wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 40 (Alpha A-crystallin-binding protein 1) (Alpha A-CRYBP1) (Alpha A-crystallin-binding protein I) (Transcription factor alphaA-CRYBP1) (Q03172)
Organism: Mus musculus (Mouse)
Function: Transcription factor which binds specifically to the palindromic sequence 5'-GGGAAATCCC-3' in the alpha-A crystallin promoter.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MPRTKQIHPRNLRDKIEEAQKELNGAEVSKKEVLEAGVKGTSESLKGVKRKKIVAENHLKKIPKSPLRNPLQTKHKQNTEEPPFSVLPSASESHKKHNCVPAKQGRQFTKQNGETPGMTAESSESGDLVSPKKTSSPHQRSELRRWRSEGSDPTRLSGLDGQRDSSSSSSKARTDNSECSSPCCSTTPPSYTSTAFDVLLKAMEPELSTLSQKGSSCAIKTEKLRPNKTVRSPSKLKNSSLDAPNATSPDLVVESPCPPCTSYPVHVASTQKSEQVAAQCVSHLYSSQDHLVPKLSQQNQQLPGHLGFTGSLTNLHTLESTKLEPIYNTAVTSTVGLTSPSTRTQVTPPHQQMDSVSPLSVSPASSTQSPPGPIYSSAHVASVVSQSVEQMCSLLLRDQKPKKQGKYICEYCNRACAKPSVLLKHIRSHTGERPYPCVTCGFSFKTKSNLYKHKKSHAHTIKLGLVLQPEAGGLFLSQECPKALSVHSDIEDSGESDEEGLADGRQNNPCVKDLQPVQTMKTVSNPESLPKLIPSNSDHVVRGFSSQDRPSDSQAPTELPKVVVHPVSMPPLKTDCLQVANPNPELPSPQSPRDLHVASILSHSASVSSLEMDESCHQKGDVIQSEGKPDSHSGTAHAQLQRQQATEDPQEQQGKLLLSPRSLGSTDSGYFSRSESADQAVSPPTPFARTFPTMDPDPAKNGGAPGPRISAPAPSALATGEKSSVVTGQMRPPLATKTLEERISKLISDNEALVDDKQLDSVKPRRTSLSRRGSIDSPKSYIFKDSFQFDLKPMGRRTSSSSDIPKSPFTPTEKSKQVFLLSVPSLDCLPITRSNSMPTTGYSAIPANIIPPPPSLRGSQSFDDKIGTLYDDVFVSGPNPSMPPSGHHRPLVRQAAVEDSTASESHVPGSGQSVDESCQGCPSSSEAGPVQSKAAQTPHLEKKKSHQGRGTMFECETCRNRYRKLENFENHKKFYCSELHGPKTKAAVREAEHGPAPGGAQPQVLHYRVAAPTAVWEQTPQIRKRRKMKSVGDEEDLQPHESGRSPESADALQLQPVPGAAPSPSKHTSATAADQAHRGVQLVARGPERALPLKQCPMVEQQLNAAAQDKMEVKRQGGGISVIQHTNSLSRPNSFDKPEPLEGGITFSLQELGRTGMPGALKVIGMAPEEGHPPQDAMHQTALSHNLRGEPRESARKIPSERYVLGQPLRLVRQHNIQVPEILVTEEPDRDLEAQSHDEEKSEKFTWPQRSETLSKLPTEKLPPKKKRLRLAEIEHSSTESSFESTLSRSLSRESSLSHASSFSASLDLEDISKVELAPKIDFPSKAEFLLIPLGSNTLSVPGSHREMRRAASEQISCVPTLMEVSDFRSKSFDCGSIAPSHVVPALVESQPSYSPSAVGGTAHVPLLERRRGPLIRQISLNIASDSHLSPGSAAALQTIVLPSVNTVPFQAPRLPDMASADCPAHTVHPQALAKDLQAEISSSSSTDTFPPQQLFGAHLLNKTNTSLSHQNTPLPLPVSAQGGKPDAAPTACVSSTGEGSFAPKYQLQCQAFTSDQGCSAPLRSSPNQVLPGQAGADPCPASEAPPAKAADPMAKPCPLPPLELGLPRDEVLQKQLPSFVLPVPQKRNVTVDCFTPVTSLPQILVTQDLPNMPICQTNQSLVPVSEEQNSMPKSQNYLQNASPTPEKELACKTVLPEVGQSVPVSESSPTVQKVSVGRLSPQQESSASSKRMLSPANSLDIAMEKHQKRAKDENGAVCSTNIRALELPSSRANESHKQKKPVLVRQLCTTEPLEGAALEQGACSASGRSSNKAANLTQVLPTDSLSSRPSTFAVTDHVNELQEFKNTKVSTSLTPTVGSFPAPSESACVLPLKSIDNNQEKGSPGVRHEENKVIQGQRPPLVSGLSLVSSSDTQQPSFPSLKTATSFTWCYLLRQKALPLAQNDQKTSAYTGWTVSSSNPNPLGLPTKVALSLLNSKQKTGKSLYCQAITTHSKSDLVVYSSKWKNNLSKRALGNQKATVVEFSNKDDSEINSEQDKENSLIKSEPRRIKIFDGGYKSNEDYVYVRGRGRGKYICEECGIRCKKPSMLKKHIRTHTDVRPYHCSYCNFSFKTKGNLTKHMKSKAHSKKCVDLGVSVGLIDEQDTEESDEKQRFGCERSGYDLEESDGPDEDDNDNEEDDDDSQAESGLSAAPSVTASPQHLPSRSGLQDPGSVEEELRVSSCFSGVHTDPMDILPRALLTKMTVLSTVQSSPNRTDLPAKARQSTEKDEHEQAPPADTPRSPGHQLSVHSSESDVLRSPAAGNPAAGSPGAAVQDSSVGLPPAVAQLNPQPAARISSSVSPHPDSQDQKQQIILQPPPGLPSPQTHLFSHLPLHSQQQSRTPYNMVPVGGIHVVTAGLTYSTFVPIQAGPMQLTIPAVSVIHRTVGTSGDTITEASGSPNRPTGVAELSSVVPCIPIGQIHVPGLQNLSPPALQSLTSLGMETVNLVGLANATVGPQGHPPGLALNAVGLQVLANAPAQSSPAPPAHIQGLQILNIALPTLIPSVGPVAVGTTGTPETTAPNSKAMELQMPAGQGHSAEPPQGSPEGPQETPQTVSGPSADHARPEDSTKMDTKKGPSAGHVLPGRSPAQAQPAPTPEALQKVATSAPPSLPTDRAAPRPPVPHRQPIVHFSDVSSDDDEDRLVIAT
Protein: tRNA (adenine(58)-N(1))-methyltransferase TrmI (EC 2.1.1.220) (tRNA(m1A58)-methyltransferase) (tRNA(m1A58)MTase) (P9WFZ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA.
Interaction partners:
- tRNA
- S-adenosyl-L-methionine-dependent methyltransferase
- S-adenosyl-L-methionine-dependent methyltransferase
- PD-
- Large ribosomal subunit protein uL30
- Cystathionine gamma-synthase
- Conserved alanine and valine and glycine rich protein
Sequence:
MSATGPFSIGERVQLTDAKGRRYTMSLTPGAEFHTHRGSIAHDAVIGLEQGSVVKSSNGALFLVLRPLLVDYVMSMPRGPQVIYPKDAAQIVHEGDIFPGARVLEAGAGSGALTLSLLRAVGPAGQVISYEQRADHAEHARRNVSGCYGQPPDNWRLVVSDLADSELPDGSVDRAVLDMLAPWEVLDAVSRLLVAGGVLMVYVATVTQLSRIVEALRAKQCWTEPRAWETLQRGWNVVGLAVRPQHSMRGHTAFLVATRRLAPGAVAPAPLGRKREGRDG
Protein: COP9 signalosome complex subunit 4 (Signalosome subunit 4) (Q54B82)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6
- Cullin-4
- RING-box protein 1
- DNA damage-binding protein 1
Sequence:
MDVNNLKQILEETSALSDHKTKTEKYKSILQQLVESKQVAPLKVFITHLTDESTPLVISRTILLSFTSSHKTLPEDIQMELGIFVLDRIQNRVVAFEEQVSEIRYNLAKLYERQENWRESARCLIAIPLDSSQRVISPEYKVKIYVKIARLFLEEEESGQAETYINRASDSLHLVKNQKLILAHKTCFARIMDYKRMFLKASLRYYDLSQCLPKDTERMHALSCAIVCAILDKAGPQRSRTLATLYKDERSQQLGVYTFLEKMFLERILKKTEVKKFAEQLKPHQMALLSDGNTVLDRAVIEHNLLSASKLYNNITFDELGSLLEIQAEKAEKVASKMVCEERLIGSIDQIERLIQFENVGDSLTQWDKKIEGLCIHMNNIIESISKYPEFIV
Protein: Serine/threonine-protein kinase ppk21 (EC 2.7.11.1) (Q9Y7J6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Note=Located at the cell tips and septum.
Interaction partners:
- Serine/threonine-protein kinase tor1
Sequence:
MMDLEHKRISRSTLPDYADPDYFEARGERNPVKPQSSNVVPGTSHIGSIKSPADYVFGDIIGDGSFSKVRRATDKKSWKEYAIKVLDKKYIVKENKVKYVNIERDSMMRLNGFPGISRLFHTFQDDLKLYYVLELAPNGELLQYIKKYRFLDENCVRFYAAEILSSIEYMHSCGIIHRDLKPENILFDGNMHVKITDFGTAKILPPKYVNSPDYTTFPSSFVGTAEYVAPELLSRQVVSKSSDLWAFACVVYQMIVGSPPFHGSNPNNIFKKIMSLEYELPKLLPPDIVPLFSHLFRIQPSDRSTTQQIKQFPFFATITWDNLWTQDPPPMQSFRPNYNIAIPNAPAYYRSNVTAAAAANAAAAFASASIVKHQETARRQELPTVNRFTAPTAHYGYASLRSHQMPVDRLYYKLVPSSESIIESTSVFVSPIPSVPEGNKFPSGLSKMFLKRKQRVMLLTDVGRCAFVCKGKHERLFIEMEVNLKDSSVVVIFDENSSKRFLIEDKVQSWIIEDSSGDVTKYKDKILKFADVASSHQSRSSEENVEENEEE
Protein: Centromere protein N (H3BMC7)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDETVAEFIKRTILKIPMNELTTILKAWDFLSENQLQTVNFRQRKESVVQHLIHLCEEKRASISDAALLDIIYMQFHQHQKVWEVFQMSKGPGEDVDLFDMKQFKNSFKKILQRALKNVTVSFRETEENAVWIRIAWGTQYTKPNQYKPTYVVYYSQTPYAFTSSSMLRRNTPLLGQ
Protein: RH39096p (A1ZAU4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQSNIISASPFHPSTTKPVGTNSFVFWQISMKLLLVLPLLVAVVSGQGFGGGGFGGGFGGGLGGGFGGGLGGLGNNRVGGALQNVAGAVQNAVGNIAKAVPKVPLLSNVQDFGDFLSQSGKTYLSAADRALHEGAFASTKNLVEAGNAAFAQGVHTFKQAVNAFADLTHSEFLSQLTGLKRSPEAKARAAASLKLVNLPAKPIPDAFDWREHGGVTPVKFQGTCGSCWAFATTGAIEGHTFRKTGSLPNLSEQNLVDCGPVEDFGLNGCDGGFQEAAFCFIDEVQKGVSQEGAYPYIDNKGTCKYDGSKSGATLQGFAAIPPKDEEQLKKVVATLGPVACSVNGLETLKNYAGGIYNDDECNKGEPNHSILVVGYGSEKGQDYWIVKNSWDDTWGEKGYFRLPRGKNYCFIAEECSYPVV
Protein: Z band alternatively spliced PDZ-motif protein 66, isoform B (Q7KUB5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSPKLHEFAVVLLRDGQATPWGIRLVGGNDLDTPLIITRVQVGSPAHGELLRGDIISKIGEYDARDLSHADAQQLFRGAGNEIRLVVHRDNKIAYTQGATQEAGPGSRSNSTLPPVTPDLMPHRGPSPFLPGPSHFERALQLPVDTLPQTVFPQLNSSGGYEVPSTVFSPKPTRDHQQDVDEEQAAIVNQPYRTTPLVLPGAKVKKDAPTTESYLRHYPNPAVRAHPGHDYHDSIMKQRVADTMLHKVVGSEADTGRVFHKQFNSPIGLYSNNNIEDTIRSTVPNQYQRQYPGRRTMW
Protein: Ubiquitin-conjugating enzyme E2, putative (EC 6.3.2.19) (Q57TW2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin, putative
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-activating enzyme E1 regulatory subunit
- Telomerase-associated protein, putative
- Defective in cullin neddylation protein
- Defective in cullin neddylation protein
- RING-type domain-containing protein
- Polyubiquitin, putative
- RING-type domain-containing protein
- Cullin, putative
Sequence:
MLSRIKRQQEEAQAATRSGGESAINQPGQKESMAVLRLKNDLDNLDGICSKVVIPDPDNMLRMKVTVRPSRPSIWHGGFFDFLLEFREEYPYEGPRVRYVGPNRVWHPNIEGSEFAEKEGMEKASRKTEWSVCLSFQTDWKPTFSLRDVIIMIELLFQDPNPDDPLHGTSKQAAQMMKDDPVRFRTKARYWMSGHYID
Protein: CLaudin-like in Caenorhabditis (Q23532)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Suppressor of organelle fusion 2
Sequence:
MAMQFTGLQVVSWILLLVGTGMLVIALISDYWSIHQPRNQMDNLQMHRGVLRQCITTRQYGSCNFRLSSMFKQLRNFMDGYDMYSERSMYRHLPTQTYEVFVALFLAISCMIASTVLLFGPFCCQRCKPSTTLLIFITGVFSGSGCLIYWNANREGKTFTLQQLQFQDVYHYDYGSDMNILSWSFWMAVVSTGILLCSAFLLCVSSRVDPDVEYENPPVTEV
Protein: Phenolic glucoside malonyltransferase 2 (EC 2.3.1.-) (Q9LRQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Malonyltransferase acting on xenobiotic glucosides. Has activity toward 2-Naphthol glucoside (2NAG), 1-Naphthol glucoside (1NAG), kaempferol 7-O-glucoside, hydroxycoumarin glucosides and phenol-glucosides, but not toward kaempferol 3-O-glucoside or daidzin. Prefers phenol glucosides rather than naphtol glucosides. In vivo, seems to be involved in the malonylation of 4-methylumbelliferone glucoside or 4-nitrophenyl glucoside while PMAT1 would be involved in the malonylation of 2-Naphthol glucoside.
Interaction partners:
- Protein ECERIFERUM 26-like
- Protein ECERIFERUM 26
- UDP-glycosyltransferase 73C6
Sequence:
MTLHVIETARVTPTDYSVINSANLHKLPLTFFDLPWLLFQPVKRVFFYELTESTRDHFHSIILPKLKDSLSLILRNYLPLTGHITWEPNEPKPSIIVSENGVVLVTIAESDADFSHLSGYGQRPLSELHALVPKLPVSDDSATAFSIQITLFPNQGFSIGVAAHHAVLDGKTSSTFIKAWAQICKQELQSMPENLTPSYDRSLIKYPTYLDEKMIELVRSLKEDQTNIRSLTSLPSSKLGDDVVLATLVLSRADIERLREQVKNVSPSLHLSTFVIAYAYAWTCFVKARGGNKDRSVSLLFVGDFRDRLDPKLPGTYFGNCMIPVGCYNRKAAEFMEEKGFVTAAEIISDLVKGLSSRKIETIADTFVEGFSFQSWSTQFGTIAGSTRLGVYEADFGWGRPVKVDIVSIDQGEAIAMAERRDESGGVEIGMCLKKTEMDSVVSFFNNGLHS
Protein: AT01345p (GH10272p) (Mitochondrial translation elongation factor Tu 2) (Q7K3V6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Elongation factor Ts, mitochondrial
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- 40S ribosomal protein S15
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL20m
Sequence:
MSGLLPKLWRQCEAGLVRRISQALIGPGASQSRWTGTRLLATSADKNPAPGLRELPHCNVGTIGHVDHGKTTLTAAITRIQSQKGLAEYLSYDQIDRAPEEKARGITINACHIGYSTTERTYAHTDCPGHADYIKNMISGASQMDGAILVVAATDGQMPQTREHLLLAKQVGIQRIIVFINKADLVDQEVLELVEIEMREMLSDFGFDGVNSPVICGSALLALREDKSEFGVPSIEKLLEQCDSYIPTPQRDISSPFILPIDNAFTVPGRGTVVVGTIKRGTIPRNADADLLGFNQNLKTSISDIQIFRKSVPQAQAGENVGALLRGIKISAVERGMLLCATGSEDISNHFEGSMYLLSRAEGGRVKPMLSKYIQQLFSQTWNVPARIDIVPSEAMLMPGEHGQVRVTLLRKMVMTPGQAFTIRENGATVATGMVTQRLPSLDLPKNKLSKVFVDC
Protein: Cholera enterotoxin subunit A (Cholera enterotoxin, A chain) [Cleaved into: Cholera enterotoxin subunit A1 (EC 2.4.2.-) (Cholera enterotoxin A1 chain) (Cholera enterotoxin alpha chain) (NAD(+)--diphthamide ADP-ribosyltransferase); Cholera enterotoxin subunit A2 (Cholera enterotoxin A2 chain) (Cholera enterotoxin gamma chain)] (P01555)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: The A1 chain catalyzes the ADP-ribosylation of Gs alpha, a GTP-binding regulatory protein, to activate the adenylate cyclase. This leads to an overproduction of cAMP and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The A2 chain tethers A1 to the pentameric ring.
Interaction partners:
- Cholera enterotoxin subunit B
- Zona occludens toxin
- Cholera toxin transcriptional activator
- Accessory cholera enterotoxin
Sequence:
MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL
Protein: DNA repair protein RAD7 (P06779)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) which removes DNA damage from nontranscribing DNA. This protein is one of 10 proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents.
Interaction partners:
- DNA repair protein RAD16
- DNA repair protein RAD4
- Elongin-C
- UV excision repair protein RAD23
- DNA repair protein RAD2
- DNA repair protein RAD14
- Cullin-3
- DNA repair and recombination protein RAD26
- DNA repair protein RAD10
- ARS-binding factor 1
Sequence:
MYRSRNRPKRGGENEVKGPNSALTQFLREEGISAENIKQKWYQRQSKKQEDATDEKKGKAEDDSFTAEISRVVEDEEIDEIGTGSGTETERAQVSYDARMKLVPADSDEEEYETSHISDTPVSLSSANDRESLTKKRQNTAKIIQNRRRKRKRAADLLDRRVNKVSSLQSLCITKISENISKWQKEADESSKLVFNKLRDVLGGVSTANLNNLAKALSKNRALNDHTLQLFLKTDLKRLTFSDCSKISFDGYKTLAIFSPHLTELSLQMCGQLNHESLLYIAEKLPNLKSLNLDGPFLINEDTWEKFFVIMKGRLEEFHISNTHRFTDKSLSNLLINCGSTLVSLGLSRLDSISNYALLPQYLVNDEFHSLCIEYPFNEEDVNDEIIINLLGQIGRTLRKLVLNGCIDLTDSMIINGLTAFIPEKCPLEVLSLEESDQITTDSLSYFFSKVELNNLIECSFRRCLQLGDMAIIELLLNGARDSLRSLNLNSLKELTKEAFVALACPNLTYLDLGFVRCVDDSVIQMLGEQNPNLTVIDVFGDNLVTEKATMRPGLTLIGRQSDSI
Protein: Taste receptor type 2 (G1NQR8)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}.
Interaction partners:
Sequence:
MLPPVLIVSMCVVAVEVVVGFMGNGFITAVNSINWIKSKRISAADMILIFLSTSRFILQVTVMMYIHSLYFTDVFKLASVYKTFGAIWMFVNHASLWFSTWLYVLYCVKIINVTQWLLLQIKLRITAMIPWLLLGSLLISSVTSFPLLWITPNTYLCRSTGNCGDNSTTHISGWDSSHLYLLLLYFTGCFFPLVLSIITSGLLINSLWKHTKKMQCYVDSFRDPLIDVHLIAIKSIISFLILYISSFVAQILLTLSTSQSKDFVKVAVSLVVTGAYPSIHSIILIIVNSKLKLAFRMLCQHFMCHLENVKL
Protein: Alcohol dehydrogenase 2 (EC 1.1.1.1) (P48815)
Organism: Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata)
Interaction partners:
Sequence:
MGLSGKNVIFVGGLGFIGYEACKQLMAKNMASFFVFDVLDKPENIKALQALNPKTKVYYTKFDITSKQSIKSALADVVAKVKYIDALINGAGILTDPNVELTMNINLIGLINTTLEGLPLMDKNKQGRGGVIVNIASVLGLEPCPPAAVYCASKFGVMGFSRSIGDPYYYNITGVAVVTFCPGLTETPLKNNIGSKYTFEYSKKISEELNSTKTQKPEVCGAHLAQVVESHENGGIYISNQGTLAKVTPTVYWQPTYH
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit (F1MAA3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Protein phosphatase 2 scaffold subunit A alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Shugoshin 1
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Meiotic recombination protein REC8 homolog
- D
- Apoptosis regulator Bcl-2
- Protein phosphatase 1 regulatory subunit 1A
- Troponin I, cardiac muscle
Sequence:
MPYKLKKDKEPPKLAKGTAKPSSSSKDGGGENTDTEAQPQPQPQPPSSNKRPSNSTPPPTQLSKIKYSGGPQIVKKERRQSSSRFNLSKNRELQKLPALKDSPTQEREELFIQKLRQCCVLFDFVSDPLSDLKFKEVKRAGLNEMVEYITHSRDVVTEAIYPEAVTMFSVNLFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFLLDLFDSEDPRERDFLKTILHRIYGKFLGLRAYIRRQINHIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKMFLIRVLLPLHKVKSLSVYHPQLAYCVVQFLEKESSLTEPVIVGLLKFWPKTHSPKEVMFLNELEEILDVIEPSEFSKVMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAARVLPIMFPALYRNSKSHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQYKAEKQKGRFRMKEREEMWQKIEELARLNPQYPMFRAPPPLPPVYSMETETPTAEDIQLLKRTVETEAVQMLKDIKKDKVLLRRKSELPQDVYTIKALEAHKRAEEFLTASQEAL
