wanglab/gogpt-training-data huggingface dataset:
Protein: Anion exchange protein 3 (AE 3) (Anion exchanger 3) (Band 3-related protein 3) (B3RP-3) (Neuronal band 3-like protein) (Solute carrier family 4 member 3) (P23348)
Organism: Rattus norvegicus (Rat)
Function: Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10548554}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium-independent sulfate anion transporter
Sequence:
MANGVIPPPGGPSPLPQVRVPLEEPPLGPDVEEEDDDLGKTLAVSRFGDLISKTPAWDPEKPSRSYSERDFEFHRHTSHHTHHPLSARLPPPHKLRRLPPTSARHARRKRKKEKTSAPPSEGTPPIQEEGGAGAEEEEEEEEEEEGESEAEPVEPPPPGPPQKAKFSIGSDEDDSPGLSIKAPCAKALPSVGLPSDQSPQRSGSSPSPRARASRISTEKSRPWSPSASYDLRERLCPGSALGNPGPEQRVPTDEAEAQMLGSADLDDMKSHRLEDNPGVRRHLVKKPSRIQGGRGSPSGLAPILRRKKKKKKLDRRPHEVFVELNELMLDRSQEPHWRETARWIKFEEDVEEETERWGKPHVASLSFRSLLELRRTIAQGAALLDLEQTTLPGIAHLVVETMIVSDQIRPEDRASVLRTLLLKHSHPNDDKDSGFFPRNPSSSSVNSVLGNHHPTPSHGPDGAVPTMADDLGEPAPLWPHDPDAKEKPLHMPGGDGHRGKSLKLLEKIPEDAEATVVLVGSVPFLEQPAAAFVRLSEAVLLESVLEVPVPVRFLFVMLGPSHTSTDYHELGRSIATLMSDKLFHEAAYQADDRQDLLGAISEFLDGSIVIPPSEVEGRDLLRSVAAFQRELLRKRREREQTKVEMTTRGGYVAPGKELSLEMGGSEATSEDDPLQRTGSVFGGLVRDVKRRYPHYPSDLRDALHSQCVAAVLFIYFAALSPAITFGGLLGEKTEGLMGVSELIVSTAVLGVLFSLLGAQPLLVVGFSGPLLVFEEAFFKFCRAQDLEYLTGRVWVGLWLVVFVLALVAAEGSFLVRYISPFTQEIFAFLISLIFIYETFHKLYKVFTEHPLLPFYPPEEALEPGLELNSSALPPTEGPPGPRNQPNTALLSLILMLGTFLIAFFLRKFRNSRFLGGKARRVIGDFGIPISILVMVLVDYSITDTYTQKLTVPTGLSVTSPHKRTWFIPPLGSARPFPPWMMVAAAVPALLVLILIFMETQITALIVSQKARRLLKGSGFHLDLLLIGSLGGLCGLFGLPWLTAATVRSVTHVNALTVMRTAIAPGDKPQIQEVREQRVTGVLIASLVGLSIVMGAVLRRIPLAVLFGIFLYMGVTSLSGIQLSQRLLLIFMPAKHHPEQPYVTKVKTWRMHLFTFIQLGCIALLWVVKSTVASLAFPFLLLLTVPLRRCLLPRLFQDRELQALDSEDAEPNFDEDGQDEYNELHMPV
Protein: TLE family member 3, transcriptional corepressor (H0YL70)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYPQGRHPAPHQPGQPGFKFTVAESCDRIKDEFQFLQAQYHSLKVEYDKLANEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTILAQIMPFLSQEHQQQVAQAVERAKQVTMTELNAIIGVRGLPNLPLTQQQLQAQHLSHATHGPPVQLPPHPSGLQPPGIPPVTGSSSGLLALGALGSQAHLTVKDEKNHHELDHRERESSANNSVSPSESLRASEKHRGSADYSMEAKKRKAEEKDSLSRYDSDGDKSDDLVVDVSNEDPATPRVSPAHSPPENGLDKARSLKKDAPTSPASVASSSSTPSSKTKDLGHNDKSSTPGLKSNTPTPRNDAPTPGTSTTPGLRSMPGKPPGMDPIGIMASALRTPISITSSYAAPFAMMSHHEMNGSLTSPGAYAGLHNIPPQMSAAAAAAAAAYGRSPMVSFGAVGFDPHPPMRATGLPSSLASIPGGKPAYSFHVSADGQMQPVPFPHDALAGPGIPRHARQINTLSHGEVVCAVTISNPTRHVYTGGKGCVKIWDISQPGSKSPISQLDCLNRDNYIRSCKLLPDGRTLIVGGEASTLTIWDLASPTPRIKAELTSSAPACYALAISPDAKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISHDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHHTKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISADDKYIVTGSGDKKATVYEVIY
