wanglab/gogpt-training-data huggingface dataset:
Protein: Microfibrillar-associated protein-like protein (Putative microfibril-associated protein) (T15F16.8 protein) (O22281)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-splicing factor 38
- Pre-mRNA-processing protein 40C
- Protein STABILIZED1
- Suppressor of mec-8 and unc-52 protein homolog 1
- Suppressor of mec-8 and unc-52 protein homolog 2
- SART-1 family protein DOT2
- DEAD-box ATP-dependent RNA helicase 42
- Nuclear protein-like
- Ubiquitin-like superfamily protein
- Ubiquitin-like protein 5
Sequence:
MSVTAGVSESAIAVREKLKGGIGQTKVRRYWPGKAPEWAEEAEEDDDVRMQKFSVLDRAFPKNDDLGVARKDDPRLRRLAQTKVENRDEVRADHRRIRQAEIISTEEEESRNQENRDEDDDEDALEERRRRIKEKNLRRAQEEAALLPLEEEDEIQEEEEEEEESEYETDSEDDMPGIALIKPVFVPKAERDTIAERERLEAEEEALEELAKRKLEQRKIETKQIVVEEVRKDEEIRKNILLEEANIGDVETDDELNEAEEYEVWKTREIGRIKRERDAREAMLREREEIEKLRNMTEQERRDWERKNPKPSSAQPKKKWNFMQKYYHKGAFFQADPDDEAGSAGTDGIFQRDFSAPTGEDRLDKSILPKVMQVKHFGRSGRTKWTHLVNEDTTDWSNPWTSNDPLREKYNKKMAGMDAPIAKPKGSKKMKDWET
Protein: DUF6787 domain-containing protein (Q557J7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MFSKLITPQIKNYKNFSKFSIFSLSNTSSLLNKSNKNINFIKYNIATKDYQLSKTIINDQFTLINNNRYYSIRKSMATLSSSSSSSSPTTPPTPPTPSSPSSMKTEVVSSISNTTTVENNNNNNNSTSEPTINPIFNNNENNKTLFDKIMKNTYEYPRFSKQWWTEKAYIFIVFGITGTSSLHVVKFLLKYLIGYQNPVSPFRGGLELIQNDPKYVIVYFLTMYTVYPFILISYGTLFGRFQYFIKLFNRMSIFSQLKRLFLKFSKKSSNKKE
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (A0A8I6G9K0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAEKARGEGEEGSFSLTVEEKKALCGLDSSFFGFLSLCKDGVKMKTLLNKAIHCYESLIVKAEGKVESDFFCQLGHFNLLLEDYSKALSSYQRYYSLQTDYWKNAAFLYGLGLVYFYYNAFQWAIRAFQEVLYVDPNFCRAKEIHLRLGFMFKVNTDYESSLKHFQLALRDSNVCTLSSVEIQFHIAHLFEIQRKYHSAKAAYEQLLQIESLPSQVKATVLQQLGWMHHNMDLVGDNTTKERYAIQYLQKSLEEDPNSGQSWYFLGRCYSCIGKVQDAFVSYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGILYESCNQTQDAIKCYLNATRSKSCSNTSVLISRIKFLQNVSDSWNSVHTASHHPVQQQVYTQCFTTQKLQGLGKDQQRPFQTGSTRYIHAACVDNQNQNGNHTLPQNSKGDTQNHSSLHIPTSEEQKIFNFTKESKDSRSKSLSPKTSRQDRDTSNIYVNAKEHSKNIHEITSVPISSLNNEDSVSPNLIIVDNPQLSVLVGEAMDSVDHDSRTCDKVNNVHPTLHKKPDNLTASSPSSASSTETLSLKVTEQMHTHIVTSFISPNSGLDTINGGPENSESSISVSVGLRPRPQIIPSMSVSIYSSSTEVLKACRNLGKNGLSNGHILLDICPPPRPPTSPYPPLPKEKLNPPTPSIYLENKRDAFFPPLHQFCINPKNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHIVEVRTQFLQPADENWDPSGTKKIWRYENKSSHTTIAKYAQYQACSFQESLREENERKTQVKDYSDNESTCSDISRRRQKVPFKTIKCGINIDLSDNKKWKLQLHELTKLPAFVRVVSAGNLLSHVGYTILGMNSVQLCMKVPGSRIPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNNLNFLMSSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNITWNVGPLTAFQYKLAVERYEWNKLQSIKSVVPMVHLSWNMARNIKVSDPKLFEMIKYCLLKILKQCQTLREALVAAGKEVLWHGRINDEPAPYCSICEVEVFNLLFVTNESNSQKTYIVHCQNCARKTSGNLENFVVLEQYKMEDLIQVYDQFTLAPSLSSSS
