wanglab/gogpt-training-data huggingface dataset:
Protein: Protein GLUTAMINE DUMPER 1 (O81775)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable subunit of an amino acid transporter involved in the regulation of the amino acid metabolism. Stimulates amino acid export by activating nonselective amino acid facilitators. Required the interaction with the RING-type E3 ubiquitin-protein ligase LOG2 to fulfill its function. Plays a role in the Gln export at hydathodes, at xylem parenchyma into xylem sap and from mesophyll into leaf apoplasm. Acts upstream genes involved in the salicylic acid (SA) pathway and in the geminivirus-host interaction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15208395, ECO:0000269|PubMed:22291198, ECO:0000269|Ref.9}; Single-pass membrane protein {ECO:0000269|PubMed:15208395, ECO:0000269|PubMed:22291198, ECO:0000269|Ref.9}.
Interaction partners:
- Probable E3 ubiquitin-protein ligase LUL1
- Probable E3 ubiquitin-protein ligase LOG2
- WAT1-related protein At2g39510
- WAT1-related protein At1g25270
- WAT1-related protein At1g44800
- WAT1-related protein At1g09380
- WAT1-related protein At2g40900
- WAT1-related protein At4g01430
- WAT1-related protein At1g01070
- WAT1-related protein At1g70260
Sequence:
MRPLSVQSKFEDVATSTSVNHHGVTPQSPWHSPVPYLFGGLAAMLGLIAFALLILACSYWRLSSSGEEDGQNVDEEKESRSGDKAANGAYEEKFLVIMAGEDLPRYLATPAMKKCTCGGHEGKMVISQEESVAKEEEKMREGEEEKVKDTGETTTTSH
Protein: V-type proton ATPase subunit H (Q5XIL1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRCSEEKQEMLQTEGSQCAKTFINLMTHISKEQTVQYILTMVDDMLQENHQRVSIFFDYAKRSKSTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTISASDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKFGESVQDLRILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS
Protein: Adhesion G protein-coupled receptor A3 (G-protein coupled receptor 125) (S4X0Q8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Orphan receptor that acts as a critical modulator of planar cell polarity during gastrulation. Controls the localization of dishevelled.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23821037}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Adhesion G protein-coupled receptor G7, tandem duplicate 1.
Sequence:
MSVLCVLLLAFVLPLRGSSSAGSTECKTYDERSRSAGKSSPSGATLDRKVVCSNMEFRQVPSPDTFPNRTVSLILSNNKIQELLNGSFVGLSSLERLDIKNNIITHIEPGAFYGLFSLKRLDLSKNLIGCLHVDVFKGLTNLVKLNLSENKFSSLSQGIFDSLGSLKILEFDSPYLLCDCNLQWLVVWIKEKAIGVKETRCSFPRSLQGQLITTLRAETLTCDAPLELPSFQMTPSQHQIVFQGDSLPFQCMASFVDEDMQVLWYQDGKMVEPDATQGIYIEKSMVQNCSLIASALTISNIQPGFTGNWECRVRTSRGNNTRTVHIVVLESSAKYCLPDRVSNNKGEYRWPRTLAGITAYLPCKRQVTGAGIYSGSSAEDRRAWRRCDRGGQWAEDDYSRCEYMKDVTRVLYIINQMPLNLTNVVQTAQQLLAYTAEAPNFSDKVDVIFVAEMIEKIGKFAEKYKELGDVMVDISSNLLLADERVLWMAQREARACSRMVESLQRIALLRVSNGALAYSTNSPNIALEAHAIKASSFNGMTCTLFQKLSPERTVMAHHGEISPERQLSFKCNVTSNLSALALKNTIVEASLQLPPTLFSSLGSSGQAEEAVYKLHLLAFRNGKLFPPTGNSSILSDGSKRRSVVTPVMITKIEGFPLRDLLSPVNVTLRRFLQGSDAVPAFWNFSLQGGQGGWQSDGCRILHQDDNFTTVSCHSLNSYAVLMDLNRTGYNVFIFRPLHPVIYSTALVLVLCLLSVIVSYIYHHKSVRISKKCWHMLVNLCLHILLTCAVFVGGINQTYNASVCQAMGIVLHYSTLATALWSGVTARNIYKQVTRKAKRYEELDEPPPPPRPMLRFYLIGGGIPIIVCGITAAANIKNYGSQVNAPYCWMAWEPSLGAFYGPAAFIVFVDCMYFLSILIQLRRHPERRFELKEQSEEQQHLSVTEATEITPVHLESSPTAQPVPMSALENEHTFVSQLMGVAGSLTLYAALWVFGALAISQEHPADLVFACLFGALALGLGAFLVAHHCVNRQDMRRHWSQACCLIRRNYAVQVDSLLLPIAGSSGSVMTSRGNGEATKCPASSAESSCTNKSAPSLRNSTQGCKLTNLQVEAAQCKVVAPSTANGTAVLDNSLTEHSVDNEIKMHVAPIEIQYRPSSVNNNNLPGNANITGHPGRHHKNRSRAHRASRLTVLREYSYDVPTSVEGSVQSVPNKRHHHESLHARNSRRAAYLAYRERQQSQLQQDSSDAASTSVPRRSRHFSKGTRIGNGFGHGISNGGLLDGSEADVTNQTKECPKQTLTVELEVQPKSYGLNLACQNGSAKDSERLNVESSGNVKTGLWKHETTV
Protein: Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART) (A0A0H2UMT9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKKIAVFASGNGSNFQVIAEEFPVEFVFSDHRDAYVLERAKQLGVLSYAFELKEFESKADYEAALVELLEEHQIDLVCLAGYMKIVGPTLLSAYEGRIVNIHPAYLPEFPGAHGIEDAWNAGVGQSGVTIHWVDSGVDTGQVIKQVRVPRLADDTIDRFEARIHEAEYRLYPEVVKALFTD
Protein: DeHydrogenases, Short chain (P90781)
Organism: Caenorhabditis elegans
Interaction partners:
- SLC41A/MgtE integral membrane domain-containing protein
- Nuclear receptor domain-containing protein
- NADP-dependent oxidoreductase domain-containing protein
- NADP-dependent oxidoreductase domain-containing protein
- Serine carboxypeptidase ctsa-1.2
Sequence:
MSPKSVVVTGSNRGLGFGLVQQFLKDPNVQHVIATARDVDKATALKGICDPRLHILQLSLGSDESIANFAEKVSEIVGESGLTLLINNAAVMLPYVTKQKPDRKVVLDLFESNTIGPMMLTQSLVPLIIKASKRQEGDTLSVSRGAIINIASEFLGSISENTSGSGEYKAMAYRMTKCAVNQFTKTLSIDLKDDHILTAGICPGMVQTDMSKGKGQLTIEESSSQILAAFNKLGATHNGGYFRRDLSIIPY
Protein: Hemolysin E (Cytotoxin ClyA) (Silent hemolysin SheA) (Q8Z727)
Organism: Salmonella typhi
Function: Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells (By similarity).
Subcellular location: Secreted {ECO:0000250}. Periplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Exported from the cell by outer membrane vesicles. Also found in the periplasmic space (By similarity). {ECO:0000250}.
Interaction partners:
- Cytolethal distending toxin subunit B homolog
Sequence:
MTGIFAEQTVEVVKSAIETADGALDLYNKYLDQVIPWKTFDETIKELSRFKQEYSQEASVLVGDIKVLLMDSQDKYFEATQTVYEWCGVVTQLLSAYILLFDEYNEKKASAQKDILIRILDDGVKKLNEAQKSLLTSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDRIRKEAYAGAAAGIVAGPFGLIISYSIAAGVIEGKLIPELNNRLKTVQNFFTSLSATVKQANKDIDAAKLKLATEIAAIGEIKTETETTRFYVDYDDLMLSLLKGAAKKMINTCNEYQQRHGKKTLFEVPDV
Protein: 2-oxoglutarate dehydrogenase, mitochondrial (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1) (OGDC-E1) (Alpha-ketoglutarate dehydrogenase) (P81895)
Organism: Solanum tuberosum (Potato)
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:10510296}.