Protein: SNARE protein, putative (Q8IKY7)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
Sequence:
MSDIYFYSEEINNLLEDFKRILQELEKEEVKNEKTEKYCNDIHFINERIKTAKDAYFIEIRNLSEEEQIENISKIKNKMIILENLNIQFDFKKSKLIYEEDKQAKENKKLLKVRYVSAKDIETKGDIIQDQTDDAIFRMKMMVDESENITKDAADKLNIQNEKLQKARDKIEDVDINVYSAKQTLKEIAKEAVTDRFVRLMSILIFIVVSVLITVIIISRKQTPVVIHDVMTENEHIRKNKSVRRQEMSPKLT
Protein: Defective proboscis extension response 19, isoform A (Defective proboscis extension response 19, isoform B) (Defective proboscis extension response 19, isoform C) (LP09705p) (Q9VKX8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein epsilon
Sequence:
MEPKRWHLHLSCFLLLLSSTFSDVGKITSSQNHFGNTLQSQFNTKNNTRVIAQKGGLAILPCVVKVNSPATVSWIRRKDFQLLTVGLSTHSSDKRFLVEHTRHMGHWSLRIKAVREEDRGFYECQLSIYPTQSIVIELKIVEAVAEISSAPELHIDETSTLRLECKLKRATENPAFVFWYHDSKMINYDSQGGFVVTSIGQSNPQSGQFYRSSPANKSRATMPMESSNGVLNSLLGSSDAIKAPAANVPSSTPYMTQQHQSAYLLNPSVSVLTVKQVNFRHAGNYTCAPSNARPASITVHVLRGEKTAAMQHANRSILDTETNGNGTFGLITLGGLNGTSGVTLAGGILYFSGLFLLMGAVVFDRFSLAATHKVFVAFIIVTMHS
Protein: TATA-box binding protein associated factor 4 (E9QAP7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 1
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPELRAAAAGALGNHVVSGSPAGAAGAGPAASAEGAPAAAPEPPPAGRARPAGGGPRRPGSSSPRRLLVPAGPAPAPAKLRPLPEASAGPCPAAAAAAAATAAAVAGPDPAAAAPPAGPGASKPGPPGPPGPGAAQTLNGSAAPPTAPHAAPAVSPVNNGPAPPPAAGSVIQAAPAPAAPSPPAAPAPAAPPPPAPPAPVAPARPPGHPAAPAPPVSPAAAAAAAAAAAAAQNGAAPAPAAASGGAAGLGQPGAGAQGAKAEAPKPGPGPGPGPAAAAAAAGVAGGGAAGSVLLGPAMPGALPGPAPGTPAGLAKGAAAATPSLPRTPAATTGAIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAHAQAQPQSTMAPRPATPTGAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPTTTLQRSPGVQPQLVLGGSAQPASLGTATAVQTGTPQRTVPGASTTSTAATETMENVKKCKSFLSTLIKLASSGKQSTETAANVKDLVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQQPPASQATTALTAVVLSSSVQRTAGKTAASVTSALQPPVISLTQPTQVGVGKQAPPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNQLQPVPVVKPTVLPGTKALSTVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDDTFLLPAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCTGPGSGAEGSGPGAAVPGGSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK
Protein: Taste receptor type 2 member 119 (T2R119) (Taste receptor type 2 member 1) (T2R1) (Taste receptor type 2 member 19) (T2R19) (Q9JKU1)
Organism: Rattus norvegicus (Rat)
Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MMEGHILFFFLVVMVQFVTGVLANGLIVVVHAIDLIMWKKMAPLDLLLFCLATSRIILQLCILFAQLCLFSLVRHTLFEDNITFVFIINELSLWFATWLGVFYCAKIATIPHPLFLWLKMRISRLVPWLILGSVLYVIITTFIHSRETSAILKPIFISLFPKNATQVGTGHATLLSVLVLGLTLPLFIFTVAVLLLIYSLWNYSRQMRTMVGTREYSGHAHISAMLSILSFLILYLSHYMVAVLISTQVLYLGSRTFVFCLLVIGMYPSIHSIVLILGNPKLKRNAKMFIVHCKCCHCTRAWVTSRSPRLSDLPVPPTHPSANKTSCSEACIMPS
Protein: General transcription factor II-I repeat domain-containing protein 1 (GTF2I repeat domain-containing protein 1) (General transcription factor III) (MusTRD1/BEN) (Muscle TFII-I repeat domain-containing protein 1) (Slow-muscle-fiber enhancer-binding protein) (USE B1-binding protein) (Williams-Beuren syndrome chromosomal region 11 protein) (Williams-Beuren syndrome chromosomal region 12 protein) (Q9UHL9)
Organism: Homo sapiens (Human)
Function: May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8 (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- General transcription factor II-I
- cGMP-dependent protein kinase 1
- CAP-Gly domain-containing linker protein 2
- cGMP-dependent protein kinase 2
- Peptidyl-prolyl cis-trans isomerase FKBP10
- Inactive peptidyl-prolyl cis-trans isomerase FKBP6
- Transducin beta-like protein 2
- Tyrosine-protein kinase BAZ1B
- LIM domain kinase 1
- E3 SUMO-protein ligase PIAS2
Sequence:
MALLGKRCDVPTNGCGPDRWNSAFTRKDEIITSLVSALDSMCSALSKLNAEVACVAVHDESAFVVGTEKGRMFLNARKELQSDFLRFCRGPPWKDPEAEHPKKVQRGEGGGRSLPRSSLEHGSDVYLLRKMVEEVFDVLYSEALGRASVVPLPYERLLREPGLLAVQGLPEGLAFRRPAEYDPKALMAILEHSHRIRFKLKRPLEDGGRDSKALVELNGVSLIPKGSRDCGLHGQAPKVPPQDLPPTATSSSMASFLYSTALPNHAIRELKQEAPSCPLAPSDLGLSRPMPEPKATGAQDFSDCCGQKPTGPGGPLIQNVHASKRILFSIVHDKSEKWDAFIKETEDINTLRECVQILFNSRYAEALGLDHMVPVPYRKIACDPEAVEIVGIPDKIPFKRPCTYGVPKLKRILEERHSIHFIIKRMFDERIFTGNKFTKDTTKLEPASPPEDTSAEVSRATVLDLAGNARSDKGSMSEDCGPGTSGELGGLRPIKIEPEDLDIIQVTVPDPSPTSEEMTDSMPGHLPSEDSGYGMEMLTDKGLSEDARPEERPVEDSHGDVIRPLRKQVELLFNTRYAKAIGISEPVKVPYSKFLMHPEELFVVGLPEGISLRRPNCFGIAKLRKILEASNSIQFVIKRPELLTEGVKEPIMDSQGTASSLGFSPPALPPERDSGDPLVDESLKRQGFQENYDARLSRIDIANTLREQVQDLFNKKYGEALGIKYPVQVPYKRIKSNPGSVIIEGLPPGIPFRKPCTFGSQNLERILAVADKIKFTVTRPFQGLIPKPDEDDANRLGEKVILREQVKELFNEKYGEALGLNRPVLVPYKLIRDSPDAVEVTGLPDDIPFRNPNTYDIHRLEKILKAREHVRMVIINQLQPFAEICNDAKVPAKDSSIPKRKRKRVSEGNSVSSSSSSSSSSSSNPDSVASANQISLVQWPMYMVDYAGLNVQLPGPLNY
Protein: Fatty acid conjugase FAC2 B (CoFac2) (EC 1.14.19.14) (CoFadX-1) (Q9FPP7)
Organism: Calendula officinalis (Pot marigold)
Function: Fatty acid conjugase converting 18:2(9Z, 12Z) to calendic acid 18:3(8E, 10E, 12Z). Converts alpha-linolenic acid (18:3(9Z, 12Z, 15Z)) into 18:4(8E, 10E, 12Z, 15Z). Also has weak activity on the mono-unsaturates 16:1(9Z) and 18:1(9Z) producing two conjugated double bonds at delta(8) and delta(10) position (By similarity).
Subcellular location: Microsome membrane {ECO:0000269|PubMed:11067856}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGKAASAKKVLERVPISKPPFEYNDLKKAVPPHCFSRPLSRSLYFLFHDIIVTCILFYVASNYIHMLPRFLSCIVWPVYWISQGVFLGRLWMIGHECGHHSFSNYRWVDDTVGFLIHTATLTPYFSFKYSHRNHHAHTNSMEYDEVHIPKRKSEALYFEFLGNNPIGLMITMLCKLTFGYAAYIMFNYTGKKHKSGGLASHFYPQSPLFNDSERNHVLFSDIGICIVLYACYRIVTVTGAMPAFYVYGIPWVIMSAILFAATYLQHTHPSIPHYDTTEWNWLRGALSTIDRDLGFFNMNKTHYHVIHHLFPVIPEYHAQEATEAIKPILGQYYKYDGTPFLKALWREMKECIYVESDEGQKKQGIYWFKNKT
Protein: Transketolase (TK) (EC 2.2.1.1) (P68) (P40142)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Triosephosphate isomerase
- Ribokinase
- Phosphoglucomutase-1
- Fructose-1,6-bisphosphatase 1
- Fructose-bisphosphate aldolase A
Sequence:
MEGYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSKKKILATPPQEDAPSVDIANIRMPTPPSYKVGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLVTKG
Protein: Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Glucosidase I) (A0A1D8PMH9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU368089}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU368089}.
Interaction partners:
- Glucosidase II subunit alpha
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycotransferase
- Calnexin
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit delta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
Sequence:
MRLLSWLPFVFLLEVIFASNQIKFDLYDNNELQSNNDTVDLATQYSQISNSSLLWGPYRSALYFGLRPRFPRSLLSGLMWFSINDYEGIGKIRHFYEQHDKMSKANWVSYDPRIGGRQIIDDDECHIKIIIDFVKSDDGLSWGVKIRAKPHKGFENIKTSFIWYSGLEGEQKVIEENGDETTSRTGFLKLENPKNVLGYEGNVKFAGVSEELGAFELEINDGPKTNVHPAGRTDVDPELDPRKAHHYSLTVPDDNVWRARDIFMTMLQESIQKLVEKFGGVEAIPPENLFILRDLQDFEGNLHFVQKVYQGSCEFDVVYNNALTPITERITFENLKFRIQNSLKAFDEKFNNHFELAPPFNSKKYKKFGKEVLSGLLGGLSYFYGDQLVDRETVFDEDSFESYKLEGTFEGPYELFTLVPSRPFFPRGFLWDEGFHLLPLLNYDSDLVLEITKSWFNLIDEDGWIAREQILGKESRSRVPAEFVVQSPQIVNPPTLTLVLTYLLDSVVGNYDTINEPKNVDESLSRENLGGFVLKNPEVLTNYTKQVYPKLKSHLDMFRRTQKGYVEEFDRGTNPEAYRWRGRTLTHCLASGLDDYPRALPADVAELNVDLISWIGIMTRSIRLMAEILNIDEDVETYKNLENDIIDNIEKLHWSPEDKTYCDVSVNDDDENIFVCFKGYISLFPFLTKLIPEANTDKLEHIINLISNPEELWTPYGIRSLSKADEFYKTGEDYWRSPIWIPINYLILDSIQDYYIRSKHHMSTNLQEKFAKTYHDLRINIVKNVFDQADKTGFVWEQYNDETGEAQRAKNFLGWSSLVLIMMTMPEHLQ
Protein: Histone deacetylase (EC 3.5.1.98) (C8V606)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037919}.
Interaction partners:
- Transcription factor
- Nucleoporin NSP1
- Response regulatory domain-containing protein
- sterol 14alpha-demethylase
- histone deacetylase
- leucine--tRNA ligase
- leucine--tRNA ligase
- GATA-type domain-containing protein
- Kinetochore protein
- Histone H2B
Sequence:
MVDDEDIIMGEAGYHSANPNTAIAAGQQTTHGHLNGRSDPYLAPPLLSQPMQMPVVQAGNSQTQESSATTDEARVLSPKIDLNSTVPADAADITPDYQDSLVDEYSDYAEESKEAPGLPLASLPSGLCYDVQMRYHCEVRPTSDVHPEDPRRIYYIYKELCRAGLVDDIESTRPLVARPLKRIHARNATEEEISLVHTAAHYAFVESTKDMSDEELIALEHTRDSIYFNNLTFASSLLSVGGAIETCLAVATRKVKNAIAVIRPPGHHAEHDKTMGFCLFNNVSVAARVCQQRLGLSCRKIMILDWDVHHGNGIQKAFYDDPNVLYISLHVYQNGSFYPGEKDGDADFCGAGAGEGKNVNIPWPSQGMGDGDYIYAFHQVVMPIAQEFDPDLVIIASGFDAAAGDTLGGCFVTPACYAHMTHMLMTLAQGKVAVCLEGGYNFRSISKSALAVTKTLMGNPPDRLSFTCPSEAAISTIRRVSSIQSDYWKCMYPKAIKNEGVWTDRLHDIIRAYQAKQLYDNYKLTSLYIYRTAISKSFENQVLARPEIMGLPHPLTNNLEAHNCWLADVMKDYVQWAVGKGYAVIDVNIPKHVTTEPSSGRFEEEDENRPTATEELAGYLWDNYIDPNEATEIFLVGIGNAFYGVANLLINRETLYQRVNGVISFVAKDPVRAVASHTQVWLSRWYRDNSLVFVSKAHGVWKSDRKATKRYGKLIQSSREGLSDMLMHHKDEVFQWIEDRIEPESEETEEEKPVKRSPTKAAPKAA
Protein: Clarin-2 (A0A2R8RY99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a key role to hearing function. Required for normal organization and maintenance of the stereocilia bundle.
Subcellular location: Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:B2RVW2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MPTLWKQIVFSFASILSIGSVVLLVVALSTERWVTGTTLCQTGVDLVNASRPELEQFTGHIYYGLFQGGKTRRCGLGIRRAKIYIFPKLIKKINSGLHMIIIFFLFTAIGFAVVSLAFCIYNARKVPYQSIKGPFGLYIWNFIAGKSIAMGFACFLAAIQCHKLTEHVANYSESLFTLVILEENLGFSFWLVVASAVTHGANILVVASSKIHLPKIQTKKPEEPTATGEDFLY
Protein: Copper transport protein CTR1 (Copper transporter 1) (P49573)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity copper transporter of plasma membrane that mediates copper uptake under low copper conditions. Copper transport through the high affinity system requiring CTRl supplies the iron transport multicopper ferroxidase FET3 with copper, which in turn is required for ferrous iron uptake. The energy for translocation is unlikely to be directly derived from ATP hydrolysis and the exact mechanism driving the transmembrane transport of copper has still to be determined. Binds 4 copper ions via its C-terminal cystein-rich domain and is able to deliver Cu(I) directly to both the chaperone ATX1 and to an N-terminal domain of the CCC2 protein. Also able to mediate the uptake of the anticancer drug cisplatin.
Subcellular location: Cell membrane {ECO:0000269|PubMed:8293472}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Copper transport protein CTR2
- Copper transport protein CTR3
- Putative uncharacterized protein YPR123C
- FKBP12-associated protein 1
- Histone H4
- Superoxide dismutase 1 copper chaperone
- Cytochrome c oxidase copper chaperone
Sequence:
MEGMNMGSSMNMDAMSSASKTVASSMASMSMDAMSSASKTILSSMSSMSMEAMSSASKTLASTMSSMASMSMGSSSMSGMSMSMSSTPTSSASAQTTSDSSMSGMSGMSSSDNSSSSGMDMDMSMGMNYYLTPTYKNYPVLFHHLHANNSGKAFGIFLLFVVAAFVYKLLLFVSWCLEVHWFKKWDKQNKYSTLPSANSKDEGKHYDTENNFEIQGLPKLPNLLSDIFVPSLMDLFHDIIRAFLVFTSTMIIYMLMLATMSFVLTYVFAVITGLALSEVFFNRCKIAMLKRWDIQREIQKAKSCPGFGNCQCGRHPEPSPDPIAVADTTSGSDQSTRLEKNNESKVAISENNQKKTPTQEEGCNCATDSGKNQANIERDILENSKLQEQSGNMDQNLLPAEKFTHN
Protein: DNA primase (EC 2.7.7.-) (P10236)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011, ECO:0000269|PubMed:8811024}. Note=Requires the presence of the primase associated factor to properly localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011, ECO:0000269|PubMed:8811024}.
Interaction partners:
Sequence:
MGQEDGNRGERRAAGTPVEVTALYATDGCVITSSIALLTNSLLGAEPVYIFSYDAYTHDGRADGPTEQDRFEESRALYQASGGLNGDSFRVTFCLLGTEVGGTHQARGRTRPMFVCRFERADDVAALQDALAHGTPLQPDHIAATLDAEATFALHANMILALTVAINNASPRTGRDAAAAQYDQGASLRSLVGRTSLGQRGLTTLYVHHEVRVLAAYRRAYYGSAQSPFWFLSKFGPDEKSLVLTTRYYLLQAQRLGGAGATYDLQAIKDICATYAIPHAPRPDTVSAASLTSFAAITRFCCTSQYARGAAAAGFPLYVERRIAADVRETSALEKFITHDRSCLRVSDREFITYIYLAHFECFSPPRLATHLRAVTTHDPNPAASTEQPSPLGREAVEQFFCHVRAQLNIGEYVKHNVTPRETVLDGDTAKAYLRARTYAPGALTPAPAYCGAVDSATKMMGRLADAEKLLVPRGWPAFAPASPGEDTAGGTPPPQTCGIVKRLLRLAATEQQGPTPPAIAALIRNAAVQTPLPVYRISMVPTGQAFAALAWDDWARITRDARLAEAVVSAEAAAHPDHGALGRRLTDRIRAQGPVMPPGGLDAGGQMYVNRNEIFNGALAITNIILDLDIALKEPVPFRRLHEALGHFRRGALAAVQLLFPAARVDPDAYPCYFFKSACRPGPASVGSGSGLGNDDDGDWFPCYDDAGDEEWAEDPGAMDTSHDPPDDEVAYFDLCHEVGPTAEPRETDSPVCSCTDKIGLRVCMPVPAPYVVHGSLTMRGVARVIQQAVLLDRDFVEAIGSYVKNFLLIDTGVYAHGHSLRLPYFAKIAPDGPACGRLLPVFVIPPACKDVPAFVAAHADPRRFHFHAPPTYLASPREIRVLHSLGGDYVSFFERKASRNALEHFGRRETLTEVLGRYNVQPDAGGTVEGFASELLGRIVACIETHFPEHAGEYQAVSVRRAVSKDDWVLLQLVPVRGTLQQSLSCLRFKHGRASRATARTFVALSVGANNRLCVSLCQQCFAAKCDSNRLHTLFTIDAGTPCSPSVPCSTSQPSS
Protein: Protein fucoxanthin chlorophyl a/c protein (Protein fucoxanthin chlorophyll a/c protein) (B7FRW2)
Organism: Phaeodactylum tricornutum (strain CCAP 1055/1)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
- Protein fucoxanthin chlorophyll a/c protein
- Photosystem II subunit
- Photosystem II reaction center protein Y
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein J
- Photosystem II reaction center protein H
- Cytochrome b559 subunit beta
- Photosystem II reaction center protein L
- Oxygen-evolving enhancer protein 1
- Cytochrome b559 subunit alpha
Sequence:
MKTAVIASLIAGAAAFAPAKNAARTSVATNMAFEDELGAQPPLGFFDPLGLVADGDQEKFDRLRYVEIKHGRISMLAVVGYLVQEAGVRLPGTIDYSGKTFAEIPNGFAAFKEIPAGGLVQLLFFIGVLESSVMRDLTGEAEFVGDFRNGAIDFGWDTFDEETQFKKRAIELNQGRAAQMGILALMVHEQLGVSLLPQ
Protein: GABA permease (Q5B918)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKDIPAADDIQLAALGHKAELKRNFSMLSMLGLAFAILNSWTALSTSLNLSLPSGGCTSVVWGLVTAGVCNICTAASLAEFLSAWPTAGGQYHWVAGSIIVSWKRQMPMLSWVTGWANVAGWLALTATGGLLSSTLIGGIIGLVYPLFEFQRWHQFLIYIAINIIAFAINAFMNVGLPLVTKSAFIWSLTGFVVISITILSCASPDYNSGKFVFGEFINTTGWPDGVAWLLGLLQGGFGLTGFDGVAHMIEEIPNPTVLGPRIMIGCVCIGITTGLIFLIVLLFVAGDINLVIESAATPLLQIFHDATNSNAGSICLLMFPLVCTVFAATTIMTTSSRMVYAFARDGGLPASPFFSRVHPKLQVPLNGLYLTMFCVIVFGCIFLGSSSAFNAITSSSVVMLDVAYGIPIAINCLRGRQMIPERAFVLPQALGWMVNLIALAYISLTTVLFLFPPELPVTGSNMNYCVAAFGIVLIISAFQWIVDGRKHFTGPRVDAEVLAAVESYSGPNIDGAAEIREQK
Protein: B-cell CLL/lymphoma 7 protein family member A (Q9CXE2)
Organism: Mus musculus (Mouse)
Interaction partners:
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- Actin-like protein 6A
- B-cell CLL/lymphoma 7 protein family member C
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF complex subunit SMARCC1
- SWI/SNF complex subunit SMARCC2
- Bromodomain-containing protein 9
Sequence:
MSGRSVRAETRSRAKDDIKRVMAAIEKVRKWEKKWVTVGDTSLRIYKWVPVTEPKVDDKNKNKKKGKDEKCGSEVTTPENSSSPGMMDMHDDNSNQSSIADASPIKQENSSNSSPAPETNPPVPSDGTEAKADEAQADGKEHPGAEDASEEQNSQSSMENSVNSSEKAERQPSAESGLAAETSAVSQDLEGVPPSKKMKLEASQQNSEEM
Protein: F-box protein ETP1 (EIN2 targeting protein 1) (Q9LJ68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of EIN2 protein stability.
Interaction partners:
- Ethylene-insensitive protein 2
- EIN3-binding F-box protein 1
- Serine/threonine-protein kinase CTR1
- Protein ETHYLENE INSENSITIVE 3
- ETHYLENE INSENSITIVE 3-like 1 protein
- Protein EIN4
- Ethylene receptor 1
- EIN3-binding F-box protein 2
- Ethylene response sensor 1
- Ethylene response sensor 2
Sequence:
MTIPDLCNDLVDEILCRVPARNLKRLRSTSKRWNRLFKDDRRFAREHMHKAPKEYLPLMLTSEYRICPVSINLQGDVPSVVLKRELSLPDPDYSHQFDIGRVFHCDGLLVCNHVGKNPRYGSKIVVWNPLTGQTRWIEAGYRWKEYEVRFVLGYCYQQDENNSCSKKIYKILCFYPNGQDTEIYELNYSDRWTRTIPDGDLTPGWTLIYSEQTVSMNGNLYLFASEKSKPHLGVSLLRFDFSTEKSSLCVTLPYQRPRYEILSISAVRGGENLSLLLQLDFESKTEIWVTNKIDDTTTKGAAVSWTKVLAFDLSPDLQLFSEEVNFLLDEDKKVAVCCERWLEPQEHHRYQCRREYKITDKIYILGEDNKVDEVGSGEGEATDSLEGISQVILNYAPSLVQIEQAGGGKTKRGDD
Protein: Cellular tumor antigen p53 (S4R334)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD
Protein: Glyceraldehyde-3-phosphate dehydrogenase 2 (GAPDH 2) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) (PL-sensitive glyceraldehyde-3-phosphate dehydrogenase) (E3VWI2)
Organism: Streptomyces arenae
Function: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MTVRIGINGFGRIGRNVFRAAAARSSELEIVAVNDLGDVPTMAHLLAYDSILGRFPEEVTAEPGAIRVGDRTIKVLAERDPGALPWGDLGVDIVIESTGIFTDAAKARSHVDGGAKKVIIAAPASGEDFTVVLGVNDGDYDPERHTIISNASCTTNCLGVLAKVLHDAVGIDSGMMTTVHAYTQDQNLQDAPHKDLRRARAAALNIVPTSSGAAKAIGLVLPELAGRLDAFALRVPVPTGSVTDLTVTTRRGTSVEEVKEAYAAAASGPYKGLLSYVDAPLVSTDIVGDPASCVFDAGLTRVSGPQVKVVGWYDNEWGYSNRLIDLATLIGSSL