Protein: Putative transcription factor SOX-14 (P40656)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Ecdysone receptor
Sequence:
MIAKPNQATTEPPLSLRPGTVPTVPATTPARPATITIQRRHPAPKADSTPHTLPPFSPSPSPASSPSPAPAQTPGAQKTQSQAAITHPAAVASPSAPVAAAAPKTPKTPEPRSTHTHTHTHSQHFSPPPRESEMDGERSPSHSGHEMTLSMDGIDSSLVFGSARVPVNSSTPYSDATRTKKHSPGHIKRPMNAFMVWSQMERRKICERTPDLHNAEISKELGRRWQLLSKDDKQPYIIEAEKLRKLHMIEYPNYKYRPQKKQTRSPGSLKPNQDADGCEARNDTTNNNNSLTTLAINGTTTAGRKSKRSTSTCQSGSASKRLRNDSGDTSSKPKYEVKMESAEQLNSADIILPSADNLISYQSSEYLPLSTLSNADCDEKLHSELSSGPLESRENLSEVVNRFLPLFLGGNEDSQLGVSSLTQSQHNQSDPTAGLMDNISDISPINDREELTEEVMRYLPYLEVNPSSDGLTLKVESSSLLGKPLNEPVFDSEDNIVNDANLHSASHQIPPYVPDSHDCFAEDCGGDSSSHQVEFEVVRPQTVTMTMTCTLPYGGPDAGHTTFQADDFNAIPSAAEDSECSILTTSNSPQIGFNGSSFVEADAIGSTCTYAQQDYTGSVIETHNDLNYAAHDNNGALLAYTFEDLPPQPTGSHLEFNTNKYEFASYYKM
Protein: Tryptophan--tRNA ligase, mitochondrial (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) (P04803)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the attachment of tryptophan to tRNA(Trp).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Tyrosine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Lysine--tRNA ligase, mitochondrial
Sequence:
MSNKQAVLKLISKRWISTVQRADFKLNSEALHSNATVFSMIQPTGCFHLGNYLGATRVWTDLCELKQPGQELIFGVADLHAITVPKPDGEMFRKFRHEAVASILAVGVDPEKASVIYQSAIPQHSELHWLLSTLASMGLLNRMTQWKSKSNIKQSTNGDYLVNDSDVGKVRLGLFSYPVLQAADILLYKSTHVPVGDDQSQHLELTRHLAEKFNKMYKKNFFPKPVTMLAQTKKVLSLSTPEKKMSKSDPNHDSVIFLNDEPKAIQKKIRKALTDSISDRFYYDPVERPGVSNLINIVSGIQRKSIEDVVEDVSRFNNYRDFKDYVSEVIIEELKGPRTEFEKYINEPTYLHSVVESGMRKAREKAAKNLADIHKIMGF
Protein: BICD family-like cargo adapter 2 (Bicaudal D-related protein 2) (BICD-related protein 2) (BICDR-2) (Coiled-coil domain-containing protein 64B) (Q8CHW5)
Organism: Mus musculus (Mouse)
Interaction partners:
- Ras-related protein Rab-12
Sequence:
MDSPGEPSFPSGLLSGGASPSGDEGFFPFVLERRDSFLGGGPGPEEPEDLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLNTQHLEHEERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSERQDSGRERARALGELSEQNLRLSQQLAQASRTEQELQRELDTLRERCQTQALAGAELGARLESLQAENQMLQDRRQDLEAQIRGLREEVDKGQNRLQTTHEELLLLRRERKEHKLELERARFEAGEALRTLRGLQRRVSELEEESRLQDTEISGASLQTELAHSLDSDQDQDQQVNECGGSQAILSPETQETSSPQPSIQEEILEPPKKRASLSPVEILEEKEAEVARLQDEITLHRTELQTLRDELQRQKELRAQDNPEEALSSALSDRDEAVNKAMKLSLELSRVSLERDSLSRELLRAIRQKVALTQELEAWQDDMQVVIGQQLRSQRQKELSEAAAAPRRAKTRFSLRLGSGQSGGFLSNLFRRT
Protein: Kunitz-type trypsin inhibitor alpha chain (AKTI) (P85498)
Organism: Albizia kalkora (Kalkora mimosa) (Mimosa kalkora)
Function: Inhibits trypsin with a Ki of 0.25 uM. Inhibits the trypsin-like proteases in midguts of larval H.armigera, S.exigua, and P.rapae.
Interaction partners:
Sequence:
KELLDADGDILRNGGPAYPGLMPGVERDLPASGWGLPRRTGDESCPLNVKAVR
Protein: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit K) (NADH-plastoquinone oxidoreductase subunit K) (P0C343)
Organism: Oryza sativa subsp. japonica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01356}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01356}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH dehydrogenase iron-sulfur protein 2
- NAD
- NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial, putative, expressed
Sequence:
MSLIEFPLLDQTSSNSVISTTLKDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDALTKLRKKISREIVEDRTLSQKKNRCFTTSHKLYVRRSTNTGTYEQELLYQSPSTLDISSETFFKSKSPVSSYKLVN
Protein: Galactan beta-1,4-galactosyltransferase GALS1 (EC 2.4.1.-) (Beta-1,4-galactan synthase) (Galactan synthase 1) (O22807)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of beta-1,4-galactan. Can transfer galactose residues from UDP-galactose to beta-1,4-galactopentaose in vitro. Forms specifically beta-1,4-galactosyl linkages and can add successive beta-1,4-galactosyl residues to the acceptor. Beta-1,4-galactans are abundant polysaccharides in plant cell walls and are found as side-chain of rhamnogalacturonan I, which is a major component of pectin.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:23243126}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-rhamnose/UDP-galactose transporter 1
- Probable arabinosyltransferase ARAD1
- Probable arabinosyltransferase ARAD2
- UDP-glucose 4-epimerase 2
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 3
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- AT3g56750/T8M16_80
- Protein BASIC PENTACYSTEINE2
- At3g26950
- Polygalacturonate 4-alpha-galacturonosyltransferase
Sequence:
MRKEVLPPVLSTTTVCFEKKPIIATLLALSLVMIVWNLPPYYHNLISTARPCSAVTTTTTTTLLSSSNFTSAENFTTSLSTTTAAASQKYDSTPSDPNKRVFQPFGNAAALFVLMGAYRGGPTTFSVIGLASKPIHVYGKPWYKCEWISNNGTSIRAKAQKILPDWGYGRVYTVVVVNCTFNSNPNSDNTGGKLILNAYYNESPKLFERFTTLEESAGIYDESKYSPPYQYDYLYCGSSLYGNVSASRMREWMAYHAWFFGDKSHFVFHDAGGVSPEVRKVLEPWIRAGRVTVQNIRDQSQYDGYYYNQFLIVNDCLHRYRYAANWTFFFDVDEYIYLPHGNTLESVLDEFSVNTQFTIEQNPMSSVLCINDSSQDYPRQWGFEKLLFKDSRTKIRRDRKYAIQAKNAFATGVHMSENIVGKTLHKTETKIRYYHYHNTITVHEELCREMLPNSAKKKVTLYNKLPYVYDDNMKKLVKTIKEFEQKKLGTDVKNFS
Protein: Transmembrane protein (Q57ZL5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDSHALRRLLYAGAEEGSVAPRGHHHGGSYGTLISSVAVEQPAAVQPRSGLRLSSACLAGCFLGCATMRAANRERWWLGLFFMGGLYYNAVKAHKVGNGLVGHQSGFFAAGLGAIGCVGRLLVRVGNPKANRRLLCMFAALMWYEVGRYHLWSEHATEFRKEVTPEHAYGLLTEYVPPHIDTDLLPYRSVSRRRD
Protein: Trypsin inhibitor 1 (MCoTI-I) (Trypsin inhibitor I) (P82408)
Organism: Momordica cochinchinensis (Spiny bitter cucumber) (Muricia cochinchinensis)
Function: Inhibits trypsin; probably participates in a plant defense mechanism.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
SGSDGGVCPKILQRCRRDSDCPGACICRGNGYCG
Protein: Surfeit locus protein 1-like (Surfeit 1-like) (Cytochrome c oxidase assembly protein SURF1-like) (Q9LP74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the biogenesis of the COX complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Heme A synthase COX15
- Pentatricopeptide repeat-containing protein At3g48810
- Cytochrome c oxidase assembly protein COX11
- ATP synthase subunit a-1
- Cytochrome c-type biogenesis CcmH-like mitochondrial protein
- Replication factor C subunit 2
- NADH dehydrogenase subunit 9
- Glycine-rich RNA-binding protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- Uncharacterized mitochondrial protein AtMg01280
Sequence:
MTKLVSKIFKRLISQSQYMSSSTTSNLPAASQTSNLESQLLSSAPPPAKKKRGSALLWYLVGFTTYGLGETYKFLQTQVEHLDSRKQCLEMKPMKLNTTKDLDGLGFRRVVCKGIFDEQRSIYVGPKPRSMSKSSEIGFYVITPLLPIPNEPNSMKSPILVNRGWVPSDWKENSLESLGTGGLVAAAKESRKANKLLSSQQSLLSKFWYKLNNPMIVEDQVSRAMHVEVVGVVRKSETPGIYTLVNYPSSLAWFYLDVPKLALAMGFGEDTMYIESTYTDMDESRTYPVPRDVENLTRSKDIPLDYHLYTVLWHWSSLTCFIKASSILMRRLTKSDPIGVEPILIPISILVFICTKIYSLRNLFCKIDTIGVGCVTKLDTGKVK
Protein: Mucolipin-2 (Transient receptor potential channel mucolipin 2) (TRPML2) (Q8K595)
Organism: Mus musculus (Mouse)
Function: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity. May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway (By similarity). May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells. In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration. Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8IZK6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Lysosome membrane {ECO:0000305|PubMed:17050035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Recycling endosome membrane {ECO:0000269|PubMed:26432893}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Note=Localizes to recycling endosomes in activated macrophages and microglia. {ECO:0000269|PubMed:26432893}.
Interaction partners:
- Mucolipin-3
- Mucolipin-1
Sequence:
MPGDEETLDLPAWNRVPDLTWGPHHRSAMASLDSEVREECLREDLKFYFMSPCEKYRARRQIPWKLGLQILKIVMVTTQLVRFGLSNQLVVAFKEDNTVAFKHLFLKGFSGVDEDDYSCSIYTQENTYESIFFAIKQYRHLKNISLATLGYGESEDNRTGLKVCKQHYKTGAMFSSNETLNIDSDIETDCIHLDLQVLTTEPEDWAQTSFFRLDFYRLVQVDISFALKGIDLQAVHSREIPDCYLFQNTITFDNTAHSGKIKIYLNSEANIEECKNMNISGSTQRSTHYLLVFDVFVIMICLASLILCTRSIVLALRLRKRFLNFFLEKYKQRVCGADQWEFVNGWYVLVTISDLMTIIGSILKMEIKAKKLTNYDVCSILLGTSTLFVWVGVIRYLGYFQTYNVLILTMQASLPKVLRFCACAGMIYLGYTFCGWIVLGPYHEKFENLNIVAECLFSLVNGDDMFATFAQIQQKSILVWLFSRLYLYSFISLFIYMVLSLFIALITDSYHTIKKYQQHGFPETDLQKFLKESGSKDGYQKQPSALLSCLCCLRRRRSNDHLILID
Protein: Adenylosuccinate lyase (A0A0H2UMS9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MFSQLHMREEQVLLAQDYALETARAEGLEQGLERGKVEGRAERKLFAFLDIVRQGLLTSEVASQQLGMSVSEFEALL
Protein: Tyrosine--tRNA ligase, cytoplasmic (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) [Cleaved into: Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed] (P54577)
Organism: Homo sapiens (Human)
Function: Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable). Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity. Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16429158, ECO:0000269|PubMed:30304524, ECO:0000305|PubMed:9162081}. Nucleus {ECO:0000269|PubMed:22291016, ECO:0000269|PubMed:25533949}. Note=Cytoplasmic in normal conditions (PubMed:25533949). Resveratrol-binding in response to serum starvation promotes relocalization to the nucleus (PubMed:25533949). {ECO:0000269|PubMed:25533949}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Tryptophan--tRNA ligase, mitochondrial
- Glycine--tRNA ligase
- Lysine--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, mitochondrial
Sequence:
MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS
Protein: BRISC and BRCA1 A complex member 1 (J3KQS6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEAIEVEATV
Protein: Choline dehydrogenase, mitochondrial (CDH) (CHD) (EC 1.1.99.1) (Q8NE62)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- Alpha-aminoadipic semialdehyde dehydrogenase
- Phosphatidylethanolamine N-methyltransferase
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Intraflagellar transport protein 52 homolog
- Regucalcin
- Choline/ethanolaminephosphotransferase 1
- Interleukin-17 receptor B
- Eukaryotic translation initiation factor 3 subunit D
- Ethanolaminephosphotransferase 1
- Phospholipase D2
Sequence:
MWCLLRGLGRPGALARGALGQQQSLGARALASAGSESRDEYSYVVVGAGSAGCVLAGRLTEDPAERVLLLEAGPKDVLAGSKRLSWKIHMPAALVANLCDDRYNWCYHTEVQRGLDGRVLYWPRGRVWGGSSSLNAMVYVRGHAEDYERWQRQGARGWDYAHCLPYFRKAQGHELGASRYRGADGPLRVSRGKTNHPLHCAFLEATQQAGYPLTEDMNGFQQEGFGWMDMTIHEGKRWSAACAYLHPALSRTNLKAEAETLVSRVLFEGTRAVGVEYVKNGQSHRAYASKEVILSGGAINSPQLLMLSGIGNADDLKKLGIPVVCHLPGVGQNLQDHLEIYIQQACTRPITLHSAQKPLRKVCIGLEWLWKFTGEGATAHLETGGFIRSQPGVPHPDIQFHFLPSQVIDHGRVPTQQEAYQVHVGPMRGTSVGWLKLRSANPQDHPVIQPNYLSTETDIEDFRLCVKLTREIFAQEALAPFRGKELQPGSHIQSDKEIDAFVRAKADSAYHPSCTCKMGQPSDPTAVVDPQTRVLGVENLRVVDASIMPSMVSGNLNAPTIMIAEKAADIIKGQPALWDKDVPVYKPRTLATQR
Protein: Probable transcriptional regulatory protein (Q11028)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1354c
- Uncharacterized protein Rv1359
- Uncharacterized protein Rv1357c
- Uncharacterized protein Rv1355c
- Uncharacterized protein Rv1356c
- Uncharacterized protein Rv1366
- Putative diacyglycerol O-acyltransferase Rv0895
- Uncharacterized protein Rv0894
- HTH-type transcriptional repressor Rv1353c
- Possible phosphatase
Sequence:
MFLSAPAFRVEPTRSRHSALRWARHRRFADGPRWQMLRSLQIADQIARTGHMPVRRLDLIWISARNAARRELDLGVAALVEAVTLLTADVEGSTRLSQTRLNELAADYPTLDQNISEAVAAHGGVTRPVDQEVGSGLVVAFLRAGDAIACALELQLSTLAPMRPRVGVHTGDVRLRGDGTITGSAINESACLRDLAHEGQTLLSAATGDLVIDQLPANTWLTDVGKYPLRGLHRQERVIQLCHRDLRNEFPPLRMSVGNRSSLPAQFTTFVGRDAQINEVQEVLTNYRLVTLRGEGGVGKTRLAIQIAAASEFRDGLCFVDLAPIADPGMVSTTAAHALGLIDRPGSSTFDTLSHAIGNCHMLMVLDNCEHVLDACAELVVELLGACPELSILATSRESIGVTGEVTWVVPSLSPANEAIQLFTERARLVQPNFEIVADNFDAVSEICRRLDGMPLAIELAAARLRSLSPNEIANSLDDRFRLLTGGARSTVQRQQTLRASMDWSYALLTDTERILFRRLAVFVGGFDLTAASEVAAAGGDDFVERYSVLDQLTLLVDKSLVVAEESRGSTRYRLLETVRQYALEKLNESEEIDGVRARHRTHYATMAAGLNVPASTDYEQRLLQAEAEIDNLRAAFTWSRGNGDIAAALQLASALQPLWSQGRMREGLAWLESILEREGDNHLVPAGVWARALAEKVILKAWPATSPMGAPDIVAQAHHALALARDAGDCAVLARALVACGCGSGCDTEAAQPYFAEAIELARAINDEWTLSQIDYWQVVGIFISGQPIPLRAAAEQARELADSIGNRFVSRQCRLFACLAQIWEGDANGALALSRDVTAEAEVANDVVTKVLGLYVEAMALSYIGDSAARTIAGAALEAATELGGIYQDLGYGAITRAALAAGDVAAIEASEASWDLRNQHNVVTAHHELMAQAALVRGDVTTARRFADEAVLASTGWHLMMALIARARVAIAQDELGKARDDAHAAVACGVGVQTYLAMPDALELLAGLAGEAGNHGQAVRLFGAAAAQRQRTGEVRHKIWDAGYEAATAALRDAMGDEDFTAAWAEGAAAPLDEAIAYAQRGRGERKRPSNGWDALTPAEHKIVKLVTEGLVTKDIAARLFVSPRTVQTHLTHIYTKLDVTSRVQLVQEAAQHST
Protein: Protein ARG5,6, mitochondrial [Cleaved into: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) (N-acetyl-glutamate semialdehyde dehydrogenase) (NAGSA dehydrogenase); Acetylglutamate kinase (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (AGK)] (Q01217)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion.
Interaction partners:
- Amino-acid acetyltransferase, mitochondrial
- Ornithine carbamoyltransferase
- Ornithine aminotransferase
- Argininosuccinate synthase
- Acetylornithine aminotransferase, mitochondrial
- Argininosuccinate lyase
- Arginine biosynthesis bifunctional protein ArgJ, mitochondrial
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Carbamoyl phosphate synthase arginine-specific large chain
- Carbamoyl phosphate synthase arginine-specific small chain
Sequence:
MPSASLLVSTKRLNASKFQKFVSSLNKSTIAGFASVPLRAPPSVAFTRKKVGYSKRYVSSTNGFSATRSTVIQLLNNISTKREVEQYLKYFTSVSQQQFAVIKVGGAIISDNLHELASCLAFLYHVGLYPIVLHGTGPQVNGRLEAQGIEPDYIDGIRITDEHTMAVVRKCFLEQNLKLVTALEQLGVRARPITSGVFTADYLDKDKYKLVGNIKSVTKEPIEASIKAGALPILTSLAETASGQMLNVNADVAAGELARVFEPLKIVYLNEKGGIINGSTGEKISMINLDEEYDDLMKQSWVKYGTKLKIREIKELLDYLPRSSSVAIINVQDLQKELFTDSGAGTMIRRGYKLVKRSSIGEFPSADALRKALQRDAGISSGKESVASYLRYLENSDFVSYADEPLEAVAIVKKDTNVPTLDKFVCSDAAWLNNVTDNVFNVLRRDFPALQWVVSENDANIAWHFDKSQGSYLKGGKVLFWYGIDDINTISELVENFVKSCDTASTLNSSASSGVFANKKSARSYSTRSTPRPEGVNTNPGRVALIGARGYTGKNLVSLINGHPYLEVAHVSSRELKGQKLQDYTKSEIIYESLQIQDIRKLEEQNAVDFWVMALPNKVCEPFVETIQSVHGKSKIIDLSADHRFVSESDWAYGLPELNDRAKIANAAKIANPGCYATGSQLTISPLTKYINGLPTVFGVSGYSGAGTKPSPKNDPKFLNNNLIPYALSDHIHEREISARIGHNVAFMPHVGQWFQGISLTVSIPIKKGSLSIDEIRKLYRNFYEDEKLVHVIDDIPLVKDIEGTHGVVIGGFKLNDAEDRVVVCATIDNLLKGAATQCLQNINLAMGYGEYAGIPENKIIGV
Protein: Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (N-formylkynurenine formamidase) (FKF) (Q63HM1)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03014}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03014}. Note=Predominantly cytosolic. Some fraction is nuclear. {ECO:0000255|HAMAP-Rule:MF_03014}.
Interaction partners:
- Tryptophan 2,3-dioxygenase
- Kynureninase
- Kynurenine 3-monooxygenase
- Indoleamine 2,3-dioxygenase 2
- Indoleamine 2,3-dioxygenase 1
- Kynurenine--oxoglutarate transaminase 1
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Aromatic-L-amino-acid decarboxylase
- Malate dehydrogenase, mitochondrial
Sequence:
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATRKSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVAVVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTKHGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNSPQLKVAQAQPVDPTCRVLVVVGQFDSPEFHRQSWEFYQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQIILKTIFQ
Protein: BG1 (Bcl-2 ortholog dBorg-1) (Death executioner Bcl-2) (Drob-1) (IP01389p) (Proapoptotic Bcl-2 homolog DEBCL) (Q9V9C8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- BNIP3, isoform A
- Apoptosome protein Dark
- AT03047p
- Cytochrome c-1
- Cytochrome c-2
- Beclin-1-like protein
- AT16536p
- Autophagy protein 12-like
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- dynamin GTPase
Sequence:
MAPTTSPPPKLAKFKSSSLDHEIYTANRRGTIATASSDWKALRGGVGGGAGGPGSVPNPSNGRSLHAGGPMTRAASTSSLASSTRTMTNYQEYKMDIINQGKCLCGQYIRARLRRAGVLNRKVTQRLRNILDPGSSHVVYEVFPALNSMGEELERMHPRVYTNISRQLSRAPFGELEDSDMAPMLLNLVAKDLFRSSITWGKIISIFAVCGGFAIDCVRQGHFDYLQCLIDGLAEIIEDDLVYWLIDNGGWLGLSRHIRPRVGEFTFLGWLTLFVTISAGAYMVSNVCRRIGGQLYSLLF
Protein: Olfactory receptor 2B11 (Q5JQS5)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MKSDNHSFLGDSPKAFILLGVSDRPWLELPLFVVLLLSYVLAMLGNVAIILASRVDPQLHSPMYIFLSHLSFLDLCYTTTTVPQMLVNMGSSQKTISYGGCTVQYAVFHWLGCTECIVLAAMALDRYVAICKPLHYAVLMHRALCQQLVALAWLSGFGNSFVQVVLTVQLPFCGRQVLNNFFCEVPAVIKLSCADTAVNDTILAVLVAFFVLVPLALILLSYGFIARAVLRIQSSKGRHKAFGTCSSHLMIVSLFYLPAIYMYLQPPSSYSQEQGKFISLFYSIITPTLNPFTYTLRNKDMKGALRRLLARIWRLCG