wanglab/gogpt-training-data huggingface dataset:
Protein: Coiled-coil domain containing 24 (E9PUW8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPGDSPALWELVEEHVPLPERPEVKRILGEAAVDLSLELREEVAMLKALLQEIQSSQVSNSDPPSLLAPPPLLRDLIRQELRQLLQGLRLKAISEGRDQTQMWAQYSPRVLRFALEDTRCDSTQQELPMRADEPSTCPRDLTVIKDQLNVSNIDQVVRHLRSLLEEECHMLQNEISDLQHCLEMEQMQACQPSKDTQMPTLGEIKDQKAAMERELQVSLGPSCTAAKHRQKPLRSSIPSLRPFPCLHGYMPTPPSERCPHPQGQTSTRRWGRQLRYSYRKETTSTSVSSAASQAPT
Protein: Cabut, isoform A (RE07124p) (Q9VPQ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMDTLLPSPPATPPLRENKLEIVAKDEQQVNENLLKAKLKLVAQKSQKNGGIITPNPSDTEDEAPEIAVPNKKPRLEQPAMSMTPPPDQKLDDDQKAERVSVIMRVNSSGAVSSSSQDENSSSSTSCCSSSSNTNTSTSSVPPTVEDDYPEANVWRNLKFKMNRKRAAEVALPPVQTPETPVAKLVTPPAPAECIKEEEIKPILTPIYVSPVASSASQLILLSTVAAQQSPTPVPKTPTMSEEKLTTRITAAQAAATRSRIYECSFPDCGKNYFKSSHLKAHQRVHTGERPFICKWENCDKRFSRSDELSRHKRTHTGEKKFQCSVCQKKFMRSDHLSKHVKRHNKDKANGVNRHVSLANNNTSASVAASLCDASLHLRAIAPAGSSASSSPISSASLQVYSAQDLLRLQQQASSFTFGGTLLQVQR
Protein: Dual specificity phosphatase 11 (H7C0E6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
QWHHPRSGWGRRRDFSGRSSAKKKGGNHIPERWKDYLPVGQRMPGTRFIAFKVPLQKSFEKKLAPEECFSPLDLFNKIREQNEELGLIIDLTYTQRYYKPEDLPETVPYLKIFTVGHQVPDDETIFKFKHAVNGFLKENKDNEVRSRRKD
Protein: Vascular endothelial zinc finger 1 (Putative transcription factor DB1) (Zinc finger protein 161) (Q14119)
Organism: Homo sapiens (Human)
Function: Possible transcription factor. Specifically binds to the CT/GC-rich region of the interleukin-3 promoter and mediates tax transactivation of IL-3.
Subcellular location: Nucleus {ECO:0000269|PubMed:8035792}.
Interaction partners:
Sequence:
MEANWTAFLFQAHEASHHQQQAAQNSLLPLLSSAVEPPDQKPLLPIPITQKPQGAPETLKDAIGIKKEKPKTSFVCTYCSKAFRDSYHLRRHESCHTGIKLVSRPKKTPTTVVPLISTIAGDSSRTSLVSTIAGILSTVTTSSSGTNPSSSASTTAMPVTQSVKKPSKPVKKNHACEMCGKAFRDVYHLNRHKLSHSDEKPFECPICNQRFKRKDRMTYHVRSHEGGITKPYTCSVCGKGFSRPDHLSCHVKHVHSTERPFKCQTCTAAFATKDRLRTHMVRHEGKVSCNICGKLLSAAYITSHLKTHGQSQSINCNTCKQGISKTCMSEETSNQKQQQQQQQQQQQQQQQQQQHVTSWPGKQVETLRLWEEAVKARKKEAANLCQTSTAATTPVTLTTPFSITSSVSSGTMSNPVTVAAAMSMRSPVNVSSAVNITSPMNIGHPVTITSPLSMTSPLTLTTPVNLPTPVTAPVNIAHPVTITSPMNLPTPMTLAAPLNIAMRPVESMPFLPQALPTSPPW
Protein: Baseplate protein W (Gene W protein) (GpW) (P51768)
Organism: Escherichia phage P2 (Bacteriophage P2)
Function: Baseplate protein that is part of the outer wedges of the baseplate. Probably plays a role as a connector between the central and peripheral parts of the baseplate. Plays a role in tail assembly.
Subcellular location: Virion {ECO:0000269|PubMed:24097944}.
Interaction partners:
Sequence:
MTARYLGMNRSDGLTVTDLEHISQSIGDILRTPVGSRVMRRDYGSLLASMIDQPQTPALELQIKVACYMAVLKWEPRVTLSSVTTARSFDGRMTVTLTGQHNDTGQPLSLTIPVS
Protein: Uncharacterized protein (Q54VJ6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNFKSVILLLSFLYFISIVGCLKTEDINYYQDGEKLVFQINPNSGFNGNNLVISEFPSIASKGNFNQSKQLLNMPFFNLDNGSVSYNLTLLKLSPNSLPYKAYLSPFIGDGYNYTLYFNLFEKTNYCSKANFKNSEEYTYQSCINGGKNNDSFSQAGDLFEASYDISQVDLVRINYKATQFNYGCSRNTWFNIYCDKNQDFKLLGMGANYCNYEVNILSSHACPVYSSIPYNKIGDSTYELNVGPLYNHTALFYYINGSMIKFDLNSTSQYTPSPTPSETPSLTPSETPSPTPSETPSETPSETPSPTPSETPSPTPSETPSLTPSETPSPTPSETPSLTPSETPSLTPSETPTPTPSETPSPTPSETPSLTPSETPSLTPTSTPVPSPKVYCRSNRFGITINSTETVSCRGFGKTKCITKLGSECSTDNLDGEIVCTSKSLQCFGTNIQCISGDVYCSIDF
Protein: Suppressor of tumorigenicity 14 protein homolog (EC 3.4.21.109) (Serine protease 14) (Q9JJI7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Kunitz-type protease inhibitor 1
- Kunitz-type protease inhibitor 2
- Hsc70-interacting protein
- Ig-like domain-containing protein.
Sequence:
MGNNRGRKAGGGSQDFGAGLKYNSRLENMNGFEEGVEFLPVNNAKQVEKRGPRRWVVMVAVVFSFLLLSLMAGLLVWHFHYRNVRIQKVFNGHLRITNENFLDAYENSTSTEFISLASQVKEALKLMYSEVPVLGPYHKKSTVTAFSEGSVIAYYWSEFSIPPHLEEEVDRAMAVERVVTLPPRARALKSFVLTSVVAFPIDPRMLQRTQDNSCSFALHARGRTVTRFTTPGFPNSPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDGHDSDLVTVYDSLSPMEPHAVVRLCGTFSPSYNLTFLSSQNVFLVTLITNTDRRHPGFEATFFQLPKMSSCGGLLSEAQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNIPVGSCTKDYVEINGEKFCGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEYLSYDSNDPCPGMFMCKTGRCIRKDLRCDGWADCPDYSDERHCRCNATHQFMCKNQFCKPLFWVCDSVNDCGDGSDEEGCSCPAGSFKCSNGKCLPQSQQCNGKDDCGDGSDEASCDNVNAVSCTKYTYRCQNGLCLNKGNPECDGKKDCSDGSDEKNCDCGLRSFTKQARVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDETIFKYSDHTMWTAFLGLLDQSKRSASGVQEHKLKRIITHPSFNDFTFDYDIALLELEKPAEYSTVVRPICLPDNTHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQTTCEELLPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSVEKDGRIFQAGVVSWGEGCAQRNKPGVYTRIPEVRDWIKEQTGV
Protein: Secologanin synthase 2 (EC 1.14.19.62) (Cytochrome P450 72C) (CrCYP72C) (Secologanin synthase) (CrSLS) (U5NDT8)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. secologanin) biosynthesis pathway. Catalyzes the conversion of loganin into secologanin. Catalyzes the conversion of secologanin into secoxyloganin.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26285573}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEMDMDIIRKAIAATIFALVMAWAWRVLDWAWFTPKRIEKRLRQQGFRGNPYRFLVGDVKESGKMHQEALSNPMEFDNDIVPRLMPHINHTIKTYGRNSFTWMGRIPRIHVMEPELIKEVLTHSSKYQKNFDVHNPLVKFLLTGVGSFEGAKWSKHRRIISPAFTLEKLKSMLPAFAICYHDMLTKWEKLAEKEGSHEVDIFPTFDVLTSDVISKVAFGSTYDEGGKIFRLLKELMDLTIDCMRDVYIPGWSYLPTKRNKRMKEINKEITDMLRFIINKRMKALKAGEPGEDDLLGVLLESNIQEIQKQGNRKDGGMTINDVIEECKLFYFAGQETTGVLLTWTTILLSKHPEWQERAREEVLQAFGKNKPEFERLNHLKYVSMILYEVLRLYPPVIDLTKIIHEDTKLGPYTIPAGTQVMLPTVMLHREKSIWGEDAMEFNPMRFADGVANATKNNVTYLPFSWGPRVCLGQNFALLQAKLGLAMILQRFKFDVAPSYVHAPFTILTVQPQFGSHVIYKKLERQNF
Protein: PSP1 C-terminal domain-containing protein (Q581A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIVRTPLADCTVGTFQEENVANGVSGCAKRLMKRTYTHNPYRHITVIPVSVAGPCDWARSHEAAFGAPVFAPNRGVDVAQPPHTYGEPASSSVPCHEGGMCPRSMTYARYGAAPYACPATAAYEAPMEVDESINTSIGADKTVNLSNSTVSCCNAGTPTTSTPNKGSNTLYKMYVDGRPKVVRGVTRAEVSVKLRLGNEVFLVDDVPAVLGAVMVPEELVGRYVIVEGDRGEDLGCIASVSHSGARSAGDASEAGRRLARVLREATAEELEAFQRLDELEESALRFCRAAVQSLNLRVPLQVERAVFQFDRKKLTFTYSSDSYVEFKTLLRALNRQYQCRIWMHQLNWDMNCRDKRQSAGGEGEGRKRSGLKDEGGRRCEAGAVAA
Protein: Lectin alpha chain (DwL) [Cleaved into: Lectin beta chain; Lectin gamma chain] (P86624)
Organism: Macropsychanthus wilsonii (Wilson's clusterpea) (Dioclea wilsonii)
Function: D-mannose/D-glucose-binding lectin with hemagglutinating activity towards rabbit and human erythrocytes. In rats, elicits an acute inflammatory response by inducing neutrophil migration and induces dose-dependent paw edema.
Subcellular location: Vacuole, aleurone grain {ECO:0000250|UniProtKB:P58907}.
Interaction partners:
Sequence:
ADTIVAVELDSYPNTDIGDPNYPHIGIDIKSIRSKSTARWNMQTGKVGTVHISYNSVAKRLSAVVSYSGSSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNSIADENSLHFSFHKFSQNPKDLILQGDAFTDSDGNLELTKVSNSGDPQGNSVGRALFYAPVHIWEKSAVVASFDATFTFLIKSPDREPADGITFFIANTDTSIPSGSGGRLLGLFPDAN
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FTZ6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MQFTTAFSVALIAMAKLALADSQAFGLLAIHSGSPVQNTPVDSQNGALVLKTGGSFAGTVTDAGKLKFSDNTYAVVNSDGSIKTGSESEGTSGFALSGSHLTYKGNSGFFAIPSGSEYKFSTAQGTGAIDIVISPRSTKDGSVVADFTPAGSASSAASSAKPSSAAASSAAPTKAAISQIGDGQIQATSTIHQQTTNGAAKAAAGMGAGAIAAIAMLL
Protein: Ssy1p (A0A1D8PH27)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ssy5p
- Ptr3p
- Transcriptional regulator STP2
Sequence:
MIDLEGSDSDSSSLSIHENILFPSLGNSKNNKTRNTQKSSRDDVNSLETNSDSVNHLRSTFIARDRQLPSSTNDDYALEEVDLSDVSPLASRQHVVSPFSTTSISDTVSLDSSILNKIASNIGGNTDGIDQTGKFKYLRLYEKWKKIKIKTQDQKLTKPGQDIPLQTMSSRASSVFNLSQLDDFTRYVKETSLNDRIFHDLQERLPQRNQGGQSGRQDENFQNYLDLDLDVVDEKDLADKFYPTQEDEEKETDRNKRRLFPKRSKKKSLGMSAESRTATNDFLDSYQSSSSDVVSDDPRFLQRKLSVRHLQMISFGGTIGVGLFLNSGKAIAMAGGFGASLAFTIVGTLVLCTIMSFCEMVTFVSVIDGVSGLSSRFIDDAFGFAAGWLYFLSFSTGVAGEVVAGVIMLSYYPHLNTATNTGSTAGFVTLFLALILGSNLVHIQFFGELEYISSLVKMIWAIIMMIVMVVLNRGGFPNTPVMGFKYWQYSKSDFANNIIFGLFRPAFNLHDDGTSSPSEGIGGDKGRFMSLLTAILVVCYAYSGTEIVCIAACEAKNPRKALPSATRRVFWRIIIFYVLSAFLVSLNVYAGDPRLLRYYSGSTGISPSEFATNPAVIQAGGEHCSIDYKVVAGYGSGAQSPWIVALQSSSLCQFSSITNGFLVFFAVSCGNAQLYVSSRTAYSLALQGKAPKFLTYCNRFGIPYNAVLFAGSFGLLAFACVNESATVVFQNLTSLIASSGIFVWFTMCLTFIRFYYGLKRRPDILDRNDKSYPYKSPFQPYSAIVGCIGTLFILFSMGFVVFLKGEWDTMFFFSSYGSIMIFTVLYVGYRFIKGTSVPSLDKLDFDSGRTEMDRYIWDGGRSYNKRNVKEVAHKLVSFLA
Protein: Forkhead box protein D3 (F1R5S7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Transcription factor SOX-10
- Paired box 3a
- Zinc finger protein SNAI2
- Odd-paired-like)
- Transcription factor AP-2-alpha
- Zinc finger protein SNAI2
- Muscle segment homeobox 1a.
- Crestin
- Melanocyte inducing transcription factor a isoform 1
- Transcription factor Sox-2
Sequence:
MTLSGGTSASNMSGQTVLTADDVDIDVVGEGDEGMEQDSDCESQCMQDRGDEVEEIEVKERSDSPCESNADGETKGDAQESSTGPMQNKPKSSLVKPPYSYIALITMAILQSPQKKLTLSGICEFISNRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPQSEDMFDNGSFLRRRKRFKRHQPDILRDQTALMMQSFGAYGIGNPYGRHYGIHPAAYTHPAALQYPYIPPVGPMLPPAVPLLPSAELNRKAFSSQLSPSLQLQLNSLSTASIIKSEPSSRPSFSIENIIGVSSSSTSAQTFLRPPVTVQSALLSAQSLSLTRTSAAIAPILSVPSNIISGQFLPTASTAAVSKWPSQ
Protein: Prostaglandin E2 receptor EP3 subtype (PGE receptor EP3 subtype) (PGE2 receptor EP3 subtype) (PGE2-R) (Prostanoid EP3 receptor) (P43115)
Organism: Homo sapiens (Human)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor can couple to both the inhibition of adenylate cyclase mediated by G(i) proteins, and to an elevation of intracellular calcium. Required for normal development of fever in response to pyrinogens, including IL1B, prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for normal potentiation of platelet aggregation by prostaglandin E2, and thus plays a role in the regulation of blood coagulation. Required for increased HCO3(-) secretion in the duodenum in response to mucosal acidification, and thereby contributes to the protection of the mucosa against acid-induced ulceration. Not required for normal kidney function, normal urine volume and osmolality (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:7883006, ECO:0000269|PubMed:7981210, ECO:0000269|PubMed:8117308, ECO:0000269|PubMed:8307176}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Prostaglandin G/H synthase 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MKETRGYGGDAPFCTRLNHSYTGMWAPERSAEARGNLTRPPGSGEDCGSVSVAFPITMLLTGFVGNALAMLLVSRSYRRRESKRKKSFLLCIGWLALTDLVGQLLTTPVVIVVYLSKQRWEHIDPSGRLCTFFGLTMTVFGLSSLFIASAMAVERALAIRAPHWYASHMKTRATRAVLLGVWLAVLAFALLPVLGVGQYTVQWPGTWCFISTGRGGNGTSSSHNWGNLFFASAFAFLGLLALTVTFSCNLATIKALVSRCRAKATASQSSAQWGRITTETAIQLMGIMCVLSVCWSPLLIMMLKMIFNQTSVEHCKTHTEKQKECNFFLIAVRLASLNQILDPWVYLLLRKILLRKFCQIRYHTNNYASSSTSLPCQCSSTLMWSDHLER
Protein: 14-3-3 protein beta/alpha-A (Q5PRD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- M-phase inducer phosphatase
- Si:ch211-263k4.2.
- Uncharacterized protein.
- Phospholipid-transporting ATPase
- Transmembrane protein 266.
- Protein C, a.
- Kelch-like family member 17.
- Cadherin-related family member 2
- Solute carrier family 35 member F4.
- Solute carrier family 2 member 15b
Sequence:
MDKSDLVQKAKLAEQAERYDDMAASMKAVTEGGVELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTEGNEKKQQMAREYREKIEAELQEICNDVLGLLEKYLIPNASQAESKVFYLKMKGDYYRYLSEVASGDSKRTTVENSQKAYQDAFEISKKEMQPTHPIRLGLALNFSVFYYEILNTPEQACSLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN
Protein: Protein SOK2 (P53438)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a general regulatory role in the cyclic AMP-dependent protein kinase-stimulated (PKA) signal transduction pathway by regulating the expression of genes important in growth and development. May inhibit the switch from unicellular to filamentous growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00630}.
Interaction partners:
- cAMP-dependent protein kinase type 2
- cAMP-dependent protein kinase type 1
- cAMP-dependent protein kinase type 3
- AP-1-like transcription factor YAP6
- Zinc finger protein MSN2
- Ty transcription activator TEC1
- rRNA-processing protein EFG1
- CRE-binding bZIP protein SKO1
- Putative transcription factor PHD1
- AP-1-like transcription factor YAP4
Sequence:
MPIGNPINTNDIKSNRMRQESNMSAVSNSESTIGQSTQQQQQQQQYLGQSVQPLMPVSYQYVVPEQWPYPQYYQQPQSQSQQQLQSQPQMYQVQESFQSSGSDSNASNPPSTSVGVPSNATATALPNGSAITTKKSNNSTNISNNVPYYYYFPQMQAQQSMAYSYPQAYYYYPANGDGTTNGATPSVTSNQVQNPNLEKTYSTFEQQQQHQQQQQLQAQTYPAQPPKIGNAFSKFSKSGPPSDSSSGSMSPNSNRTSRNSNSISSLAQQPPMSNYPQPSTYQYPGFHKTSSIPNSHSPIPPRSLTTPTQGPTSQNGPLSYNLPQVGLLPPQQQQQVSPLYDGNSITPPVKPSTDQETYLTANRHGVSDQQYDSMAKTMNSFQTTTIRHPMPLIATTNATGSNTSGTSASIIRPRVTTTMWEDEKTLCYQVEANGISVVRRADNDMVNGTKLLNVTKMTRGRRDGILKAEKIRHVVKIGSMHLKGVWIPFERALAIAQREKIADYLYPLFIRDIQSVLKQNNPSNDSSSSSSSTGIKSISPRTYYQPINNYQNPNGPSNISAAQLTYSSMNLNNKIIPNNSIPAVSTIAAGEKPLKKCTMPNSNQLEGHTITNLQTLSATMPMKQQLMGNIASPLSYPRNATMNSASTLGITPADSKPLTPSPTTTNTNQSSESNVGSIHTGITLPRVESESASHSKWSKEADSGNTVPDNQTLKEPRSSQLPISALTSTDTDKIKTSTSDEATQPNEPSEAEPVKESESSKSQVDGAGDVSNEEIAADDTKKQEK
Protein: GH08104p (Serpin 4) (Q8MPN7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDYRLVPCGCWLLPLLGLALFPFPPVHTADVTMADAAHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTEAAAATVWRVMAVAAFSRKHFIANHPFAFYVKTHYDLPIFTGRYLG
Protein: ATP synthase peripheral stalk subunit OSCP, mitochondrial (ATP synthase subunit O) (Oligomycin sensitivity conferral protein) (OSCP) (Sperm flagella protein 4) (Q06647)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- LRRGT00139
- Uncharacterized protein
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase subunit ATP5MPL, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MAAPATSVLSRQVRSFSTSVVRPFSKLVRPPVQVYGIEGRYATALYSAASKQKRLDQVEKELLRVGQLLKDPKVSLAVLNPYIKRSIKVKSLKDITTKEKFSPLTANLMNLLAENGRLGNTQGVISAFSTIMSVHRGEVPCTVTTAFPLDEAVLSELKTVLNSFLSKGQILNLEVKTDPSIMGGMIVRIGEKYVDMSAKSKIQKLSKAMRDLL
Protein: Purple acid phosphatase 17 (EC 3.1.3.2) (Acid phosphatase type 5) (Peroxidase) (EC 1.11.1.7) (Q9SCX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Metallo-phosphoesterase involved in phosphate metabolism. Has a peroxidase activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Nudix hydrolase 23, chloroplastic
- Bifunctional riboflavin kinase/FMN phosphatase
- FAD synthetase 1, chloroplastic
- Purple acid phosphatase 8
- Purple acid phosphatase 4
- Purple acid phosphatase 7
- Purple acid phosphatase 3
- Riboflavin synthase
- Alkaline-phosphatase-like family protein
- FAD synthetase 2, chloroplastic
Sequence:
MNSGRRSLMSATASLSLLLCIFTTFVVVSNGELQRFIEPAKSDGSVSFIVIGDWGRRGSFNQSLVAYQMGKIGEKIDLDFVVSTGDNFYDNGLFSEHDPNFEQSFSNIYTAPSLQKQWYSVLGNHDYRGDAEAQLSSVLREIDSRWICLRSFVVDAELVEMFFVDTTPFVKEYYTEADGHSYDWRAVPSRNSYVKALLRDLEVSLKSSKARWKIVVGHHAMRSIGHHGDTKELNEELLPILKENGVDLYMNGHDHCLQHMSDEDSPIQFLTSGAGSKAWRGDINPVTINPKLLKFYYDGQGFMSARFTHSDAEIVFYDVFGEILHKWVTSKQLLHSSV
Protein: Thioredoxin O2, mitochondrial (AtTrxo2) (Q93VQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase that may participate in various redox reactions. Possesses insulin disulfide bonds reducing activity. Reduced by thioredoxin reductases NTRA and NTRB.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Thioredoxin reductase 1, mitochondrial
- Thioredoxin reductase 2
- NifU-like protein 5, mitochondrial
- Peroxiredoxin-2F, mitochondrial
- NifU-like protein 4, mitochondrial
Sequence:
MKSQWSNFHQIGRNSFLAASTVYVSNEFNFLNTSLLNRRSFCFAEGDRSSFVVLKSEAEFNSALSKARDGSLPSVFYFTAAWCGPCRLISPVILELSNKYPDVTTYKVDIDEGGLSNAIGKLNVSAVPTLQFFKGGVKKAEIVGVDVVRLKSVMEQLYK
Protein: Neutral ceramidase 1 (AtNCER1) (N-CDase 1) (NCDase 1) (EC 3.5.1.23) (Acylsphingosine deacylase 1) (N-acylsphingosine amidohydrolase 1) (F4HQM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Regulates sphingolipid homeostasis. Promotes oxidative stress resistance.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9VA70}. Endoplasmic reticulum {ECO:0000269|PubMed:26150824}. Golgi apparatus {ECO:0000250|UniProtKB:Q0JL46}.
Interaction partners:
- Alkaline ceramidase
- Ceramide kinase
- Sphingosine kinase 1
- Sphingosine kinase 2
- Non-lysosomal glucosylceramidase
- 3-dehydrosphinganine reductase TSC10B
- Non-lysosomal glucosylceramidase
- 3-dehydrosphinganine reductase TSC10A
- Non-lysosomal glucosylceramidase
- Non-lysosomal glucosylceramidase
Sequence:
MELSLVRLWNTCFPSFFYISTVLFLLTGGGVYSHSEYLIGLGSYDITGPAADVNMMGYANMEQVASGIHFRLRARTFIVSEPQGKRVVFVNLDACMASQIVKLKVIERLKARYGDLYTEQNVGISGIHTHAGPGGYLQYVVYIVTSLGFVRQSFDALVDGIENSIIQAHENLRPGSIFLNNGELLDAGVNRSPSAYLNNPSKERSKHKYNVDKEMTLLKFVDDQWGPVGSFNWFATHGTSMSRTNSLISGDNKGAASRFMEDWYEQNTAERSYSEEFISDEIPRRVSSLIENHQDSHHELLELASYFESQPGKPVTRISSSARRVRSALRKADKPGFVSAFCQTNCGDVSPNVLGAFCLDTGLPCDFNHSTCGGKNEMCYGRGPGYPDEFESTRIIGERQFKMALELFNKASEQLQGKVDYRHVYVDFSQLNVTLPKKDGKSEVVKTCPAAMGFAFAAGTTDGPGAFDFTQGDDKGNPFWRLVRNVLKTPDKKQIDCHYPKPILLDTGEMTKPYDWAPSILSLQVLRIGQLFILSVPGEFTTMAGRRLRYAVKTQLKNSGNKDLSGEIHVVIAGLANGYSQYVTTFEEYQVQRYEGASTLYGPHTLSGYIQEFKKLSKSLVLDMPVQPGPQPPDLLDKQLSFLTPVMMDTTPSGDSFGDVISDVPKNLSLKRGNGQVTVVFRSACPRNDLLTEGTFTLVERLEQKDKTWTPVYDDDDLCLRFKWSRHKKLSSRSQATVEWRIPESASPGVYRITHFGAAKKLFGSVHHFTGSSSAFVVT
Protein: Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Arachidonate--CoA ligase ACSBG2) (EC 6.2.1.15) (Bubblegum-related protein) (Q2XU92)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of fatty acids such as long chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. Has increased ability to activate oleic and linoleic acid. May play a role in spermatogenesis.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein.
Interaction partners:
- Fatty acid synthase
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2
- Monoglyceride lipase
- Lipoprotein lipase
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Fatty acid CoA ligase Acsl3
- Long-chain-fatty-acid--CoA ligase 4
- Long-chain-fatty-acid--CoA ligase 5
- Carnitine O-palmitoyltransferase 1, liver isoform
Sequence:
MTQEKKAEDLERGTDATSAVPRLWSTHCDGEVLLRLSKHGPGHETPMTIPELFQESAERFSAYPALASKNGKKWDTLTFSQYYEMCRKAAKSLIKLGLQRFQCVGILGFNSVEWVVTALGTILAGGLCVGIYATNSAEACQYVIQQANVSILIVENDQQLQKILLIPPDKMETVKAIVQYKLPLMESMANLYSWNDFMELGNDIPNIQLDRVILSQKANQCAVILYTSGTTGTPKGVLLSHDNITWTAGAMSQEMEINRVSGKQNTIVSYLPLSHIAAQLTDIWIPIKIGALTFFAQPDALRGTLVYTLQEVKPTLFMGVPRIWEKMQDTIKENVARSSRLRKKAFAWAKMLGLKVNTKRMLGKRDIPMNYRMAKALVFAKVRTSLGLDNCHAFFSSASPLSQDVSEFFLSLDIPIGEIYGMSECSGPHTVSNKSVYRVLSCGKVLSGCKNMLYNQNKEGVGEVCMWGRHVFMGYLNKEEATLEALDENGWLHSGDIGRLDSHDFLYITGRIKEILITAGGENVSPIPIETLVKEKIPIISHAMLVGDKAKFLCMLLTLKCETDRKSGEPLNKLSVEAKSFCQMLGSQATTVSDILKSRDQVVYTAIQYGIDIVNQQAMSDSHRIRKWIILEKDFSIQGGELGPTSKLKRSVITQKYKAQIDSMYLS
Protein: tRNA selenocysteine 1-associated protein 1 (SECp43) (tRNA selenocysteine-associated protein 1) (Q9NX07)
Organism: Homo sapiens (Human)
Function: Involved in the early steps of selenocysteine biosynthesis and tRNA(Sec) charging to the later steps resulting in the cotranslational incorporation of selenocysteine into selenoproteins. Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins synthesis (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Abundant in the nucleus. {ECO:0000250}.
Interaction partners:
- Pre-mRNA-processing factor 39
- L-seryl-tRNA
- O-phosphoseryl-tRNA
- Selenocysteine insertion sequence-binding protein 2
- Selenocysteine-specific elongation factor
- Selenide, water dikinase 2
- RNA-binding protein 25
- U1 small nuclear ribonucleoprotein C
- Splicing factor U2AF 65 kDa subunit
- U2 small nuclear ribonucleoprotein A'
Sequence:
MAASLWMGDLEPYMDENFISRAFATMGETVMSVKIIRNRLTGIPAGYCFVEFADLATAEKCLHKINGKPLPGATPAKRFKLNYATYGKQPDNSPEYSLFVGDLTPDVDDGMLYEFFVKVYPSCRGGKVVLDQTGVSKGYGFVKFTDELEQKRALTECQGAVGLGSKPVRLSVAIPKASRVKPVEYSQMYSYSYNQYYQQYQNYYAQWGYDQNTGSYSYSYPQYGYTQSTMQTYEEVGDDALEDPMPQLDVTEANKEFMEQSEELYDALMDCHWQPLDTVSSEIPAMM
Protein: Cinnamyl alcohol dehydrogenase 2 (AtCAD2) (EC 1.1.1.195) (Q9SJ25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Interaction partners:
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Flavone 3'-O-methyltransferase 1
- Aldehyde dehydrogenase family 2 member C4
- F5F19.5 protein
- Cytochrome P450 84A1
- Trans-cinnamate 4-monooxygenase
- Peroxidase 70
Sequence:
MVDQNKAFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRSSDGTSRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHALLPLFSLLKVNGKLVALGLPEKPLDLPIFSLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSDINSAMDRLAKSDVRYRFVIDVANSLLPESSAEILTEQVDHGVSITSRF