wanglab/gogpt-training-data huggingface dataset:
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q57XI8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MSTKKHLVSLIHVYAAASIKESNAAAGEGKNIREFHILCSLVELCKKTPINLPGSSLLDDDVRAIELVNMSGSTDEWQSQFPTTDKVSGEKSIDCEKQPKQISCHEKYDKWRATRKALEAEPNKEIKQTPAKGIQNTAYGRRIHIQINDIAKEAQVIYNNYKAETAPVLNGINDKLRIHFGDALYGKQDRPLAGAPADKWQASGTRNNDCKGAKAGISPRGDLFCLCAQDTTIAEHMCGDTVTAAGSNWLLATVAPLIDGMASKCAGKAKPTITASYIRHALETFDSALKSHTQGTKDAVVLGTPHSSGVCGGQASVACVDYTAAVMPKEQGKHNDIKWYNELTDASKALDNYAAAMAEEKAAQTKIQKLKQEANRLFQTLKVQEPAAIPPISQLPRIDPLELKKKCEQFHNKSKECTENGCKWKGTDETTGTCDVDETKVTSQTNAAGTGEASNEETATSGCAKHKDKTECDADKKDDKQNCAFRKGKDVEDDKDTEKCRSSGFLVNNKLVQSIAAVFVSLVPS
Protein: Eukaryotic translation initiation factor 3 subunit M (eIF3m) (Fetal lung protein B5) (hFL-B5) (PCI domain-containing protein 1) (Q7L2H7)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit L
Sequence:
MSVPAFIDISEEDQAAELRAYLKSKGAEISEENSEGGLHVDLAQIIEACDVCLKEDDKDVESVMNSVVSLLLILEPDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKNTPVRYTVYCSLIKVAASCGAIQYIPTELDQVRKWISDWNLTTEKKHTLLRLLYEALVDCKKSDAASKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNAFLFDHLLTLKPVKFLEGELIHDLLTIFVSAKLASYVKFYQNNKDFIDSLGLLHEQNMAKMRLLTFMGMAVENKEISFDTMQQELQIGADDVEAFVIDAVRTKMVYCKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLNAWKQNLNKVKNSLLSLSDT
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M9NGC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD40489p
- Serine-arginine protein 55
- Cell division cycle 5, isoform A
- U1 small nuclear ribonucleoprotein 70 kDa
- Zinc finger matrin-type protein CG9776
- LD32469p
Sequence:
MAGLIGAANGKHHHPHLISPTHTSLPAGICSSDSGISTLSAISPPLSTSTTTASGAGGGVGGSPQLRTSPALSMLGSATATASGVTASSGCGLTAGILGPAASIDLGSSPLSHRNYSNSLKGFSFRRSFDDKIINTPYLSRAPAYTHGIPYPHFHGTQPAATTPHHLHLHHHGNGTAAGSGSGVGSGPGSGSGAGGLYQQPLSLASMTAALPLAPLYGSPLSLPLTSSQSTTKLSYRDDFLQQIGYLPTTRIYSTPTSIVDEDKAQQDFLSLSLSPPLNRRRDMPALRGPFVSLSEPRGTLSTTDEIYPDSSDSSLYVSDEEQEDASQYCRGGYHPVVIGDIFDNRFRVVRKLGWGHFSTVWLCRDLKDEKYVALKVVKSAPHYIETAADEIRLLEAIRDADPMDVKRERIVRLMNHFTVRGVNGMHTCLVFEALGCSLYKLIVKNNYQGLAIAQVRNIIRQVLEGLDYLHSKCSIIHTDIKPENILLVIDNAAAMNQQIDDEINSLRVKGVDFPDSYISSIEKQTKSRAKWPLIEPNGSTNTNTNTSNSTATNSNSSTPLAAVIMSTLDKEDTTTTTSSTLNSNTTSSLASKYSSLLGDSECNGGLGGSANINNRYRTEKKITAKSSGDCDEDAESDTLGEQSTLASTMDSPTDLDPEPELDSKPNTVPEPSEGPIPEQPTPNSTNSSCPSHNTATIAKSKINSNILSTCTSLTSTNEYCFTNTNTTTASTPSAPPSATPSSAPALASATPPSTCTPSFTQIAPSATAPATSTTCTTSAEFYDGDHKTTSTSTTTTSNAISSATTTTATTTTAIAKLNVHANAIPSQNQSQSSQNNTYTIQSLIDNSNVRVKIADLGNACYDYHHFTEDIQTRQYRSIEVLLGAPYNYTADIWSTACLAFELATGDYLFDPHAGESYSRDEDHLAHIVELLGSIPQSVIFRGKHGLKYFTSYGSLRNITKLKPWSLMNVLVEKYDWDPVEAKKFSDFLLPMLEYNPVIRASAAECLQHPWLEQEEFV
Protein: Amyloid beta precursor like protein 2 (Amyloid beta (A4) precursor-like protein 2) (Amyloid protein homolog) (Amyloid-like protein 2) (APLP-2) (CDEI box-binding protein) (CDEBP) (Sperm membrane protein YWK-II) (Q06335)
Organism: Mus musculus (Mouse)
Function: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein (By similarity). Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Major prion protein
- Amyloid-beta precursor protein
- Nicastrin
- Beta-secretase 1
Sequence:
MAATGTAAAAATGKLLVLLLLGLTAPAAALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCLGTKEEVLQYCQEIYPELQITNVMEANQPVNIDSWCRRDKRQCKSHIVIPFKCLVGEFVSDVLLVPDNCQFFHQERMEVCEKHQRWHTLVKEACLTEGLTLYSYGMLLPCGVDQFHGTEYVCCPQTKTVDSDSTMSKEEEEEEEDEEDEEEDYDLDKSEFPTEADLEDFTEAAADEEEEDEEEGEEVVEDRDYYYDPFKGDDYNEENPTEPSSEGTISDKEIVHDVKVPPTPLPTNDVDVYFETSADDNEHARFQKAKEQLEIRHRNRMDRVKKEWEEAELQAKNLPKTERQTLIQHFQAMVKALEKEAASEKQQLVETHLARVEAMLNDRRRIALENYLAALQSDPPRPHRILQALRRYVRAENKDRLHTIRHYQHVLAVDPEKAAQMKSQVMTHLHVIEERRNQSLSLLYKVPYVAQEIQEEIDELLQEQRADMDQFTSSISENPVDVRVSSEESEEIPPFHPLHPFPSLSENEDTQPELYHPMKKGSGMAEQDGGLIGAEEKVINSKNKMDENMVIDETLDVKEMIFNAERVGGLEEEPESVGPLREDFSLSSNALIGLLVIAVAIATVIVISLVMLRKRQYGTISHGIVEVDPMLTPEERHLNKMQNHGYENPTYKYLEQMQI
Protein: Guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) (Q9WTT6)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Interaction partners:
- Purine nucleoside phosphorylase
- Xanthine dehydrogenase/oxidase
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Disks large homolog 4
- Dihydropyrimidinase-related protein 1
- Uracil phosphoribosyltransferase homolog.
- Histidine ammonia-lyase
- Stress-induced-phosphoprotein 1
- Adenosine deaminase
Sequence:
MCAARRRELALIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEESSQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKYTFPTEKRFQSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNNTVPEYKETTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPGYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINPRASDSPIDLFCGDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
Protein: Mitogen-activated protein kinase kinase kinase (EC 2.7.11.25) (Mixed lineage kinase) (Protein slipper) (dMLK) (Q95UN8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Activates the JUN N-terminal pathway during dorsal closure.