Protein: E3 ubiquitin-protein ligase SIAH1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SIAH1) (Seven in absentia homolog 1) (Siah-1) (Siah-1a) (Q920M9)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes. Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP. Confers constitutive instability to HIPK2 through proteasomal degradation (By similarity). It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription, spermatogenesis and TNF-alpha signaling (By similarity). Has some overlapping function with SIAH2 (By similarity). Induces apoptosis in cooperation with PEG3 (By similarity). Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus. GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins. Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1.
Subcellular location: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Partially nuclear.
Interaction partners:
- Calcyclin-binding protein
- Glyceraldehyde-3-phosphate dehydrogenase
- Catenin beta-1
- Glyceraldehyde-3-phosphate dehydrogenase.
- Glyceraldehyde-3-phosphate dehydrogenase
- glyceraldehyde-3-phosphate dehydrogenase
- Synphilin-1
- Ubiquitin carboxyl-terminal hydrolase 19
- Glyceraldehyde-3-phosphate dehydrogenase
- glyceraldehyde-3-phosphate dehydrogenase
Sequence:
MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKAEHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC
Protein: Myristoylated alanine-rich C-kinase substrate (MARCKS) (Protein kinase C substrate 80 kDa protein) (P30009)
Organism: Rattus norvegicus (Rat)
Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24662485}; Lipid-anchor {ECO:0000269|PubMed:24662485}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P29966}. Cytoplasm {ECO:0000250|UniProtKB:P29966}. Note=PKC-dependent phosphorylation displaces MARCKS from the cell membrane and subsequent dephosphorylation is accompanied by its reassociation with the membrane. {ECO:0000250|UniProtKB:P29966}.
Interaction partners:
- Calmodulin-like protein 4
- Calmodulin-1
- Calmodulin-like protein 3
- Protein kinase C delta type
- MARCKS-related protein
- Protein kinase C epsilon type
- Protein kinase C alpha type
- Brain acid soluble protein 1
Sequence:
MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGGAATPAAADKDEAAAAPEPGAATADKEAAEAEPAEPGSPSAETEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKEAGEGAEAEGATADGAKDEAAAAAGGDAAAAPGEQAGGAGAEGAEGGESREAEAAEPEQPEQPEQPAAEEPRAEEPSEAVGEKAEEPAPGATADDAPSAAGPEQEAPAATDEPAASAAPSASPEPQPECSPEAPPAPVAE
Protein: Polyneuridine-aldehyde esterase (EC 3.1.1.78) (Polyneuridine aldehyde esterase) (Q9SE93)
Organism: Rauvolfia serpentina (Serpentine wood) (Ophioxylon serpentinum)
Function: Catalyzes the hydrolysis of polyneuridine aldehyde into epi-vellosimine, which is the immediate precursor for the synthesis of ajmaline.
Interaction partners:
Sequence:
MHSAANAKQQKHFVLVHGGCLGAWIWYKLKPLLESAGHKVTAVDLSAAGINPRRLDEIHTFRDYSEPLMEVMASIPPDEKVVLLGHSFGGMSLGLAMETYPEKISVAVFMSAMMPDPNHSLTYPFEKYNEKCPADMMLDSQFSTYGNPENPGMSMILGPQFMALKMFQNCSVEDLELAKMLTRPGSLFFQDLAKAKKFSTERYGSVKRAYIFCNEDKSFPVEFQKWFVESVGADKVKEIKEADHMGMLSQPREVCKCLLDISDS
Protein: Ribonuclease H (RNase H) (EC 3.1.26.4) (Q9UST8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Interaction partners:
- Ribonuclease H2 subunit A
- Uncharacterized ATP-dependent helicase C29A10.10c
- Helicase sen1
- Protein argonaute
- Protein Dicer
- Probable thymidylate synthase
- ATP-dependent DNA helicase pfh1
Sequence:
MGGNKRAYYAVARGRNTGIYSTWDEASDQVKGYGGNRYKKFDSYEAAQEFCRTEGSRYSSSSGPYRRSTTSYGYSPYSSSSSNYSARHSDKYRKKISRSYSTEKDIEIFSNDTHEKSIACSDRQVVYADGSSLRNGKKGAVAGCGVFFGNDDPRNISVPLAGEEQTNNRAELQAIILALENTSGDLTIRSDSNYSIKSLTTWLPKWKKNDFKTSNSQPVKNLDLINRASDLMSDRNVSLEYVKGHSTDYGNQQADMLARRGASE
Protein: Aryl hydrocarbon receptor repressor (AhR repressor) (AhRR) (Class E basic helix-loop-helix protein 77) (bHLHe77) (A9YTQ3)
Organism: Homo sapiens (Human)
Function: Mediates dioxin toxicity and is involved in regulation of cell growth and differentiation. Represses the transcription activity of AHR by competing with this transcription factor for heterodimer formation with the ARNT and subsequently binding to the xenobiotic response element (XRE) sequence present in the promoter regulatory region of variety of genes. Represses CYP1A1 by binding the XRE sequence and recruiting ANKRA2, HDAC4 and/or HDAC5. Autoregulates its expression by associating with its own XRE site.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17980155}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17980155}. Note=Predominantly in the nuclear compartment. First cytoplasmic, translocates into the nuclear compartment upon interaction with ARNT in the cytoplasmic compartment.
Interaction partners:
- Cytochrome P450 1A1
- Aryl hydrocarbon receptor nuclear translocator
- Aryl hydrocarbon receptor nuclear translocator 2
- AH receptor-interacting protein
- Heat shock protein HSP 90-beta
- Cytochrome P450 1B1
- Basic helix-loop-helix ARNT-like protein 2
- Basic helix-loop-helix ARNT-like protein 1
- Ankyrin repeat family A protein 2
- Proteinase-activated receptor 4
Sequence:
MPRTMIPPGECTYAGRKRRRPLQKQRPAVGAEKSNPSKRHRDRLNAELDHLASLLPFPPDIISKLDKLSVLRLSVSYLRVKSFFQVVQEQSSRQPAAGAPSPGDSCPLAGSAVLEGRLLLESLNGFALVVSAEGTIFYASATIVDYLGFHQTDVMHQNIYDYIHVDDRQDFCRQLHWAMDPPQVVFGQPPPLETGDDAILGRLLRAQEWGTGTPTEYSAFLTRCFICRVRCLLDSTSGFLTMQFQGKLKFLFGQKKKAPSGAMLPPRLSLFCIAAPVLLPSAAEMKMRSALLRAKPRADTAATADAKVKATTSLCESELHGKPNYSAGRSSRESGVLVLREQTDAGRWAQVPARAPCLCLRGGPDLVLDPKGGSGDREEEQHRMLSRASGVTGRRETPGPTKPLPWTAGKHSEDGARPRLQPSKNDPPSLRPMPRGSCLPCPCVQGTFRNSPISHPPSPSPSAYSSRTSRPMRDVGEDQVHPPLCHFPQRSLQHQLPQPGAQRFATRGYPMEDMKLQGVPMPPGDLCGPTLLLDVSIKMEKDSGCEGAADGCVPSQVWLGASDRSHPATFPTRMHLKTEPDSRQQVYISHLGHGVRGAQPHGRATAGRSRELTPFHPAHCACLEPTDGLPQSEPPHQLCARGRGEQSCTCRAAEAAPVVKREPLDSPQWATHSQGMVPGMLPKSALATLVPPQASGCTFLP