wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock protein 60, mitochondrial (Antigen HIS-62) (P50142)
Organism: Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Function: May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins.
Subcellular location: Mitochondrion.
Interaction partners:
Sequence:
MQRALSSTSRASVLSSAPTRAPVSRFRSAGLSLQQQRFAHKELKFGVEGRAALLKGIDTLAKAVCTTLGPKGRNVLIESSYGSPKITKDGVTVAKAVTLQDKFENLGARLLQDVASKTNEVAGDGTTTATVLARAIFSETVKNVAAGCNPMDLRRGIQAAVEAVVEYLQANKRDITTTEEIAQVATISANGDTHVGKLISNAMEKVGKEGVITVKDGKTIEDELEVTEGMRFDRGYVSPYFITDTKAQKVEFEKPLIVLSEKKISAVQDIIPALEASTTLRRPLVIIAEDIEGEALAVCILNKLRGQLQVAAVKVPGFGDNRKSILGDIGILTNATVFTDELDMKLEKATADMLGSTGSITITKEDTIILNGDGSKDSIAQRCEQIRGVIADPTTSDYEKEKLQERLAKLSGGVAVIKVGGASEVEVGEKKDRVVDALNATRAAVEEGILPGGGTALLKAAANGLASVKPTSSDQLRRISSLVSAITRPARTIVENAGLEGSVIVGKLTDEHASDFNRGFDSAKGEYVDMIASGIVDPLKVVRTALVDASGVASLLGTTEVAIVEAPEEKGPAGPPGGMGGMGGMGGGMF
Protein: Small ribosomal subunit protein uS7 (40S ribosomal protein S5) (Q54MA6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P97461}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P46782}.
Interaction partners:
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein uS3
- Uncharacterized protein
Sequence:
MTSEVALFGKWSYSGVTCPDISLQDYICVKKNVFTPHSAGRYNKVRFRKAQCPIVERLANSMMMFGRNAGKKVMAVRIIEQAFEIIYLLTDKNPLQVLVEAVMNSGPREDSTRIGSAGTVRRQAVDVSPMRRVNHAVYLLTQGTRAAAFRNIRTVAECLADELINASKGSPNSYSIKQKDALERTAKSHR
Protein: LIM homeodomain (O42108)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- LIM domain-binding protein 1
- Homeobox protein SIX3
- Forkhead box protein G1
- Homeobox protein SIX6
- Sonic hedgehog protein
- Empty spiracles homeobox 2.
Sequence:
MLFHSLSGSEMHGVIDEMDRRTKTEAAAISSAIDRGETETQTMPSISSDRAALCAGCGGKISDRYYLLAVDKQWHMRCLKCCECKLNLESELTCFSKDGSIYCKEDYYRRFSVQRCARCHLGISASEMVMRARDLVYHLNCFTCTTCNKMLTTGDHFGMKDNLVYCRLHFETLIQGEYQVHFNHSDVAAGKGPALGAGSANTLGLPYYNGVGTVQKGRPRKRKSPGPGADLAAYNAALSCNENDGDHLDRDQQYPSNQKTKRMRTSFKHHQLRTMKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNLLRQENTGVDKTSDSTLQAGTPSGPASEISNASMSPSSTPTTLTDLTNPTMPTVTSVLTSVPGSLEVHESRSPSQTTLTNLF
Protein: Exodeoxyribonuclease III (EXO III) (Exonuclease III) (EC 3.1.11.2) (AP endonuclease VI) (P09030)
Organism: Escherichia coli (strain K12)
Function: Major apurinic-apyrimidinic endonuclease of E.coli. It removes the damaged DNA at cytosines and guanines by cleaving on the 3'-side of the AP site by a beta-elimination reaction. It exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair diesterase and ribonuclease H activities.
Interaction partners:
- Endonuclease III lyase)
- Endonuclease 4
- Adenine DNA glycosylase
- Uracil-DNA glycosylase
- DNA polymerase I
- DNA-3-methyladenine glycosylase 2
- DNA polymerase II
- Formamidopyrimidine-DNA glycosylase
- Flap endonuclease Xni
- Beta sliding clamp
Sequence:
MKFVSFNINGLRARPHQLEAIVEKHQPDVIGLQETKVHDDMFPLEEVAKLGYNVFYHGQKGHYGVALLTKETPIAVRRGFPGDDEEAQRRIIMAEIPSLLGNVTVINGYFPQGESRDHPIKFPAKAQFYQNLQNYLETELKRDNPVLIMGDMNISPTDLDIGIGEENRKRWLRTGKCSFLPEEREWMDRLMSWGLVDTFRHANPQTADRFSWFDYRSKGFDDNRGLRIDLLLASQPLAECCVETGIDYEIRSMEKPSDHAPVWATFRR
Protein: DNA mismatch repair protein (A0A2R8Y6P0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005813}.
Interaction partners:
Sequence:
MAVQPKETLQLESAAEVGFVRFFQGMPEKPTTTVRLFDRGDFYTAHGEDALLAAREVFKTQGVIKYMGPAGAKNLQSVVLSKMNFESFVKDLLLVRQYRVEVYKNRAGNKASKENDWYLAYKASPGNLSQFEDILFGNNDMSASIGVVGVKMSAVDGQRQVGVGYVDSIQRKLGLCEFPDNDQFSNLEALLIQIGPKECVLPGGETAGDMGKLRQIIQRGGILITERKKADFSTKDIYQDLNRLLKGKKGEQMNSAVLPEMENQVAVSSLSAVIKFLELLSDDSNFGQFELTTFDFSQYMKLDIAAVRALNLFQGSVEDTTGSQSLAALLNKCKTPQGQRLVNQWIKQPLMDKNRIEERLNLVEAFVEDAELRQTLQEDLLRRFPDLNRLAKKFQRQAANLQDCYRLYQGINQLPNVIQALEKHEGKHQKLLLAVFVTPLTDLRSDFSKFQEMIETTLDMDQVENHEFLVKPSFDPNLSELREIMNDLEKKMQSTLISAARDLGLDPGKQIKLDSSAQFGYYFRVTCKEEKVLRNNKNFSTVDIQKNGVKFTNSKLTSLNEEYTKNKTEYEEAQDAIVKEIVNISSGYVEPMQTLNDVLAQLDAVVSFAHVSNGAPVPYVRPAILEKGQGRIILKASRHACVEVQDEIAFIPNDVYFEKDKQMFHIITGPNMGGKSTYIRQTGVIVLMAQIGCFVPCESAEVSIVDCILARVGAGDSQLKGVSTFMAEMLETASILRSATKDSLIIIDELGRGTSTYDGFGLAWAISEYIATKIGAFCMFATHFHELTALANQIPTVNNLHVTALTTEETLTMLYQVKKGVCDQSFGIHVAELANFPKHVIECAKQKALELEEFQYIGESQGYDIMEPAAKKCYLERENLRVTEPKDQCLILLTWKRKLRGGKRSACSRPERQNQGSATPSASA
Protein: Uncharacterized protein (Q383T8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Heat shock protein 83
- Heat shock protein, mitochondrial, putative
Sequence:
MSTGESAELHEPTMGPIKYVFIPVEETREPKELLFAGGSDEEFRGSITQYFRQKLLSQEQKNEMTKHLVQKASESGNRGDDTAPPQVSAQQQNELISEYLEQTSFEIVPIVMPARDNKFVGTSLYIDDSGRFKDLPLNCRASKIAQRDIRGDAFLLSNHDDPALDEWGRVDCSLSTYNELLANPPTTKYDASDRAQMASLTMQRESETKCISEVDVSKAKEAKEAGNKFFTEGDIKAAVQAYSECADLTEGRRDLLPNEAEVTSLRVSALLNRSLCLYRLGKNDDAAHDARAVLQIDAKNLKAHHHLTKALCGSRDYDEAAKSLEAYEKLGGQPQDIAQIRQSIVEGKKRLMQEEKNKYAKMFAST
Protein: Myosin, heavy polypeptide 13, skeletal muscle (B1AR69)
Organism: Mus musculus (Mouse)
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin light chain 3
