wanglab/gogpt-training-data huggingface dataset:
Protein: Multidrug transporter DTR1 (Acetic acid exporter DTR1) (Drug:H(+) antiporter DTR1) (DHA DTR1) (Q6FJH4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Plasma membrane acetic acid exporter, relieving the stress induced upon cells within hemocytes, and thus enabling increased proliferation and virulence against Galleria mellonella larvae. Confers resistance to weak acid and oxidative stress, but not to antifungal drugs.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29184852}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSTSSNTSGECSPFSITDSIVVQATDDNADKILQEVDLSDPNIDKNDTFELRQQVSIKESPLYYLRDIPYSAYTSFQVSLIFLIVIYNGFLGPLAGNVFIPALPLLQKEFNVSETTINATVSVFMATFSISPLFWGALADKGGRKILYIISISLMVIINILLASVPKKIGSLIFLRIIQAFASSSVISLGAGTVADLTPPKDRGKAMAYFMLGPNLGPILAPIIAGLILLDNNNWRWLFGFLCIVSGLGLIMVILLLPETLRCIVGNGDRQWENWSQNENDMSTQPVDFSSPISRWSFVSDIGFLNPITQDSIFKGLYPHPPKFSVWTYLRIMTFPPVILTSIANALLFCTYYSISVTLSHFLATEYSYSNLKIGACYVCPGVCMLLGSQIGGHLSDSMRKSWKKENYNTEYPLEFRLILTVCGVLLAIGGSIGYGWCIQFHYHISAVLVFAGLMAFGLTWCNNTIMTYLSELLSLRVSSAIAVSSFFRNIAAAISSALIAKLCQKMGIGFCFLGLGLINLVSLFSILVLINNRNKWVKDSF
Protein: ORF224 (Q35317)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MPQLDKLTYFSQFFWFCLLLVSSSRGMGGQIPSISRYERIVSKFIGKFFFSGLWTDRPYLIFIFISLIFLGLYIVRRRREAFSSTLIGSFSGLFSFFFVEGPEVASAMENPPGPGPSEAGPSGSAAGKSAEASTPSSSFFNGLSGQIPAPDSPGEEVPQGEQPRFDPYSIPEVPLEHVFGAVPDRGEPSTSHTPPNPEPQLGEENAGPSNHQIQHDVIRSRLET
Protein: Nucleoporin NUP35 (35 kDa nucleoporin) (Mitotic phosphoprotein 44) (MP-44) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53) (Q8R4R6)
Organism: Mus musculus (Mouse)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000250|UniProtKB:Q8NFH5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NFH5}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}.
Interaction partners:
- Nucleoporin NUP188
- Nuclear pore complex protein Nup93
- Nucleoporin 205
- Nuclear pore complex protein Nup155
- Nucleoporin NDC1
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup153
- Nucleoporin SEH1
Sequence:
MAAFAVDPQAPTLGSEPMMLGSPTSPKTGANAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVPAHKDKSGAPPVRSIYDDISSPGLGSTPLTSRRQANISLLQSPLVGATTPVPGQSMFSPANIGQPRKTTLSPAQLDPFYTQGDSLTSEDHLDDTWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVKPCIDKNVMENSDRGVLSSPSLAFTTPIRTLGTPTQSGSTPRVSTMRPLATAYKASTSDYQVISDRQTPKKDESLVSRAMEYMFGW
Protein: TBC domain-containing protein C215.01 (O43048)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May act as a GTPase-activating protein for Rab family protein(s).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Also localizes to the barrier septum.
