wanglab/gogpt-training-data huggingface dataset:
Protein: Tropomyosin 1 (Alpha) isoform 4 (Tropomyosin 1 (Alpha), isoform CRA_c) (D9YZV5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNNM
Protein: V-type proton ATPase proteolipid subunit (A0A1D8PK00)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Vacuole membrane {ECO:0000256|ARBA:ARBA00004128, ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128, ECO:0000256|RuleBase:RU363060}.
Interaction partners:
- V-type proton ATPase subunit a
- V-type proton ATPase subunit
- H
- V-type proton ATPase subunit a
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit D
- V-type proton ATPase subunit C
- H
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B
Sequence:
MSDLCPVYAPFFGSIGCAAAIVFTCFGASYGTAKSGVGICATSVTRPDLLVKNVVPVVMAGIIAIYGLVVSVLVSDSLSQKQALYTGFIQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALLLNSRASQDVTC
Protein: Cytotoxic T-lymphocyte protein 4 (Cytotoxic T-lymphocyte-associated antigen 4) (A0A096MJE4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- T-lymphocyte activation antigen CD86
- T-lymphocyte activation antigen CD80
- Inducible T-cell costimulator
- ICOS ligand
- T-cell surface glycoprotein CD4
- Forkhead box P3
- Lymphocyte activation gene 3 protein
- Interferon gamma
- Tyrosine-protein phosphatase non-receptor type 6
- T-cell-specific surface glycoprotein CD28
Sequence:
MARLGVQRYKTHLQLPSRTWPFGVLLSLLFIPIFSEAIQVTQPSVVLASSHGVASFPCEYASSHNTDEVRVTVLRQTNDQVTEVCATTFTVKNTLGFLDDPFCSGTFNESRVNLTIQGLRAADTGLYFCKVELMYPPPYFVGMGNGTQIYVIDPEPCPDSDFLLWILAAVSSGLFFYSFLVTAVSLNRTLKKRSPLTTGVYVKMPPTEPECEKQFQPYFIPIN
Protein: Adenosine monophosphate-protein hydrolase SidD (De-AMPylase SidD) (DeAMPylase SidD) (EC 3.1.4.-) (Adenylyl-[Rab1] hydrolase) (Q5ZSQ2)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Virulence effector that plays a role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as an adenosine monophosphate-protein hydrolase (de-AMPylase) by mediating the hydrolysis of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby releasing RAB1B from bacterial phagosomes and rendering RAB1B accessible for inactivation by LepB. De-AMPylation of RAB1B cannot take place when LidA is bound to RAB1B.
Subcellular location: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:21680813}.
Interaction partners:
Sequence:
MVYYEIIKDIVFTYNLQFTHLIHNDRISEVNLGGVTMRSIITQICNGVLHGQSYQSGSNDLDKGNSEIFASSLFVHLNEQGKEIIKHKDSDDKIVIGYTKDGMAFQIVVDGFYGCERQAVFSFIDNYVLPLIDNFSLDLTRYPDSKKVTESLIHTIYSLRSKHAPLAEFTMSLCVTYQKDEQLFCAGFGIGDTGIAIKRNEGTIEQLVCHTEVDGFKDAFDNYSSANIDLVIERNSVFNTKVMPGDELVGYTYVPPMLEMTEKEFEVETVDGKKINKRIVRHLNLDPGNFDDKDPLFSQLLQVVKSKQKQLVEQAKETGQIQRFGDDFTVGRLVIPDQLLINQLRIHALSIGVSDGLLSYIKNENENKGFLGIYGFFTGADKNIEKATLYKNLIAKYQNNHFISLIILSALVSDSKTPLMTQYLVGYLDFPSKALLANKITELLLKELENPDMREILGSRLATDVIEELETKIIRYIHNPAGSDIHSTLNLWTADKIKAATNSSLTI
Protein: Subtilisin-like protease SBT1.8 (EC 3.4.21.-) (Subtilase subfamily 1 member 8) (AtSBT1.8) (Q9ZUF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 64
- Cystatin/monellin superfamily protein
- Tripeptidyl-peptidase 2
- At5g52430
- Uncharacterized protein At3g62650; F26K9_80
- At5g07400
- AT1G56000 protein
- Paramyosin
- Probable cytosolic oligopeptidase A
- Spectrin beta chain, brain
Sequence:
MASSSSSSSSITIITTFLFLLLHTTAKKTYIIRVNHSDKPESFLTHHDWYTSQLNSESSLLYTYTTSFHGFSAYLDSTEADSLLSSSNSILDIFEDPLYTLHTTRTPEFLGLNSEFGVHDLGSSSNGVIIGVLDTGVWPESRSFDDTDMPEIPSKWKGECESGSDFDSKLCNKKLIGARSFSKGFQMASGGGFSSKRESVSPRDVDGHGTHTSTTAAGSAVRNASFLGYAAGTARGMATRARVATYKVCWSTGCFGSDILAAMDRAILDGVDVLSLSLGGGSAPYYRDTIAIGAFSAMERGVFVSCSAGNSGPTRASVANVAPWVMTVGAGTLDRDFPAFANLGNGKRLTGVSLYSGVGMGTKPLELVYNKGNSSSSNLCLPGSLDSSIVRGKIVVCDRGVNARVEKGAVVRDAGGLGMIMANTAASGEELVADSHLLPAIAVGKKTGDLLREYVKSDSKPTALLVFKGTVLDVKPSPVVAAFSSRGPNTVTPEILKPDVIGPGVNILAGWSDAIGPTGLDKDSRRTQFNIMSGTSMSCPHISGLAGLLKAAHPEWSPSAIKSALMTTAYVLDNTNAPLHDAADNSLSNPYAHGSGHVDPQKALSPGLVYDISTEEYIRFLCSLDYTVDHIVAIVKRPSVNCSKKFSDPGQLNYPSFSVLFGGKRVVRYTREVTNVGAASSVYKVTVNGAPSVGISVKPSKLSFKSVGEKKRYTVTFVSKKGVSMTNKAEFGSITWSNPQHEVRSPVAFSWNRF
Protein: Transmembrane protein 140 (Q9NV12)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAGPRPRWRDQLLFMSIIVLVIVVICLMFYALLWEAGNLTDLPNLRIGFYNFCLWNEDTSTLQCHQFPELEALGVPRVGLGLARLGVYGSLVLTLFAPQPLLLAQCNSDERAWRLAVGFLAVSSVLLAGGLGLFLSYVWKWVRLSLPGPGFLALGSAQALLILLLIAMAVFPLRAERAESKLESC
Protein: Spermatogenesis-associated protein 22 (Q5SV06)
Organism: Mus musculus (Mouse)
Function: Meiosis-specific protein required for homologous recombination in meiosis I.
Subcellular location: Chromosome {ECO:0000269|PubMed:24240703, ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}. Note=Localizes on meiotic chromosome axes. Accumulates on resected DNA. Localization is dependent on MEIOB. {ECO:0000269|PubMed:24240703}.
Interaction partners:
- Meiosis-specific with OB domain-containing protein
- Heat shock factor 2-binding protein
- Meiotic recombination protein DMC1/LIM15 homolog
Sequence:
MKRNLNESSARSTAGCLPVPLFNQKKRNRQPLTSNPLQNDPGVSTVSDSYGSPSFPTDWAWEAVNPEVAPLKKTVNTGQIPASASYPWRSQDSVSKSIQSNAERSQSAWGYRGNNRNTSLRTWDFRPQHKTVSPAANSEFSSCPVNLGAQQQKQFQTPEFPNLPGHKEAEVPRQTCLSKLPGSTMKGPDRASALQAFKPSFQQNPFKKTVLGDIPRENSLKEGTLHQLKEKDNSLRIISAVIESMKYWRAHVQKTVLLFEILAVLDSAVTSGPHYSKTFLMRDGKNILPCVFYEIDRELPRLIRGRVHRCVGHYDPDKNIFKCVSVRPASASEQKTFQAFVTIADAEMKYHTKVTNEM
Protein: Mitochondrial import receptor subunit TOM40-1 (Translocase of outer membrane 40 kDa subunit homolog 1) [Cleaved into: Mitochondrial import receptor subunit TOM40-1, N-terminally processed] (Q9LHE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the translocation pore. Directly involved in the pore formation.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14730085, ECO:0000269|PubMed:31118221}; Multi-pass membrane protein {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14730085}.
Interaction partners:
- Mitochondrial import receptor subunit TOM9-2
- Mitochondrial import receptor subunit TOM9-1
- Mitochondrial outer membrane import complex protein METAXIN
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit TIM10
- Outer membrane OMP85 family protein
- Outer membrane OMP85 family protein
- Mitochondrial outer membrane protein porin 1
- Mitochondrial import inner membrane translocase subunit TIM8
- Mitochondrial import inner membrane translocase subunit TIM9
Sequence:
MADLLPPLTAAQVDAKTKVDEKVDYSNLPSPVPYEELHREALMSLKSDNFEGLRFDFTRALNQKFSLSHSVMMGPTEVPAQSPETTIKIPTAHYEFGANYYDPKLLLIGRVMTDGRLNARLKADLTDKLVVKANALITNEEHMSQAMFNFDYMGSDYRAQLQLGQSALIGATYIQSVTNHLSLGGEIFWAGVPRKSGIGYAARYETDKMVASGQVASTGAVVMNYVQKISDKVSLATDFMYNYFSRDVTASVGYDYMLRQARVRGKIDSNGVASALLEERLSMGLNFLLSAELDHKKKDYKFGFGLTVG
Protein: Cytochrome c oxidase subunit 8B, mitochondrial (Cytochrome c oxidase polypeptide VIII-heart) (Cytochrome c oxidase subunit 8-1) (Cytochrome c oxidase subunit 8H) (P48772)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 8C, mitochondrial
Sequence:
MPRLPPILRLLQAPAKFTVVPKAHVSAKPAKTPTSAVEQAVGISAIVVGFMVPAGWVLAHLESYKKSSAA
Protein: Xin actin-binding repeat-containing protein 1 (Cardiomyopathy-associated protein 1) (Q702N8)
Organism: Homo sapiens (Human)
Function: Protects actin filaments from depolymerization.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:15454575}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q5PZ43}. Note=Colocalizes with actin stress fibers. {ECO:0000269|PubMed:15454575}.
Interaction partners:
- Oxidoreductase NAD-binding domain-containing protein 1
- Filamin-C
- Calpain-7
- Alpha-actinin-2
- Cysteine and glycine-rich protein 3
Sequence:
MADTQTQVAPTPTMRMATAEDLPLPPPPALEDLPLPPPKESFSKFHQQRQASELRRLYRHIHPELRKNLAEAVAEDLAEVLGSEEPTEGDVQCMRWIFENWRLDAIGEHERPAAKEPVLCGDVQATSRKFEEGSFANSTDQEPTRPQPGGGDVRAARWLFETKPLDELTGQAKELEATVREPAASGDVQGTRMLFETRPLDRLGSRPSLQEQSPLELRSEIQELKGDVKKTVKLFQTEPLCAIQDAEGAIHEVKAACREEIQSNAVRSARWLFETRPLDAINQDPSQVRVIRGISLEEGARPDVSATRWIFETQPLDAIREILVDEKDFQPSPDLIPPGPDVQQQQHLFETRALDTLKGDEEAGAEAPPKEEVVPGDVRSTLWLFETKPLDAFRDKVQVGHLQRVDPQDGEGHLSSDSSSALPFSQSAPQRDELKGDVKTFKNLFETLPLDSIGQGEVLAHGSPSREEGTDSAGQAQGIGSPVYAMQDSKGRLHALTSVSREQIVGGDVQGYRWMFETQPLDQLGRSPSTIDVVRGITRQEVVAGDVGTARWLFETQPLEMIHQREQQERQKEEGKSQGDPQPEAPPKGDVQTIRWLFETCPMSELAEKQGSEVTDPTAKAEAQSCTWMFKPQPVDRPVGSREQHLQVSQVPAGERQTDRHVFETEPLQASGRPCGRRPVRYCSRVEIPSGQVSRQKEVFQALEAGKKEEQEPRVIAGSIPAGSVHKFTWLFENCPMGSLAAESIQGGNLLEEQPMSPSGNRMQESQETAAEGTLRTLHATPGILHHGGILMEARGPGELCLAKYVLSGTGQGHPYIRKEELVSGELPRIICQVLRRPDVDQQGLLVQEDPTGQLQLKPLRLPTPGSSGNIEDMDPELQQLLACGLGTSVARTGLVMQETEQGLVALTAYSLQPRLTSKASERSSVQLLASCIDKGDLSGLHSLRWEPPADPSPVPASEGAQSLHPTESIIHVPPLDPSMGMGHLRASGATPCPPQAIGKAVPLAGEAAAPAQLQNTEKQEDSHSGQKGMAVLGKSEGATTTPPGPGAPDLLAAMQSLRMATAEAQSLHQQVLNKHKQGPTPTATSNPIQDGLRKAGATQSNIRPGGGSDPRIPAAPRKVSREEQALPRGLPGGWVTIQDGIYTAHPVRTFDPPGGVQLSQREPQSRHRETALSVQAPRPLQGGPGQSTGPGREEPGGCTQMAWGPPGKAMAEVCPGGLQAAETTLKTAPLGRHILASGPQAAGASPHPHNAFVPPPPTLPAAVTGPDFPAGAHRAEDSIQQASEPLKDPLLHSHSSPAGQRTPGGSQTKTPKLDPTMPPKKKPQLPPKPAHLTQSHPPQRLPKPLPLSPSFSSEVGQREHQRGERDTAIPQPAKVPTTVDQGHIPLARCPSGHSQPSLQHGLSTTAPRPTKNQATGSNAQSSEPPKLNALNHDPTSPQWGPGPSGEQPMEGSHQGAPESPDSLQRNQKELQGLLNQVQALEKEAASSVDVQALRRLFEAVPQLGGAAPQAPAAHQKPEASVEQAFGELTRVSTEVAQLKEQTLARLLDIEEAVHKALSSMSSLQPEASARGHFQGPPKDHSAHKISVTVSSSARPSGSGQEVGGQTAVKNQAKVECHTEAQSQVKIRNHTEARGHTASTAPSTRRQETSREYLCPPRVLPSSRDSPSSPTFISIQSATRKPLETPSFKGNPDVSVKSTQLAQDIGQALLHQKGVQDKTGKKDITQCSVQPEPAPPSASPLPRGWQKSVLELQTGPGSSQHYGAMRTVTEQYEEVDQFGNTVLMSSTTVTEQAEPPRNPGSHLGLHASPLLRQFLHSPAGFSSDLTEAETVQVSCSYSQPAAQ
Protein: Tail completion protein Z (Gene product Z) (GpZ) (Minor tail protein Z) (Tail terminator protein) (P03731)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Stabilizes the tail structure and acts as a connector between the end of tail and the portal vertex of the capsid.
Subcellular location: Virion {ECO:0000269|PubMed:1003470}. Host cytoplasm {ECO:0000269|PubMed:1003470}.
Interaction partners:
Sequence:
MAIKGLEQAVENLSRISKTAVPGAAAMAINRVASSAISQSASQVARETKVRRKLVKERARLKRATVKNPQARIKVNRGDLPVIKLGNARVVLSRRRRRKKGQRSSLKGGGSVLVVGNRRIPGAFIQQLKNGRWHVMQRVAGKNRYPIDVVKIPMAVPLTTAFKQNIERIRRERLPKELGYALQHQLRMVIKR
Protein: F-box domain-containing protein (Q389D6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRGSCSEGALSGGCLPSRATTNPLGGPSSAGSLEMAEMLGAEAFYGLPILCSLWSERKLPKRRGARGRGQHWSCASGESGKKRNCNLPPQLLFTIMSYLLPEGMLKMRLVCRTFNDVFLTYSVQETFAVSLPRSFMEPTVGFQTLSGLIKEREAVLRNKERSWSKWLSAYVVMWLRKEANNDTISKATVEGQALWVQLQRSRVLCRLAMEEWLGHLSDCRRAQYNIRRNWFNPTNLGCTLRTGVPPVFLPDGTLCINDPPDVVKFYAKRDRGLPLCEDALSHKTVSRKNDSLKDMWAPFEELAFPAYVCLMYYDPYVDALHISLASGTCTLWRVNSIGIEAAAHRTASEADFESSSHQLWRKTDLPCRSIPSRIEVVGNYTISSEFLACSVTMTRDGIKLEDYRWSEDEVMSKVRLFGEGANGDTSRIIVASCGRDVSASLLPRATAGDAHLTKEDVAVLNILQNQLSNASNSVNRPRAGPTRGEASANESHRPSATNSVDGINGGHNDVESGNNGGNIISIAGGPGNGAFELLVDDIEHEGVGTAASEVTANHLEGERGDRITDFRPSSITINSTERIDIKRHVFGVFNEQARLMCTVAITHEVAVFILTQSGCRTLGVNYSGGIHAASVLSSPVFKRCESPTAEHPCEEGDALFLCASQHNVLICQQKLYRRLEEVEILVIHQNHREAATSRGALRPSEQRYGTWYFLKGYSYHSPPMILRPLVEVSSLMLQAFVQPRPLLPEHLEWLSKRSNEGTCKVDCQRQREEHLPPYKSSWWCPQRDGHPYFHKPFVMFISKFVGYLLAGCDCTSGGYQEVSTDDREHFHSVPLLDGIAVKRLHPSAVALSPSHAFFVLGMENGSILMVSPSCRKCDQAKDGQGGCTTDAQVNGAHLIEQLDTISIPEGGEGYLASREAPQLLVAGEDLHEEGADEGESSSSSEDEAAHPRSQHPHTSHLYRTTIISNRVRGSARQKRNLRSFTPQQLFGCAFHEDPYISALQRCSSSILNSMERLEGEQRRHHPTPIHAVWIHAPRDCYRFSRKSGIWSMHLDDWKLTVLNRLYELTVYDLSMQSFVGKDNVKGSVVFAPLLTLSPYLSHPFLGVPMKDEEKWLCSKIRRRMRAETERTASGWEIVWHNGVLVVLGVSKGWRYSVFDFHARFSDPDVKNFSDPAPVAYSAKRDEYYESISGSQMLVPLDFGKKGTHKLALPRHFPLLRRDENMYLVRLSVRAVTLVFLCVALILVMLRIDGYITAPHWVAAAAYAPYALDVIANSFTDYDRYYIVRSDVPFYIRLFSDLLLYIVFPVVFTLRRDLYPRFNTPWIVLTIPLCVAIAMKSLPDIYINMHPGQRHWFAWVTTSRLLKALYEWLIISTIVLLALYFDGPSGRDPLAPKFHIALALTPVMLLILILKVKSAAAFVRTGNWRLYLTCLFPLLLLALQVMLFVGEFKDYYEYIGKPITTPKPSASQSLFILPFSVIVVAIYKGYTVASVLCR
Protein: C2H2-type domain-containing protein (H2KZ82)
Organism: Caenorhabditis elegans
Interaction partners:
- BED-type domain-containing protein
- NR LBD domain-containing protein
- Nuclear Hormone Receptor family
Sequence:
MSDDEDEGRLQIDESPSDSEDKPSISAPPPLPPPLQETPEFQTTYDAHDQAETSGKEDGELDEDDENDDIEPMEIDEEIQLEIDEKPEDLVKDEQISEPTDKMREEFLKVEKTDENAVVESTSSFSPKLIDEQDLKVEEMSDEKHAQSPVSSDMTTSKSPTPSKKENGLMKPPQSTEKAQRKRKESTDIFSSEKRKLSLETVASSSSSSGSSNLSTTPQRSKRSSSHMATIAISACFTDEDIVSVPMMPIQKTPDTAPHSKRAKRDIGTNVITTRSTDTSGLLCNEAIMDTPPGSQMTLEVTVMYRTKNSLAFRVKGCDLIGFIGDGLPPMASSLTNNIASSMGNNNNKKKTASSSGNEEGKDGRSSSASSNGRGARGGSVLKDGKGDKQKGKRKKEETNDDDLEDENQNNEQYGSKKCELVEVDVAQLHDCHYDGCEKRFQKTTDLEYHISKNHKRRVMMYESICTQTSISSLETQNNSTQIDDDLPPMPQMPILKKEVPIKTPIGNVYEDLSDDDSETKPTDLVLKTPSSSASSAVATLMGIAQVSSSTTSATTSVVPPVGAQRSTPATPVSAKIGINPSMVANALAEKNKQQQQQQQKLNQLQPPHNPSLSTAPSSSSAQPPTMIQAHPMAGVFIPPPFHPAMMNPQMAAMMDQQRIAVAMSQQQQMSRTPSRQTISVSDSHKIHELAKSRENQQRQQSATPKTPSESVSTTGVVTPQRQFLPPQMMQPGTPQSILLQQQQQQQQQQQQAAAQHQIIQQMQMQMQRGMAPQMANQELLMMMMGMPHMVQGVPGFPGVPQLPPK
Protein: Glycerol-3-phosphate acyltransferase, putative (Q38BT6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- glycerol kinase
- glycerol kinase
- glycerol kinase
- glycerol kinase
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase
- Glycerol-3-phosphate dehydrogenase [NAD
- Dihydroxyacetone phosphate acyltransferase, putative
- Lipin, putative
- Phosphatidic acid phosphatase, putative
Sequence:
MEGKSVVGGSHKLADGSSSCGTIGANPGYAGTSTPLDASSSLYFGKVVEDAVPVRVEVGETTTRHTDPQGASVPLTRKATAKDRIAVEKTSDFVFCDECGQNIPVSEWADHREHPRVVEHVTSWVGRLNKLLIRLFIDFFMWVLMNIYFREVVVVNEKSIPKTGGVVFYGNHQNQFIDAMMIRANCGRPVRFVMAEKSFQRPIIGLFGHMTDAVPVIRPQDAPLNSGEGRLIRMDGDMIYGEGTKFTMCLSDRDVIIWYREDVKCTAQVLKINSDTVLQLTMPVAACDAVTKPVGFQVSRRIDHSEMYASVYQTLQSGQCIGIFPEGGSHDRTSLLPLKAGVALFSLGAAVRGIDVKVVPCGLTYFYGHKFRSRAHVEFGEPITPSAEVVALFNTDKRKATGIFLEQLNEELRGFTINVPNMSALNFLHGFRQLYQPQNCILATRDHLRLTRRLSVIMEEQKGNPEFIDYRSRVENYQDYCNALLVRDSQAATLGKLGSNEARQLHLMFRRCFTLFLMGVILVPFFVVGLPIGILAKSLSERHRKKALSQSNIKIVGTDVMGSYKLIVGFISVPVVFSIVSIITYVYTDLRTALTVSVCLPMTMYVSLLILQEAAIEMRAALPLFMSLISKHKQFCKLYERRRALVALTKVLVKKWDPELEEELQHYVQESKQSMKLREPSLFSLRHGGLRRLADIKN
Protein: WRKY transcription factor 55 (WRKY DNA-binding protein 55) (Q9SHB5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MYSYKKISYQMEEVMSMIFHGMKLVKSLESSLPEKPPESLLTSLDEIVKTFSDANERLKMLLEIKNSETALNKTKPVIVSVANQMLMQMEPGLMQEYWLRYGGSTSSQGTEAMFQTQLMAVDGGGERNLTAAVERSGASGSSTPRQRRRKDEGEEQTVLVAALRTGNTDLPPDDNHTWRKYGQKEILGSRFPRAYYRCTHQKLYNCPAKKQVQRLNDDPFTFRVTYRGSHTCYNSTAPTASSATPSTIPISSVTTGHSVDYGLAVVDMADVMFGSGGVGTNMDFIFPKNDPS
Protein: Cytochrome b-c1 complex subunit 8 (Complex III subunit 8) (Complex III subunit VIII) (Ubiquinol-cytochrome c reductase complex 9.5 kDa protein) (Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C) (Q9CQ69)
Organism: Mus musculus (Mouse)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 6C
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b
Sequence:
MGREFGNLARIRHVISYSLSPFEQRAFPSYFSKGIPNVLRRTRERILRVAPPFVVVYLIYTWGNQEFEQSKRKNPAMYENDK
Protein: Integral membrane protein (A0A0H3MBG2)
Organism: Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
Interaction partners:
Sequence:
MGFGTVRGKGKAVKSFFLRPLQNLEVGLFSLPIVLLLGEIGCVSSISSVSLVAVLSIVGVFVALVSFFRSWGYGLSVVGAIFFGLALCNNFPVSVFWGGLLTVSFIISYGILLLSVSLVEGHIKEKAVSLSELTASHNSLQDSYNREVQERKEKELLAQSKITALEQELSVSHEQLQEVSRKYTHTSEDLQILIDQRDSWLKDYMTLHQEYVRVVAGDEENVIFPWKVFQGNSEKDSGYQQRVQDAEHKIAHLEKLCEEENSGKRYAEECLDKALADLLESTRLREILEKEIFQKDEEIASLKQEIAAEKLLSSSVSDDRAAYKGKYLQLREQFTVKDSFLKKARRERFLAQEQLLVLKRAKEEEALNLSTTDSFSIIQNLLLQIEALEEEVTYLEELVLHNQNR
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB (EC 3.2.1.113) (Mannosidase alpha class 1A member 2) (Processing alpha-1,2-mannosidase IB) (Alpha-1,2-mannosidase IB) (O60476)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- Alpha-mannosidase 2
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
- Alpha-mannosidase 2x
Sequence:
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDSSKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALEEAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFIHLSYLTGDLTYYKKVMHIRKLLQKMDRPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEARKMYDDAIEAIEKHLIKKSRGGLTFIGEWKNGHLEKKMGHLACFAGGMFALGADGSRADKAGHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWYLWRFTHDPRYRQWGWEAALAIEKYCRVNGGFSGVKDVYSSTPTHDDVQQSFFLAETLKYLYLLFSGDDLLPLDHWVFNTEAHPLPVLHLANTTLSGNPAVR
Protein: 2',5'-phosphodiesterase 12 (2'-PDE) (2-PDE) (EC 3.1.4.-) (Mitochondrial deadenylase) (EC 3.1.13.4) (Q6L8Q7)
Organism: Homo sapiens (Human)
Function: Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. Degrades triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme increases cellular 2-5A levels and decreases viral replication in cultured small-airway epithelial cells and Hela cells.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:21245038, ECO:0000269|PubMed:21666256, ECO:0000269|PubMed:22285541}.
Interaction partners:
- 2-5A-dependent ribonuclease
- Filamin-A
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 9
- Probable ATP-dependent RNA helicase DDX6
- SRA stem-loop-interacting RNA-binding protein
Sequence:
MWRLPGARAALRVIRTAVEKLSRAEAGSQTAAGAMERAVVRCVPSEPKLSLSFALADGSHKNMQRDQSEPLGRVLSRIATNALKGHAKAAAAKKSRKSRPNASGGAACSGPGPEPAVFCEPVVKLYYREEAVAEDVLNVDAWQDGAVLQIGDVKYKVERNPPAFTELQLPRYIMAGFPVCPKLSLEFGDPASSLFRWYKEAKPGAAEPEVGVPSSLSPSSPSSSWTETDVEERVYTPSNADIGLRLKLHCTPGDGQRFGHSRELESVCVVEAGPGTCTFDHRHLYTKKVTEDALIRTVSYNILADTYAQTEFSRTVLYPYCAPYALELDYRQNLIQKELTGYNADVICLQEVDRAVFSDSLVPALEAFGLEGVFRIKQHEGLATFYRKSKFSLLSQHDISFYEALESDPLHKELLEKLVLYPSAQEKVLQRSSVLQVSVLQSTKDSSKRICVANTHLYWHPKGGYIRLIQMAVALAHIRHVSCDLYPGIPVIFCGDFNSTPSTGMYHFVINGSIPEDHEDWASNGEEERCNMSLTHFFKLKSACGEPAYTNYVGGFHGCLDYIFIDLNALEVEQVIPLPSHEEVTTHQALPSVSHPSDHIALVCDLKWK
Protein: Minor cardiolipin synthase ClsB (P45865)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the biosynthesis of cardiolipin.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Major cardiolipin synthase ClsA
- Probable cardiolipin synthase YwiE
- UV DNA damage endonuclease
Sequence:
MKVFIVIMIIVVIFFALILLDIFMGRAGYRKKAYEPVFSKKKSDIELIHCGADLVERMMNDIRQAASSVHMMFFIMKNDEVSHNMYTLLKTKAQAGVSVYLLLDWAGCRAIKKTALQTMKNAGVHVHVMNRPRFPFFFFHMQKRNHRKITVIDGKIGYIGGFNIAEEYLGKKAKFGNWEDYHLRMIGEGVHDLQTLFASDLKRNTGIELGSDVWPKLQQGTISHKIYATDGYSLENIYLANIAQAKNRLTVCTPYYIPSKPLQEALINARKNGVSVRIIVPMKSDHPLVREAAFTYYSELLDAGCLIYRYYQGFYHVKALIIDDHLSIIGTANFDKRSLFLNEEVNVEIDDEAFTSEVYATIEEDMKKSELLTMEDFSKRTFRQRPAEWLGRALSYFL