- Myosin light chain 6B
- Myosin light polypeptide 6
- Myosin light chain 4
- Myosin regulatory light polypeptide 9
- Myosin-2
- Myosin-1
- Titin
- Myosin, light chain 12A, regulatory, non-sarcomeric
Sequence:
MSSDAEMAIFGEAAPYLRKPEKERIEAQNRPFDSKKACFAVDDKEMYVKGMIQSRENDKVIVKTLDDRELTLNSDQVFPMNPPKFDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDILGFSPEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPTKGKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSAGGKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQFRFGHTKVFFKAGLLGLLEEMRDEKLVTLMTRTQAVCRGYLMRVEFKKMMERRESIFCIQYNVRSFMNVKHWPWMNLFFKIKPLLKSAEAEKEMATMKEDFERAKEDLARSEARRKELEEKMVSLLQEKNDLQLQVQSETENLMDAEERCEGLIKSKIQLEAKVKELNERLEEEEEMNSELVAKKRNLEDKCSSLKRDIDDLELTLTKVEKEKHATENKVKNLSEEMTALEETISKLTKEKKSLQEAHQQTLDDLQVEEDKVNGLIKINVKLEQQTDDLEGSLEQEKKLRADLERVKRKLEGDLKMSQESIMDLENDTQQLEEKLKKKEFEMSQLQTRIDDEQVLSLQLQKKIKELQARTEELEEEIEAEHTVRAKIEKQRSDLARELEEISERLEEASGATSAQIEMNKKRESEFQKLRRDLEEATLQHEATAATLRKKHADTVAELGEQIDNLQRVKQKLEKEKSELKMEIDDMASNIETVSKSKSNMERMCRSVEDQFNEIKAKDDQQTQLIHDLNMQKARLQTQNGELSHQVEEKESLVSQLTKSKQALTQQLEELKRQLEEETKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEENTEASNSKCASLEKTKQRLQGEVDDLMLDLERANTACATLDKKQRNFDKVLAEWKQKLDESQAELEAAQKESRSLSTEIFKMRNAYEEVVDQLETLRRENKNLQEEISDLTEQIAETGKNLQEVEKTKKQVEQEKSDLQAALEEVEGSLEHEESKILRVQLELSQVKSELDRKVTEKDEEIEQIKRNSQRAVEAMQSVLDAEIRSRNDALRLKKKMEGDLNEMEIQLSHANRQVAETQKHLRTVQGQLKDSQLHLDDAQRSNEDLKEQLAIVERRNGLLQEELEEMKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKMEE
Protein: 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform D (EC 2.3.-.-, EC 2.3.1.51) (GEO04450p1) (GH25976p) (Q961F9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSLLHGKSVEPHLLMRRIPLEQVPEDEKEAAAWLQNLFVEKDKIIDSFLETGSFFKTSGIKEVPAYVNKRRLCSLVNFVCWAVFSLSCIFYYVITSLLAANWTAFITALSVLGLFYWLMGQAINKTQISKASNYGSSKSVAK
Protein: PHD finger protein 23 (PDH-containing protein JUNE-1) (Q9BUL5)
Organism: Homo sapiens (Human)
Function: Acts as a negative regulator of autophagy, through promoting ubiquitination and degradation of LRSAM1, an E3 ubiquitin ligase that promotes autophagy in response to starvation or infecting bacteria.
Subcellular location: Nucleus {ECO:0000269|PubMed:25484098}. Cytoplasm {ECO:0000269|PubMed:25484098}. Note=Mainly present in the nucleus and part in the cytoplasm. {ECO:0000269|PubMed:25484098}.
Interaction partners:
- Nuclear pore complex protein Nup98-Nup96
- Lysine-specific demethylase 5A
- Sin3 histone deacetylase corepressor complex component SDS3
- Paired amphipathic helix protein Sin3b
- Paired amphipathic helix protein Sin3a
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
Sequence:
MLEAMAEPSPEDPPPTLKPETQPPEKRRRTIEDFNKFCSFVLAYAGYIPPSKEESDWPASGSSSPLRGESAADSDGWDSAPSDLRTIQTFVKKAKSSKRRAAQAGPTQPGPPRSTFSRLQAPDSATLLEKMKLKDSLFDLDGPKVASPLSPTSLTHTSRPPAALTPVPLSQGDLSHPPRKKDRKNRKLGPGAGAGFGVLRRPRPTPGDGEKRSRIKKSKKRKLKKAERGDRLPPPGPPQAPPSDTDSEEEEEEEEEEEEEEMATVVGGEAPVPVLPTPPEAPRPPATVHPEGVPPADSESKEVGSTETSQDGDASSSEGEMRVMDEDIMVESGDDSWDLITCYCRKPFAGRPMIECSLCGTWIHLSCAKIKKTNVPDFFYCQKCKELRPEARRLGGPPKSGEP
Protein: V-type proton ATPase subunit H (A0A8I5ZQ24)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRCSEEKQEMLQTEGSQCAKTFINLMTHISKEQTVQYILTMVDDMLQENHQRVSIFFDYAKRSKSTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTISASDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS
Protein: Transcription termination factor MTEF1, chloroplastic (Mitochondrial transcription termination factor 1) (Protein EMBRYO DEFECTIVE 93) (Protein SINGLET OXYGEN-LINKED DEATH ACTIVATOR 10) (Q84X53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription termination factor required for plastid-specific rRNA accumulation and protein synthesis in plastids. Essential for embryogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19563435, ECO:0000269|PubMed:21464319}.
Interaction partners:
- Transcription termination factor MTEF18, mitochondrial
- Holliday junction resolvase MOC1, chloroplastic
- Mitochondrial transcription termination factor family protein
- Mitochondrial transcription termination factor family protein
- Mitochondrial transcription termination factor-related / mTERF-like protein
- RNA polymerase sigma factor sigF, chloroplastic
Sequence:
MMIARCSLFPPPCFSAVRIRCFAGETSDTGILFREKLIYLQDLNVDPHKALRVNPSLRSAPISSVVSVETLLSSTGLSRPAVGRILDMFPDLLTSDPESEILPVLRFLSNEISISEQDIPKSISRCPRLLISSVDYQLRPALTFLKTLGFVGRDTITSRNTVLLVSNVERTLIPKIEYLEEGLGFTREEVAKMVVRSPALLTYSVDNNLVPKVEFFIEEMRGDVKELKRFPQYFSFSLERKIKPRHRLLKEHGILMPLSEMLKVSDGQFNHWLLELRLRSAERR
Protein: Citrate lyase subunit beta-like protein (EC 4.1.-.-) (P9WPE1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May play a role in fatty acid biosynthesis.
Interaction partners:
- Possible oxidase regulatory-related protein
- Possible acyl-CoA dehydrogenase FadE19
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase beta1 subunit
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit A
- Conserved protein
- Probable succinyl-CoA:3-ketoacid coenzyme A transferase subunit B
- Probable transcriptional regulatory protein
- Dihydrolipoyllysine-residue acyltransferase component of branched-chain alpha-ketoacid dehydrogenase complex
- Long-chain-fatty-acid--CoA ligase FadD13
Sequence:
MNLRAAGPGWLFCPADRPERFAKAAAAADVVILDLEDGVAEAQKPAARNALRDTPLDPERTVVRINAGGTADQARDLEALAGTAYTTVMLPKAESAAQVIELAPRDVIALVETARGAVCAAEIAAADPTVGMMWGAEDLIATLGGSSSRRADGAYRDVARHVRSTILLAASAFGRLALDAVHLDILDVEGLQEEARDAAAVGFDVTVCIHPSQIPVVRKAYRPSHEKLAWARRVLAASRSERGAFAFEGQMVDSPVLTHAETMLRRAGEATSE
Protein: H-N-H endonuclease F-TflI (EC 3.1.21.-) (HNH endodeoxyribonuclease F-TflI) (HNH endonuclease F-TflI) (Q6QGM3)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Endonuclease that cleaves only one strand of asymmetric DNA substrates thereby introducing interruptions into the template or coding strand.