Interaction partners:
Sequence:
AQAAPVPRPVXLSKKTDSF
Protein: AT-rich interaction domain 1B (A0A1B0GVK1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPPQPPGSQSESSSHPALSQSPMPQERGFMAGTQRNPQMAQYGPQQTGPSMSPHPSPGGQMHAGISSFQQSNSSGTYGPQMSQYGPQGNYSRPPAYSGVPSASYSGPGPGMGISANNQMHGQGPSQPCGAVPLGRMPSAGMQNRPFPGNMSSMTPSSPGMSQQGGPGMGPPMPTVNRKAQEAAAAVMQAAANSAQSRQGSFPGMNQSGLMASSSPYSQPMNNSSSLMNTQAPPYSMAPAMVNSSAASVGLADMMSPGESKLPLPLKADGKEEGTPQPESKSKDSYSSQGISQPPTPGNLPVPSPMSPSSASISSFHGDESDSISSPGWPKTPSSPKSSSSTTTGEKITKVYELGNEPERKLWVDRYLTFMEERGSPVSSLPAVGKKPLDLFRLYVCVKEIGGLAQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQYLFAFECKIERGEEPPPEVFSTGDTKKQPKLQPPSPANSGSLQGPQTPQSTGSNSMAEVPGDLKPPTPASTPHGQMTPMQGGRSSTISVHDPFSDVSDSSFPKRNSMTPNAPYQQGMSMPDVMGRMPYEPNKDPFGGMRKVPGSSEPFMTQGQMPNSSMQDMYNQSPSGAMSNLGMGQRQQFPYGASYDRRHEPYGQQYPGQGPPSGQPPYGGHQPGLYPQQPNYKRHMDGMYGPPAKRHEGDMYNMQYSSQQQEMYNQYGGSYSGPDRRPIQGQYPYPYSRERMQGPGQIQTHGIPPQMMGGPLQSSSSEGPQQNMWAARNDMPYPYQNRQGPGGPTQAPPYPGMNRTDDMMVPDQRINHESQWPSHVSQRQPYMSSSASMQPITRPPQPSYQTPPSLPNHISRAPSPASFQRSLENRMSPSKSPFLPSMKMQKVMPTVPTSQVTGPPPQPPPIRREITFPPGSVEASQPVLKQRRKITSKDIVTPEAWRVMMSLKSGLLAESTWALDTINILLYDDSTVATFNLSQLSGFLELLVEYFRKCLIDIFGILMEYEVGDPSQKALDHNAARKDDSQSLADDSGKEEEDAECIDDDEEDEEDEEEDSEKTESDEKSSIALTAPDAAADPKEKPKQASKFDKLPIKIVKKNNLFVVDRSDKLGRVQEFNSGLLHWQLGGGDTTEHIQTHFESKMEIPPRRRPPPPLSSAGRKKEQEGKGDSEEQQEKSIIATIDDVLSARPGALPEDANPGPQTESSKFPFGIQQAKSHRNIKLLEDEPRSRDETPLCTIAHWQDSLAKRCICVSNIVRSLSFVPGNDAEMSKHPGLVLILGKLILLHHEHPERKRAPQTYEKEEDEDKGVACSKDEWWWDCLEVLRDNTLVTLANISGQLDLSAYTESICLPILDGLLHWMVCPSAEAQDPFPTVGPNSVLSPQRLVLETLCKLSIQDNNVDLILATPPFSRQEKFYATLVRYVGDRKNPVCREMSMALLSNLAQGDALAARAIAVQKGSIGNLISFLEDGVTMAQYQQSQHNLMHMQPPPLEPPSVDMMCRAAKALLAMARVDENRSEFLLHEGRLLDISISAVLNSLVASVICDVLFQIGQL
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q38EW0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
MVRTTRFSRNSSKPLFQQLQLITSYGLFQEYPPIWSLPLPPQQPRDTGKPTLVLDIDETLIHTVGMRNEGSDSVSFSFFLRPHAKEFLAEVRELYEVVFWTAGTASYCSAVMDALEVQVLQLPRSFYNIDELRVEARGGISTKNVNFYALSRTQTLQGHNYMKYLPMLGRPLNRVIVIDSDVRSFPLHPRNGVKIEPFLPNERVLSEYARVVTDEVKYGQVGQRQYEGEMAKVIERGEEEVARLQADHALMDLIPMLRSAASSTDLTHELDHWRTDEYTKCDDFRETMNSLSVTRQKILGNVLKERRNVPIPPLKQHVMNHGFMEEANAAMKLEQMRHTPSRL
Protein: Putative nitroreductase HBN1 (EC 1.-.-.-) (Homologous to bacterial nitroreductases protein 1) (Q96VH4)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB11
- Transcription elongation factor SPT5
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MSAVATYLKTLTARRTIYALKPELPGEITINDIQSVVQTIIKETPTAFNSQPNRAVILTGETHKKVWDEVTKAIESPAGQKRPASARDEAFGSVIFFTDDKVTEKLKADFPAYAAAFPSFADHTSGAAQINSWVALEAMGLGGHLQHYNGYIKAALPSKIPESWTVQAQLVFGTPAAPPGEKTYIKNDVEIFN
Protein: Phycocyanobilin lyase subunit CpcS (EC 4.-.-.-) (A8HTM2)
Organism: Picosynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Function: Attaches a phycocyanobilin (PCB) chromophore to 'Cys-82' of the C-phycocyanain beta subunit (PhcB) and the unique PCB that is attached to allophycocyanin alpha and beta subunits (ApcA and ApcB). In vitro, and probably also in vivo, chromophorylates ApcD and ApcF.
Interaction partners:
- Phycocyanobilin lyase CpcT
- C-phycocyanin subunit beta
- Phycocyanobilin lyase subunit alpha
- C-phycocyanin subunit alpha
- Allophycocyanin alpha subunit
- Allophycocyanin beta subunit
- Phycocyanobilin lyase subunit beta
- Allophycocyanin subunit beta-18
- Allophycocyanin subunit alpha-B
- Phycobilisome rod-core linker polypeptide CpcG
Sequence:
MQSFADAKEFFQYSAGQWQSRRVTHHLPFRRAESGGSNIQVETLEKDDPRIIEICQMHDMDASLSVGGSYVTWAGTMQWDKDDENHEGSTVFALIPDADNPRQGKLLRERGYAEIVPVAGEYHLDHEDGLVLTTEYETMTIYERFWFANPDLRLRTSTVKRFGGFNTTTFCMEERIQTSPVTATAAAETNPLYAISGW
Protein: LP12374p (Sterol regulatory element binding protein, isoform A) (Sterol regulatory element binding protein, isoform B) (Sterol regulatory element binding protein, isoform C) (Sterol regulatory element binding protein, isoform D) (Q9VW37)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Membrane-bound transcription factor site-2 protease
- Niemann-Pick type C-1a, isoform A
- Mediator of RNA polymerase II transcription subunit 15
- Sterol regulatory element-binding protein cleavage-activating protein
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Importin subunit beta
- Fatty acid synthase
- Membrane-bound transcription factor site-1 protease
- NPC intracellular cholesterol transporter 1 homolog 1b
- FI24210p1
Sequence:
MDTTLMNLIDAPLDESMDLFKAEDVFEPFDADLHSDMLDIILNDMDLAPTQMYNMLLDEPRTHTQQTQSVDQQPQSVEQQPHVKSEHSSPVHIKEELHQQQQQSPLLVYKPDPLIATSYNCPQQQPTGLLKAAQPTATIHHMDAQRMPPNTAVYPPSLGSSFVYQSMSPPTSPVESANQNVNVMQPVAATPAPASAPLPQQSYPQPFITYNSKAGMTSDEAMYFLLQPTVASPTPSPPVAPPPTSTGSRASKVRVAPLAPSPAAMEVQGKVPINRVQPKVKEVKRSAHNAIERRYRTSINDKINELKNLVVGEQAKLNKSAVLRKSIDKIRDLQRQNHDLKAELQRLQRELMARDGSKVKDLLQLGTRPGRASKKRRESSQTFTTDAGLTPPRSDESDPSLSPMHSDISLPPSPYGGSTASCSSGSSSSNEEPLVVPSSMRGMATHSRLGLCMFMFAILAVNPFKTFLQRGHYDSNDDLGDMSGQRRILSYDVEGEGFAVWQQSSWIWLLNFTLMLGCLVKLLVYGDPQLDAQTDAYCQHRQRADFYFSQGQSSQAYAGYLNCLHMFGLSLPASRLECYLQTTWQFLRFLFHRLWLGRVLSRRSGGLFSNAASRKQALASARELALLFNRLNQLQLTGNGSRGDMNGIMMALFASNMAEVAHNLLTPRETICIHVMTALRMKRSAPKWLQQLFARYYMSRARQECGLTRATEQTQELRWAFTAYGYRYCATHVFTYDLSDSGEQDGFFTRLRNPCDPAAHVIKQYREHLLFKAIQCLVGAGHKSGGLPTSSVSGEAEQLQQQQHSGTIVSNVLKYTSLLKDTLWADEDERDTNVVWWADVLETAVHWLLGEDTLAEQLYGRIKQMPTQLQQCGENDHLPKALHAVLRAKMILLKNNGNALDKSLKQLVNILCDESSVELQECLTVNRITDAKGIKLLFQLLTCDWLLETRTALWELEHMNMEDDGFYQVPGEVLEKFQTDLNSLRNIVENIPNAQSRIYLYEAVCRLMAGASPCPTQQLLDRSLRSRNAHSSIFCGSKDRRQQNFVGGERERASAMYVACKYLPPALLSSPGERAGMLAEAAKTLEKVGDKRKLKECYQLMKSLGNGIGSVKA
