEPETISEDISVDTSWKNKDEMMPTTVVSLLSTTDLEKGSVCISDQFNSVNFSEAEGTEVTYEDESQRQPFVKYATLISNSKPSETGEEQGLINSSVTKCFSSKNSPLKDSFSNSSWEIEAQAFFILSDQHPNIISPHLTFSEGLDELLKLEGNFPEENNDKKSIYYLGVTSIKKRESGVLLTDKSRVSCPFPAPCLFTDIRVLQDSCSHFVENNINLGTSSKKTFASYMPQFQTCSTQTHKIMENKMCDLTV
Protein: Crossover junction endonuclease eme1 (EC 3.1.21.10) (Essential meiotic endonuclease 1) (Q9C103)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Interacts with mus81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
Subcellular location: Nucleus {ECO:0000269|PubMed:11719193}.
Interaction partners:
- Crossover junction endonuclease mus81
- Structure-specific endonuclease subunit slx1
- ATP-dependent DNA helicase hus2/rqh1
- Exodeoxyribonuclease 1
- DNA topoisomerase 3
- DNA repair protein rhp54
- RecQ-mediated genome instability protein 1
- Serine/threonine-protein kinase chk1
- DNA repair and recombination protein rad22
- DNA repair protein rhp51
Sequence:
MTLQSTDSAIVIDSEADVDISSSQASPSKDNIALSEHNVITVLDTPQRSTQCDSLLKSFSTPLVSGSEDVLPSPRDALNITNKKSVTDNLLLSLTSSNQSTNTNLNPSSRVEIINLNSSPPNSLSSQPKHQEFHLFHTPTIPRTTQLSSKTSSPIVIPDDNEQVASPLSKKAASLTSSPLKDFQSSPPLSTVLQKSHSLHDILLDTNDDDHFPFTQSPLTKTKSFNDALTSSSSILKPCMPSIASPTSNRLSHAPSTPNLFPNQDSSNTIDLINNRSKTSVENQERTFNLTSDVHLDSPTSPSKHSSIEPNTSQEDSFQELPSLNKLSIQSRAFKKMRLPKISRTTDTPPASTSNSNKKNLDKLKKMRKLCSRSLEPYELDSNTQRKRKRYEDSLKKSKTLDKVDSLNRKMAKELDRKNSKELQKINKVKRTKEECLSEIILLSPDDWASSWYSTVRSQLDSYNCQFVVNSNQPKDSIMWKRKVNNVFNSSTNRFELSIEHEQIEPFALLRLKCRDFIKYIEEDQADTFFHEMSEKFKGCKLILLLEGIPNYFKSLKAELNRQYAAAVNSGTRPLLFGSLSKYQNFTKEKLESEIVRFSFEHSILINTSNDEKETAQWIVSFTGDIALSRYKHFSKFSARASTTEIGHVKSADRIENSLNFMLRQILRVTPNIANAICDQFDSIPSLIHHLKTHGEESLTNVVIQSSISERNLGPVLSRRIYNTFLCKEASSDAP
Protein: Creatine kinase S-type, mitochondrial (EC 2.7.3.2) (Basic-type mitochondrial creatine kinase) (Mib-CK) (Sarcomeric mitochondrial creatine kinase) (S-MtCK) (Q6P8J7)
Organism: Mus musculus (Mouse)
Function: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- ADP/ATP translocase 1
- Creatine kinase U-type, mitochondrial
- Non-selective voltage-gated ion channel VDAC2
- Non-selective voltage-gated ion channel VDAC1
- Non-selective voltage-gated ion channel VDAC3
- Creatine kinase M-type
- Myoglobin
- Myozenin-2
- Telethonin
- Histidine rich calcium binding protein
Sequence:
MASAFSKLLTGRNASLLFTTLGTSALTTGYLLNRQKVSADAREQHKLFPPSADYPDLRKHNNCMAECLTPTIYAKLRNKMTPSGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKLRHNGYDPRVMKHPTDLDASKITHGQFDERYVLSSRVRTGRSIRGLSLPPACSRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGRK
Protein: V-type proton ATPase subunit C 2 (V-ATPase subunit C 2) (Vacuolar proton pump subunit C 2) (Q8NEY4)
Organism: Homo sapiens (Human)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Interaction partners:
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit G 2
- V-type proton ATPase subunit H
- V-type proton ATPase subunit G 1
Sequence:
MSEFWLISAPGDKENLQALERMNTVTSKSNLSYNTKFAIPDFKVGTLDSLVGLSDELGKLDTFAESLIRRMAQSVVEVMEDSKGKVQEHLLANGVDLTSFVTHFEWDMAKYPVKQPLVSVVDTIAKQLAQIEMDLKSRTAAYNTLKTNLENLEKKSMGNLFTRTLSDIVSKEDFVLDSEYLVTLLVIVPKPNYSQWQKTYESLSDMVVPRSTKLITEDKEGGLFTVTLFRKVIEDFKTKAKENKFTVREFYYDEKEIEREREEMARLLSDKKQQYQTSCVALKKGSSTFPDHKVKVTPLGNPDRPAAGQTDRERESEGEGEGPLLRWLKVNFSEAFIAWIHIKALRVFVESVLRYGLPVNFQAVLLQPHKKSSTKRLREVLNSVFRHLDEVAATSILDASVEIPGLQLNNQDYFPYVYFHIDLSLLD
Protein: Lysine-specific demethylase 9 (KDM9) (EC 1.14.11.-) (Round spermatid basic protein 1) (Rosbin) (Q80T69)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that specifically demethylates dimethylated 'Lys-20' of histone H4 (H4K20me2), thereby modulating chromosome architecture.
Subcellular location: Nucleus {ECO:0000269|PubMed:14724137}.
Interaction partners:
- Protein PHTF1
Sequence:
MFRSTRTTDQWRVGERLQCPAGHARAALARTADGGAVGPFKCVFVGEMAAQVGAVRVVRAVAAQEEPDKEGKEKPHVGVSPRGVKRQRRASSGGSQEKRGRPSQDPPLAPPHRRRRSRQHPGPLPPTNAAPTVPGPVEPLLLPPPPPPSLAPAGPTVAAPLPAPGTSALFTFSPLTVSAAGPKHKGHKERHKHHHHRGSDGDPGACVPGDLKHKDKQENGERSGGVPLIKAPKRETADENGKTQRADDFVLKKIKKKKKKKHREDMRGRRLKMYNKEVQTVCAGLTRISKEILTQGQLNSTSGVNKESFRYLKDEQLCRLNLGMQEYRVPQGVQTPFTTHQEHSIRRNFLKTGTKFSNFIHEEHQSNGGALVLHAYMDELSFLSPMEMERFSEEFLALTFSENEKNAAYYALAIVHGAAAYLPDFLDYFAFNFPNTPVKMEILGKKDIETTTISNFHTQVNRTYCCGTYRAGPMRQISLVGAVDEEVGDYFPEFLDMLEESPFLKMTLPWGTLSSLQLQCRSQSDDGPIMWVRPGEQMIPTADMPKSPFKRRRSMNEIKNLQYLPRTSEPREVLFEDRTRAHADHVGQGFDWQSTAAVGVLKAVQFGEWSDQPRITKDVICFHAEDFTDVVQRLQLDLHEPPVSQCVQWVDEAKLNQMRREGIRYARIQLCDNDIYFIPRNVIHQFKTVSAVCSLAWHIRLKQYHPVVETAQNTESNSNMDCGLEVDSQCVRIKTESEERCTEMQLLTTASPSFPPPSELHLQDLKTQPLPVFKVESRLDSDQQHSLQAHPSTPV
Protein: Stromal interaction molecule 1a (A0A2R8RIM0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MEFSGLVTFWIACICFLLQCRADKLNPVNTDPLPADNGVSELCRIDEPLCQDENAILSFEAIRSIHKQMDDDDNGNVDVLETDGFLREDLNYHDPKGKHNTFHGDDQFISVEDLWNAWKSSEVYNWTVDEVVKWLIDYVELTQYVEAIKKLNFSGTAMPRLAVKNNTLTQTVLKILDRSHVQKLQLKALDTVLFGAPMMNRHNHLKDFMLVVSIVIGMGGCWFAYIQNRHSKDHMKKMMKDLDSLQRAEQSLHDLQQKLQIAQEEHRSVEVEKVNLEQKLRDEINTAKQEAQRLKELREGTENELSRQKYAEEELEQVRMALKKAEKELESRSSWSPPEALQKWLQLTHEVEVQYYNIKKQNAERQLQVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILAAKQALGEVTAALRERLHRWQQIELLTGFTLVHNPGLPSLASALNLDPSFMGGRGTPQHFMSDDMDDMDEDIVPPGTLQYAAWLMGRRASDLWSLNSDCQSFWKNSAPSMMSLRQRHIDPQMALGSQRDLNRSDSDSSLCISQTGEQLRLSYSSKGFPVKPTSLLHGPHSRSEEGAQSHTHNGGNRVHDGGPSPDGVPDSPILMKKLYGIEKSASMSEIHGSQAAMSMSESSRSLSPNSTEPDTPSPTGLTGGKAGNRIPQISSKKSPLEEDSGSTGEDTDSAASRKKHTFKIFKKQKK