wanglab/gogpt-training-data huggingface dataset:
Protein: Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC 6.3.4.16) (Carbamoyl-phosphate synthetase I) (CPSase I) (P31327)
Organism: Homo sapiens (Human)
Function: Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22002106}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Cell membrane {ECO:0000250|UniProtKB:Q8C196}; Peripheral membrane protein {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:Q8C196}. Note=Localizes to the cell surface of hepatocytes. {ECO:0000250|UniProtKB:Q8C196}.
Interaction partners:
- Argininosuccinate synthase
- Ornithine transcarbamylase, mitochondrial
- Glutamine synthetase
- Glutamate dehydrogenase 1, mitochondrial
- Glutamate dehydrogenase 2, mitochondrial
- Glutaminase liver isoform, mitochondrial
- N-acetylglutamate synthase, mitochondrial
- Glutaminase kidney isoform, mitochondrial
- Multifunctional protein CAD
- Argininosuccinate lyase
Sequence:
MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKYLESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQADTVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
Protein: DumPY: shorter than wild-type (Q94185)
Organism: Caenorhabditis elegans
Interaction partners:
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MRYAWVVSFAFLILGNVVQSSSLLSKTINSDGSRDFKIVKHIKKNTCTCSCKCVPDAPSNPFDVSTTISSINNDNVDIGPSGDSNPTGSSWFQEIEATVGGQTVKSEHNIDSSVEVEKKVTTSTDASTTNAPTTGKDSTTPEIITGIVVINSKSESVTDMSTTRFSTTLSPTTELLTSPETLVSTDSSTSTEQTSPDNTTEIASPMETNTTTEATTTSVEPSVSTLASEDETTVTAIAESTTTVIAEVSTTTEEPTTTAESTTKKSTTKAPATTEEPTPTTTEEVTTTEAETSTTTSSETSTEKPTTPLIDNKIAGPATGKPETTHFPVTGTTPNFDTATETPFVAKSEDKMTLSKTAATETTQQTTEVTDGPEKETTKNVSIEIPITTVPLVETTSTTSTASKESDGFHTTLKLKVTTADSDSTESATTVKPFNEETTTKSHVVPKPTKKGTVKVTPKLELSFDEPTEITKAPHPVKPRKTTTTTTSTTTTTEKPVITEGSTTNKQPTTSEHESTTEVPTTTEEPTTTTGQHKTEKAITTEEPTTTEESSTTEEVTTTEEPANTGNPPTTENPTTTEQPTSTAESTTTALPFTTEQTVTTEEPTTAEKSTATQKPTTTQESVSTEKTSTTKKASTTEEPTTTDEPTTTTESSTTGKATTPELSTTSEETTTTELKITTEGSTTTEEPTTTAIFAEASTGIITTDEETTSTTSTTPEITSTKEIVTESAITQTSVSVVESSTPRQLPERWKAIVNKFKHNLEVLKEKKRLLKEKESTSTTGSDSSETTTVVAENIDEVTTTEKEKVVQTTPITTEKSTTQEETTTTTTTTEKTTSKTTTEKPTTSESATTETTTSEPSTTESTTVDTSSATTEESSTAAETTTTSAETSETTTSESAAFITGESPENTALQSSSQKSEENESSAEKPGARRDFVPKKHKTTVKPAETTSAVAASTTTTEPITTTEKSTTLETTPIEATTLNEVTGPAFVTGAPVDETTINTLELLSKINNTQISQPKPTDISKTDALSSLISGLIGSFTKAPMAPTIHTTTDAAFVTATEASLNDGSDKKIIDEAQPTDEIRRAQPTNEMDKEMEFEKRIREQRIQMEQAKRLREEELLEKQLQEQEIEEKARNEMIERKQKMLQQLEELKEAEERQRVLLEQERLQEQERQRLIAEKEAEIAFGSISTTTEASKFKYRLRPAQCAAINKFTRVFNITDPSEWIQKNCEFAKRYFPEASCPQIQALIESCFAFL
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Q6DEJ9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol kinase.
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Dol-P-Man:Man
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- ALG1 chitobiosyldiphosphodolichol beta-mannosyltransferase.
- Dolichyldiphosphatase 1.
- SMAD family member 9.
- Alpha-1,3-glucosyltransferase
Sequence:
MASRRSNAKSRDKPDKYSVLLPTYNERENLPLIVWLLVKYFGESGYNYEIIVIDDGSPDGTLQIAEQLQKIYGADKILLRPRAEKLGLGTAYIHGIKHATGNFVIIMDADLSHHPKFIPQFIEKQKEGGYDLVSGTRYRGDGGVYGWDLRRKLISRGANFVTQVLLRPGASDLTGSFRLYKKEVLEKLVEQCVSKGYVFQMEMIVRARQLGYTIGEVPISFVDRVYGESKLGGNEIVSFLKGLLTLFATT
Protein: Homeobox protein unc-62 (Uncoordinated protein 62) (Q9N5D6)
Organism: Caenorhabditis elegans
Function: Acts redundantly with ceh-20 and ceh-40 to perform overlapping roles during embryogenesis. Required for postembryonic development of the ectoderm, including the Q, V and P cell lineages, playing a crucial role in ensuring that these cells and their descendants undergo their invariant patterns of cell division, migration, fusion and morphogenesis. Has a role in the mig-13 pathway to promote anterior migration of neuroblasts in the Q lineage. Required for multiple roles in regulating vulva development. Associates with homeobox ceh-60 to regulate gene expression, including repression of genes involved in innate immunity and activation of genes involved in vitellogenesis. Involved in lipid homeostasis, contributing to the formation of the cuticle.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein ceh-20
- Homeobox protein ceh-60
- Homeobox protein ceh-40
- Homeobox protein lin-39
- Homeobox protein php-3
- Homeobox protein mab-5
- Homeobox protein nob-1
- Zinc finger transcription factor pqm-1
- Putative serine/threonine-protein kinase F31E3.2
- Homeobox protein ceh-43
Sequence:
MSGDSKVWAHASADTWAVQNGISTYDLDTSSIKREKRDHNEQFNDGYGPPPGSASADPASYIADPAAFYNLYTNMGGAPTSTPMMHHEMGEAMKRDKESIYAHPLYPLLVLLFEKCELATSTPRDTSRDGSTSSDVCSSASFKDDLNEFVRHTQENADKQYYVPNPQLDQIMLQSIQMLRFHLLELEKVHELCDNFCNRYVVCLKGKMPLDIVGDERASSSQPPMSPGSMGHLGHSSSPSMAGGATPMHYPPPYEPQSVPLPENAGVMGGHPMEGSSMAYSMAGMAAAAASSSSSSNQAGDHPLANGGTLHSTAGASQTLLPIAVSSPSTCSSGGLRQDSTPLSGETPMGHANGNSMDSISEAGDEFSVCGSNDDGRDSVLSDSANGSQNGKRKVPKVFSKEAITKFRAWLFHNLTHPYPSEEQKKQLAKETGLTILQVNNWFINARRRIVQPMIDQNNRAGRSGQMNVCKNRRRNRSEQSPGPSPDSGSDSGANYSPDPSSLAASTAMPYPAEFYMQRTMPYGGFPSFTNPAMPFMNPMMGFQVAPTVDALSQQWVDLSAPHE
Protein: Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Polynucleotide phosphorylase) (PNPase) (Vegetative protein 15) (VEG15) (P50849)
Organism: Bacillus subtilis (strain 168)
Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Necessary for competence development in Bacillus subtilis. May be necessary for modification of the srfA transcript (stabilization or translation activation). Involved in processing precursor type I toxin-antitoxin RNAs antitoxin SR4 and SR5 RNAs to their mature forms.
Subcellular location: Cytoplasm.