Interaction partners:
Sequence:
MSSLASLIKTKLKLPDSSKNLNKLRWKFRLLESQFALYSLPCQLRFVHYNNLEDPNSFNGLLYLFTDYIAFQGDDESNQFCMPYTIIRKVSRVKSNDLEQLLSVSTSNGYEYRISLQVSETTAAHFCQLLREELVSHKADMQRSSEFSKQFFSERLCKPNVPEPETKDSYGFGARYGYPTDPRISRERAKLRMWKEYFLLYGANLSLIRVSLFSKLVRIELPNKLRGEIWELTSGSMYFRLENSDEYDHLLKVYSGQTSFSLEEIEKDLGRSLPEYPAYQNEEGINALRNVLVAFSWKNQEVGYCQAMNIVAAALLIHCTEEQTFFLMHKICEDYIPGYYSKTMYGTLIDQQVYESLVQRSMPNLHAHFVSKDIQLSIISLPWFLSLFLCTMPLPYAFRLLDFFFLEGPRVLFQIGMAILYDNEAEIMKATEDTMLISILKNYFSSLGDKAYKDATDKRVASITKFQLLLVTAFKKFSHITHSLIEDERKKHYEGVMNSIESFAKRTQIRSLQNYGTLTRTDLSNIYDRYHEVLSSKHRVGLGSSTDTRLEFDEFCIFLAGVTEWAKGLDAAAINNSSSFLRHLFLRFDKSMTGSLSLQDLVSGIAELKFRDVMRNISFIFELYDFNGDGFMDKPDVLKVSEAILWLTRFMGDEYLSAVSEFIQRCFHFADEASPDGHSDTLIDISDHMSSTGSENRSVGANSDIKVSLPTFRMVVLSIGLLEQLFSGGLADSIVLAPVQEKSSTTGGLRGLLDSLVIDTNRIGKTFRGHKPASRPSTANGTSNQNTTSEITTSETTATEKTPSNSSDTEDDVGDVVENDKDLLQFDPYKKNDA
Protein: Glucuronide carrier protein homolog (P0CE44)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Beta-glucuronidase
- Membrane-associated protein UidC
Sequence:
MNQQLSWRTIVGYSLGDVANNFAFAMGALFLLSYYTDVAGVGAAAAGTMLLLVRVFDAFADVFAGRVVDSVNTRWGKFRPFLLFGTAPLMIFSVLVFWVLTDWSHGSKVVYAYLTYMGLGLCYSLVNIPYGSLATAMTQQPQSRARLGAARGIAASLTFVCLAFLIGPSIKNSSPEEMVSVYHFWTIVLAIAGMVLYFICFKSTRENVVRIVAQPSLNISLQTLKRNRPLFMLCIGALCVLISTFAVSASSLFYVRYVLNDTGLFTVLVLVQNLVGTVASAPLVPGMVARIGKKNTFLIGALLGTCGYLLFFWVSVWSLPVALVALAIASIGQGVTMTVMWALEADTVEYGEYLTGVRIEGLTYSLFSFTRKCGQAIGGSIPAFILGLSGYIANQVQTPEVIMGIRTSIALVPCGFMLLAFVIIWFYPLTDKKFKEIVVEIDNRKKVQQQLISDITN
Protein: Spliceosomal U5 snRNP-specific protein, putative (Q57XD3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR017199}.
Interaction partners:
- PRP8 protein homologue
- PRP1 splicing factor N-terminal domain-containing protein
- U5 small nuclear ribonucleoprotein component, putative
- Sm protein G
- Sm protein B
- Sm protein F
- RNA helicase
- Small nuclear ribonucleoprotein E
- Uncharacterized protein
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MTELTRLHSAWDVDRHIVLEGEKLVLIRFSHYGEATEQEEDMAHTLSTRQIDEVLVALAPKVRKYCTIYVVSTLEVPEFNVMYELGHSREPFAVMFFYRNAHIRVDVGTGNNNKINFVVSEDELLSIADAAYRAGRSGKTIAYSEKKFTTAAVRR
Protein: Aldo-keto reductase family 1 member D1 (EC 1.3.1.3) (3-oxo-5-beta-steroid 4-dehydrogenase) (Delta(4)-3-ketosteroid 5-beta-reductase) (Delta(4)-3-oxosteroid 5-beta-reductase) (P51857)
Organism: Homo sapiens (Human)
Function: Catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of bile acid intermediates and steroid hormones carrying a delta(4)-3-one structure to yield an A/B cis-ring junction. This cis-configuration is crucial for bile acid biosynthesis and plays important roles in steroid metabolism. Capable of reducing a broad range of delta-(4)-3-ketosteroids from C18 (such as, 17beta-hydroxyestr-4-en-3-one) to C27 (such as, 7alpha-hydroxycholest-4-en-3-one).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7508385}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase type 7
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Aldo-keto reductase family 1 member C3
- Aldo-keto reductase family 1 member C1
- 11-beta-hydroxysteroid dehydrogenase 1
- 11-beta-hydroxysteroid dehydrogenase type 2
- 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Cytochrome P450 11B1, mitochondrial
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
Sequence:
MDLSAASHRIPLSDGNSIPIIGLGTYSEPKSTPKGACATSVKVAIDTGYRHIDGAYIYQNEHEVGEAIREKIAEGKVRREDIFYCGKLWATNHVPEMVRPTLERTLRVLQLDYVDLYIIEVPMAFKPGDEIYPRDENGKWLYHKSNLCATWEAMEACKDAGLVKSLGVSNFNRRQLELILNKPGLKHKPVSNQVECHPYFTQPKLLKFCQQHDIVITAYSPLGTSRNPIWVNVSSPPLLKDALLNSLGKRYNKTAAQIVLRFNIQRGVVVIPKSFNLERIKENFQIFDFSLTEEEMKDIEALNKNVRFVELLMWRDHPEYPFHDEY
Protein: Armadillo repeat-containing protein 5 (Q5EBP3)
Organism: Mus musculus (Mouse)
Function: Involved in fetal development, T-cell function and adrenal gland growth homeostasis. Negatively regulates adrenal cells survival. Plays a role in steroidogenesis, modulates steroidogenic enzymes expression and cortisol production (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28169274}.