Protein: Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) (Protein M46) [Cleaved into: Ghrelin; Obestatin] (Q9EQX0)
Organism: Mus musculus (Mouse)
Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation.
Subcellular location: Secreted {ECO:0000269|PubMed:10930375}.
Interaction partners:
- Growth hormone secretagogue receptor type 1
- Leptin
- Membrane-bound ghrelin O-acyltransferase MBOAT4
- Insulin-2
- Pro-glucagon
- Pro-neuropeptide Y
- Agouti-related protein
- Peptide YY
- G-protein coupled receptor 39
- Cholecystokinin
Sequence:
MLSSGTICSLLLLSMLWMDMAMAGSSFLSPEHQKAQQRKESKKPPAKLQPRALEGWLHPEDRGQAEETEEELEIRFNAPFDVGIKLSGAQYQQHGRALGKFLQDILWEEVKEAPADK
Protein: ATP-binding cassette sub-family C member 10 (EC 7.6.2.2) (EC 7.6.2.3) (Multidrug resistance-associated protein 7) (Q5T3U5)
Organism: Homo sapiens (Human)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Lipophilic anion transporter that mediates ATP-dependent transport of glucuronide conjugates such as estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Mediates multidrug resistance (MDR) in cancer cells by preventing the intracellular accumulation of certain antitumor drugs, such as, docetaxel and paclitaxel. Does not transport glycocholic acid, taurocholic acid, MTX, folic acid, cAMP, or cGMP.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12566991, ECO:0000269|PubMed:15256465}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:12566991, ECO:0000269|PubMed:15256465}. Basolateral cell membrane {ECO:0000269|PubMed:23087055}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the basal membrane of Sertoli cells. {ECO:0000269|PubMed:35307651}.
Interaction partners:
Sequence:
MERLLAQLCGSSAAWPLPLWEGDTTGHCFTQLVLSALPHALLAVLSACYLGTPRSPDYILPCSPGWRLRLAASFLLSVFPLLDLLPVALPPGAGPGPIGLEVLAGCVAAVAWISHSLALWVLAHSPHGHSRGPLALALVALLPAPALVLTVLWHCQRGTLLPPLLPGPMARLCLLILQLAALLAYALGWAAPGGPREPWAQEPLLPEDQEPEVAEDGESWLSRFSYAWLAPLLARGACGELRQPQDICRLPHRLQPTYLARVFQAHWQEGARLWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTVLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGRLLQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMGLFSPQLLLFSPGNLYIPVFPLPKAAPNGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQEPQGQPLQLGTGWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQPHSLFQQLLQSSQQGVPASLGGP
Protein: T-box transcription factor T (Brachyury protein) (Protein T) (P20293)
Organism: Mus musculus (Mouse)
Function: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence and activates gene transcription when bound to such a site.