Interaction partners:
- Ribonuclease Y
- DEAD-box ATP-dependent RNA helicase CshA
- Ribonuclease J1
- Ribonuclease R
- Transcription termination factor Rho
- Ribonuclease J2
- RNA-binding protein Hfq
- Small ribosomal subunit protein uS15
- ATP-dependent 6-phosphofructokinase
- Transcription termination/antitermination protein NusA
Sequence:
MGQEKHVFTIDWAGRTLTVETGQLAKQANGAVMIRYGDTAVLSTATASKEPKPLDFFPLTVNYEERLYAVGKIPGGFIKREGRPSEKAVLASRLIDRPIRPLFADGFRNEVQVISIVMSVDQNCSSEMAAMFGSSLALSVSDIPFEGPIAGVTVGRIDDQFIINPTVDQLEKSDINLVVAGTKDAINMVEAGADEVPEEIMLEAIMFGHEEIKRLIAFQEEIVAAVGKEKSEIKLFEIDEELNEKVKALAEEDLLKAIQVHEKHAREDAINEVKNAVVAKFEDEEHDEDTIKQVKQILSKLVKNEVRRLITEEKVRPDGRGVDQIRPLSSEVGLLPRTHGSGLFTRGQTQALSVCTLGALGDVQILDGLGVEESKRFMHHYNFPQFSVGETGPMRGPGRREIGHGALGERALEPVIPSEKDFPYTVRLVSEVLESNGSTSQASICASTLAMMDAGVPIKAPVAGIAMGLVKSGEHYTVLTDIQGMEDALGDMDFKVAGTEKGVTALQMDIKIEGLSREILEEALQQAKKGRMEILNSMLATLSESRKELSRYAPKILTMTINPDKIRDVIGPSGKQINKIIEETGVKIDIEQDGTIFISSTDESGNQKAKKIIEDLVREVEVGQLYLGKVKRIEKFGAFVEIFSGKDGLVHISELALERVGKVEDVVKIGDEILVKVTEIDKQGRVNLSRKAVLREEKEKEEQQS
Protein: Kininogen-1 (BVK-1) [Cleaved into: [Ala3,Thr6]-bradykinin; Kininogen-1-associated peptide] (P83056)
Organism: Bombina variegata (Yellow-bellied toad)
Function: [Ala3,Thr6]bradykinin: produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. Possesses insulin-releasing activity. May target bradykinin receptors (BDKRB).
Subcellular location: Secreted {ECO:0000269|PubMed:12230583, ECO:0000269|PubMed:15134346}.
Interaction partners:
Sequence:
MRLWFCLSFLIILCVEHFPGTLAVERNVPESEEKTEQFLRDLFEISRLQRRPAGFTPFRGKFHSQSLRGLSETKRIYNAIWPCKHCNKCKPGLLCKK
Protein: chitinase (EC 3.2.1.14) (Q4WGI4)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MALYKLGLWASLWATFHTAAAKLDLNSQTNIAIYWGMLYLYQYVVHPPVSPHSNDCPIIVRVFQLAFVTRINGANGLPEVNFANAGDNCTTFEGTNLLSCPQIEEDIPICQSLGKTILLSIGGATYTEGGFTSESAAIAGANSVWQTFGPPSNNPSTLRPFGKAAVDGFDLDFESPVANMPAFANQLRSLFSSDPSKQYYLTAAPQCPYPDAADGPMLDGAVSFDAIWVQFYNNYCGLQAYNPGSTSQNNFNFATWDTWAKSVSRNKNVKVFLGVPGSSTAAGSGYVSVEALAQIIAYTKGFSSFGGVMAWDVSQVMANSGFLAGVRAALGSGSGSGSGSTTVSPTTASTTTSTSTPTTTTSSTTSAPTTSTSVTTTSTTSSTTAPTGSCPTAGARCSGGGAACNGASFGLCDNGVWVMQPCPGGLVCIQGGAGVYCGYPADKPAGSC
Protein: Chloroplastic import inner membrane translocase subunit HP30-1 (Hypothetical inner plastid envelope protein of 30 kDa 1) (AtHP30-1) (Hypothetical protein 30) (Q9SCK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with HP30-2 and HP20, triggers the import and insertion of transit sequence-less multi-pass transmembrane proteins (e.g. CEQORH) into the chloroplastic inner membrane.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:17098851, ECO:0000269|PubMed:24248378}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chloroplastic import inner membrane translocase subunit TIM22-2
- Mitochondrial import inner membrane translocase subunit TIM22-3
- Triglyceride lipase
- Outer envelope pore protein 16-4, chloroplastic
- E3 ubiquitin-protein ligase SPL1
- YlmG homolog protein 1-1, chloroplastic
- F20H23.8 protein
- Mitochondrial import inner membrane translocase subunit TIM22-1
- ATP-dependent DNA helicase
- Mitochondrial import inner membrane translocase subunit TIM22-4
Sequence:
MVVGGGGEGDQKRSSGEMMAMASLFNDQQNPIQQFQVKFKEVETNFKTWLSKQSIPVEAAVVSTMSGVQGAFIGGLMGTLSPEMPQAGVDPQAIASMKQAQALVGGPWVQARNFAAITGVNAGIASVMKRIRGKEDIESAVVAALGSGFAYSLVSQGLQGQPMNAITTAAGFAVFQGVFFKLGERFSKPSTEDPFFTRGRTMLVKLGLEKYEKNFKKGLLTDPTLPLLTDSALKDANIPPGPRLMILDHIQRDPEIKGKRK
Protein: AP-1-like transcription factor YAP3 (P38749)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription activator involved in the regulation of genes expressed in response to environmental changes. When overexpressed it activates transcription of the multidrug resistance ABC transporter PDR5, thus conferring resistance to the fungicide fluconazole (FCZ) and cycloheximide. When overexpressed, it also confers, independent of PDR5, increased resistance to 4-nitroquinoline-N-oxide (4-NQO) (By similarity). Preferentially binds 5'-TTACTAA-3'.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase
Sequence:
MTPSNMDDNTSGFMKFINPQCQEEDCCIRNSLFQEDSKCIKQQPDLLSEQTAPFPILEDQCPALNLDRSNNDLLLQNNISFPKGSDLQAIQLTPISGDYSTYVMADNNNNDNDSYSNTNYFSKNNGISPSSRSPSVAHNENVPDDSKAKKKAQNRAAQKAFRERKEARMKELQDKLLESERNRQSLLKEIEELRKANTEINAENRLLLRSGNENFSKDIEDDTNYKYSFPTKDEFFTSMVLESKLNHKGKYSLKDNEIMKRNTQYTDEAGRHVLTVPATWEYLYKLSEERDFDVTYVMSKLQGQECCHTHGPAYPRSLIDFLVEEATLNE
Protein: NAD(P)H-dependent FAD/FMN reductase GTNG_3158 (FAD/FMN reductase) (EC 1.5.1.45) (A4IT49)
Organism: Geobacillus thermodenitrificans (strain NG80-2)
Function: Involved in the pathway of tryptophan degradation. Reduces FAD/FMN to FADH(2)/FMNH(2), which are subsequently used for the hydroxylation of anthranilate. It can reduce either FAD or flavin mononucleotide (FMN) but prefers FAD. The enzyme has a slight preference for NADPH as acceptor.
Interaction partners:
Sequence:
MKLLGISGTLVGTKTCILVEQVLVEAKRICPEVDIQLLDLKDYQVEFCDGRQQSSYNEDTQKVIELVSVADCYVIGTPIFQGSITGALKNLFDLISPQALRHKVMGFVANGGTYQHYLVIENQLKPIASFFRAFVAPGSVYAHTDHFNEKNELVDPEVRERVAQLAWEVVHMHWSLKSGGVHAHR
Protein: Apyrase apy-1 (EC 3.6.1.6) (Uridine-diphosphatase) (UDPase) (Q19202)
Organism: Caenorhabditis elegans
Function: Hydrolyzes UDP and to a lesser extent GDP. By preventing the accumulation of NDP, may promote the reglucosylation of incompletely folded glycoproteins in the endoplasmic reticulum following the unfolded protein response.
Subcellular location: Endomembrane system {ECO:0000303|PubMed:18216284}; Single-pass type II membrane protein {ECO:0000305|PubMed:18216284}.
Interaction partners:
- Bifunctional purine biosynthesis protein ATIC
- UMP-CMP kinase 1
- UMP-CMP kinase 2
- Nucleoside diphosphate kinase
- Ribonucleoside-diphosphate reductase large subunit
- Uroporphyrinogen-III synthase
- Adenine phosphoribosyltransferase
- Ribonucleoside-diphosphate reductase small chain
- Nucleoside-diphosphatase mig-23
- Nucleoside-diphosphatase uda-1
Sequence:
MTQESNSNFFNFLLFGFVTAIAFYSGTQFNKSSEQEEHINHANLYSVKKFDDGAKEYSIMLITDLDHDSKDGKKWKSLVSRGFLKVSADHKHADIHFDKDSEYYVDTNIAAGGRAMELSDLAVFNGKLYSIDDRTGLIYQISDKKALPWVLLNDGPGNVVKGFKGEWITVKDTELIVGGLGKEWTTTDGVYVNDHPMWVKHVSAHGAVHHENWKDVYIRVRRAAGIEYPGYMIHEAVQWSAIHRKWFFLPRRMSNEKYSEAEDENRGTNVLVIGNEELTDFEVVRVGSENNKSRGFAAFQFVPNTHHQLIVAIKSEEKDGKPVASYASVFDIHGNVILDEYLLHGPYKYEGIAFA
Protein: Kaurene synthase like 2, chloroplastic (EC 4.2.3.-) (Ent-isopimaradiene like synthase) (A0A1X9ISP7)
Organism: Isodon rubescens (Rabdosia rubescens)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities. Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-isopimaradiene like compounds.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLLLSNSALVGPKFRSSRISHASASLDIGLQRATSPQNASVATCFEETKGRIAKLFHKNELSVSTYDTAWVAMVPSPTSSEEPCFPACLNWLLENQCHDGSWARPHHHHMLKKDVLSSTLACILALKKWGVGEEQISRGLHFVELNFASATEKGQITPMGFDIIFPAMLDNARGLSLNLQLEPTTLNDLIYKRDLELKRCNQSNSAEKEVYWAHIAEGMGKLQDWESVMKYQRKNGSLFNSPSTTAAAFIALRNSDCLNYLYSAMNKFGSAVPAVYPLDIYSQLCLVDNLERLGISRFFSTEIQSVLDDTYRCWLDGDEEIFMDASTCALAFRTLRMNGYSVTSDSFTKAVQDCFSSSIPSHMRDVNTTLELYRASEIMLYPDEIELEKQHSRLRSLLEHELSSGSIQSSQLNAVVKHALDYPFYAILDRMAKKKTIEHYEFDDTRILKTSFCSPTFGNKDFLSLSVEDYNRCQAIHRKEFRELDRWFKETKLDELKFARQKYTYSYCTAAASFASPELSDARMSWAKNSVLIGIVDDLFDVKGSVEEKQNLIKLVELWDVDVSTQCCSQSVQIIFSALRSTICEIGDKGFKIQGRSITDHIIAIWLDVLYNMMKESEWAENKSVPTIDEYMKISHVSSGLGPVVLPSLYLVGPKLSQEMVNHSEYHSLFKLMSTCCRLLNDIRSYEREVEGGKPNALALYRVSSGGEMMMSKEAAISELERLIERQRRELMRTILEESVIPKCCKEIFGH
Protein: Stretchin-Mlck, isoform G (EC 2.7.11.17, EC 2.7.11.18) (A1ZA70)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNDYGVEAAAASVAVEGPPEPPSGQPSVSLGPDRVAVAWCGPPYDGGCMITGFIIEMQTIGDENCDEDSWQQVTRVVDSLAYTVKNLQPERQYRFRVRAENIHGRSAPGQASELVQITNTPQRSTSSDASDRFGQATVSVQSGGDFKSRFEIIEELGKGRFGIVYKVQERGQPEQLLAAKVIKCIKSQDRQKVLEEISIMRALQHPKLLQLAASFESPREIVMVMEYITGGELFERVVADDFTLTEMDCILFLRQVCDGVAYMHGQSVVHLDLKPENIMCHTRTSHQIKIIDFGLAQRLDTKAPVRVLFGTPEFIPPEIISYEPIGFQSDMWSVGVICYVLLSGLSPFMGDTDVETFSNITRADYDYDDEAFDCVSQEAKDFISQLLVHRKEDRLTAQQCLASKWLSQRPDDSLSNNKICTDKLKKFIIRRKWQKTGNAIRALGRMANLSVSRRNSAIAMGVLSSPRPSISGLGMLTTSAIGSGTSSQMTSLHEEEDDFSGEMPPVEKRTVLKLRDKSQCSERSDSGYSECSNCSGAQETLLLSLAKSKLEAIAKASTLPTVVHDTEQPVSLELPTKGEAIMRSDFTNTIKMRKKSLEDSAAREKPRSKPQVKPLLSEEPGRSGRGAPSVSGKGKSPQVRSMPSSPLPQRSATPTRLMSQRVREAAERLAQQHTVASAQRHLGNGRGTGTGNGNGNSNSNGNGNGNTAETNRESRARRLINRFNSETQHITS
Protein: Cbb3-type cytochrome c oxidase subunit CcoP (Cbb3-Cox subunit CcoP) (C-type cytochrome CcoP) (Cyt c(P)) (Cytochrome c oxidase subunit III) (D5ARP7)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. CcoP subunit is required for transferring electrons from donor cytochrome c via its heme groups to CcoO subunit. From there, electrons are shuttled to the catalytic binuclear center of CcoN subunit where oxygen reduction takes place. The complex also functions as a proton pump.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}.
Interaction partners:
- Cytochrome c oxidase, Cbb3-type, subunit II
- Cytochrome c oxidase, Cbb3-type, subunit IV
- cytochrome-c oxidase
- Cytochrome c oxidase, Cbb3-type, accessory protein CcoG
- Cytochrome c oxidase, Cbb3-type, biogenesis protein CcoH
- Ubiquinol-cytochrome c reductase iron-sulfur subunit
- Cytochrome b
- Cytochrome c1
- Cytochrome c oxidase, Cbb3-type, maturation protein CcoS
- DUF465 domain-containing protein
Sequence:
MSKKPTTKKEVQTTGHSWDGIEELNTPLPRWWLWTFYATIVWGVAYSIAMPAWPIFASGATPGILGSSTRADVEKDIAKFAEMNKAVEDKLVATDLTAIAADPELVTYTRNAGAAVFRTWCAQCHGAGAGGNTGFPSLLDGDWLHGGSIETIYTNIKHGIRDPLDPDTLPVANMPAHLTDELLEPAQIDDVVQYVLKISGQPADEARATAGQQVFADNCVSCHGEDAKGMVEMGAPNLTDGIWLYGGDANTITTTIQLGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ
Protein: Vacuolar protein sorting-associated protein 51 (GARP complex subunit vps51) (O14146)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in retrograde transport from early and late endosomes to late Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 52
- Vacuolar protein sorting-associated protein 54
- t-SNARE affecting a late Golgi compartment protein 1
- Vacuolar protein sorting-associated protein 53
- Enhancer of rudimentary homolog 1
Sequence:
MSSKRRQALRDFYNLPGSNSSSSTVSTTRKPSSSNTVSPVEETALDKVDPEFSDPNFDSNAYVSKFMEKATPAELLQRDKSLVASIQGLSVDHRSLVYNHYKHLLEASDAINSFCKNLNTLLPALNDAYQACPKPTRKNGNNDTYSAPQSFNGNEFSAP
Protein: RAS guanyl-releasing protein 2 (Calcium and DAG-regulated guanine nucleotide exchange factor I) (CalDAG-GEFI) (Cdc25-like protein) (hCDC25L) (F25B3.3 kinase-like protein) (Q7LDG7)
Organism: Homo sapiens (Human)
Function: Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway.
Subcellular location: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Synapse, synaptosome {ECO:0000305}. Cell projection, ruffle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Found both in the cytosol and associated with membranes. Isoform 2 mainly localizes to the cell membrane. Enriched at juxtamembrane areas and membrane ruffles through association with F-actin. Localizes to the cell bodies and axons of striatal neurons (By similarity). {ECO:0000250}.
Interaction partners:
- Ras-related protein Rap-1A
- Ras-related protein Rap-1b
- GTPase NRas
- GTPase HRas
- GTPase KRas
- RAS guanyl-releasing protein 1
- Fermitin family homolog 3
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- Ras-related protein R-Ras2
Sequence:
MAGTLDLDKGCTVEELLRGCIEAFDDSGKVRDPQLVRMFLMMHPWYIPSSQLAAKLLHIYQQSRKDNSNSLQVKTCHLVRYWISAFPAEFDLNPELAEQIKELKALLDQEGNRRHSSLIDIDSVPTYKWKRQVTQRNPVGQKKRKMSLLFDHLEPMELAEHLTYLEYRSFCKILFQDYHSFVTHGCTVDNPVLERFISLFNSVSQWVQLMILSKPTAPQRALVITHFVHVAEKLLQLQNFNTLMAVVGGLSHSSISRLKETHSHVSPETIKLWEGLTELVTATGNYGNYRRRLAACVGFRFPILGVHLKDLVALQLALPDWLDPARTRLNGAKMKQLFSILEELAMVTSLRPPVQANPDLLSLLTVSLDQYQTEDELYQLSLQREPRSKSSPTSPTSCTPPPRPPVLEEWTSAAKPKLDQALVVEHIEKMVESVFRNFDVDGDGHISQEEFQIIRGNFPYLSAFGDLDQNQDGCISREEMVSYFLRSSSVLGGRMGFVHNFQESNSLRPVACRHCKALILGIYKQGLKCRACGVNCHKQCKDRLSVECRRRAQSVSLEGSAPSPSPMHSHHHRAFSFSLPRPGRRGSRPPEIREEEVQTVEDGVFDIHL
Protein: Cytochrome P450 98A9 (EC 1.14.-.-) (p-coumarate 3-hydroxylase) (Q9CA60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with CYP98A8 as tricoumaroylspermidine meta-hydroxylase. Involved in phenolamide synthesis, but a recombinant CYP98A9 is unable to hydroxylate triferuloylspermidine. Unable to use 5-O-(4-coumaroyl) D-quinate or 5-O-(4-coumaroyl) shikimate as substrates.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 98A8
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Cinnamoyl-CoA reductase 1
- Tapetum-specific methyltransferase 1
- Cinnamoyl-CoA reductase 2
- Shikimate O-hydroxycinnamoyltransferase
- Phenylalanine ammonia-lyase 4
- Phenylalanine ammonia-lyase 2
- Phenylalanine ammonia-lyase 3
Sequence:
MDLLLISLTTIIIAAYMQNLRRRGSNIPPGPPTRFLVGNLHQLKPLWTQSFSEWSQTYGPIISVWLGSQLAVVVSSSDLAKQVLRDKDYQLCNRHRTARMTQNGSDLIWSDYGAHYVKMRKLCTLELFSLKSIECFRSMREMEVSSMVKSIFNDFMSDDQKPVVLRNYLDSVALNIVSRLVIGKTFEPKDGREFRSIVERETRLPGATKMLDYTVWLKRLSSWFTSDKAFMKHMARKRNWFKRAVMDEVYGGRDQKCFVQSLLELKEKDELTEETVMGLVWNMLTAGADTTAITIEWAMAEMIRCPTVKEKVQDELDSVVGSGRLMSDADIPKLPFLQCVLKEALRLHPPTPLMLPHKASESVQVGGYKVPKGATVYVNVQAIARDPANWSNPDEFRPERFLVEETDVKGQDFRVLPFGSGRRVCPAAQLSLNMMTLALGSLLHCFSWTSSTPREHIDMTEKPGLVCYMKAPLQALASSRLPQELYL