Interaction partners:
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 41 homolog
Sequence:
MAAARPALTDSLSFCLAQLTAAAGEGPGGGKDPATNETPLGRALLALRTRHIKAAEGIERFRARGGLRPLLALLRRTAAAGPAPSQAASGSAPSSVASAGSTPGHAPAAESLLTPSLPMRLRKTLDLALSILANCCTEGACRAEVRRLGGILPLVTILQCVKTDSIQNRTARALGNLAMEPESCRDIHSAGAVPFLVESLTACQDSQCLQSIVRALRNLADSPQHRLALAQQGAVRPLAELLATAPDPALTAALVRALLELSRGCSRACAEQLSLGGALGPLVSLASHPKRAIREAAILILANLCAQGLVRPALGNAGGVEVLLGELRRRRSPGGSSSATQQPLVRAVCLLCREAINRARLRDAGGLELLMGLLQDPGASAWHPRVVAALVGFLYDTGALGKLQALGLVPLLARQLCGEAGEEEEEGIEAASWDFPEERTSGQAEGGSFRSLRLWLISEGYAAGPGDISPDWSPERCPMPEPSESVSPTPGQTSMSTPRTLRKPGRIPAATPEEPWGQEGPALLLLSRFSQAPDPSGALVTGPALCGLLAYVTGAPGPPNPRALRILARLTCNPACLEAFVRTYGAALLRAWLVLGVSPDDWPVPHARPVHRSQHRELGEMLLQNLTVQAESPFGVGALTHLLLSGSPEDRVACALTLPFICRKPTLWRRLLLDQGGLRLLLTALTQPAPHPLFLFFAADSLSCLQGLVSPTASPVPLPALPLELDSPPPCLYEPLLGPAPAPAPDLHFVLDSGLQLPAQRAASAAASPFFRALLSGSFAEAQMDLVPLRGLSPGAAWPVLHHLHGCRGCGAALGPVPPPGQPLLGSKAEEALEAAGRFLLPALEEELEEAVGRIHLSPRGGPESVGEVFRLGRPRLAAHCARWTLEPGQCPRKRALALTGLVEAAGEEAGPLTEALLAVVMGIES
Protein: Proprotein convertase subtilisin/kexin type 5 (EC 3.4.21.-) (Proprotein convertase 5) (PC5) (Proprotein convertase 6) (PC6) (Subtilisin-like proprotein convertase 6) (SPC6) (Subtilisin/kexin-like protease PC5) (Q04592)
Organism: Mus musculus (Mouse)
Function: Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive and regulated secretory pathways. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha-integrins. May be responsible for the maturation of gastrointestinal peptides. May be involved in the cellular proliferation of adrenal cortex via the activation of growth factors.
Subcellular location: [Isoform PC5A]: Secreted. Note=Secreted through the regulated secretory pathway.; SUBCELLULAR LOCATION: [Isoform PC5B]: Endomembrane system; Single-pass type I membrane protein. Note=Type I membrane protein localized to a paranuclear post-Golgi network compartment in communication with early endosomes.
Interaction partners:
- Lipoprotein lipase
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Sequence:
MDWDWGNRCSRPGRRDLLCVLALLAGCLLPVCRTRVYTNHWAVKIAGGFAEADRIASKYGFINVGQIGALKDYYHFYHSRTIKRSVLSSRGTHSFISMEPKVEWIQQQVVKKRTKRDYDLSHAQSTYFNDPKWPSMWYMHCSDNTHPCQSDMNIEGAWKRGYTGKNIVVTILDDGIERTHPDLMQNYDALASCDVNGNDLDPMPRYDASNENKHGTRCAGEVAATANNSHCTVGIAFNAKIGGVRMLDGDVTDMVEAKSVSYNPQHVHIYSASWGPDDDGKTVDGPAPLTRQAFENGVRMGRRGLGSVFVWASGNGGRSKDHCSCDGYTNSIYTISISSTAESGKKPWYLEECSSTLATTYSSGESYDKKIITTDLRQRCTDNHTGTSASAPMAAGIIALALEANPFLTWRDVQHVIVRTSRAGHLNANDWKTNAAGFKVSHLYGFGLMDAEAMVMEAEKWTTVPQQHVCVESTDRQIKTIRPNSAVRSIYKASGCSDNPNHHVNYLEHVVVRITITHPRRGDLAIYLTSPSGTRSQLLANRLFDHSMEGFKNWEFMTIHCWGERAAGDWVLEVYDTPSQLRNFKTPGKLKEWSLVLYGTSVQPYSPTNEFPKVERFRYSRVEDPTDDYGAEDYAGPCDPECSEVGCDGPGPDHCSDCLHYYYKLKNNTRICVSSCPPGHYHADKKRCRKCAPNCESCFGSHGNQCLSCKYGYFLNEETSSCVTQCPDGSYEDIKKNVCGKCSENCKACIGFHNCTECKGGLSLQGSRCSVTCEDGQFFNGHDCQPCHRFCATCSGAGADGCINCTEGYVMEEGRCVQSCSVSYYLDHSSEGGYKSCKRCDNSCLTCNGPGFKNCSSCPSGYLLDLGTCQMGAICKDGEYIDDQGHCQTCEASCAKCWGPTQEDCISCPVTRVLDDGRCVMNCPSWKFEFKKQCHPCHYTCQGCQGSGPSNCTSCRADKHGQERFLYHGECLENCPVGHYPAKGHACLPCPDNCELCYNPHVCSRCMSGYVIIPPNHTCQKLECRQGEFQDSEYEECMPCEEGCLGCTEDDPGACTSCATGYYMFERHCYKACPEKTFGVKWECRACGTNCGSCDQHECYWCEEGFFLSGGSCVQDCGPGFHGDQELGECKPCHRACENCTGSGYNQCSSCQEGLQLWHGTCLWSTWPQVEGKDWNEAVPTEKPSLVRSLLQDRRKWKVQIKRDATSQNQPCHSSCKTCNGSLCASCPTGMYLWLQACVPSCPQGTWPSVTSGSCEKCSEDCVSCSGADLCQQCLSQPDNTLLLHEGRCYHSCPEGFYAKDGVCEHCSSPCKTCEGNATSCNSCEGDFVLDHGVCWKTCPEKHVAVEGVCKHCPERCQDCIHEKTCKECMPDFFLYNDMCHRSCPKSFYPDMRQCVPCHKNCLECNGPKEDDCKVCADTSKALHNGLCLDECPEGTYKEEENDECRDCPESCLICSSAWTCLACREGFTVVHDVCTAPKECAAVEYWDEGSHRCQPCHKKCSRCSGPSEDQCYTCPRETFLLNTTCVKECPEGYHTDKDSQQCVLCHSSCRTCEGPHSMQCLSCRPGWFQLGKECLLQCRDGYYGESTSGRCEKCDKSCKSCRGPRPTDCQSCDTFFFLLRSKGQCHRACPEHYYADQHAQTCERCHPTCDKCSGKEAWSCLSCVWSYHLLKGICIPECIVGEYREGKGENFNCKKCHESCMECKGPGSKNCTGCSAGLLLDMDDNRCLHCCNASHSRRSQDCCDCQSSTDECILPAREAEFYEHTKTALLVTSGAMLLLLLGAAAVVWRKSRSRPVAKGRYEKLAEPTVSYSSYRSSYLDEDQVIEYRDRDYDEDDEDDIVYMGQDGTVYRKFKYGLLDETEDDELEYDDESYSYQ
Protein: Septum site-determining protein MinD (Cell division inhibitor MinD) (Q9AG19)
Organism: Neisseria gonorrhoeae
Interaction partners:
Sequence:
MAKIIVVTSGKGGVGKTTTSASIATGLALRGYKTAVIDFDVGLRNLDLIMGCERRVVYDLINVIQGEATLNQALIKDKNCENLFILPASQTRDKDALTREGVEKVMQELSGKKMGFEYIICDSPAGIEQGALMALYFADEAIVTTNPEVSSVRDSDRILGILQSKSRKAEQGGSVKEHLLITRYSPERVAKGEMLSVQDICDILRIPLLGVIPESQNVLQASNSGEPVIHQDSVAASEAYKDVIARLLGENREMRFLEAEKKSFFKRLFGG
Protein: ABC transporter, ATP-binding protein (A0A0H2URQ2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MIDIQGLEKKFNDRAIFSGLNLKLEKGKVYALIGKSGSGKTTLLNILGKLEKIDGGRVLYQGKDLKTIPTREYFRDQMGYLFQNFGLLENQSIKENLDLGFVGQKISKVERLERQVGALEKVNLGYLDLEQKIYTLSGGEAQRVALAKTILKNPPLILADEPTAALDPENSEEVMNLLVDLKDENRIIIIATHNPLVWNKADEIIDMRKLAHV
Protein: Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE) (P17182)
Organism: Mus musculus (Mouse)
Function: Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By similarity). ENO1 is localized to the M-band. {ECO:0000250, ECO:0000269|PubMed:11229603}.
Interaction partners:
- Pyruvate kinase PKM
- Plasminogen
- Phosphoglycerate mutase 1
- Glucose-6-phosphate isomerase
- Phosphoglycerate kinase 1
- Triosephosphate isomerase
- Pyruvate kinase PKLR
- Phosphoglycerate mutase 2
- Bisphosphoglycerate mutase
- Transaldolase
Sequence:
MSILRIHAREIFDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDNDKTRFMGKGVSQAVEHINKTIAPALVSKKVNVVEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNPEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKTAIAKAGYTDQVVIGMDVAASEFYRSGKYDLDFKSPDDPSRYITPDQLADLYKSFVQNYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAASEKSCNCLLLKVNQIGSVTESLQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQILRIEEELGSKAKFAGRSFRNPLAK
Protein: Ras-related protein Rab-4 (Q54DA7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- RabGAP/TBC domain-containing protein
- Vacuolar protein sorting-associated protein 35
- Uncharacterized protein
- Rac guanine nucleotide exchange factor B
Sequence:
MGKPLYLVKFIIIGSQSVGKSCLLFRFIDNKFKSQSTHTIGVDFSSRVVDIQGKNVKLQIWDTAGQERFRSVVISYYRGSAGVALVYDVTNRESYNHITNWLSDVKSLASPDVTIILVGNKADLTEQREVTFLEASRIAQENGLLFMETSALTGEGVEEMFLKCTRTIMTKIDSGEVNLEHLGVQISSDSGNVTKKPGDSSNCSC
Protein: KU70 protein (Q582N4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- KU80 protein
- Protein artemis
- Endo/exonuclease Mre11
- non-specific serine/threonine protein kinase
- DNA repair protein RAD50
- DNA ligase, putative
- DNA ligase, putative
- DNA ligase
- Telomerase reverse transcriptase
- Exonuclease, putative
Sequence:
MSVDGLDFHDEDDSYFNETYATEDEPSLRTGSVSSLDQFDVVLCLVDFQQRMFQGVVAHDCKNPFAGGAEQVYDDIAEVKVKETPTVFEKAICCVQQLYKDKGISDSNDMVALVLYNTRECTHPDYPGVYVFHTFCSAEIQSVLDLEELVAAGRVPSAGYENIVTKIGHSTEAKSHLGDALRAARHLFSQLPSEVKHRRIFLFTNDVNPHRGDEELLQKCAIQIESLSSGGVGLVCYDMSPTALPSPAASTQSGEAAAMSERWATQFGGVDEFWSALTGAVPKATNSSRVGTIDIVHLNSDDSVMLGALSTAVRWRTHPRGASQTTTLTIGVGAKGSALPRLTVGMYFPMTNAQRRLSKWLDGRAGEMVMLRQRAVGVGAPILLPCHAGKSGAPPAHISTGQLGKSRPSTGPGTCPNVPLSCKKHIAEVVGAGLTLGFSIICFKNADDVLHPQYVLGKSCVLHPDPQDGSDGSLRLFIRLARALKEQRKVAMAQHITRYATPPRLVALVPPGLNGDHMDTASFPVMHGLGLYVVPLSYADDVRTTPRSPLFGDATKPMERDIALAQRLLATLPSKYNVNVVPNPALELRYKAIESIVQQTQQQSGLSKEIPGVAPFSQLSKAVDRTWGDRGAMAKYGSVFDEFKAVLLPSYNRDETCGPKTKAARNVKARAELADEDIKGVERIISAVESAFRFQSMGMLTEPQLKEYLRVMEGGAFGVRRNPDIIQAVISQLQGDI
Protein: Chloride intracellular channel protein 1 (Glutaredoxin-like oxidoreductase CLIC1) (EC 1.8.-.-) (Glutathione-dependent dehydroascorbate reductase CLIC1) (EC 1.8.5.1) (Q6MG61)
Organism: Rattus norvegicus (Rat)
Function: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O00299}. Nucleus membrane {ECO:0000250|UniProtKB:O00299}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00299}. Cytoplasm {ECO:0000250|UniProtKB:O00299}. Cell membrane {ECO:0000250|UniProtKB:O00299}; Single-pass membrane protein {ECO:0000250|UniProtKB:O00299}. Endoplasmic reticulum {ECO:0000269|PubMed:26777142}. Note=Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. Might not be present in the nucleus of cardiac cells. {ECO:0000250|UniProtKB:O00299, ECO:0000269|PubMed:26777142}.
Interaction partners:
Sequence:
MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTSGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGISQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVARALK
Protein: Autophagy-related protein 8 (Autophagy-related ubiquitin-like modifier atg8) (Q2UBH5)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Required for both the differentiation of aerial hyphae and conidial germination.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:16896216, ECO:0000269|PubMed:21204928}; Lipid-anchor {ECO:0000269|PubMed:16896216}. Vacuole membrane {ECO:0000250|UniProtKB:P38182, ECO:0000269|PubMed:21204928}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Lipid droplet {ECO:0000269|PubMed:16896216}.
Interaction partners:
- Autophagy-related protein 3
- ZZ-type domain-containing protein
- Probable cysteine protease atg4
- Serine/threonine-protein kinase atg1
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like protein ATG12
- Autophagy protein 5
- Autophagy-related protein 9
- Autophagy-related protein 18
- GTPase-activating protein GYP7
Sequence:
MRSKFKDEHPFEKRKAEAERIRQKYADRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVDEVLPPTAALMSSIYEEHKDEDGFLYITYSGENTFGDL
Protein: Large ribosomal subunit protein uL14 (50S ribosomal protein L14) (P9WHD9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
Interaction partners:
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein bL9
- Large ribosomal subunit protein bL21
- Small ribosomal subunit protein uS3
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein bL33B
Sequence:
MIQQESRLKVADNTGAKEILCIRVLGGSSRRYAGIGDVIVATVKDAIPGGNVKRGDVVKAVVVRTVKERRRPDGSYIKFDENAAVIIKPDNDPRGTRIFGPVGRELREKRFMKIISLAPEVL
Protein: Oxygenase-alpha NBDO (Q8RTL4)
Organism: Comamonas sp. JS765
Interaction partners:
Sequence:
MSYQNLVSEAGLTQKLLIHGDKELFQHELKTIFARNWLFLTHDSLIPSPGDYVKAKMGVDEVIVSRQNDGSVRAFLNVCRHRGKTLVHAEAGNAKGFVCGYHGWGYGSNGELQSVPFEKELYGDAIKKKCLGLKEVPRIESFHGFIYGCFDAEAPPLIDYLGDAAWYLEPTFKYSGGLELVGPPGKVVVKANWKSFAENFVGDGYHVGWTHAAALRAGQSVFSSIAGNAKLPPEGAGLQMTSKYGSGMGVFWGYYSGNFSADMIPDLMAFGAAKQEKLAKEIGDVRARIYRSFLNGTIFPNNSFLTGSAAFRVWNPIDENTTEVWTYAFVEKDMPEDLKRRVADAVQRSIGPAGFWESDDNENMETMSQNGKKYQSSNIDQIASLGFGKDVYGDECYPGVVGKSAIGETSYRGFYRAYQAHISSSNWAEFENASRNWHIEHTKTTDR
Protein: Agouti-related peptide 2 (Agouti-signaling protein 2b precursor) (Agouti-signaling protein, nonagouti homolog (mouse) 2b) (J3JQX9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Agouti-related neuropeptide.
- Agouti-signaling protein
- Leucine-rich repeats and transmembrane domains 2a.
Sequence:
MTTAVLKGFVLFICLFFTVVQSITCEASKIESRKKHENDVAHQGSAITTGVWNQEKPKRLFARTRYLSQQRHHGARPKPRPEAVSPAQTPARRCAGLTESCSSLTPCCDPCASCHCRLFNTICHCWRLGHLCPKKT
Protein: Uncharacterized protein, isoform E (A0A6M3Q835)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIPTSVTNSPPPAGLGQNGASASLGSATAAAGGGMLSGLGMVAVSGCGSAGTGAQNNYGSVVLGLASLILEGRPIADDEYQQQTVGVVGSGAATAGSGGGRLSPRPSTSRAAINITTNPYGSMGGSENRAVNGSGSTGSPSSSSLTHQRWTQKLCQLRQISPAAQTMSAEPELVSLAINDLNKDHGDYEIVRRVMLNRAGGTGLVSSAGGGTNNSSAASSPGSNSSDNILHSLQSLATTCLRGGPALAPPPSVESRPLNLAFHWSGLGGSGGRGLGFGGGAASISNTPTTTATATASSGASSSASRPKHGPHCDQFLRKMGLAKGEMPSEAEEHICDMSYVNMTCNRWRAYCMKMEAILARREPVCIEVYLGPVSHKLLLEQWIICGREKVPPPTMTLPSLCSAIRSQLYFSQIVAWCDLLRKCDPSVYDSGRVIFSNCGNNAGDLATSYTTCGGQKRPRLNIFYRIKQHTTTNSNSGLHQEDGFSAKANVHNFPNVNVSESYSISVSVRSLPRINGGLPHVEPLPPSPAPRSLRPCGGDPASTPTGGGGLHAATPTGLGARTSALTPTTTAGGSNCDNGKPGMGQILDELDGDTSLSHRERQLQKYRKRMQRRDKKRERKATPDRLNSRQQSEEPMDEGEESQTQSQTTSETQSLALTLQQPRRIAMISTGTQTSLSSCQQCGSEKTLLCLSCTGGGGAHGGSNGTANGSTNGATDDGDDSDTTASEMEETSSCSLSSADLIVGTPRNNAELLLQAIQRTPKNRNRKPHPGVLDQVSCRNADLNGGQNNNLLKATPATSGCQVCKRQKTQHNFANGKVHQPTNGKQASNGYASMHLEAEKQPDVVQILATKLTPNIERCSLNPVERCKTPPPGVADHIVVQFKTPLSQVPAKHQPDAMVPLQQQQLGKSSSKPAQLRLNCGSNLLESETPPPMTSPQMRKALPKVNLTTIFCSSAPIAIGCPAFSFDPAALSHARSQLLAPDVSVTPPVQKSFSAPTLPHAASLSVSPRFSKQALAAHKRRSRHLSDRSDRSSLGSDEQLSDEDLESGLCSPAGGSPLKCRARLAAQFGGRPLLGNLEESLLQRRLMPKIEVMGFTLQLGASGGFCPTQVNIPAVSYFYELHGETLSTPYLCEIRLPRKGYSVPRSGTVQATLLNPIGTVVRMFVIPYDMRDMPPLHRTFIRQRILAEELSQDQDEGHKVPRSPTVTSTTSKLGHFISAEQMKRLRYSIHLKFQTSRSGRLCLHTDIRLLISRRTDCDTAAAHAKGVLEAPNELVTDTMMPAEPRYSARQESAGRIXXLLQALGGTFELLRRLCKQLQNKWQQREARELWQLPRYQL