wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock protein beta-7 (HspB7) (Cardiovascular heat shock protein) (cvHsp) (Q9UBY9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Nucleus, Cajal body {ECO:0000269|PubMed:19464326}. Note=Resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Interaction partners:
- Filamin-A
- Heat shock protein beta-8
- Filamin-C
- BAG family molecular chaperone regulator 3
- Heat shock protein beta-9
- Heat shock protein beta-3
Sequence:
MSHRTSSTFRAERSFHSSSSSSSSSTSSSASRALPAQDPPMEKALSMFSDDFGSFMRPHSEPLAFPARPGGAGNIKTLGDAYEFAVDVRDFSPEDIIVTTSNNHIEVRAEKLAADGTVMNTFAHKCQLPEDVDPTSVTSALREDGSLTIRARRHPHTEHVQQTFRTEIKI
Protein: Leucine-rich repeat protein (LRRP) (Q383Z2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MENVVMEAGEGGSKSNAPQNDDASVMNALYEPPPPLASDGVDDAFIGMALEECSLRDVYSYSCHRFGVRPNENILRQLPPVAGDEWVRKIKVLDFSAVYLGGKGCLSLVPIIERCTEATHLMMPNVGLTHEAAAPLFEVMRYHPSVSWMDVSKNRLNDDVGRWILNAVIENPRIRFVLLRDAGISPPLLQKIENRLHERMYGTVEAITPSIRVTYAEGFSQLFESSLGTGANDTARVPVHYVPPSVAAGLVELRHQLYRNAESMRCVYNCFTHNLTPESGGCASDAGTDAEELPETNSEAGFGAPHPDRCSWRSFFCGLRLLGVRAVCKSLEDSVAFANLCGICNVETVLFGKLIQLLRPHVAIKDEMTPESPPVRGNTIPNQFADVSPPLDVQQGASMDAEEIPSRDLSGNMRAATPEMGKPQADTPSVPTQEAARMASEARCSPLTLRPLHCTLHEKRSSLGPSLLDTFVTTPSIAGVHASGPLEARLRLDRTFDSRNKQTVVDQLYDERVTLSEVFKKTGGEDPDASAPSYLVDIDEVIKHAVSRVGESNREIVKSLVEPWAVGVEDRVLVNTEGWLSSMYVPQLEASTLMPFSFSEEKLIWAGVTVEELRESVDLW
Protein: LL-diaminopimelate aminotransferase, chloroplastic (AtDAP-AT) (DAP-AT) (DAP-aminotransferase) (LL-DAP-aminotransferase) (EC 2.6.1.83) (Protein ABERRANT GROWTH AND DEATH 2) (Q93ZN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for lysine biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli. Not active with meso-diaminopimelate, lysine or ornithine as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:14729919}.
Interaction partners:
- Diaminopimelate epimerase, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic
- Diaminopimelate decarboxylase 1, chloroplastic
- Diaminopimelate decarboxylase 2, chloroplastic
- Aminotransferase ALD1, chloroplastic
- Biotin synthase, mitochondrial
- Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic
- aspartate-semialdehyde dehydrogenase
Sequence:
MSSTHQLVSSMISSSSSTFLAPSNFNLRTRNACLPMAKRVNTCKCVATPQEKIEYKTKVSRNSNMSKLQAGYLFPEIARRRSAHLLKYPDAQVISLGIGDTTEPIPEVITSAMAKKAHELSTIEGYSGYGAEQGAKPLRAAIAKTFYGGLGIGDDDVFVSDGAKCDISRLQVMFGSNVTIAVQDPSYPAYVDSSVIMGQTGQFNTDVQKYGNIEYMRCTPENGFFPDLSTVGRTDIIFFCSPNNPTGAAATREQLTQLVEFAKKNGSIIVYDSAYAMYMSDDNPRSIFEIPGAEEVAMETASFSKYAGFTGVRLGWTVIPKKLLYSDGFPVAKDFNRIICTCFNGASNISQAGALACLTPEGLEAMHKVIGFYKENTNIIIDTFTSLGYDVYGGKNAPYVWVHFPNQSSWDVFAEILEKTHVVTTPGSGFGPGGEGFVRVSAFGHRENILEACRRFKQLYK
Protein: NAD-specific glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) (NAD(+)-dependent glutamate dehydrogenase) (O53203)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible conversion of L-glutamate to 2-oxoglutarate.
Interaction partners:
- Glutamate synthase large chain
- Conserved protein
- Glutamine synthetase
- Glutamate decarboxylase
- Probable glutamine synthetase GlnA4
- Glycogen accumulation regulator GarA
- Alanine aminotransferase
- Glutamine synthetase
- Probable glutamine synthetase GlnA3
- Probable glycine dehydrogenase
Sequence:
MTIDPGAKQDVEAWTTFTASADIPDWISKAYIDSYRGPRDDSSEATKAAEASWLPASLLTPAMLGAHYRLGRHRAAGESCVAVYRADDPAGFGPALQVVAEHGGMLMDSVTVLLHRLGIAYAAILTPVFDVHRSPTGELLRIEPKAEGTSPHLGEAWMHVALSPAVDHKGLAEVERLLPKVLADVQRVATDATALIATLSELAGEVESNAGGRFSAPDRQDVGELLRWLGDGNFLLLGYQRCRVADGMVYGEGSSGMGVLRGRTGSRPRLTDDDKLLVLAQARVGSYLRYGAYPYAIAVREYVDGSVVEHRFVGLFSVAAMNADVLEIPTISRRVREALAMAESDPSHPGQLLLDVIQTVPRPELFTLSAQRLLTMARAVVDLGSQRQALLFLRADRLQYFVSCLVYMPRDRYTTAVRMQFEDILVREFGGTRLEFTARVSESPWALMHFMVRLPEVGVAGEGAAAPPVDVSEANRIRIQGLLTEAARTWADRLIGAAAAAGSVGQADAMHYAAAFSEAYKQAVTPADAIGDIAVITELTDDSVKLVFSERDEQGVAQLTWFLGGRTASLSQLLPMLQSMGVVVLEERPFSVTRPDGLPVWIYQFKISPHPTIPLAPTVAERAATAHRFAEAVTAIWHGRVEIDRFNELVMRAGLTWQQVVLLRAYAKYLRQAGFPYSQSYIESVLNEHPATVRSLVDLFEALFVPVPSGSASNRDAQAAAAAVAADIDALVSLDTDRILRAFASLVQATLRTNYFVTRQGSARCRDVLALKLNAQLIDELPLPRPRYEIFVYSPRVEGVHLRFGPVARGGLRWSDRRDDFRTEILGLVKAQAVKNAVIVPVGAKGGFVVKRPPLPTGDPAADRDATRAEGVACYQLFISGLLDVTDNVDHATASVNPPPEVVRRDGDDAYLVVAADKGTATFSDIANDVAKSYGFWLGDAFASGGSVGYDHKAMGITARGAWEAVKRHFREIGIDTQTQDFTVVGIGDMSGDVFGNGMLLSKHIRLIAAFDHRHIFLDPNPDAAVSWAERRRMFELPRSSWSDYDRSLISEGGGVYSREQKAIPLSAQVRAVLGIDGSVDGGAAEMAPPNLIRAILRAPVDLLFNGGIGTYIKAESESDADVGDRANDPVRVNANQVRAKVIGEGGNLGVTALGRVEFDLSGGRINTDALDNSAGVDCSDHEVNIKILIDSLVSAGTVKADERTQLLESMTDEVAQLVLADNEDQNDLMGTSRANAASLLPVHAMQIKYLVAERGVNRELEALPSEKEIARRSEAGIGLTSPELATLMAHVKLGLKEEVLATELPDQDVFASRLPRYFPTALRERFTPEIRSHQLRREIVTTMLINDLVDTAGITYAFRIAEDVGVTPIDAVRTYVATDAIFGVGHIWRRIRAANLPIALSDRLTLDTRRLIDRAGRWLLNYRPQPLAVGAEINRFAAMVKALTPRMSEWLRGDDKAIVEKTAAEFASQGVPEDLAYRVSTGLYRYSLLDIIDIADIADIDAAEVADTYFALMDRLGTDGLLTAVSQLPRHDRWHSLARLAIRDDIYGALRSLCFDVLAVGEPGESSEQKIAEWEHLSASRVARARRTLDDIRASGQKDLATLSVAARQIRRMTRTSGRGISG
Protein: C-X-C motif chemokine 17 (6-Cys CXCL17) (Dendritic cell and monocyte chemokine-like protein) (DMC) (VEGF coregulated chemokine 1) [Cleaved into: 4-Cys CXCL17] (Q6UXB2)
Organism: Homo sapiens (Human)
Function: Chemokine that acts as chemoattractant for monocytes, macrophages and dendritic cells. Plays a role in angiogenesis and possibly in the development of tumors. Acts as an anti-inflammatory in the stomach. May play a role in the innate defense against infections. Activates the C-X-C chemokine receptor GPR35 to induce a rapid and transient rise in the level of intracellular calcium ions.
Subcellular location: Secreted {ECO:0000269|PubMed:23115081}.
Interaction partners:
- C-C motif chemokine 17
- C-C motif chemokine 20
- C-X-C motif chemokine 14
- C-C motif chemokine 25
- C-C motif chemokine 5
- C-C motif chemokine 2
- C-X-C motif chemokine 9
- C-X-C motif chemokine 10
- Stromal cell-derived factor 1
- C-C motif chemokine 8
Sequence:
MKVLISSLLLLLPLMLMSMVSSSLNPGVARGHRDRGQASRRWLQEGGQECECKDWFLRAPRRKFMTVSGLPKKQCPCDHFKGNVKKTRHQRHHRKPNKHSRACQQFLKQCQLRSFALPL
Protein: Sterol 14-demethylase (EC 1.14.14.154) (Cytochrome P450 51A2) (Cytochrome P450 51G1) (AtCYP51) (Obtusifoliol 14-demethylase) (Protein EMBRYO DEFECTIVE 1738) (Q9SAA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in sterol biosynthesis. Catalyzes the 14-alpha demethylation of obtusifoliol to 4 alpha-methyl-5 alpha-ergosta-8,14,24(28)-trien-3 beta-ol.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Delta
- Lanosterol synthase
- Cycloeucalenol cycloisomerase
- Delta
- 7-dehydrocholesterol reductase
- Methylsterol monooxygenase 2-2
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 1-2
- Methylsterol monooxygenase 1-1
- Delta
Sequence:
MELDSENKLLKTGLVIVATLVIAKLIFSFFTSDSKKKRLPPTLKAWPPLVGSLIKFLKGPIIMLREEYPKLGSVFTVNLVHKKITFLIGPEVSAHFFKASESDLSQQEVYQFNVPTFGPGVVFDVDYSVRQEQFRFFTEALRVNKLKGYVDMMVTEAEDYFSKWGESGEVDIKVELERLIILTASRCLLGREVRDQLFDDVSALFHDLDNGMLPISVLFPYLPIPAHRRRDRAREKLSEIFAKIIGSRKRSGKTENDMLQCFIESKYKDGRQTTESEVTGLLIAALFAGQHTSSITSTWTGAYLMRYKEYFSAALDEQKNLIAKHGDKIDHDILSEMDVLYRCIKEALRLHPPLIMLMRASHSDFSVTARDGKTYDIPKGHIVATSPAFANRLPHIFKDPDTYDPERFSPGREEDKAAGAFSYIAFGGGRHGCLGEPFAYLQIKAIWSHLLRNFELELVSPFPEIDWNAMVVGVKGNVMVRYKRRQLS
Protein: Ethanolaminephosphotransferase, putative (EC 2.7.8.1) (Q38A84)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- phosphatidylserine decarboxylase
- Lipin, putative
- Phosphatidyl serine synthase, putative
- Phosphatidic acid phosphatase protein, putative
- Phosphatidic acid phosphatase, putative
- Ubiquitin-conjugating enzyme variant Kua homologue, putative
- Phosphatidic acid phosphatase alpha, putative
- ethanolamine kinase
- Choline/ethanolamine kinase, putative
Sequence:
MNAPHRTPGSNSAGNTGPGSHRSRCISLDPRVHEHIPPHFLPNLAKYKYSGSDSGIISNYVMQPYWNFIVSLVPMTVAPNAITVTGFVMCLSSALLVMFFYYFGNAEYPCWVWLYAVICLFAYQTLDAIDGKQARRTNTGSPLGELFDHGCDVILTPFVQMMICCALNTPPCVTFVYITLSSCAVFGAIWEQFVTGTLDFGYVNGPTDGILLACGIFLITAIMSPAVWDTQVAGPYEVPLPSWLGSCGGSFVIGSVRSMLFTFYVVSGTLTLLTNILHVLKRPNIQKPGMAVTTALPVVCLLVLHVWMYLVYRPIHEKYPYALELSFHVLISYTATRMTVSRLCAMPFNLFSGLFIITLLFTVAPLFIHTYLPLAEEKYVLPSLGSATVALAVLGFWQYFHMILSVITQMAYFLRISVFSITSRHDSNTKWE
Protein: Ras GTPase-activating protein gap-1 (GTPase-activating protein 1) (Q22720)
Organism: Caenorhabditis elegans
Function: GTPase-activating protein, which inhibits the vulval induction by acting as a negative regulator for the member of the Ras family let-60. Probably decreases the signaling activity of Ras by stimulating its intrinsic GTPase activity, thereby lowering the levels of GTP-bound, active Ras.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- SH2 domain-containing protein
- Ras protein let-60
- Receptor tyrosine-protein kinase let-23
- Protein lin-3
- E3 ubiquitin-protein ligase CBL
- Protein lin-2
Sequence:
MVLSCRVVDCGGLKLKENQTLLLLVSTIHNSSEVGKLSIDAEEKRSKEWLEMPCAEGMLSLKLTLWQDLLKGINSVFHGQVRVDVDENWKSGPAKWFYLRSKANEDGEGGEDGGDIGDATVKVTYQIDHILRMQVYKPLLDLLFLAGDVQPLTASLVAVIEALPKVELGPVSRSLVELMAQSDRIRPVLSSLYVNSILKCQDENTLFRGQSLSGKMLFEILTTYGKMYLITTLKPVVDKIYKERKNCEVDPARVAVGASLEKNRNNLLVYFQMLFERVTTSSTNCPHLIKQLLYDLRNVVGTHSSRSGVQRLAVSSFVIMRFFAAAILNPKAFEIRKDQPDLRVSRTLLLLSKLLQRLSNCSVSEGPLSSKEIWLNGVFETVTSEQHKSVMASFLDNISLVGDRSEPQKCTVFKFGNLQQVDRSRLAWKKVLHYKKRYVQLTNTHLIWQKDVQCAPKGTVPLSDIKFVNVDNKNIITIVCETMQLQFEAPGGVEATDWLNAIERQRNRAAHEIAETPGEHFFVDAERHVDKIHTLLYKYRETMIEWRDQLQSNVELDEKTAPELLKASYVVEEERQSHKDSLIATLCSTIDVTDAIQLAHTEYEKENKVSRRIDAIITAKKRQKSFSVK
Protein: RNA polymerase III subunit G (D6R9U7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLALKQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAGPKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDDDAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDE
Protein: Uncharacterized protein (Q3TDL2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKGATSKSNHCLILSLFILLSYLGTILADDSLSCELTFNYRNLHGQCSVNGKTLLDFGDKKHEENATKMCADLSQNLREISEEMWKLQSGNDTLNVTTQSQYNQGKFIDGFWAINTDEQHSIYFYPLNMTWRESHSDNSSAMEQWKNKNLEKDMRNFLITYFSHCLNKSSSHFREMPKSTLKVPDTTQRTNATQIHPTVNNFRHNSDNQGLSVTWIVIICIGGLVSFMAFMVFAWCML
Protein: Transcriptional regulator ATRX homolog (EC 3.6.4.12) (ATP-dependent helicase xnp-1) (X-linked nuclear protein 1) (Q9U7E0)
Organism: Caenorhabditis elegans
Function: Required for embryonic development and gonadogenesis. Also, functions redundantly with the transcriptional repressor lin-35 to regulate somatic gonad development.
Subcellular location: Nucleus.
Interaction partners:
- DNA repair protein RAD51 homolog
- Hpc2-related domain-containing protein
- THO complex subunit 2
- Protein HIRA
- Retinoblastoma-like protein homolog lin-35
Sequence:
MRVGVSESEDSDGHVIEDEDLEMARQIENERKEKRAQKLKEKREREGKPPPKKRPAKKRKASSSEEDDDDEEESPRKSSKKSRKRAKSESESDESDEEEDRKKSKSKKKVDQKKKEKSKKKRTTSSSEDEDSDEEREQKSKKKSKKTKKQTSSESSEESEEERKVKKSKKNKEKSVKKRAETSEESDEDEKPSKKSKKGLKKKAKSESESESEDEKEVKKSKKKSKKVVKKESESEDEAPEKKKTEKRKRSKTSSEESSESEKSDEEEEEKESSPKPKKKKPLAVKKLSSDEESEESDVEVLPQKKKRGAVTLISDSEDEKDQKSESEASDVEEKVSKKKAKKQESSESGSDSSEGSITVNRKSKKKEKPEKKKKGIIMDSSKLQKETIDAERAEKERRKRLEKKQKEFNGIVLEEGEDLTEMLTGTSSQRKLKSVVLDPDSSTVDEESKKPVEVHNSLVRILKPHQAHGIQFMYDCACESLDRLDTEGSGGILAHCMGLGKTLQVITFLHTVLMHEKIGEKCKRVLVVVPKNVIINWFKEFQKWLVDNDEELDTIDVNELDSYKTIEDRRRALKAWHSSKTPSVMIIGYDLFRILTVEDDPKKKKPKNRNRRLEKAKEDFRKYLQNPGPDMVVCDEAHKLKNDDSALSKCMVKILTKRRICLTGTPLQNNLMEYHCMVNFVKPGLLGTKTEFANRFVNIINRGRTKDASPLEVSFMKRRCHVLYDHLKKCVDRKDYRVLTEAIPPKQEYVINVRQTERQCALYNAFLNDIVGDSGLSKRLLPDYHMFSRIWTHPYQLVLHEQRMERERVMREDAEEEADFIDDGDGSESESEGSFKSGSESDSGKSVVLSSDDEGSSKKKKNGNKPEIKKTAPQKKRKFLNSDDEDEEDGEDTAMAILQDGIRQSKRLAGEEADLRDTDTPPEYTGWFARLGLVKEEDRDDFALSNKLILLVEIIKKCEEIGDKLLVFSQSLESLTLIKRMLEYMAGTGQWFADGHEALNAEGEETWSWLEGEDYMTIDGSVQSGKRDAVQTSFNDPLNLRARLMLISTRAGSLGTNMVAANRVIIFDACWNPSHDTQSLFRVYRFGQTKPVYIYRFIAQGTMEERIYKRQVTKESTSMRVVDEAQIQRHYLGNDLTELYQFTPSTFDPDVEISCAPPKDRLLADVIHKNQHAVVDYIEHDTLFANVEDEKLTEQEMKDAWTDYEKDKSGMPVRAQYAAPPMPGFPNGMIVGQNVQALLQNRMNQGIRVDQMQHDILFKELQKMRIKDAGTAVKIVLLRNLLEQILPYIPDEMRGGMSEFNTHFIRLVHETDRKMETPADLLRKSLESFKTVIKMVKMIPTCREPLARMTRDYPYLFA
Protein: Dysbindin protein homolog (Biogenesis of lysosome-related organelles complex 1 subunit 8) (BLOC-1 subunit 8) (Q9VVT5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses. In response to high synaptic activity at neuromuscular junctions, stabilizes Pldn protein levels and, together with Pldn, plays a role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- SNAPIN protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Uncharacterized protein, isoform A
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- BLOC-2 complex member HPS5 homolog
- Hermansky-Pudlak syndrome 4, isoform A
Sequence:
MFGNLKKKLSSAIQEGLVISENLQQQYRQRVSSGNSGSSQASGITTPISPLGLNESLSSSRSSSLSLSAPFQLTDGVPSHLNVAAGCSLLAKYEDDWQQIHGANEKNAEKAAQIANQISGIQDQASHQHRIMSELNSSLAGIPTLIAQLQNSSQVLNSLEEMGKQLEIELEKLEDLREECELQEFILEQQFQLSRHKQKKLNELEQYRQQIAQKHQSKIKDQEQTLLKLQRERQAVFDDAFREDMEEYKQRGQLTKIQTTSNKLALEEVVLEANEVETKDALEQFLNG
Protein: (S)-3-amino-2-methylpropionate transaminase (EC 2.6.1.19) (EC 2.6.1.22) (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT) (Q8MYV0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRSLWLNTLTKQSLYRLSTKRYSTNVEPKEPVVKTKSIPGPKSIELKKQLDSVQATGTIQFFADYEKSIGNYIYDVDGNILLDVYTQISSVPLGYNHPRLYKVFNNEQNMKTLINRPALGVFPGKEWPGKLHSVLLNIAPKGLNKITTMMCGSCSNENAYKSIFIWYQNKLRGNAPLTEQEKNSCMINIPPGAPKLSILSFKGAFHGRTLGALSTTHSKYIHKLDVPSFDWPIASFPEYRYPLDENVAHNKKEDEKCLSEVQDLIQQYASKNPVAGIVVEPIQSEGGDNEASPEFFRSLQAICKKNGIALLIDEVQTGGGSTGKFWAHEHFELESPPDVVTFSKKLQLGGYFHNDDFIPNEPYRIFNTWMGDPGKVLLLEEVVKVIQEEKLLANVDVAGKVLKNGLLSLEKEFPHILNSTRGRGTFLAVNCTNTKVRDQIIGALKLHGIQTGGCGEISIRFRPALIFKEYHANIVLDRFRKVLQGI
Protein: Erg K+ channel (Potassium voltage-gated channel subfamily H member 6a) (Q8JH78)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPVRRGHVALQNTYLDTIIRKFDGQNRKFLIANAQMKNCGIIYCNEGFCQMFGFSRAEIMQQSCTCQFLVGPGTMKSALGQLAQALLGSEERKVEILYYSKEGTCRPCLIDVIPVKNEEGVVIMFILNFQELLDPSMKKGGLKQRMANSWLRAGQRRRMHLRMPSLRVKRQPSLPKDHFEGVVVDYLQPSHEEVALKDLQMSPDSCLKSETQALIQQTPSSCELSPPPSRPSDRLEPSGPLLKHSHSRESMHSLRRASSLHDIDGMRDQWSDLKPSNLNSTSDSDLMRHRTIGRIPQVTISFGSDRLRPPSPTEIEIIAPSKIKDRSQNVSEKVTQVTQVLSLGADVLPEYKLQAPRIHKWTILHYSPFKAVWDWIILLLVLYTAVFTPYSAAFLLNEQEDERRRTCGYTCNPLNVVDLVVDVMFIIDILINFRTTYVNHNDEVVSNPARIAQHYFKGWFLIDIVAAIPFDLLIFRSGSDEPQTTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLFLLMCTFALIAHWLACIWYAIGNMERTSSARIGGMKIGWLDNLADQIGKQYNDSNSFSGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNPEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHTQMLRVKEFIRFHQIPGGLRQRLEEYFQHAWPYTNGIDMNAVLKGFPECLQADICLHLNRSLLQSCKAFRGASKGCLRALAMRFRTTHAPPGDTLVHSGDVLTALYFISRGSIEILRDDVVVAILGKNDIFGEPISLYARPGKSSADVRALTYCDLHKILRDDLLEVLDMYPDFSDNFWSNLEITFNLRDVDRIMHPTPSEDSDCGYRRPRHRRNPLRRNRPDGMDRDGMDTYPVQPCSPVGNHRGAIPLSQWDELCSDGSPASLSSEEDMKPLVSGQGDMYSLGTEMQEFSPSAVSLMPSAHSTASAMAGPLTGAHQYTAAPLNISGVYSYLSDRRASEYSESQRRSSAVQACYHHHSPCVGDRPNQLQARLELLQSQLNRLETRMTADINVILQLLQRQMAPVPPAYSAVSPDPLAHPVPPAHPTSLYTTAAHNTTPSLQITDASSPGKSPDVDSLKEKSPDSLSSGIHLTVASTDTMSMSPETELSVPSAGPLLQPPGLLCSSLRFPSLPDSLEGPGTLEGSPEIQRHVSDPVLPGS
Protein: Cold shock protein cspD (A0A0H3C7D5)
Organism: Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
Interaction partners:
Sequence:
MSGYDFEDAAAHEEFVRISGKVKWFDAGKGYGFIVPDDPGQTGLKDVLLHVTSLRNCGRETAMEGAIIVCDVVRRPKGWQVSEVVNLDESGAPSPLERQRRTFAEGPVRRDGLRDGHGRSALTPEGPAEHAKVKWFNRTKGYGFVIRDAEPGDIFVHIETLRRGGLEDLQPGDDVLVRFARGPKGLVVAEISAGDA
Protein: Myelin transcription factor 1 (MyT1) (Myelin transcription factor I) (MyTI) (PLPB1) (Proteolipid protein-binding protein) (Q01538)
Organism: Homo sapiens (Human)
Function: Binds to the promoter region of genes encoding proteolipid proteins of the central nervous system. May play a role in the development of neurons and oligodendroglia in the CNS. May regulate a critical transition point in oligodendrocyte lineage development by modulating oligodendrocyte progenitor proliferation relative to terminal differentiation and up-regulation of myelin gene transcription.
Subcellular location: Nucleus.
Interaction partners:
- E3 ubiquitin-protein ligase HERC2
- Myelin proteolipid protein
- Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
Sequence:
MSLENEDKRARTRSKALRGPPETTAADLSCPTPGCTGSGHVRGKYSRHRSLQSCPLAKKRKLEGAEAEHLVSKRKSHPLKLALDEGYGVDSDGSEDTEVKDASVSDESEGTLEGAEAETSGQDEIHRPETAEGRSPVKSHFGSNPIGSATASSKGSYSSYQGIIATSLLNLGQIAEETLVEEDLGQAAKPGPGIVHLLQEAAEGAASEEGEKGLFIQPEDAEEVVEVTTERSQDLCPQSLEDAASEESSKQKGILSHEEEDEEEEEEEEEEEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEAAPDVIFQEDTSHTSAQKAPELRGPESPSPKPEYSVIVEVRSDDDKDEDTHSRKSTVTDESEMQDMMTRGNLGLLEQAIALKAEQVRTVCEPGCPPAEQSQLGLGEPGKAAKPLDTVRKSYYSKDPSRAEKREIKCPTPGCDGTGHVTGLYPHHRSLSGCPHKDRIPPEILAMHENVLKCPTPGCTGQGHVNSNRNTHRSLSGCPIAAAEKLAKSHEKQQPQTGDPSKSSSNSDRILRPMCFVKQLEVPPYGSYRPNVAPATPRANLAKELEKFSKVTFDYASFDAQVFGKRMLAPKIQTSETSPKAFQCFDYSQDAEAAHMAATAILNLSTRCWEMPENLSTKPQDLPSKSVDIEVDENGTLDLSMHKHRKRENAFPSSSSCSSSPGVKSPDASQRHSSTSAPSSSMTSPQSSQASRQDEWDRPLDYTKPSRLREEEPEESEPAAHSFASSEADDQEVSEENFEERKYPGEVTLTNFKLKFLSKDIKKELLTCPTPGCDGSGHITGNYASHRSLSGCPLADKSLRNLMAAHSADLKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGVKVAPTKDDKEDPELMKCPVPGCVGLGHISGKYASHRSASGCPLAARRQKEGSLNGSSFSWKSLKNEGPTCPTPGCDGSGHANGSFLTHRSLSGCPRATFAGKKGKLSGDEVLSPKFKTSDVLENDEEIKQLNQEIRDLNESNSEMEAAMVQLQSQISSMEKNLKNIEEENKLIEEQNEALFLELSGLSQALIQSLANIRLPHMEPICEQNFDAYVSTLTDMYSNQDPENKDLLESIKQAVRGIQV
Protein: Gem nuclear organelle associated protein 4 (I3L4A4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFEACSQGPLNICEEMTILHGGFLLAEQLFHPKALAELTKSDWERVGRPIVEALREISSAAAHSQPFAWKKKALIIIWAKVLQPHPVTPSDTETRWQEDLFFSVGNMIPTINHTILFELLKSLEASGLFIQLLMALPTTICHAELERFLEHVTVDTSAEDVAFFLDVWWEVMKHKGHPQDPLLSQFSAMAHKYLPALDEFPHPPKRLRSDPDACPTMPLLAMLLRGLTQIQSRILGPGRKCCALANLADMLTVFALTEDDPQEVSATVYLD
Protein: Ankyrin repeat and MYND domain-containing protein 2 (Q8IV38)
Organism: Homo sapiens (Human)
Function: May be involved in the trafficking of signaling proteins to the cilia.
Subcellular location: Cell projection, cilium {ECO:0000250}.
Interaction partners:
- Protein argonaute-3
- Peptidyl-prolyl cis-trans isomerase FKBP8
Sequence:
MVHIKKGELTQEEKELLEVIGKGTVQEAGTLLSSKNVRVNCLDENGMTPLMHAAYKGKLDMCKLLLRHGADVNCHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCVTIINNFFPRERLDYYTKPQGLDKEPKLPPKLAGPLHKIITTTNLHPVKIVMLVNENPLLTEEAALNKCYRVMDLICEKCMKQRDMNEVLAMKMHYISCIFQKCINFLKDGENKLDTLIKSLLKGRASDGFPVYQEKIIRESIRKFPYCEATLLQQLVRSIAPVEIGSDPTAFSVLTQAITGQVGFVDVEFCTTCGEKGASKRCSVCKMVIYCDQTCQKTHWFTHKKICKNLKDIYEKQQLEAAKEKRQEENHGKLDVNSNCVNEEQPEAEVGISQKDSNPEDSGEGKKESLESEAELEGLQDAPAGPQVSEE
Protein: Heat shock protein 75 kDa, mitochondrial (HSP 75) (TNFR-associated protein 1) (Tumor necrosis factor type 1 receptor-associated protein) (TRAP-1) (Q9CQN1)
Organism: Mus musculus (Mouse)
Function: Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA.
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}. Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Cytochrome c, testis-specific
- Cytochrome c, somatic
- 60 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- Stress-induced-phosphoprotein 1
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Activator of 90 kDa heat shock protein ATPase homolog 1
- Prostaglandin E synthase 3
- Hsp90 co-chaperone Cdc37
- Serine/threonine-protein phosphatase 5
Sequence:
MACELRAVLLWGRGLQTVLRAPALAGVRRGKPVLHLQKTTVQFRGPTQSLASGISAGQLYSTQAAEDKEEESLHSIISNTEAVRGSVSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVCEGQVLPEMEIHLQTDAKKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLEALQNQAETSSKIIGQFGVGFYSAFMVADKVEVYSRSAAPESPGYQWLSDGSGVFEIAEASGVRPGTKIIIHLKSDCKDFASESRVQDVVTKYSNFVSFPLYLNGKRINTLQAIWMMDPKDISEFQHEEFYRYIAQAYDKPRFTLHYKTDAPLNIRSIFYVPEMKPSMFDVSRELGSSVALYSRKVLIQTKAADILPKWLRFIRGVVDSEDIPLNLSRELLQESALIRKLRDVLQQRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTTAEQDIKEDIAKLLRYESSALPAGQLTSLPDYASRMQAGTRNIYYLCAPNRHLAEHSPYYEAMKQKHTEVLFCYEQFDELTLLHLREFDKKKLISVETDIVVDHYKEEKFEDTSPADERLSEKETEDLMAWMRNALGSRVTNVKVTFRLDTHPAMVTVLEMGAARHFLRMQQLAKTQEERAQLLQPTLEINPRHTLIKKLCQLRESEPELAQLLVDQIYENAMIAAGLVDDPRAMVGRLNDLLVKVLEKH
Protein: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (6PF-2-K/Fru-2,6-P2ase 1) (PFK/FBPase 1) (6PF-2-K/Fru-2,6-P2ase liver isozyme) [Includes: 6-phosphofructo-2-kinase (EC 2.7.1.105); Fructose-2,6-bisphosphatase (EC 3.1.3.46)] (P16118)
Organism: Homo sapiens (Human)
Function: Synthesis and degradation of fructose 2,6-bisphosphate.
Interaction partners:
- ATP-dependent 6-phosphofructokinase, muscle type
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-1,6-bisphosphatase 1
- ATP-dependent 6-phosphofructokinase, liver type
- Fructose-2,6-bisphosphatase TIGAR
- ATP-dependent 6-phosphofructokinase, platelet type
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
Sequence:
MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYKNYEFFLPDNMEALQIRKQCALAALKDVHNYLSHEEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREKVLEDFLKRIECYEVNYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTPRSIYLCRHGESELNIRGRIGGDSGLSVRGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYLNVEAVNTHREKPENVDITREPEEALDTVPAHY