Interaction partners:
- Ras-related protein Rac1
- Dual specificity mitogen-activated protein kinase kinase hemipterous
- AT17867p
- mitogen-activated protein kinase kinase
- Alphabet, isoform E
- Ras-like GTP-binding protein RhoL
- Ras-related protein Rac2
- CG6036 protein
- Ubiquitin thioesterase trabid
- Ubiquitin carboxyl-terminal hydrolase Usp2
Sequence:
MPSQVSRGLDTTNMLPISEEQQLQQQQQQQQLEQLHHPQIPEIPIPDLEQVETQVGDGSLWTALYDYDAQGEDELTLRRGEIVVVLSTDSEVSGDVGWWTGKIGDKVGVFPKDFVTDEDPLQLNVSSAIGDIQPHEIEYNELDIKEVIGSGGFCKVHRGYYDGEEVAIKIAHQTGEDDMQRMRDNVLQEAKLFWALKHENIAALRGVCLNTKLCLVMEYARGGSLNRILAGKIPPDVLVNWAIQIARGMNYLHNEAPMSIIHRDLKSSNVLIYEAIEGNHLQQKTLKITDFGLAREMYNTQRMSAAGTYAWMPPEVISVSTYSKFSDVWSYGVLLWELITGETPYKGFDPLSVAYGVAVNTLTLPIPKTCPETWGALMKSCWQTDPHKRPGFKEILKQLESIACSKFTLTPQESFHYMQECWRKEIAGVLHDLREKEKELRNKEEQLLRVQNEQREKANLLKIREQNLRERERVLIERELVMLQPVPSKRKHKKGKKNKPLQISLPTGFRHTITAVRDKAEQPGSPSFSGLRIVALTDGHKGKTWGPSTMHQRERSLLPSQLSGGQPEWPAQTSTHSSFSKSAPNLDKKQQQQNQQQVASLTPPPGLGILGGSGGAGGTPATPLLYPGIPIILTRPNNNNIGNCKAITTTITTTTTTTTNNNNNNNNSISANNNNQLNNISTINSNNNNNQTNLTSQPNTIIVLQNGRNNSNSSTTSQSPAKIYHRARSQEYGLDHPLAYQPPPLYLVTDDSSETDTVASPTGCFHFLKSGNSSAASGAVHLHRFGGSLGNSPAVGRKKHSLDSSSHHPPANGSNSFALPNQLTLPSEDNNTYDHAFYRDVIKKMSMASSERVNSKSSGDLTMYNSSTPLTARDCDDAEEAFEGGRFQRNFSGSQFPRHCFFTRQEEEGEAEDEDAVAAEVDTADADADDECQVPASQMRQNSTTSRKSSVTFQSVSFEEPDFVATPRTTARSDLYTSSASISFATYRSASPSLSSSSTTASASPSIASTEAVNGYHMQENSILNTRRMQDVQPHPDVIKLRAQEQRQQTKNQKKQRPKHITKSKSVEAPVEGQHHEHDDHNDPQHQHHSAGSSKIRALFNLFTRSRKKYSKLAEHNMVGGPEFCAIDPYQTDLAMGGSSRSLKRKGKKPQTQSCEQLERC
Protein: PRS fimbrial major pilin protein (PRS pili) (P42184)
Organism: Escherichia coli
Function: Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs.
Subcellular location: Secreted. Fimbrium.
Interaction partners:
Sequence:
GANAAPQGQGKVTFNGTVVDAPCGIDAQSADQSIEFGQVSKVLLNNGGSSTPKNFDIKLTDCDVTNYKKAGKAGTVSLTFSGVQAGTDMLQTVGTTGTAILVKDPHGKAVKFDGATATGVSSLVDGDNTIHFTALVKKDTSGNDVAEGAFSAVANFNLIYQ
Protein: Lipin, isoform E (EC 3.1.3.4) (A0A0B4JD27)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSLARVFSNFRDFYNDINAATLTGAIDVIVVEQRDGEFQCSPFHVRFGKLGVLRSREKVVDIEINGVPVDIQMKLGDSGEAFFVEECLEDEDEELPANLATSPIPNSFLASRDKANDTMEDISGVVTDKNASEELLLPLPLPRRNSIDFSKEEPKEAVVEGSKFENQVSDYTQRRHTDNTLERRNLSEKLKEFTTQKIRQEWAEHEELFQGEKKPADSDSLDNQSKASNEAETEKAIPAVIEDTEKEKDQIKPDVNLTTVTTSEATKEVSKSKTKKRRKKSQMKKNAQRKNSSSSSLGSAGGGDLPSAETPSLGVSNIDEGDAPISSATNNNNTSSSNDEQLSAPLVTARTGDDSPLSEIPHTPTSNPRLDLDIHFFSDTEITTPVGGGGAGSGRAAGGRPSTPIQSDSELETTMRDNRHVVTEESTASWKWGELPTPEQAKNEAMSAAQVQQSEHQSMLSNMFSFMKRANRLRKEKGVGEVGDIYLSDLDAGSMDPEMAALYFPSPLSKAASPPEEDGESGNGTSLPHSPSSLEEGQKSIDSDFDETKQQRDNKYLDFVAMSMCGMSEQGAPPSDEEFDRHLVNYPDDAIEQLMSQTVDGKCLPGDEKQEAVAQADNGGQTKRYWWSWRRSQDAAPNHLNNTHGMPLGKDEKDGDQAAVATQTSRPTSPDITDPTLSKSDSLVNAENTSALVDNLEELTMASNKSDEPKERYKKSLRLSSAAIKKLNLKEGMNEIEFSVTTAYQGTTRCKCYLFRWKHNDKVVISDIDGTITKSDVLGHILPMVGKDWAQLGVAQLFSKIEQNGYKLLYLSARAIGQSRVTREYLRSIRQGNVMLPDGPLLLNPTSLISAFHREVIEKKPEQFKIACLSDIRDLFPDKEPFYAGYGNRINDVWAYRAVGIPIMRIFTINTKGELKHELTQTFQSSGYINQSLEVDEYFPLLTNQDEFDYRTDIFDDEESEEELQFSDDYDVDVEHGSSEESSGDEDDDEALYNDDFANDDNGIQAVVASGDERTADVGLIMRVRRVSTKNEVIMASPPKWINS
Protein: DENN domain-containing protein 2A (Q9ULE3)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) which may activate RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May play a role in late endosomes back to trans-Golgi network/TGN transport.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20937701}. Note=Associated with actin filaments.
Interaction partners:
- Ras-related protein Rab-9A
- Ras-related protein Rab-9B
Sequence:
MDMFSLDMIISDPAAEASRAGKKQLRGVQNPCPSARARPRHKSLNIKDKISEWEGKKEVPTPAPSRRADGQEDYLPSSTVERRSSDGVRTQVTEAKNGMRPGTESTEKERNKGAVNVGGQDPEPGQDLSQPEREVDPSWGRGREPRLGKLRFQNDPLSVLKQVKKLEQALKDGSAGLDPQLPGTCYSPHCPPDKAEAGSTLPENLGGGSGSEVSQRVHPSDLEGREPTPELVEDRKGSCRRPWDRSLENVYRGSEGSPTKPFINPLPKPRRTFKHAGEGDKDGKPGIGFRKEKRNLPPLPSLPPPPLPSSPPPSSVNRRLWTGRQKSSADHRKSYEFEDLLQSSSESSRVDWYAQTKLGLTRTLSEENVYEDILDPPMKENPYEDIELHGRCLGKKCVLNFPASPTSSIPDTLTKQSLSKPAFFRQNSERRNFKLLDTRKLSRDGTGSPSKISPPSTPSSPDDIFFNLGDPQNGRKKRKIPKLVLRINAIYEVRRGKKRVKRLSQSMESNSGKVTDENSESDSDTEEKLKAHSQRLVNVKSRLKQAPRYPSLARELIEYQERQLFEYFVVVSLHKKQAGAAYVPELTQQFPLKLERSFKFMREAEDQLKAIPQFCFPDAKDWVPVQQFTSETFSFVLTGEDGSRRFGYCRRLLPGGKGKRLPEVYCIVSRLGCFSLFSRILDEVEKRRGISPALVQPLMRSVMEAPFPALGKTILVKNFLPGSGTEVIELCRPLDSRLEHVDFESLFSSLSVRHLVCVFASLLLERRVIFIADKLSILSKCCHAMVALIYPFAWQHTYIPVLPPAMVDIVCSPTPFLIGLLSSSLPLLRELPLEEVLVVDLVNSRFLRQMDDEDSILPRKLQVALEHILEQRNELACEQDEGPLDGRHGPESSPLNEVVSEAFVRFFVEIVGHYSLFLTSGEREERTLQREAFRKAVSSKSLRHFLEVFMETQMFRGFIQERELRRQDAKGLFEVRAQEYLETLPSGEHSGVNKFLKGLGNKMKFLHKK
Protein: Uncharacterized transcriptional regulatory protein C1399.05c (Q9HE16)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uridylate kinase
- Putative uracil phosphoribosyltransferase urg2
- Protein urg3
- Uridine kinase
- Uracil phosphoribosyltransferase 2
- Large ribosomal subunit protein uL29
- Uncharacterized transcriptional regulatory protein C139.03
- Uncharacterized membrane protein C3H7.05c
- Uncharacterized protein UNK4,15
- Large ribosomal subunit protein uL24
Sequence:
MGEVERTRQSSSSLLTFKRKRALEACDSCRKQKTRCLAGSVEDENRACLRCRSLNMDCSLADPNHFIRKVENDNMDAISANINSKLENRLKVLEKAISSITNSPIAGQISLKSEKDVFLQGLLSMDEIELLLEIFIERYGKRWLSVDYSASQYMELLYTKSHLMLATACLIALRHNPSLKARIYTDVLNIVDRLISEELLTTSPSLQFFEAVSMLTLYRPLRLSQKQDLWLLSGFALQHRTLSSTKGWFNGFAGSSATLTYLDIVPARTWNHLCHGHLVMCMGYRRHAMLDENTFDDCRNILTNTKANEFDGNILGMLSVYSMLYRMLRSPTLDLDYAIFQLEEWRKEWCHLWEQPEPQYSRIAYFYSYNVVYEASIQTATDGNDFANIPRYVSMVQSYALKTIDAIFELSAYDMSRCSDHVLFHAGFASASLLRLIYAAKTKEVDTSIVQPKVLNDLVTKIWKWLLVISVDQYHLATKFANYLKEYQKTVNEGTAESTWFKGPLRPVSSTTLQALKPYNLGVATVERG
Protein: MutS protein homolog 4 (hMSH4) (O15457)
Organism: Homo sapiens (Human)
Function: Involved in meiotic recombination. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q99MT2}.
Interaction partners:
- MutS protein homolog 5
- DNA mismatch repair protein Mlh3
- DNA mismatch repair protein Mlh1
- Probable ATP-dependent DNA helicase HFM1
- DNA repair protein RAD51 homolog 1
- Synaptonemal complex protein 3
- PMS1 protein homolog 1
- HORMA domain-containing protein 1
- HORMA domain-containing protein 2
- Mismatch repair endonuclease PMS2
Sequence:
MLRPEISSTSPSAPAVSPSSGETRSPQGPRYNFGLQETPQSRPSVQVVSASTCPGTSGAAGDRSSSSSSLPCPAPNSRPAQGSYFGNKRAYAENTVASNFTFGASSSSARDTNYPQTLKTPLSTGNPQRSGYKSWTPQVGYSASSSSAISAHSPSVIVAVVEGRGLARGEIGMASIDLKNPQIILSQFADNTTYAKVITKLKILSPLEIIMSNTACAVGNSTKLFTLITENFKNVNFTTIQRKYFNETKGLEYIEQLCIAEFSTVLMEVQSKYYCLAAVAALLKYVEFIQNSVYAPKSLKICFQGSEQTAMIDSSSAQNLELLINNQDYRNNHTLFGVLNYTKTPGGSRRLRSNILEPLVDIETINMRLDCVQELLQDEELFFGLQSVISRFLDTEQLLSVLVQIPKQDTVNAAESKITNLIYLKHTLELVDPLKIAMKNCNTPLLRAYYGSLEDKRFGIILEKIKTVINDDARYMKGCLNMRTQKCYAVRSNINEFLDIARRTYTEIVDDIAGMISQLGEKYSLPLRTSFSSARGFFIQMTTDCIALPSDQLPSEFIKISKVKNSYSFTSADLIKMNERCQESLREIYHMTYMIVCKLLSEIYEHIHCLYKLSDTVSMLDMLLSFAHACTLSDYVRPEFTDTLAIKQGWHPILEKISAEKPIANNTYVTEGSNFLIITGPNMSGKSTYLKQIALCQIMAQIGSYVPAEYSSFRIAKQIFTRISTDDDIETNSSTFMKEMKEIAYILHNANDKSLILIDELGRGTNTEEGIGICYAVCEYLLSLKAFTLFATHFLELCHIDALYPNVENMHFEVQHVKNTSRNKEAILYTYKLSKGLTEEKNYGLKAAEVSSLPPSIVLDAKEITTQITRQILQNQRSTPEMERQRAVYHLATRLVQTARNSQLDPDSLRIYLSNLKKKYKEDFPRTEQVPEKTEE
Protein: Translocation protein SEC62 (Q9VL49)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- RE14391p
- DSec61alpha
- non-specific serine/threonine protein kinase
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 gamma-2 subunit
- STE20-related kinase adapter protein stlk
- Phosphoribosylformylglycinamidine synthase
- Protein transport protein Sec61 gamma-1 subunit
- Protein transport protein Sec61 subunit gamma
- Nucleotide exchange factor Sil1
Sequence:
MSGEEEYFQEEEEEEQEQDIYDDGTEYTEPGAQKVDKPSKDEKNVAKWLKKNVKTKKTKFLSHIVEYFTSSKAIDALLKSKFTEGSNPLFTTREQVIEFLDVMLEHKFFHRAKKVPVTLEEIRGKSGGDKKADKEKTQDKEKDKAKDEKKDTDPEGDNGQGDGGASGNEKEKEKKEKKKRKIRLDMHPEQIFVDGSEAYVWIYDPIPLHYWIFGFILLLGAVGICLFPLWPPLLRKGVYYLSIAAAGFLVFILALTIVRLIVFIIVWALTGGKLHFWIFPNLTEDVSFFASFWPLYESNYNSDPNNSSAKTDKKSKSKDKKKEKESDAEDTAVDADGDADGDVDAEVSTLEPEKIELIKEHDTDMEIRKRRKVGADDYEEDDVDEEETKAQPKDSKAGTPRNSGSDSESSSKDYEIISSSEVQNVAGN
Protein: Coiled-coil domain-containing protein 178 (Q5BJE1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTENKTVSSSSTRDDQTNIGLTCQEVKALREKAWSRTNEGNAMSQSLVLYGASKENSEGFHESKMTNTEGVNKGIYFSYPCRRHSCAVVNIPAPCVNKMISHIQDVESKIQEHLKRFETSFEEWSRTSSTKDLKEDWSVTTPVKEVKPGEKRDEKCPELKQEMETLLSEAIRLIKSLETDRADAEEALKQQRSRKNMINMKIDSWSVWKLQELPLAVQKEHEAYLSDVIELQWHLEDKANQLQHFEKQKTELEEANAKIQADIDYMNEHGPLLDSKQNQELQDLKNHYKKKMEVMDLHRKVNEELEEALEACENARLKAQQIKEEIDKDIYQDEKTIEAYKREIYQLNSLFDHYSSSVINVNTNIEEKEEEVTEAIRETKSSKNELHSLSKMLEDLRRVYDQLTWKQKSHENQYLEAVNDFYAAKKTWDIELSDVAKDFSAISLACTKLTEDNKKLEIDINKITVKTNESIRKKSKYESEIKYLTIMKLKNDKHLKNIYKEAYRIGTLFHLTKHKTDEMEDKIAEVRRKFKGREEFLKKLTQGEVAAGMVLQKKLYSIYEVQALERKELIKNRAICAMSLAELQEPLLQLEDEAERIRSLDKEHSVMLNNIIDQKDLIRRKVGKVKKKLRKKGKKTLDALIETESKRSAIFKDLEATKSKTMIFYAKINELNEELKAKEEEKKSFDQTLEILKNKFITMRFKREHAQTVFDHYMQEKKDCEERIFEEDQRFRVLLAVRQKTLQDTQKIIADSLEENLRLAQEYQQLQITFLKEKDNYFNIYDKQLSLDTSIRDKKQLCQLQRRMHTLWQEHFKLVVLFSQMRLANFQTDSQESIQKILAVQEESSNLMQHILGFFQTLTDGTCENDG
Protein: Damage-control phosphatase SPAC806.04c (EC 3.1.3.-) (Sugar phosphate phosphatase SPAC806.04c) (Q9UT55)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Acid phosphatase
Sequence:
MKFLNPPFPYSMTSDPESFGHECFTRRWGIILTGIEKDVSERLSKLASTSKDSEVVAQGKPLLNDLEAFKSDIKNDRPLVPLEGEGQDIVEYNEELKQLDNASWGNAPWLYSECYYYRRISLIFARYSEWKAYDPFFQQKDSTLKSSRAAVEELAGRYCLLEEELNSIAKKGDSHIAYMVFVEMAQISLWGNATDLSLLTNLSYEELQNLQGQKVVEESQKNILVNDFPTVWSKLKDVHNGRIDFVLDNAGFELYVDLIFAAYLLKAGIAKEIVLHPKDFPWFVSDVLPYDIEYLLTNLDTIFPTESVTKFATDLRSFSAKGQLRLRTDPFWTTAHYFGRMPDFAAGLLTELEKSDMIFFKGDLNYRKLTGDCLWPRTTPFGKTLGPIANAINACALRTCKADVVVGLPDGLYEKIAKDLPHWERTGKYAVVEFCPKA
Protein: 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42) (P62334)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC6 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 4
- Proteasome subunit alpha type-1
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 1
Sequence:
MADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKKLESKLDYKPV
Protein: B3 domain-containing protein At5g18000 (Q9FJG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- Probable U3 small nucleolar RNA-associated protein 11
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Agamous-like MADS-box protein AGL11
- Agamous-like MADS-box protein AGL5
- B3 domain-containing protein REM20
- B3 domain-containing protein REM17
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- AGAMOUS-like 77
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS24y
Sequence:
MVKNKAFFGQIMEERDNPAFFKILRREDHSTEMMRMIPHHLIRSISDKSSSFKMVLRVPWGRSWQVKISKNPNFHYMEDRGWNQFVNDNGLGENEYLTFTHEANMCFNVTIFEADGTEMLRPRKTITSSSGRNKREERKSIYKDVKKEEEIESWSESSHPCHKTAESTSGRLTQKQELNLRKKEADKTEKSKTSKKKKVETVSNDSEAGTSSLIPEFKLTIKKSHLLFLGIPKKFVDMHMPTETTMFKIHYPRGKKSWDVTYVVTDVQSRFSGGWSRLAKELGLLVGDVCTFKLIKPTEMRVKVSKE
Protein: WD repeat-containing protein pop1 (WD repeat-containing protein ste16) (P87060)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in maintenance of ploidy through proteasome dependent degradation of CDK inhibitor rum1 and S-phase initiator cdc18. Functions as a recognition factor for rum1 and cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation. Together with pop2, required for cig2 instability during G2 and M phase and cig2 degradation in exponentially growing cells. Regulates cell-cycle progression under starvation through the rum1 protein.
Subcellular location: Nucleus {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell division control protein 18
- Suppressor of kinetochore protein 1
- RING-box protein pip1
- Cullin-1
- WD repeat-containing protein pop2
- Cyclin-dependent kinase inhibitor rum1
- Ubiquitin-conjugating enzyme E2 4
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 13
- Polyubiquitin
Sequence:
MNEKKKDSLSVLDSNEFFGETTMVSPSIDVSSSPRPNVERFSPCSTKKDLLEGNNIMTRIPEELSRVSLQFDSKGSQQSMIFTNNRCLSDKENLENLQNLLYLHCDLNRPHLSCELPSEHREKCLKRRNSSLSSNLHANKRFLFNSQSDGNKKNETFPSTNYSNVFYPNNCDSKEVASETTFSLDAPNNSVNYSYFSPNLLGNDSKTRQSFPPHSSSSSHNSLHEPVIYDFSSENPSIHPSNHLSSQKNAVLKLAQLISSFEKLPESVRQYLLFHLLSRCGKHAVQNIHKILLPIFQKNFLTGFPAEITNLVLTHLDAPSLCAVSQVSHHWYKLVSSNEELWKSLFLKDGFFWDSIDSKIRTMCLEQSLSACAIMKRVYFRHFNLRERWLHAPEKIKRCSFPIHGVRLITKLQFDDDKIIVSTCSPRINIYDTKTGVLIRSLEEHEGDVWTFEYVGDTLVTGSTDRTVRVWDLRTGECKQVFYGHTSTIRCIKIVQGNQSTTDTDDVEKENRPASNDANSMPPYIISSSRDCTIRLWSLPCLDDPPFVNVNENPDQNNDFTSATTNPFYIRTLRGHTDSVREVACLGDLIVSASYDGTLRVWKASTGVCLHVLRGHVGRVYSVTINPSRQQCISAGTDAKIRIWNLESGELLQTLHGHSNLVSQVTFNQNILVSASAPPDTSLRVWDLNTGSCRDILKCPLGHIFFQHDESKVVSGSHSTLQLWDIRSGKLVRDLLTDLDIIWQVAYNENVCVAAVLRNNRFWIEVLEFGSTKSS
Protein: Epidermal growth factor receptor pathway substrate 15 (A0A8I6GAG1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAAAQLSLTQLSSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKGVLNKQEFFIALRLVACAQNGLEVSLSSLNLAVPPPRFHDSSSPLLTSGTSVAELPWAVKSEDKAKYDAIFDSLSPVDGFLSGDKVKPVLLNSKLPVEILGRVWELSDIDHDGKLDRDEFAVAMFLVYCALEKEPVPMSLPPALVPPSKRKTWVVSPAEKAKYDEIFLKTDKDMDGYVSGLEVRETFLKTGLPSTLLAHIWALCDTKNCGKLSKDQFALAFHLINQKLIKGIDPPHSLTPEMIPPSDKSSLQKNTIGSSPVADFSAIKELDTLNNEIIDLQREKNNVEQDLKEKEDTVRQRTTEAQDLQDEVQRESLNLQKLQAQKQQVQELLDELDEQKAQLEEQLKEVRKKCAEEAQLVRSSPEIAPSDVTDESEVVTAADIEKVSPRFDDDKHSKEEDPFNVESSSLTDAVADTNLDFFQSDPFVGSDPFKDDPFGKIDPFGGDPFKGSDPFASDCFFKQTSTDPFATSSTDPFSASSNSSNTSVETWKHNDPFAPGGTVVAATDSATDPFASVFGNESFGDGFADFSTLSKVSNEDPFNPTISSSASSVVIPKPVLEETPSKSEDVPPALPPKTGTPTRPCPPPPGKRPINKLDSSDPFKLNDPFQPFPGNDSPKEKDPDMFCDPFTSSSTTANKEAEPSNFANFSAYPSEEDMIEWAKRESEREEEQRLARLNQQEQEDLELAIALSKSEISEA