Interaction partners:
Sequence:
MQFVPIKDAPGYLVNEAGDVFSTFTNKVLSRYIVDGYPAVKLQINGKQTSVLIHRIISHVFGDLYNLFDPELEVDHKDRDRLNLSKDNLQVLSKIEHQRKTNKDNGWSDSRVPCPLCGSLMLQRSVTCTNCKPKPTGRLIKPELSLDDITEKVLLMGWVKAAKELEVSESTLRRRYTKLTGLSPKVLTEQRKSK
Protein: Alpha-mannosidase 2 (EC 3.2.1.114) (Golgi alpha-mannosidase II) (AMan II) (AtGMII) (Man II) (Protein hybrid glycosylation 1) (Q9LFR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. Converts GlcNAcMan(5)GlcNAc(2) (Man5Gn) into GlcNAcMan(3)GlcNAc(2) (MGn) by sequential removal of two alpha1,6- and alpha1,3-linked mannose residues from the alpha1,6-mannose branch of the substrate. To a lesser extent, also able to cleave beta1,2-xylosylated Man5Gn-glycopeptide (Man5GnX-GP) and pyridylaminated substrates Man5Gn-PA and Man5GnX-PA, but not active toward Man5-glycopeptide. Required for resistance to salt stress.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16460512}; Single-pass type II membrane protein {ECO:0000269|PubMed:16460512}.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Beta-1,3-galactosyltransferase GALT1
- Beta-1,2-xylosyltransferase
- Glycoprotein 3-alpha-L-fucosyltransferase A
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2
- Putative fucosyltransferase-like protein
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
Sequence:
MPFSSYIGNSRRSSTGGGTGGWGQSLLPTALSKSKLAINRKPRKRTLVVNFIFANFFVIALTVSLLFFLLTLFHFGVPGPISSRFLTSRSNRIVKPRKNINRRPLNDSNSGAVVDITTKDLYDRIEFLDTDGGPWKQGWRVTYKDDEWEKEKLKIFVVPHSHNDPGWKLTVEEYYQRQSRHILDTIVETLSKDSRRKFIWEEMSYLERWWRDASPNKQEALTKLVKDGQLEIVGGGWVMNDEANSHYFAIIEQIAEGNMWLNDTIGVIPKNSWAIDPFGYSSTMAYLLRRMGFENMLIQRTHYELKKDLAQHKNLEYIWRQSWDAMETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARMRGFKYELCPWGKHPVETTLENVQERALKLLDQYRKKSTLYRTNTLLIPLGDDFRYISIDEAEAQFRNYQMLFDHINSNPSLNAEAKFGTLEDYFRTVREEADRVNYSRPGEVGSGQVVGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEHTLRGAEIMMSFLLGYCHRIQCEKFPTSFTYKLTAARRNLALFQHHDGVTGTAKDYVVQDYGTRMHTSLQDLQIFMSKAIEVLLGIRHEKEKSDQSPSFFEAEQMRSKYDARPVHKPIAAREGNSHTVILFNPSEQTREEVVTVVVNRAEISVLDSNWTCVPSQISPEVQHDDTKLFTGRHRLYWKASIPALGLRTYFIANGNVECEKATPSKLKYASEFDPFPCPPPYSCSKLDNDVTEIRNEHQTLVFDVKNGSLRKIVHRNGSETVVGEEIGMYSSPESGAYLFKPDGEAQPIVQPDGHVVTSEGLLVQEVFSYPKTKWEKSPLSQKTRLYTGGNTLQDQVVEIEYHVELLGNDFDDRELIVRYKTDVDNKKVFYSDLNGFQMSRRETYDKIPLQGNYYPMPSLAFIQGSNGQRFSVHSRQSLGVASLKEGWLEIMLDRRLVRDDGRGLGQGVMDNRAMTVVFHLLAESNISQADPASNTNPRNPSLLSHLIGAHLNYPINTFIAKKPQDISVRVPQYGSFAPLAKPLPCDLHIVNFKVPRPSKYSQQLEEDKPRFALILNRRAWDSAYCHKGRQVNCTSMANEPVNFSDMFKDLAASKVKPTSLNLLQEDMEILGYDDQELPRDSSQPREGRVSISPMEIRAYKLELRPHK
Protein: Transcription factor AP4 (A0A2R8W6R9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQSINAGFQSLKTLIPHTDGEKLSKAAILQQTAEYIFSLEQEKTRLLQQNTQLKRFIQELSGSSPKRRRAEDKDEGIGSPDIWEDEKAEDLRREMIELRQQLDKERSVRMMLEEQVRSLEAHMYPEKLKVIAQQVQLQQQQEQVRLLHQEKLEREQQHLRTQLLPPPAPTHHPTVIVPAPAPPSSHHINVVTMGPSSVI
Protein: Signal recognition particle subunit SRP14 (Signal recognition particle 14 kDa protein homolog) (P38985)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP14 binds scR1 RNA to form the probable Alu domain of SRP responsible for elongation arrest.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:11352936}.
Interaction partners:
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP21
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SEC65
- Signal recognition particle subunit SRP68
- Signal recognition particle receptor subunit beta
- Signal recognition particle receptor subunit alpha homolog
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL30
Sequence:
MANTGCLSPGAFLSKVPEFFQTANEKHITVRLTAKRLIEHDPVEGNLEFDSTNHPDYDVSKKASEISVSSRSDREYPLLIRMSYGSHDKKTKCSTVVKASELDQFWQEYSSVFKGGMQNLIKKKKKKSKNGTISKTGKKNKVAKKN
Protein: Docking protein 2 (Downstream of tyrosine kinase 2) (p56(dok-2)) (O60496)
Organism: Homo sapiens (Human)
Function: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP kinase activation (By similarity).
Interaction partners:
- Ras GTPase-activating protein 1
- Cell surface glycoprotein CD200 receptor 1
- SH2/SH3 adapter protein NCK1
- Tyrosine-protein kinase Lck
- Angiopoietin-1 receptor
- SHC-transforming protein 1
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
- Tyrosine-protein kinase CSK
- Tyrosine-protein kinase Fyn
- Tyrosine-protein kinase ABL1
Sequence:
MGDGAVKQGFLYLQQQQTFGKKWRRFGASLYGGSDCALARLELQEGPEKPRRCEAARKVIRLSDCLRVAEAGGEASSPRDTSAFFLETKERLYLLAAPAAERGDWVQAICLLAFPGQRKELSGPEGKQSRPCMEENELYSSAVTVGPHKEFAVTMRPTEASERCHLRGSYTLRAGESALELWGGPEPGTQLYDWPYRFLRRFGRDKVTFSFEAGRRCVSGEGNFEFETRQGNEIFLALEEAISAQKNAAPATPQPQPATIPASLPRPDSPYSRPHDSLPPPSPTTPVPAPRPRGQEGEYAVPFDAVARSLGKNFRGILAVPPQLLADPLYDSIEETLPPRPDHIYDEPEGVAALSLYDSPQEPRGEAWRRQATADRDPAGLQHVQPAGQDFSASGWQPGTEYDNVVLKKGPK
Protein: Alpha-soluble NSF attachment protein 1 (Alpha-SNAP1) (N-ethylmaleimide-sensitive factor attachment protein alpha 1) (Q9LXZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Binds to SNARE complex and then recruits NSF to disassemble it (By similarity).
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vesicle-fusing ATPase
- Syntaxin-32
- Syntaxin-31
- VAMP-like protein YKT61
- Gamma-soluble NSF attachment protein
- VAMP-like protein YKT62
- Vesicle transport v-SNARE family protein
- Vesicle transport v-SNARE 13
- Vesicle transport v-SNARE 12
- Vesicle transport v-SNARE 11
Sequence:
MFFVKGEGFFYPLFIELRNLIRYQTTRVSNSSRDFNLSQQHCSCFRPKRRHEAHLSFIGTLQYSKQRTITRAASATIARRQLLLLFDITFSSSSSCYYFQKKAEKKLNRRRRFDTKYEDAADLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSLANTYMIMDECMDHEIAEYYESDEMFEQAIAYYETAAEFFQIEEVTTSANQCNLKVAQYASQLEQQSRFMKTQARHSLNNKLLKYGVKGHLLTAGMCHLCKADVVSITNALEKYQDLDPTFSGTRECKFLADLASAIDEEDIAKFTDVSKEIDSVSPLVWAVNHMQLFGCKLCLVLDHDNNVVEGKREVQGQGAGGGCKLYLIEGKCILDWNNVYTKRIYNYTNF
Protein: Transcobalamin-2 (TC-2) (Transcobalamin II) (TC II) (TCII) (O88968)
Organism: Mus musculus (Mouse)
Function: Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P20062}.
Interaction partners:
- CD320 antigen
- Low-density lipoprotein receptor-related protein 2
- Lactotransferrin
- E3 ubiquitin-protein ligase CBL
Sequence:
MELLKALLLLSGVFGALAEFCVIPRIDSQLVEKLGQRLLPWMDRLSSEQLNPSVFVGLRLSSMQAGTKEDLYLHSLKIHYQQCLLRSTSSDDNSSCQPKLSGGSLALYLLALRANCEFFGSRKGDRLISQLKWFLEDEKKAIGHNHEGHPNTNYYQYGLSILALCVHQKRLHDSVVGKLLYAVEHDYFTYQGHVSVDTEAMAGLALTCLERFNFNSDLRPRITMAIETVREKILKSQAPEGYFGNIYSTPLALQMLMTSPASGVGLGTACIKAGTSLLLSLQDGAFQNPLMISQLLPILNHKTYLDLIFPDCQASRVMLVPAVEDPVHISEVISVTLKVASALSPYEQTFFVFAGSSLEDVLKLAQDGGGFTYGTQASLSGPYLTSVLGKDAGDREYWQLLRAPDTPLLQGIADYKPQDGETIELRLVRW
Protein: Complex I assembly factor TMEM126B, mitochondrial (Transmembrane protein 126B) (Q9D1R1)
Organism: Mus musculus (Mouse)
Function: As part of the MCIA complex, involved in the assembly of the mitochondrial complex I. Participates in constructing the membrane arm of complex I.
Subcellular location: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Complex I intermediate-associated protein 30, mitochondrial
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Complex I assembly factor ACAD9, mitochondrial
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Transmembrane protein 186
- FAD-dependent oxidoreductase domain-containing protein 1
- NADH-ubiquinone oxidoreductase chain 2
- YjeF N-terminal domain-containing protein 3
- NADH dehydrogenase 1 alpha subcomplex assembly factor 2
Sequence:
MAASQRPSWSESKVAGVVQEGNREAPQDIKMALYKHGQLIPSLGDAKFRSPIISEIIEKKFEHYRNDKTLNIHGTLVFGTSSSLSGIMANLVFRNSFKVKYEALKTYASLTTLPVLATIVSYKLFVTDALQSGDISKESCVLRSALIGMACGVSYPSALAFYKNGRLAVKYQTVPLPPKGRVMLHWLLLCQTGMKAMAIPLFFQIVMGAFTGLHHYNICEKPRARLVPDD
Protein: BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like (Adenovirus E1B19K-binding protein B5) (BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A) (NIP3-like protein X) (NIP3L) (O60238)
Organism: Homo sapiens (Human)
Function: Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.
Subcellular location: Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Colocalizes with SPATA18 at the mitochondrion outer membrane.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GABA type A receptor associated protein like 1
- Apoptosis regulator Bcl-2
- Metalloreductase STEAP3
- GTP-binding protein Rheb
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- FUN14 domain-containing protein 1
- Bcl-2-like protein 1
- Microtubule-associated protein 1A
Sequence:
MSSHLVEPPPPLHNNNNNCEENEQSLPPPAGLNSSWVELPMNSSNGNDNGNGKNGGLEHVPSSSSIHNGDMEKILLDAQHESGQSSSRGSSHCDSPSPQEDGQIMFDVEMHTSRDHSSQSEEEVVEGEKEVEALKKSADWVSDWSSRPENIPPKEFHFRHPKRSVSLSMRKSGAMKKGGIFSAEFLKVFIPSLFLSHVLALGLGIYIGKRLSTPSASTY
Protein: cAMP-dependent protein kinase inhibitor alpha (PKI-alpha) (cAMP-dependent protein kinase inhibitor, muscle/brain isoform) (P61925)
Organism: Homo sapiens (Human)
Function: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase inhibitor gamma
- cAMP-dependent protein kinase catalytic subunit gamma
- Exportin-1
- Adenosine deaminase
Sequence:
MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES