wanglab/gogpt-training-data huggingface dataset:
Protein: C3H1-type domain-containing protein (Q38E49)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYSSEKEKEAPETLTSLPANAEEQQRERDDNHSASAQGEEDKNQDNTPVALLHLRQNFGVLTRVLEREVFRRGLINSTVEDMYSAFSGASVVLVDILRSEVEPRLLRSQLGDMLYSNLELSYGAEHARMLATVIGSSLDDVYLFHAICSPSALEALVHQAQELINPPSNRTGGSNTYSDGARGAVQSQSYGNAVGLARPSFTEFGKERRGEVQPTVEAKLPRVSNTYADGAAPAGMNQPEEEVIPSVTTGGWSNAQRKHVEAEREVLPHHAHHHQLRARLPVNQFTAPQRPQVPSVPHHHHHHHHHHHVVVGTGPVGLQQQDRHHQQLENPQNDAFPRIPVATGLPKRPVDRVLHQQSLQGHDEASHQRGAWRGMGPSPTPQQGAAGVSQPNYNVRNNSPPVPSHVNHNQHPHHIGPTGSPTSARVIAPQRHNANQYIQHPTMTKQPIPQPTPSMASQQPSPQISAMNTTAPATPAVGAVSPPPPSAQRPLPHHHHHLHLIQHHQQSQQNQQQQQQPHHHHHHHHHIHHHHHDVMQQQPIVPPSPPPPQPSYNVKQEHTAAPETKPMAHNAEAAPAQIKPLHHHNVSFHPTKLPQQPPPQPSAPSSVGGEATHQVPIVPAHHHSIFHAQHVAPVHHHHHHHHHHHHHHHHHLQQPPHRYTSSPASAPMSVDMMNDEMTWALSSANLSPPPASELRRLLRERNVPESIVNSVLEAGIKKEELLTMSREMYDERLRTYLGSQQSQTLWAALHSNEKSQHDRDGHEMNDLRSFISNNSIQNNIAQEAEDENGSSKRGRAAKPALQVPQPRTTQSRQQQQQQQQQQQSNKGVEHRMILWLSGVSSSEVNQVLKEVGKYGKVVKHGVSQDKSDMMYFKLKDCKGDLSGMQKIGNYIVEECHRVPPGEAGDGTPPARGPRPEEAEEDGTNKLRAKPNEAASPYPQQQTRPTSARQQGPAGSQVDEHEEDGNLEDSRTHRKGMRNIRGRGRGANHGYHTHRHSEGTGQVMCRYFNKGACKYGEQCPFQHPSKHPGRS
Protein: Neutrophil cytosol factor 1 (NCF-1) (47 kDa autosomal chronic granulomatous disease protein) (47 kDa neutrophil oxidase factor) (NCF-47K) (Neutrophil NADPH oxidase factor 1) (Nox organizer 2) (Nox-organizing protein 2) (SH3 and PX domain-containing protein 1A) (p47-phox) (P14598)
Organism: Homo sapiens (Human)
Function: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:2550933}. Membrane {ECO:0000269|PubMed:12356722}; Peripheral membrane protein {ECO:0000269|PubMed:12356722}; Cytoplasmic side {ECO:0000269|PubMed:12356722}.
Interaction partners:
- Neutrophil cytosol factor 2
- NADPH oxidase activator 1
- Neutrophil cytosol factor 4
- NADPH oxidase 1
- Cytochrome b-245 light chain
- Ras-related C3 botulinum toxin substrate 2
- NADPH oxidase 2
- NADPH oxidase 4
- NADPH oxidase organizer 1
- RAC-alpha serine/threonine-protein kinase
Sequence:
MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV
Protein: UspA domain-containing protein (A0A0H3LCB8)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MKTIIVGIDGSHAAITAALWGVDEAISRAVPLRLVSVIKPTHPSPDDYDRDLAHAERSLREAQSAVEAAGKLVKIETDIPRGPAGPVLVEASRDAEMICVGSVGIGRYASSILGSTATELAEKAHCPVAVMRSKVDQPASDINWIVVRMTDAPDNEAVLEYAAREAKLRQAPILALGGRPEELREIPDGEFERRVQDWHHRHPDVRVYPITTHTGIARFLADHDERVQLAVIGGGEAGQLARLVGPSGHPVFRHAECSVLVVRR
Protein: Inositol diphosphatase SIW14 (EC 3.6.1.52) (5-PP-InsP phosphatase) (Inositol pyrophosphate phosphatase SIW14) (Oxidant-induced cell-cycle arrest protein 3) (Synthetic interaction with WHI2 protein 14) (P53965)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Selectively cleaves the beta-phosphate at the 5-position of soluble inositol pyrophosphates. Converts 5-diphosphoinositol tetrakisphosphate (5-PP-InsP(4)) into inositol pentakisphosphate (InsP(5)), 5-diphosphoinositol pentakisphosphate (5-PP-IP(5) or 5-InsP(7)) into inositol hexakisphosphate (IP(6) or InsP(6)), and 1,5-bisdiphosphoinositol tetrakisphosphate (1,5-PP-IP(5) or InsP(8)) into 1-diphosphoinositol pentakisphosphate (1-PP-IP(5) or 1-InsP(7)). Modulates inositol pyrophosphate metabolism that may have an influence in stress response. Plays a role in actin filament organization and endocytosis. Functions as a prion suppressing factor possibly due to its phosphatase activity against inositol pyrophosphates, which are signal transduction molecules involved in prion propagation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Putative tyrosine-protein phosphatase OCA1
- Tyrosine-protein phosphatase-like protein OCA2
- Protein OCA4
- Oxidant-induced cell-cycle arrest protein 5
- GTP-binding protein YPT1
- Curing of [URE3] protein 1
Sequence:
MGLYQAKNDEGSDPKSSSKIDDLIENEAEIIRLIKEDGKLLIDNGDGRDIHNIIQEDKLLSVEFNEVLKRFHGEEKSDIPRKEFDEDEDDGYDSNEHHQKTIEVMNTLNHVINKEVIPPENFSHVVGEIYRSSFPRQENFSFLHERLKLKSILVLIPEEYPQENLNFLKLTGIKLYQVGMSGNKEPFVNIPSHLLTKALEIVLNPANQPILIHCNRGKHRTGCLIGCIRKLQNWSLTMIFDEYRRFAFPKARALDQQFIEMYDDDEIKRIASKNNWLPLQW
Protein: Heavy metal transport/detoxification superfamily protein (Proline-rich protein, putative) (Putative proline-rich protein) (Q9C684)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- TRM32-like protein
- Transducin/WD40 repeat-like superfamily protein
- Pathogenesis-related thaumatin superfamily protein
- Pathogenesis-related thaumatin superfamily protein
- Chromatin remodeling 34
- LS1-like protein
- Receptor-like protein 52
- Heat shock 70 kDa protein 18
- Heavy metal-associated isoprenylated plant protein 17
Sequence:
MAEKVVMMKLKVDLNCSKCYKKVKKAIRKFPQITDELFDEKSNTIIIKVVCYDPERLMNKLCYKGDGSIKSIVILEPPKPPQPQPQPPQKPTAPAPAPAQAQAPALVRPAPVPVLVSSSAPQPMPMWQPYHCGPYYEAQQYQCYGRPVYESWGGGRQCCHEDMNSQGCSIM
Protein: Apoptosis-stimulating of p53 protein 2a (Tumor protein p53 binding protein, 2) (Q6NSN9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMPMFLTVYLSNNDQHFSEVPITAETVCADVLQLCREPGENSSCYLSEVWRGSERVVGENEKMMDLLLQWGQQRPEVRFFLRHGRAASQPSDSRTQKRNGVKKPADRRLENGVNGPWMDMTLAELQEMASRQQRQIDSQQQLLSTKEQRLRYLQQQEQRQAQSSSEQKKLLQLRETLEQQEAQLKMVRALKGQVEQKRLSNGKLVEQVEQMNNLLHQKQKELVVAVAKVEELSKQLETLKSGQMDAMNSNHSSVAELDRLYRELQMRKNLNVEQNAKLQQQRENLNKRNQEVANMDKRVSELPERLWKKKAALQQKENLPLPPDGQAPPQTPGSRVAAVGPYIQSSTMPRGPDRQDLPIKHNYPEFTATAGHQDRSAQPGAGLHSGKASSKLANWSLANAKSGNNHVTSSLPRMVSQASKSQDNTDVQKRDPRVRPVSMFESTDLPAAALRKNQSSEDLVRDAQSAVKTIVKVPPPVPSKPKQANFPSGGLMGLGKNTGTYPGKSASPQPPAGPQTGTLPSKLEAPPAATVHPFSPDPPGAKDTGGQMLLKPQTVTASSIYSMYTQQPSSGKATQQSIQGALSRAQTRTGHFISVYGKPVTSAGQPSQTPHPENPYLDPPSVSETLTDHSPAEPISETPETERIPRPLSPTKLLPFISNPYRHQSDLDLEALRKKLYNAPRPLKKRSSITEPEGPGGPNIQKLLYQKTTLAAMETVSPPGEEEKETLAKPQGYDAETPEVPEETLPEFPIAPEVEAEDVPPPPPPHPAPKIDASIIIPPPQPESPPPPPPPDSFMEDFPPYPPPPYPSSAEQDNPDDTFNMKPPEVTGQVPFPPGKRTNLRKSGSERIDHSMRVRFNPLALLLDSSLEGEFDLVQRVIYEVEDPSQPNDEGITALHNAVCAGHTEIVKFLVQYGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNRGVVYGLWDYEAAQEDECSFREGDCMSVIRREDELETDWWWVCCGGAEGYVPRNLLGLYPRIKLRQRSLA
Protein: Chromosome 11 open reading frame 54 (E9PPB5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MACAEFSFHVPSLEELAGVMQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFILGAGAGPFQTLGFNSEVIEVKAKRRTGPLNFVTCMRETLEKHYGNKPIGMGGTFIIQKGKVKSHIMPAEFSSCPLNSDEEVNKWLHFYEMK
Protein: Molybdopterin converting factor, subunit 1 (MoaD) (O25482)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Cyclic pyranopterin monophosphate synthase
- Thiamin biosynthesis protein
- Molybdopterin adenylyltransferase
- Cysteine synthase
- Molybdopterin molybdenumtransferase
- GTP 3',8-cyclase
- L-seryl-tRNA
Sequence:
MMVEVRFFGPIKEENFFIKANDLKELRAILQEKEGLKEWLGVCAIALNDHLIDNLNTPLKDGDVISLLPPVCGG
Protein: Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) (Q6FK92)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- dihydroxy-acid dehydratase
- 2-isopropylmalate synthase
- Threonine dehydratase
- 2-isopropylmalate synthase
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- cystathionine gamma-lyase
- Homoserine dehydrogenase
- cystathionine gamma-synthase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Multifunctional tryptophan biosynthesis protein
Sequence:
MDASRLKITKVSTPSERKPNDQLVFGKTFTDHMLTIEWTSENGWDAPEIKPYGKLCLDPSSIVFHYAFELFEGMKAYRTKDGKIAMFRPEKNMERMNKSAARICLPTFDGEELIKLIGKLIELDKHLIPEGEGYSLYIRPTLIGTSEGLGVKEPDRALLFVICSPVGPYYKTGFKAVRLDATDYATRAWPGGVGDKKLGANYAPCVLPQTQAAAKGFQQNLWLFGPEHYVTEVGTMNAFFAFNCKETGKKELVTAPLDGTILEGVTRDSILTLARKYLDPNEWEINERYFTIHEVQEKAHKGELLEAFGSGTAAIVSPIKEIGWKDTIINVPLIPGEQSGPLTKQIASWMMDIQYGKVELDNWLRIVADIN
Protein: Activated in Blocked Unfolded protein response (Q17400)
Organism: Caenorhabditis elegans
Interaction partners:
- Activated in Blocked Unfolded protein response
- Activated in Blocked Unfolded protein response
- Activated in Blocked Unfolded protein response
- Nematode Specific Peptide family, group B
- Prion-like-
- Chitin-binding type-2 domain-containing protein
Sequence:
MRFIAIAALIASSVLLAEATTIRDKRQSCGCAPRVQPSCSCQRTTYTQPQQYSCSCQNTAPVQKSCSCAQPVQQQTYQIQASQCAPACQQSCQNQCQSAPSVSQCQSTCQQSCQTSSCYTPTTPAPVQCQPSCMPACEQSCVVQTPAPVQCVPQCQQQCQQQCVQTQPIQQCQPQCQQQCVQQCAPTTTAAPQIIKINMEISAQCVPQCQQSCQQQCVQQQVPAQQCNQQCTQQCQTTCQQAVPQCQQQCAPQCQQPSAPQCQQCQNTCQQAAPVCQQQCAPQCQQQSAPACQQCQTSCQQTQQCQQQCTPQCQQPSAPQCQQCQSACQAPVATTAAPQVVTIILEASVSQSAQCEPQCQQSCQQQCVQQQQPMQQCAPACTQSCSQSCSAAQPAQMPCQTQSVNSCSCQQNYSPCGNGQCCKRK
Protein: Cilia- and flagella-associated protein 58 central coiled coil domain-containing protein (Q584H3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calponin-homology
- Calponin-homology
- Replication Factor A 28 kDa subunit, putative
- Uncharacterized protein
- DNA repair protein, putative
- Uncharacterized protein
- Replication protein A subunit
- Crossover junction endonuclease MUS81
Sequence:
MADTLQLLGDVTDVSNAAAIVGLDTLVEEGRLIEERADYLKEKFKELHNRVLVVYKRDFFLLKRARQLRKELDAQKERMAARGKIAQDDDAEIQRLNKLLMDTEEELSDAQERESILQVEVLELDRKKFTVALEREDAIAAEEAQLRPRMEAMRQEVSSTGKELEDMVEQCKTLSAKRDVLLAQEAEATEALAKFKTTMAETTRQLANIERLPEHSLRQAQVILKSYEAALLEAKALDEKLAAQADMIAKLELKKNNRNLDYEQAVANLQKLKSKIDSKRVTIATLNTSLEMEQEARLGYQQRIAQIEDLINTTNATRAKQCEDVEQARRDLEQAREEYAELDIALCKIIKEQKDVKDNITSVMKTIERVETTRKRNAQRLDDAKRDAERRNQLFLKEQGYEKEFTAKVGAVSADIKVIEKEIINRTLQEETKRREIKALVVRLQELSKEKAKGKSRIIIGKHELRMKEMYVSDARKRLSDLELRLDSIIDTFQSIKHERTHKAAQIQAITQKMTEMTEKKAILENELVVLCRESAVKEAELVKKRRQIHKLRQSCRALRLEKNNQRKCLEKRSLEERNIKAQARRVASRIATMEEEMGGAKRNYQNIIENRDGAGIQLLDRNDELCVLYERFKTQEKVIRDGITVDNAREEEIRALRIKFTDVRRQVDLVRASVPQVKELEDRLAKILNDIDDEKWKVEVLENDLTNPKNAHRWRLLKRQNAGRSVASGVTAPQQAHSDVVATASPGEAAPSAIVTASDSCSDDVVDLQQRYQQLEERVRNVNERIREKELILEEVTELSTRLAEQVKNGREFTLALTKQVNSHHHSIRAKTRQMMATVSELSVFQASAIQLQQDVQRLEGIVEEAERLMAEGEAPFAEAEERYIREVEGKARYRNVLRRKKEELESEKSKGPKVYVEQRPNAYIPDDGLSVPKPFGALMPFKPTPAVQTSRYYRSKSERSRDSDGPKRGPYSESYSGGGSLKGNDNGPPKTNHFSLTQ
Protein: Isopenicillin N epimerase component 1 (IPN epimerase component 1) (EC 5.1.1.17) (Isopenicillin N epimerase acyl-CoA synthase component) (EC 6.2.1.-) (Q8J0E9)
Organism: Hapsidospora chrysogena (Acremonium chrysogenum)
Function: Together with cefD2, catalyzes the reversible isomerization between isopenicillin N and penicillin N. This two-component IPN epimerase system may function by two sequential steps, an activation of isopenicillin N by the acyl-CoA synthase component cefD1, followed by epimerization by the acyl-CoA racemase component cefD2.
Interaction partners:
Sequence:
MAPGGLLTLAGAAAASTAAAAYLDAKLHLTKDLNQLARAERGAQNFARAVEQRKASGFFLFEAAAARLGDAPCIWSRGHPEYSWTQTYQRACQYGHYFRDLGVVAGQHVGVYLYNSPELMFIWMGLLSIGAAPALINYNLGSDALVHCVRLSRSRFLIYDDASDCSSRIHEVGERLRDINVEAIMLSGSGTTGLPKAAPITVARNYPSASLLPKTFGQKPGPNGDRTYYCIPLYHGTGGIAAMNDLMSGISIALAPKFSLSRFWDDCIESGSTIFVYVGELIRYLLSAPASPKDRQHRVRLVWGNGLSPELWTKFQDRFGVSDIGEFYASTEGVLTLLKHYRGGGFGLGAVGHHGWLLRRKFHNDYVPVRIDPETGDIWRSPKTGFAERLPYERGGEILARLPSRSAWAGYWHAEEATQKKLVENVFEKGDLYFRTGDALRRDADGHWYFLDRLGDTYRWKGENVSTTEVGQVLGSHADIAEANVYGVQVPNHDGRAGCAAIALKNAATPDTLDWSRLTSLLRSELPSYAVPVFIRVRETVGGMSTDNHKHNKVPLRDEGVDPRSMGSKVPGSEKDRFFWLPAGASKYVPFTERDWDLLSGQSAARPRL
Protein: Siderophore exporter MmpL5 (P9WJV1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of an export system, which is required for biosynthesis and secretion of siderophores.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:23431276}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Siderophore export accessory protein MmpS5
- HTH-type transcriptional regulator MmpR5
- Siderophore export accessory protein MmpS4
- ATP synthase subunit c
- Probable transcriptional repressor protein
- Possible transcriptional regulatory protein
- ESX-3 secretion system protein EccD3
- Conserved protein
Sequence:
MIVQRTAAPTGSVPPDRHAARPFIPRMIRTFAVPIILGWLVTIAVLNVTVPQLETVGQIQAVSMSPDAAPSMISMKHIGKVFEEGDSDSAAMIVLEGQRPLGDAAHAFYDQMIGRLQADTTHVQSLQDFWGDPLTATGAQSSDGKAAYVQVKLAGNQGESLANESVEAVKTIVERLAPPPGVKVYVTGSAALVADQQQAGDRSLQVIEAVTFTVIIVMLLLVYRSIITSAIMLTMVVLGLLATRGGVAFLGFHRIIGLSTFATNLLVVLAIAAATDYAIFLIGRYQEARGLGQDRESAYYTMFGGTAHVVLGSGLTIAGATFCLSFTRLPYFQTLGVPLAIGMVIVVAAALTLGPAIIAVTSRFGKLLEPKRMARVRGWRKVGAAIVRWPGPILVGAVALALVGLLTLPGYRTNYNDRNYLPADLPANEGYAAAERHFSQARMNPEVLMVESDHDMRNSADFLVINKIAKAIFAVEGISRVQAITRPDGKPIEHTSIPFLISMQGTSQKLTEKYNQDLTARMLEQVNDIQSNIDQMERMHSLTQQMADVTHEMVIQMTGMVVDVEELRNHIADFDDFFRPIRSYFYWEKHCYDIPVCWSLRSVFDTLDGIDVMTEDINNLLPLMQRLDTLMPQLTAMMPEMIQTMKSMKAQMLSMHSTQEGLQDQMAAMQEDSAAMGEAFDASRNDDSFYLPPEVFDNPDFQRGLEQFLSPDGHAVRFIISHEGDPMSQAGIARIAKIKTAAKEAIKGTPLEGSAIYLGGTAAMFKDLSDGNTYDLMIAGISALCLIFIIMLITTRSVVAAAVIVGTVVLSLGASFGLSVLIWQHILGIELHWLVLAMAVIILLAVGADYNLLLVARLKEEIHAGINTGIIRAMGGSGSVVTAAGLVFAFTMMSFAVSELTVMAQVGTTIGMGLLFDTLIVRSFMTPSIAALLGKWFWWPQVVRQRPIPQPWPSPASARTFALV
Protein: Fibronectin-binding protein (Fibronectin-binding protein FnbB) (LPXTG cell wall anchor domain-containing protein) (Q53682)
Organism: Staphylococcus aureus
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00004168}.
Interaction partners:
Sequence:
MKSNLRYGIRKHKLGAASVFLGTMIVVGMGQEKEAAASEQNNTTVEESGSSATESKASETQTTTNNVNTIDETQSYSATSTEQPSQSTQVTTEEAPKTVQAPKVETSRVDLPSEKVADKETTGTQVDIAQPSNVSEIKPRMKRSTDVTAVAEKEVVEETKATGTDVTNKVEVEEGSEIVGHKQDTNVVNPHNAERVTLKYKWKFGEGIKAGDYFDFTLSDNVETHGISTLRKVPEIKSTDGQVMATGEIIGERKVRYTFKEYVQEKKDLTAELSLNLFIDPTTVTQKGNQNVEVKLGETTVSKIFNIQYLGGVRDNWGVTANGRIDTLNKVDGKFSHFAYMKPNNQSLSSVTVTGQVTKGNKPGVNNPTVKVYKHIGSDDLAESVYAKLDDVSKFEDVTDNMSLDFDTNGGYSLNFNNLDQSKNYVIKYEGYYDSNASNLEFQTHLFGYYNYYYTSNLTWKNGVAFYSNNAQGDGKDKLKEPIIEHSTPIELEFKSEPPVEKHELTGTIEESNDSKPIDFEYHTAVEGAEGHAEGTIETEEDSIHVDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEDSTKGIVTGAVSDHTTIEDTKEYTTESNLIELVDELPEEHGQAQGPIEEITENNHHISHSGLGTENGHGNYGVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNNGNQSFEEDTEKDKPKYEQGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPNYQFGGHNSVDFEEDTLPQVSGHNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPTEPGKPIPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVVPTKKAQSKKSELPETGGEESTNNGMLFGGLFSILGLALLRRNKKNHKA
Protein: separase (EC 3.4.22.49) (A0A1D8PCM0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein kinase
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- Rad21/Rec8-like protein N-terminal domain-containing protein
- Kleisin alpha
- Tyrosine-protein phosphatase CDC14
- Protein phosphatase PP2A regulatory subunit B
- Irr1p
- Protein kinase
- Pds5p
Sequence:
MDNSLDQKLLAFISSQSSSKPLSPSKSNNLPKADIKSLESLCVTSLDTLLNNIGGSTTNNSILPLDSLDAIEVRLRGLYLIYADDPRKSFDILRKHQLYIVKLFNIKQIDYVYQNLNVLLAQINKVFKIEFTSKSTIFTGIEFTDFNNWNDDTSFFNVNRKDITQLIIAFHFLVLQWIAQYVSKNLKSILMQKNQFISLDEFCNIPQMFLNSSNFRKWQLLPSNENIGKYNTNNVKLISGFIKVFQSIKVSSSLSKYVGLTNCLKLKLYELTKDESLLESIGFSSNLIPFINDANININEFIRKHVPIESEGSNELQTRLLKSPQLVTDSDFLRNLQNDSQLSVDKCQIIISSFNGFKDNLKTLSNQQLSILDLITIHLKDSLDESVVPILSQSFQIYSHFKLMKRMRNISNLLFNLGNKVHNEIYRNLAIDYECAIFEISPNNDNFKQLYNKLTRTQVTGSVLGNVLQCFETYISLKNNKDDPINGTIIQFICKTLSQTSNFASLNNIKNENLKYDIVNDIFQFMEKSNNTAEKTKICNSIIESTSWCNQLIECKIYYQYYNVNGLEKYLDLEEKSCDNQLVTSGIQFQRLVTFGWNETLLVECLNNLKYGLNYNSSEFDLFELNIIKQVLLYIKYNGMIDELVDIIEISLAKSIKDEQFEKFLKFEYCRALLSQTNNNPTNDVKFSQIFLDLKKRSQNWKSFDDIIQLSLLQLQYCIYVKNSTKAKDRFNGILQTLLKKPQFNISKSKNLPIVSKLQNFLILGKFQLLACHVNNHIIHNKIEAFNNIKTGIQLLYSIVKKLPTNINKTLWQELNWEITRLLFDSYKLAIDLSIDIGISRDIPLFLNEWVKLNNSIDNDVPIVNCINEFEIGRYGLLSNNEFQKYIRIAQGRLGYSLVKNNSAVQQYINRDRDDEICGHASSSRQLKSLVRTIFNSDNSLSELSKSVQLLPCIIGDSSTMCSKELLDKLVQLKNEILTEVTNYEKSSSLSLNQQQQLINNLNQVVCLLSSLTLFKGDGLLSEIYYLQDYVRNLPFANERKLMDSSKQDESNNLLPHALDFNQVVEDPSNNTINNSMIDFNVDLQLYLPHNWILVTLDICQNTGDLLISKLTKGSPNPFFMRLPLSRFPSSLGFQQLMQNFEKIIDDSNLSTKRKTTSKILTVEDRKQWWRSRFTLDFQLQDILHHVESKWFGGFISGIFTNDNDVENESKNVFHKFKQDLMKILKDCLTVSDDKSNIERFLQFNEFIYYCFYSMEEYNYELVDDLIKFITINMNSHGRIVNFGTNVKINKLHELIKNLIDKVNKNKQNVTSNNKNNSNNNSNNNNNSNNNSNSNNSQHIVLIPNANCSNFPWESMEFLRSKSISRMPSIHMLLDLVKSNTNNKNKLMFVDKSNLYYLINPSGDLIRSENRFKKLFESNHLWRGEIGKLSSNEHEDYQDSILCEILKSHLFVYIGHGGCDQYIKVSKLFKKCGNNQDSSNKLPPSLLLGCSSVKLDNCNYNYNSSMLQPSGNIYNWLNCKSSMILGNLWDVTDKDIDIFTLSLLQKWGLIDDYNGSGHDYGMKKLDLTNCVVQSRSKCTLKYLNGSAPVVYGLPMYLK
Protein: Alpha-2Da adrenergic receptor (Alpha-2Da adrenoceptor) (Alpha(2Da)AR) (Alpha-2Da adrenoreceptor) (Q8JG70)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The order of potency for this receptor is dexmedetomidine > norepinephrine > epinephrine > oxymetazoline.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSVTPTANSTEEAANITASPRLWPYTEPASAIIILVVSLIILLTIVGNVLVIVAVLTSRALRAPQNLFLVSLACADILVATLVIPFSLANEIMGYWYFGSTWCAFYLALDVLFCTSSIVHLCAISLDRYWSVTKAVRYNLKRTPRRIKCMIAVVWLISAVISFPPLIMTKHDEKECLINDETWYILSSCAVSFFAPGLIMITVYCKIYRVAKQRSSTVFVAKNGLERQPSQSETCFVRKDKFEKESPSSNSSESAQRQEELDDIDLEESAASDSRARGSRFSKRRRVEGERRGPQRSCRVSWAAHQEPGSRQQQLASKSKVAQMREKRFTFVLAVVMGVFVLCWFPFFFTYSLQAVCGERCGPPEALFKLFFWIGYCNSSVNPIIYTIFNRDFRKAFKKVVCWSAQRT
Protein: DNA-directed RNA polymerase subunit beta'' (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta'') (RNA polymerase subunit beta'') (P56764)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01324}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- ATP synthase subunit b, chloroplastic
- Photosystem I assembly protein Ycf3
- Large ribosomal subunit protein uL2cz/uL2cy
- Protein TIC 214
- Small ribosomal subunit protein bS16cz
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS14c
Sequence:
MAERANLVFHNKVIDGTAIKRLISRLIDHFGMAYTSHILDQVKTLGFQQATATSISLGIDDLLTIPSKGWLVQDAEQQSWILEKHHHYGNVHAVEKLRQSIEIWYATSEYLRQEMNPNFRMTDPFNPVHMMSFSGARGNASQVHQLVGMRGLMSDPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTSDAGYLTRRLVEVVQHIVVRRTDCGTIRGISVSPRNKNRMMSERIFIQTLIGRVLADDIYIGSRCVAFRNQDLGIGLVNRLITFGTQSISIRTPFTCRSTSWICRLCYGRSPTHGDLVELGEAVGIIAGQSIGEPGTQLTLRTFHTGGVFTGGTAEHVRAPYNGKIKFNEDLVHPTRTRHGHPAFLCYIDLSVIIESEDIIHSVTIPPKSFLLVQNDQYVESEQVIAEIREGTYTFHFKERVRKYIYSDSEGEMHWSTDVSHAPEFTYSNVHLLPKTSHLWILSGGSCGSSLIRFSIHKDQDQMNIPFLSAERKSISSLSVNNDQVSQKFFSSDFADPKKLGIYDYSELNGNLGTSHYNLIYSAIFHENSDLLAKRRRNRFLIPFQSIQEQEKEFIPQSGISVEIPINGIFRRNSIFAFFDDPRYRRKSSGILKYGTLKADSIIQKEDMIEYRGVQKIKTKYEMKVDRFFFIPEEVHILPESSAIMVQNYSIIGVDTRLTLNIRSQVGGLIRVEKKKKRIELKIFSGDIHFPDKTDKISRHSGILIPPGRGKKNSKESKKFKNWIYVQRITPTKKKFFVLVRPVATYEIADSINLATLFPQDLFREKDNIQLRVFNYILYGNGKPTRGISDTSIQLVRTCLVLNWDKNSSLEEVRAFFVEVSTKGLIQDFIRIGLVKSHISYIRKRNNSPDSGLISADHMNPFYSISPKSGILQQSLRQNHGTIRMFLNRNKESQSLLILSSSNCFRMGPFNHVKHHNVINQSIKKNTLITIKNSSGPLGTATPISNFYSFLPLLTYNQISLIKYFQLDNLKYIFQKINSYLIDENGIILNLDPYSNVVLNPFKLNWYFLHQNYHHNYCEETSTIISLGQFFCENVCIAKKEPHLKSGQVLIVQRDSAVIRSAKPYLATPGAKVHGHYSEILYEGDTLVTFIYEKSRSGDITQGLPKVEQVLEVRSIDSISLNLEKRIKGWNKCITRILGIPWGFLIGAELTIVQSRISLVNKIQKVYRSQGVQIHNRHIEIIVRQITSKVLVSEEGMSNVFLPGELIGLLRAERTGRALEEAICYRAVLLGITRASLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGVIPAGTGFNKGLVHCSRQHTNIILEKKTKNLALFEGDMRDILFYHREFCDSSISKSDFSRI
Protein: Glycoside hydrolase 131 catalytic N-terminal domain-containing protein (Q5AVT2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MKSTSILPLLSTLTPLASAATVWSGLFNESYTVADFDKWSWSSQIPPYQWYIHGSEETAHYLSLSSEYKNPNSTLDEAQGLKTTLDNTASWNGQTMMRTELIPQVESGVDIGSGKKYYHFSLSVDEDGLPNVELEHQIAFFESHFTELKYGGSSDTASSLTFYANSAAQWSTALEAGVWYNFAYGIDFDGGSVELYTSTGADDLELAVQAVSASASSNSQDWHVGVLRLDNGVDGGEESWYWSGVYVEDGEVTLAV
Protein: Histone H4 (Q59VN4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone H3.1/H3.2
- Histone acetyltransferase type B catalytic subunit
- Histone H2B.1
- Histone H3.3
- Histone H2A.1
- Histone chaperone ASF1
- Histone H2A.Z
- Histone H2A.2
- Histone H2B.2
- Protein-arginine omega-N methyltransferase
Sequence:
MSGTGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALIYEEVRVVLKQFLENVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG
Protein: Probable lipoamide acyltransferase (Q9HIA5)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Interaction partners:
- Probable 3-methyl-2-oxobutanoate dehydrogenase alpha chain
- Dihydrolipoamide dehydrogenase component
- Dihydrolipoyl dehydrogenase
- Probable 3-methyl-2-oxobutanoate dehydrogenase chain E1-beta
- Probable succinyl-CoA synthetase, beta subunit
- Succinate--CoA ligase subunit alpha
- Probable glycine cleavage system H protein
- Mercuric reductase
- Citrate synthase
- Citrate synthase
Sequence:
MYEFKLPDIGEGVTEGEIVRWDVKEGDMVEKDQDLVEVMTDKVTVKIPSPVRGKIVKILYREGQVVPVGSTLLQIDTGEEAPVQQPAGRAESTVQVAEVKQVPLPEVSGHVLASPAVRRIARENGIDLSKVGGTGEGGRVTLDDLERYMKSPAPSPAPSAGKAEAVHTAPQIPAQKPAPGREEILEMHGLRRIIFDKMTKAKQIMPHFTVMEEVDVTSMVSILDSAKARNRKVTVTGFLARIVPSILKQYPYLNAIYDETRRVYILKKYYNIGIAVDTPDGLNVFVIKDADRKSMVEISAEISDKASRARENKLQLDEVQDSTFTITNVGTIGGIMSTPIINYPEVAILGVHRILEREGRKYMYLSLSCDHRLIDGAVATRFIVDLKKVIEDPNAIIYEI
Protein: Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (PTEN-like phosphatase) (Phosphoinositide lipid phosphatase) (Protein-tyrosine phosphatase mitochondrial 1) (EC 3.1.3.16, EC 3.1.3.48) (Q66GT5)
Organism: Mus musculus (Mouse)
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production (By similarity). Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues (By similarity). Probably involved in regulation of insulin secretion in pancreatic beta cells (By similarity). May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16039589}; Peripheral membrane protein {ECO:0000250|UniProtKB:P0C089}; Matrix side {ECO:0000250|UniProtKB:P0C089}.
Interaction partners:
- Phosphatidate cytidylyltransferase, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
Sequence:
MAASAWLEAGLARVLFYPTLLYTVFRGRVRGPAHRDWYHRIDHTVLLGALPLKNMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKKAGVEQLRLSTVDMTGVPTLANLHKGVQFALKYQALGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEVLKEFHKEITARAAKN