wanglab/gogpt-training-data huggingface dataset:
Protein: Cilia- and flagella-associated protein 418 (Q96NL8)
Organism: Homo sapiens (Human)
Function: May be involved in photoreceptor outer segment disk morphogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3UJP5}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q3UJP5}. Note=In the retina, located at the base of the primary cilium (PubMed:22177090). Expressed throughout photoreceptors cell body including the basal body, inner segment and synaptic terminus, but not in the outer segment. {ECO:0000250|UniProtKB:Q3UJP5, ECO:0000269|PubMed:22177090}.
Interaction partners:
- Tetratricopeptide repeat protein 8
- Tubby-related protein 1
Sequence:
MAEDLDELLDEVESKFCTPDLLRRGMVEQPKGCGGGTHSSDRNQAKAKETLRSTETFKKEDDLDSLINEILEEPNLDKKPSKLKSKSSGNTSVRASIEGLGKSCSPVYLGGSSIPCGIGTNISWRACDHLRCIACDFLVVSYDDYMWDKSCDYLFFRNNMPEFHKLKAKLIKKKGTRAYACQCSWRTIEEVTDLQTDHQLRWVCGKH
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q9DGL4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGLGTGNDDYRLTPTSEDELKKTKKGKRKKDVDELKKEVELDDHKLTLDELSRKYGTGMIKGLSSFRAKEILERDGPNALTPPPTTPQWVKFCKLLFGGFQTLLWFGAFLCFLAYGIQVASVEDAAHDNLYLGLVLAFVVIVNGWFSFYQESKSSKIMESFRNLVPQQALVVRDGEKKVINAEEVVVGDLIEVCGGDRIPADLRIVYAQGCKVDNSSLTGESEPQSRSPEFSHENPLETKNIAFFSTNCVEGTARGIAISTGDRTIMGRIASLASSLEGGQTPIAREIEHFIHIISAVSIFLGVTFFVLSLILGYAWIEAVVFLIGIIVANVPEGLPATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTTTICSDKTGTLTQNRMTVAHMWFDSQIHEADTTENQSGTSFDRSSPTWAALARVAGLCNRAVFRAEQSHLPVLNRETAGDASESALLKCIELCCGSVIEMREKYRKICEIPFNSTNKYQLSVHKNPSSSGTKHLLVMKGAPERILDRCSTILINGKEQPMDDENKDSFQSAYVELGGLGERVLGFCQYNLPDDQFPEGFAFDPEDVNFPTENLCFLGLMSMIDPPRAAVPDAVAKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARMNIPVGEVNPREAKACVVHGGELKNMNDSDLDEILRYHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSKIPEMSPFLMFVVVGIPLPLGTVTILFIDLGTDLIPAISYAYENAENDIMKRQPRNAQKDRLVNERLISMAYGQIGMIQAVAGFFTYITVMAENGFRPSYLPGLRVGWEDRSIGDLEDSYGQQWTYEGRKIIESTCHTAFFISIVVVQWADLLIVKTRRNSILQQGMKNKVLIFAFFEEGALAAFLSYCPGMDIAVRMYPLRPLWWFTALPYALIIFFYDEIRKYILRRNPGGFVEKETYY
Protein: DNA-directed RNA polymerase subunit Rpo11 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit L) (Q980K0)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00261}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo7
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo1C
- Transcription factor S1
- DNA-directed RNA polymerase, subunit B''
Sequence:
MEIRILKSESNYLELEIEGEDHTLGNLIAGTLRRISGVSFASYYQPHPLSDKIIVKILTDGSITPKDALLKAIENIRGMTSHYIDEIKGLTK
Protein: ATP-dependent zinc metalloprotease FTSH 3, mitochondrial (AtFTSH3) (EC 3.4.24.-) (Q84WU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V of the mitochondrial oxidative phosphorylation system.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.10}; Single-pass membrane protein {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.10}; Matrix side {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.10}.
Interaction partners:
- ATP-dependent zinc metalloprotease FTSH 10, mitochondrial
- Prohibitin-3, mitochondrial
- DNAJ heat shock N-terminal domain-containing protein
- Lon protease homolog 1, mitochondrial
- Lon protease homolog 4, chloroplastic/mitochondrial
- RHOMBOID-like protein 12, mitochondrial
- Putative pentatricopeptide repeat-containing protein At5g40405
- Prohibitin-1, mitochondrial
- Serine carboxypeptidase-like 50
- ATP-dependent zinc metalloprotease FTSH 12, chloroplastic
Sequence:
MTMIFFSKLNRSISRSKGFLYGGGVRSAARLLTSPGLEAASVNEVEGGLGFIRRHFASLASRKGLVNNDLIGVFANPRLRRFFSDEAPKKKNYENYFPKDKQEPKSDQKSEHKEGSEKNENENVGDMFMNRFQNLLIPLLALAVFFSTFSFGSGEQQQISFQEFKNKLLEPGLVDHIDVSNKSVAKVYVRSTPKDQQTTDVVHGNGNGIPAKRTGGQYKYYFNIGSVDSFEEKLEEAQEALGVDRHEYVPVTYVSEMVWYQEFMRFAPTLLLLGTLIYGARRMQGGLGVGGTGGKNGRGIFNIGKATITRADKHSKNKIYFKDVAGCDEAKQEIMEFVHFLKNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESGVPFLSISGSDFMEMFVGVGPSRVRHLFQEARQAAPSIIFIDEIDAIGRARGRGGLGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFKIYLKKIKLDHEPSYYSQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFESAIDRVIGGLEKKNRVISKLERRTVAYHESGHAVVGWFLEHAEPLLKVTIVPRGTAALGFAQYVPNENLLMTKEQLFDMTCMTLGGRAAEQVLIGKISTGAQNDLEKVTKMTYAQVAVYGFSDKVGLLSFPPRDDGYDFSKPYSNKTGAIIDEEVRDWVAKAYERTVELVEEHKVKVAEIAELLLEKEVLHQDDLLKILGERPFKSAEVTNYDRFKSGFEETEKDSAATPTVEPVVDDGAPPPFEPQVVPT
Protein: Cytidine/deoxycytidylate deaminase family protein (F4K5T6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRKFLVNVYSLSITRSPECYISSELEAKDGTISVASAFSGHQQAVHDSDHKFLTQAVEEAYKGVDCGDGGPFGAVIVHNNEVVASCHNMVLKYTDPTAHAEVTAIREACKKLNKIELSECEIYASCEPCPMCFGAIHLSRLKRLVYGAKAEAAIAIGFDDFIADALRGTGVYQKSSLEIKKADGNGAAIAEQVFQNTKEKFRLY
Protein: Pseudouridine-5'-phosphate glycosidase (PsiMP glycosidase) (EC 4.2.1.70) (P33025)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible cleavage of pseudouridine 5'-phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway.
Interaction partners:
- Pseudouridine kinase
- Uracil phosphoribosyltransferase
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
- Thymidine phosphorylase
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreT
- Uridine phosphorylase
- Purine nucleoside phosphorylase DeoD-type
- FMN reductase RutF
- Pyrimidine monooxygenase RutA
- Pyrimidine/purine nucleoside phosphorylase
Sequence:
MSELKISPELLQISPEVQDALKNKKPVVALESTIISHGMPFPQNAQTAIEVEETIRKQGAVPATIAIIGGVMKVGLSKEEIELLGREGHNVTKVSRRDLPFVVAAGKNGATTVASTMIIAALAGIKVFATGGIGGVHRGAEHTFDISADLQELANTNVTVVCAGAKSILDLGLTTEYLETFGVPLIGYQTKALPAFFCRTSPFDVSIRLDSASEIARAMVVKWQSGLNGGLVVANPIPEQFAMPEHTINAAIDQAVAEAEAQGVIGKESTPFLLARVAELTGGDSLKSNIQLVFNNAILASEIAKEYQRLAG
Protein: At2g35260/T4C15.7 (CAAX protease self-immunity protein) (Expressed protein) (O82167)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Tetrapyrrole-binding protein, chloroplastic
- Photosystem I reaction center subunit VI-2, chloroplastic
- Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Photosystem I reaction center subunit II-1, chloroplastic
- Photosystem II reaction center proteins PsbY, chloroplastic
Sequence:
MELPLLSYASSASFSRTGLCSSSSSSSTSIYEFPERRRSLKLRFNGGERSRSVIASAERSSEGIEKTTDTVGGGGGGGAGRFAGTAMEVTTLDRGFANSTTVDFPIWDKIGAVVRLTYGIGIYGAMAVAGRFICSVTGIDSSGGFDPSLDALLAGLGYATPPIMALLFILDDEVVKLSPHARAIRDVEDEELRSFFFGMSPWQFILIVAASSIGEELFYRVAVQGALSDIFLKGTQLMTDSRGMASLTGVFPPFVPFAEVFAAVITATLTGSLYFLAASPKDPTYIVAPVLRSRRDDFKKLLSAWYEKRQMKKIYSPLLEGLLALYLGIEWVQTDNILAPMMTHGIYSAVILGHGLWKIHDHRRRLRRRIEHIRSEATDKLI
Protein: Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily (E0SFZ6)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}. Cell membrane {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Peptide transport system ATP-binding protein
- Peptide transport periplasmic protein
- Peptide transport system ATP-binding protein
- Dipeptide transport system permease protein DppC
- ABC transporter, permease component
- ABC transporter permease protein
- Glutathione transport system permease protein GsiD
- ABC transporter, permease protein
- Dipeptide transport system permease protein dppC
Sequence:
MIIFTLRRLLLLLVTLFLLSLIGFSLMYYTPHAPLNGAALLDAYRFYFTSLLQGDFGVSSTNGQPISEQLRDVLPATIELCLLAFSLSLLVGIPLGITTGVLQHKTADRLISGLALLGFSLPVFWLALLMTLFFSLHLGWLPVSGRFDLLYPVPQVTGFALIDAWLSDSPYRDEMIASAVQHLILPVLVLSVGPTTEVIRLMRISTTDVGTQNYIKAAVIRGLPRSTVIRRHLLHNALPPIIPQLGLQFSTMLTLEMITEVVFNWPGIGRWLVNAIRQQDFAAISAGVMVIGALVITINVLSDIWGAMANPLKHKEWYALR
Protein: Secretory 24CD, isoform C (M9PC99)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
- Protein transport protein SEC23
- Protein SEC13 homolog
- Protein transport protein Sec31A
- Secretory 24AB, isoform A
- Secretory 16, isoform I
- small monomeric GTPase
- FI09914p
- Grasp65
- General vesicular transport factor p115
- Syntaxin-5
Sequence:
MNPNMYGPPPTQFQQQPQFGAPPPNSGGWPPQQQQLPQQQPPQQQLPPQQQQQQPQYGAPPPTSAASQPYLNGNYQQQLATSMGGLSVGGGVGGANPLKPPLPQGAPAAAAPPPTGFNQFNSNAAPPPTNNNNAAFGAPPPTQAGSYVNGALPPSSTPQSVASGINQMSLNSATLAGLPHMPPPKAATPGAAPGQPPIPAAGSTSQPPLPGQPPLPGQPPFSGQIPTSQPAPSPYGVPSSRPGQPQLPPGATPPTYTQPGLPPQQQQGIPPLQQPGIPQQQPGFPPQQPGLPPLSQPGLPPQPGAPYGAPQQGGYSGGFPGQAPGGFPGAPPPLPGQQAAAPPQFGAPQPGYPGQQPGYPPQPGQQPMPGYPPQPGQQLGGPGYPPQPGAGFPGQPGRPGFNQPPMPGAGNMYQQAPQARRLDPDQMPNPIQVMIENQRLSGGPFVTNQPGLLPPLVTTKFVVHDQGNSSPRFLRSSLYCIPNTGDLLKTTALPLTLNISPLAKVGEGEMEPPIVNFGEMGPIRCNRCKAYMSPNMQFVDAGRRFQCLMCKVTSEVHQNYYQHLDHTGQRVDKHERPELLLGTYEFLATKDYCRNNTPPEVPAFIFIIDVSYNTVKSGLVHLLCSQIKNILKHLPVDQGQDKSKVRVGFITYNSTVHFYNIKSSLAQPQMMVVGDVQEMFMPLLDGFLCHPEESAAVIDALMEEIPRMFADTKETETILYPAIQAGLEALKASNAAGKLLVFNSTLPIAEAPGKLKNRDDRKLLGTDKEKTVLTPQTTAYNTLGQECVQQGCSVDLFVFNNAYIDLATIGQVSRLTGGEVFKYTYFQADVDGKRLIQDIIKNVSRPIAFDAVMRVRTSAGIRPTEFYGHFFMSNTTDVELASIDATKSISIEIKHDDKLAPEENVYLQVALLYTSCSGQRRLRILNLALRVTTTIADVFKCCDLDAMMLFFAKQACFKLMEHSPKQVKDNLIHRSAQILACYRKHCTSPTSAGQLILPECLKLLPLYASCLLKNDAISGGSDMTLDDRSYVIQFILSMDLNQSVSYLYPRFIPIHNVVPEETDLPTPVRCTHEKTQEDGAYILENGVHLFVWLGQALSPDFVQSVFGVQGLQQIALERFNIVPETPLAKRIHGILEQIMKERSRYMRITWLRQNDKLESVFRHFLVEDRGTDGSASYVDFLCHMHKEIKDLLSXHAGYSGTYKPEQRWADSYSQNRARMRRLSSMRSRLGK
Protein: Competence protein D (Q4QNA9)
Organism: Haemophilus influenzae (strain 86-028NP)
Interaction partners:
Sequence:
MKHWFFLIILFFMNCSWGQDPFDKTQRNRSQFDNAQTVMEQTEIISSDVPNNLCGADENRQAAEIPLNALKLVGVVISKDKAFALLQDQGLQIYSVLEGVDVAQEGYIVEKINQNNVQFMRKLGEQCDSSEWKKLSF
Protein: Core binding factor B subunit (Core binding factor beta subunit isoform 4) (Core-binding factor subunit beta) (Core-binding factor, beta subunit) (Q98U16)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVATGTNLSLQFFPANLHGDQRQAPTREYVDFERETGKVYLKAPMILNGVCVIWRGWLDLHRLDGMGCLEYDDERAQHEDALAQAAFEEARRRTRDFEDRDRSHREDLEPRRQQDPSPGSNMGNTDDHKMR
Protein: Epsilon tubulin (Q4FKF8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tubulin alpha chain
- Katanin p60 ATPase-containing subunit A-like 2
- Nucleoside diphosphate kinase-like domain-containing protein
- Uncharacterized protein
- Tubulin-specific chaperone A
- TOG domain-containing protein
- Basal body component
- End-binding protein 1
- Calponin-homology
- Kinesin, putative
Sequence:
MPREVVTVQVGQCGNQLGLKWWDVLLQEHKANPQFTDARDALFDVSGSAPLASVGDKACRAGSLKARCVAVDMEEGVLRAMLRGPLGHLFDATFFVSDVSGAGNNWAVGHMEYGDKYIDSITETVREQVERCDSIQSFLIMHSLSGGTGAGLGTRVLGMLEDEFPHVFRICPVVMPSAIDDVVTAPYNTAFAVRELIEHADAVLPLDNDALARMADSALGQKTIGQAAGERKEPQTTLGAPAARGYSVAQPTQTKLPYDSMNALVAQLLSNLTCAMRFPGPLNMDINEITTNLVPYPRLLFLTSAIAPLSVARHAAASAPRSVDTMIAACLDKNHQFVDVSNGLSSALTHEAGTCLATAIVARGPQITVGDLTRNIPRIRERQKLVYWNEDGCKTALCSVSPLGHRNSVLMLANHCSIAQKLQSAHERFMRLYSVRSHVHHYEPYLEQAYFDDTCDTVLTVVDDYNYLNTVQMPADVPRSMRDLVYF
Protein: Probable mitochondrial adenine nucleotide transporter BTL3 (Adenine nucleotide transporter BT1-like protein 3) (Q9LV81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable mitochondrial adenylate carrier that catalyzes the transport of ATP, ADP and AMP.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MRGLDRWIAEAIRSESLDHNGQIICGGLFLEESLPSSSVSFLSSKDCSVNSCRFSQKSSFLKFRRRNGTREPLFLSVSLSINESNGEEEEGEGYNGQNGFKSEKGSVLIGGGQESKEKRRVKENGAGALNTTKHLWAGAFAAMVSRTCIAPLERMKLEYIVRGEQGNLLELIQRIATNEGIRGFWKGNLVNILRTAPFKSINFYAYDTYRGQLLKLSGNEETTNFERFVAGAAAGVTASLLCLPLDTIRTVMVAPGGEALGGVVGAFRHMIQTEGFFSLYKGLVPSLVSMAPSGAVFYGVYDILKSAYLHTPEGKKRLEHMKQEGEELNAFDQLELGPMRTLLYGAIAGACSEAATYPFEVVRRRLQMQSHAKRLSAVATCVKIIEQGGVPALYAGLIPSLLQVLPSAAISYFVYEFMKVVLKVESSA
Protein: Cst6 protein (Q8K397)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
PHFPLAMGLGLLAFCLLTLSPDARAELRSRRTGERQNLSPTDPRVQKAAQAAVASYNMGSDSLYYFRDTKVIDAKYQLVAGIKYYLTLDIESTECRKTRVSGEHMDLTTCPLAAGGQQEKLRCNFELLEVPWKNTTQLLKHDCVQV
Protein: Apolipoprotein C-I (Apo-CI) (ApoC-I) (Apolipoprotein C1) [Cleaved into: Truncated apolipoprotein C-I] (P02654)
Organism: Homo sapiens (Human)
Function: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein.
Subcellular location: Secreted {ECO:0000303|PubMed:2835369}.
Interaction partners:
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein C-II
- Apolipoprotein A-I
- Apolipoprotein B-100
- Apolipoprotein A-II
- Apolipoprotein C-IV
- Cholesteryl ester transfer protein
- Phosphatidylcholine-sterol acyltransferase
- Apolipoprotein A-IV
Sequence:
MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS
Protein: Protein dispatched homolog 2 (Q8CIP5)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sonic hedgehog protein
- Desert hedgehog protein
- Indian hedgehog protein
Sequence:
MAPEASPERSCSLHTCPLEDPTGAPVPPPTVSTLQAIDPTSPLTAGHFAFPRAPQDYQEGSSLLGLGDQASLCAHVSNLSTSIDTSQHDGVWKQPSVQRHVVSVRQERTFRMPKSYSHMIADWPVAVIVGCLAFIFLCTLAGLLGSPPLDFSEPLLGFEPRDTEIGRRLEVWKAMQALTGPKNLLSLSPDPEMNSSSLLSTLSPAAWGRAEESVVRTKRMVGPVEVKEEENFFCGRPEKSHAKLVFVSTSGGSLWNLQAIHSMCRIEQEQIRSHISFGALCQRSAANECCPSWSLGNYLAVLSNRSSCQDTTQADTDRTLALLRFCATFYHRGVLVPACVGSSQDKPPFCAQVPAKCTGSNVVYEFLHYLLDRDFLSPQTADYQVPSLKFALLFLPIIKTSSLLDIYLDGLGDPIKVSDNYTSISGMDLGLKPRLLKYYLAEDTMYPLIALVVIFFGMSLYLRSLFITFMSLLGVLGSLMVAYFLYHVAFRMAYFPFVNLAALLLLSGVCVNYTLIFLDMWRLSRGQVPSGGMPHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPAVRCFALFMGTAVLVHMGLTLLWLPATVVLHERYLAHGCVAQAHGQRGGSDPLRLLLALHRRIRIFRKIISILSRLLFQRLLPCGVIKFRYIWICWFAALAAGGAYIGGVSPRLQLPILLPLGGQFFRSSHPFERFDAEYRQQFLFEDLPPNEGGNLPVVLVWGILPVDTSDPLDPRTNSSVVSDPDFSPSSPEAQEWLLALCHGAQNQSFFGDQPEGWPTLCLVEALQQWMESPSCGRLGPDLCCGQSEFPWAPQLYLHCLKMMALEQSPDGTRDLGLRFDTHGNLAALVLKFQTNLPYSTEYGPVHHFYTEISRWLSTEMSKAPPGLNQGWFTSNLELYSLQHSLSTEPAVVLGLALALAFATLLLSTWNVPLSLFSVAAVAGTVLLTVGLLVLLEWQLNTAEALFLSASVGLSVDLTINYCISYHLCPHPDRLSRVAFSLRQISRATAMTTGVLFASGVIMLPSTILLYRKLGIIVMMVKFLGCGFASFFFQSLCCFFGPEKNCGQILWPCAHLPWDAGTEDPDEKGRAGPPGFSEHYELQPLARRRSPSFDTSTATSKLSHRPSILSEDLQIHDGSCCLQHAQAPVSPRDLLLDHQTVFSQCPALQTSSPYKQAGPTPQTWIRQDSQGQKTEPLQALPEGPAHCPKSKVEELPDGLCSSASTLEGLSVSDDTCASEHSVRVPDSVGTSPEVMNGTGHPILERGQLNGKRDTLWLALKETIYDPNMPNSHHSSLSWKGRGGPGDISPVMLPNSQPDLPDVWLRRPSTYTSGYSS
Protein: Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein Boo) (Apoptosis regulator Bcl-B) (Bcl-2 homolog Diva) (Q9Z0F3)
Organism: Mus musculus (Mouse)
Function: Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (By similarity). Increases binding of AHCYL1/IRBIT to ITPR1 (By similarity). Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (By similarity). Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca(2+) transfer to mitochondria which promotes apoptosis (By similarity). Required for the correct formation of the microtubule organizing center during oocyte cell division, potentially via regulation of protein abundance and localization of other microtubule organizing center components such as AURKA and TPX2.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9HD36}. Nucleus membrane {ECO:0000250|UniProtKB:Q9HD36}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9HD36}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27753540}. Note=Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (By similarity). Localization to MAMs is greatly reduced under apoptotic stress conditions (By similarity). {ECO:0000250|UniProtKB:Q9HD36}.
Interaction partners:
- Bcl-2-like protein 11
Sequence:
MADSQDPLHERTRRLLSDYIFFCAREPDTPEPPPTSVEAALLRSVTRQIQQEHQEFFSSFCESRGNRLELVKQMADKLLSKDQDFSWSQLVMLLAFAGTLMNQGPYMAVKQKRDLGNRVIVTRDCCLIVNFLYNLLMGRRHRARLEALGGWDGFCRFFKNPLPLGFWRRLLIQAFLSGFFATAIFFIWKRL
Protein: Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein) (P0C432)
Organism: Oryza sativa (Rice)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}.
Interaction partners:
Sequence:
MTAILERRESTSLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAALEVPSLNG
Protein: Two pore potassium channel protein sup-9 (Suppressor of unc-93 protein 9) (n2P38) (O17185)
Organism: Caenorhabditis elegans
Function: Potassium channel involved in coordination of muscle contraction. Activity is regulated by sup-18.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Associated with dense bodies. {ECO:0000269|PubMed:14534247}.
Interaction partners:
- Putative potassium channel regulatory protein sup-10
- Putative potassium channel regulatory protein unc-93
- Iodotyrosine dehalogenase 1 homolog
- Potassium channel domain-containing protein
- Potassium channel domain-containing protein
Sequence:
MKRQNIRTLSLIVCTLTYLLVGAAVFDALETENEILQRKLVQRVREKLKTKYNMSNADYEILEATIVKSVPHKAGYQWKFSGAFYFATTVITTIGYGHSTPMTDAGKVFCMLYALAGIPLGLIMFQSIGERMNTFAAKLLRFIRRAAGKQPIVTSSDLIIFCTGWGGLLIFGGAFMFSSYENWTYFDAVYYCFVTLTTIGFGDYVALQKRGSLQTQPEYVFFSLVFILFGLTVISAAMNLLVLRFLTMNTEDERRDEQEAILAAQGLVRVGDPTADDDFGRLPLSDNVSLASCSCYQLPDEKLRHRHRKHTEPHGGPPTFSGMTTRPKY
Protein: Prostaglandin E synthase 2 (EC 5.3.99.3) (Membrane-associated prostaglandin E synthase-2) (mPGE synthase-2) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form] (Q66LN0)
Organism: Bos taurus (Bovine)
Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro). The biological function and the GSH-dependent property of PTGES2 is still under debate (By similarity). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity).
Subcellular location: Microsome membrane {ECO:0000269|PubMed:10446427}; Single-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]: Cytoplasm {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. {ECO:0000250|UniProtKB:Q9H7Z7}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin E synthase
- Prostaglandin G/H synthase 1
- Prostaglandin G/H synthase 2
- Prostaglandin-H2 D-isomerase
- Prostacyclin synthase
- Hematopoietic prostaglandin D synthase
- Carbonyl reductase 1])
- Prostamide/prostaglandin F synthase
- Carbonyl reductase
Sequence:
MAHAVRALWPHGRALAWRLGDRPALGLHAQSRAGFTGAAGGSGPAATARKGGPRLLGAAALALGGALGLYHTARWHLRAQDLRAERSATQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPIVMAQEGESLQQLNDSSVIISALKTYLVSGQPLADIITYYPPMKAVNDQGKEVTEFCNKYWLMLDEKEAQRMYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPAEALASFDYIVKEGNFGTVEGAMAKYMGAAAMYFISKRLKRRHHLRDDVREDLYEAANKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLEAFDDLMRHTHIQPWYLRVEKAIAEAPQ
Protein: RH10688p (Q8SZL6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
Sequence:
MCNVACKTGIFRYYLRASGQRTWMSVLLVLVLMGTFTAAEPLKVIYAVNAGGDEHTDLNGVQYDADPLKGVGIASDYGKHLLMIGRVQEHDEVLYRTERYHTTTFGYDLPSDGDGDYALIMKFCEVYFDAPQKKVFDVLLNRKHTVVRQLDIYNEVGRGSAHDEIVYFKINNGRLNYEGEVSDVRNGRLRLDFIKGALDNPKINAFALLKGDISQVPRMHGTEATERIKPEGKLNAEQKKAQQVERVVRNQRDDIDEDDEDLDDEEFEEELSEQNVDKLGSDQPSLQSDTKRSYSGPRQPNPYSMDDSSILLPVFIAIGAFIPLLFCLCKL
Protein: E3 ubiquitin-protein ligase parkin (EC 2.3.2.31) (Q9XUS3)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|PIRNR:PIRNR037880}.
Interaction partners:
- Serine/threonine-protein kinase pink-1, mitochondrial
- Transmembrane GTPase fzo-1
- Ataxin-3 homolog
- Mitochondrial Rho GTPase 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Glutathione-independent glyoxalase DJR-1.1
- Polyubiquitin-A
- Uncharacterized protein
- Ubiquitin-like protein 1-ribosomal protein eS31 fusion protein
- Probable voltage-dependent anion-selective channel
Sequence:
MSDEISILIQDRKTGQRRNLTLNINITGNIEDLTKDVEKLTEIPSDELEVVFCGKKLSKSTIMRDLSLTPATQIMLLRPKFNSHNENGATTAKITTDSSILGSFYVWCKNCDDVKRGKLRVYCQKCSSTSVLVKSEPQNWSDVLKSKRIPAVCEECCTPGLFAEFKFKCLACNDPAAALTHVRGNWQMTECCVCDGKEKVIFDLGCNHITCQFCFRDYLLSQLERFGFVNQPPHGFTIFCPYPGCNRVVQDVHHFHIMGQTSYSEYQRKATERLIAVDDKGVTCPNVSCGQSFFWEPYDDDGRSQCPDCFFSFCRKCFERNCVCQSEDDLTRTTIDATTRRCPKCHVATERNGGCAHIHCTSCGMDWCFKCKTEWKEECQWDHWFN