Subcellular location: Nucleus {ECO:0000269|PubMed:7588606}.
Interaction partners:
- Eomesodermin homolog
- Bone morphogenetic protein 4
- Homeobox protein MIXL1
- Homeobox protein notochord
- Zinc finger protein SNAI1
- T-box transcription factor TBX6
- Hepatocyte nuclear factor 3-beta
- Delta-like protein 1
Sequence:
MSSPGTESAGKSLQYRVDHLLSAVESELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVTADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERNDHKDVMEEPGDCQQPGYSQWGWLVPGAGTLCPPASSHPQFGGSLSLPSTHGCERYPALRNHRSSPYPSPYAHRNSSPTYADNSSACLSMLQSHDNWSSLGVPGHTSMLPVSHNASPPTGSSQYPSLWSVSNGTITPGSQTAGVSNGLGAQFFRGSPAHYTPLTHTVSAATSSSSGSPMYEGAATVTDISDSQYDTAQSLLIASWTPVSPPSM
Protein: Glutaredoxin-2 (Q9UTI2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase. Thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions. It transfers reducing equivalents to cytosolic protein and nonprotein disulfides (By similarity).
Interaction partners:
- Probable peptide methionine sulfoxide reductase
- Monothiol glutaredoxin-5
- Thioredoxin-1
- Monothiol glutaredoxin-4
- Glutathione reductase
- Thioredoxin reductase
- Ribonucleoside-diphosphate reductase large chain
- Iron-sulfur assembly protein 1
Sequence:
MTSIAKAFVEKAISNNPVTVFSKSFCPFCKAAKNTLTKYSAPYKAYELDKIENGSDIQAYLHEKTKQSTVPSIFFRNQFIGGNSDLNKLRSSGTLTKMIAELKENKSSIL
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9VFC4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Isopeptidase-T-3, isoform C
- BcDNA.GH11023
- EG:152A3.3 protein
Sequence:
MSISKLFVKVFNEDIFEQVDHDNLYSDLDDDLEGANCSTVPDPRPAKLADLSVTKQMLIVRTWLDDKFQQIQTDSNEEIRRLYMETESRIGPDLTIFDVDYTTTVRVSSDRLALRSQGSFNTVRANCCVYGGRWMYEIHLHTKGVMQIGWASNSCQFNENSGVGDTKSSYGYDGSKQQIWHISTKKYGDKWQIGDVIGVTIDVDKEVIEYYRNGRSMGVAFNKLEKGPGISFFAAISLGYTQGIEANFGNRPFMYPVSGFQPLMARPILKLQRANLLMNYLVNLAGIFSKYNAQSGMAPTNGADARVSTKKTVYCIFATLLIEKFTNEIFDPYIIEDVLLRKISSMTNLASEKENSYSVLHGLLSLFWNYMEGDEIKFVLRKLVNALLGTFTHTIQGLDYEKHRQALGMLHCLCLHEQTRKYLLEGKLFKKHCLAFFLYIHPLEFYIMEELLPDSMAWTEGIDGPKEKYLNVVEKVRKVTEPLYTAQKDLLCTLMINSDGSRESPSSRSIFLSKLRRYVIDLSMEQRPFHAFFFMQSSIQHPLDAPVALAFASILIDQTRSMFKDEMPTKNVEVNSDYFIDGTFDYMHFDRVGGVLSHLRKVHRGDIDARLGSARTQQIYEDDRQNLRVNEVDTTLYLLGENINNVPVVGHTQGANNTTYTHFLNTRPNSSTDSSPGNADMEASLCELLDLCIIFYYSAGHKYIVKIATVRDEIAALNEVLKETKFYREDIERKLGALEQHANVCMNENHQHVMGELRSKFSQRQNVFATRSIALARKQVWLRGVALNNHRRSLLIWLLERMLRTLTTASNTGSLFSFVPEVYVNTLPILLDAVMDFSHHDLKAQFEASDAECSVNAAAEFLGIHSADPRIVLASCKDSLLQALGTLTCHKSGVRALERTSKRSQASLVRALLRPYENRAWGQSNWLLLRFWMGEGYAYKDSRQPSVWQGGSLPLHQGLCRSRSRNETHTGLLHNVAPANPSKHFQRLIGAKLLEDEPFATAFLNSVLSQLNWAFSEFILLLQEIQNTAQRQENTLFEPKQLKICSMCFELTVSLMRCLEMVITTAPEIVTDESRPNSDLLLNRICQLISQVLSRVTVPPGCFQFVVDMCSADLNAVTHYPIVTAALGILLALMQEEMESDLRPQIVTRVSRAFLTDPSFQFATLEFALGEIRTPLLEQKNIPRGNFDPSSRPHIDPLTNDVRVPLPNNSKRIRADPPILKFALNDFPSHVSSEEIDNVRRLIDSLRVKQTLLSDITLPSEDSLCPICCAKPITAVFTPCKHQSCSDCIMQHMMNSKVCFYCKTTIQTIETLDGTVIFSNDDVVQTPMIERA
Protein: Negative elongation factor complex member E (E9PD43)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESDRLRELGPDGEEAEGPGAGDGPPRSFDWGYEERSGAHSSASPPRSRSRDRSHERNRDRDRDRERDRDRDRDRDRERDRDRDRDRDRDRERDRDRERDRDRDREGPFRRSDSFPERRAPRKGNTLY
Protein: F-box and leucine-rich repeat protein 19 S homeolog (Q63ZQ7)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MKKFGGPGRMKQSCLKRQCTAPVLPHTAVCLLCGDAGKEDTAQEEEQKFNLSLMECTICNEIVHPGCIKMGKSEAVINTEIPNCWECPKCKREGRTSKDSLDSSGKRRLDNGEDAVRWKLTDDPAPGKKKSSDENAGHKRKKEQGPQSETGVKKKVKAEKDKKVKKIEPPVPADPVPPPDRSHQREKIERFKQMCQMLERARSSTSSSSSDSDSDSDSKGSRGSSDTGGDGGESRISFSTSSEEEEEEGGTGDGRNGTRNGKPKPPRANWREKENRRGSGVGNNRKGITGRNTGQAISRTQLLKRPLVPSPPKPAPPQLERHVVRPPPHSPEPDSLPLDGGTDHVMQRGVWLSVFRHLGQKELCVCMRVCRTWNRWCCDRRLWTSIDLSRRKSITPPMLSGIVRRQPIRLDLSWTNISEKQLTWLIHRLQGLKELLVCGCTWSAVSSLCTASFPCLSLLDLGWVQGMKTSHLRELLSPPSSDCRTVVPDPRGRLPSLSELRLCGLEIGDSALRLLLRHTPRLHRLDLSHCVQLTDHGIHILTAASTLRDSLTHLNLTGCHRLTDQSLAFFKRCPHLQLVDPPLSRSAPHVRGEPGAKSFVDDLILGQGFVRSRAATSLR
Protein: DASH complex subunit DAD2 (DUO1 and DAM1-interacting protein 2) (Helper of ASK1 protein 1) (Outer kinetochore protein DAD2) (P36162)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095}. Chromosome {ECO:0000269|PubMed:36701236}. Note=Associates with the mitotic spindle and the kinetochore (PubMed:14562095). Associates with origin of replication (ORI) sites during interphase (PubMed:36701236). {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:36701236}.
Interaction partners:
- DASH complex subunit ASK1
- DASH complex subunit SPC34
- DASH complex subunit DUO1
- DASH complex subunit DAD4
- DASH complex subunit DAM1
- DASH complex subunit DAD3
- DASH complex subunit DAD1
- DASH complex subunit SPC19
- DASH complex subunit HSK3
- Inner kinetochore subunit CHL4
Sequence:
MDSIDEQIAIKRKELQSLQKITSLTDGLKIQLTELNEQIKEMGMNADSVAQLMNNWDSIINNISQASLGLLQYAEGDYEIGPWKDSKKKESEQSNETGLEAQENDKNDEDNDEDEDLVPLPETMVRIRVDGNE