wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (V9GXQ9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALEAVGKSENDLEGRILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASILEDDNEEEIESADQEEEAHPEYKFGNELSADDYSHKEAVANSVKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANPAKANVTPQSSSELRPTTTAALGSGQEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEIKKETEIKIQTLTTDHKSKGKQGDESPSG
Protein: Homeobox protein Hox-C4 (Homeobox protein CP19) (Homeobox protein Hox-3E) (P09017)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-C6
- Homeobox protein Hox-C5
- Homeobox protein Hox-B5
- Homeobox protein Hox-B6
- Homeobox protein Hox-A6
- Homeobox protein Hox-A5
- Homeobox protein Hox-D4
- Homeobox protein Hox-B7
- Homeobox protein Hox-A7
- Homeobox protein Hox-B4
Sequence:
MIMSSYLMDSNYIDPKFPPCEEYSQNSYIPEHSPEYYGRTRESGFQHHHQELYPPPPPRPSYPERQYSCTSLQGPGNSRGHGPAQAGHHHPEKSQSLCEPAPLSGASASPSPAPPACSQPAPDHPSSAASKQPIVYPWMKKIHVSTVNPNYNGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRIEIAHSLCLSERQIKIWFQNRRMKWKKDHRLPNTKVRSAPPAGAAPSTLSAATPGTSEDHSQSATPPEQQRAEDITRL
Protein: Zinc-dependent endopolyphosphatase (EC 3.6.1.10) (Vacuolar polyphosphatase PPN2) (P40152)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydrolysis of inorganic polyphosphate (polyP) chains of many hundreds of phosphate residues into shorter lengths. Exclusively shows endopolyphosphatase activity, cleaving inside the polyP chain. Together with PPN1, responsible for a substantial fraction of polyphosphatase activity that is necessary to mobilize polyP stores in response to phosphate scarcity.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23708375, ECO:0000269|PubMed:28302909}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Endopolyphosphatase
- Protein phosphatase PP2A regulatory subunit A
- Polyphosphatase
- Protein phosphatase methylesterase 1
- Factor arrest protein 8
Sequence:
MEDKRKRRAATLSTALILFVACCVYTLYIFKFDNPRLSPPVSLLPTISTLKKIEHVTDLNKEYVFVGDVHGNYDEFIELIDDKIGGLGENITMILLGDFIHKGPDSDKVVSYILNHKDQVKCVLGNHEILVMMAYLNPDFSKWVRRPKLMTPLTFSTETNFIPQDISKISNAHGRLARELGFSKLSQLAEHCSMAIELDLDITGDILFGAHAGMVPGDFMKPNQIPGVSSLSNMKYVDKKNWSKTSREKENKNYVRWYTLWDKYGDHFSNAKVFYGHDASMGLNLRRQTKGLDTACIKNNLLSSMKVKYDIKKGQYDYELIQVQCS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VTY8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPPKMEPISVRTARLNNLILGKGAGVCAKPAGSASGSGIPASTRRSIVPVSTTSAAVAEAICREGLLDAFCLLYNECDKDTLKKRDRNIAEFVNKFRPIIEETRKLRVNADDFLIKTLIGQGYFGNVHLVVERQTNDIYAMKKIKKSVVTTSQVKEERDIMSIRNSEWLINLQYAFQDNDNLYLVMEYMPGGDLLSLMSRHGPFDEDLARFYLAELTVALHTLHEMGYVHRDIKPENILIDRFGHIKLADFGNAAALDRDGHVLSLSPVGTPDYIAPELLQTISTYKLSKSMHDVSCDYWSMGIIGYELICETTPFHEDNVHETYSKILSHCEESHLKELISFPADLKVSVNYRNLIESLVTNPSKRLSYERIKNHPFFSEIPWGSIRSQVPPIIPTVRSDDDTSNFEDGIRHKTRREQGVAKKSLTTNMKSNDFSGKDLPFIGYSFVHMEKSAISATTDEKLQEKLKELLQKLKTRENEISMLKQDLLRAQQSLRKTDNKSQVVADAKMEIKKLQQIIKEKTMELTTCKTQIKTLQSSAKIDEEMWSKKEATITDLLRLNRQKYEEAKIASEQRYEKQLADKKQELASTLQKLDARELEFNAKFEECKHLSMKLQNYKDMLQQIKEQNLKSETNHEEQRRQMAELYEQKLTDLRKKVRDSQDTNRRMTMEIKEIRTELDESISSSKSTQEAKNATERNIEEILRRLNEEIASNNELHAEKVKLETKLQLKENETQEVRAECHRLERELQLAECRCQLAESSLATQVSPYETAPGSLTELNAIEDQLRADLLAAKESENHQKGRADQLQTLVTKLEQMLERFNEQSLSPTKSHSSRKQEGETVGDMLERQNEKLEDKLAAVREQMIVERQAARTANLSLWKVEKQLEEALSEKKLLARRMELTEDRIKKVQNASDEAQRMLKTSQEETRQRESRIEELKQELAAAKRDVLKEHRQWEKAEQERMKCKSEIIEHLANVHRLEQQETELRQKLRQIQSRFDGVTLEQKNTIRELQEEREKSRKANDSCLVLQKELKQLTDNFQRLKYACSITDSQLTEVETMLKSEQERNKSQKSQLDTLHEKLRERNDQLTDLRKQLTTVESEKRLAEQRAQVLASEIDELRLNLKEQQKKLVAQQDQLVEQTNALFATQERAELLDGQNANYEAQTADSNREMVSLKEENARILSELFHKKEEVGNLQAEIRGLESAQANLHAEIDSLQDTLAEKEQFYVQRDIKSNATLAQHKKLIDYLQLKVEDLSAKKKKTLADKLFGSSHTNKENVSPNDVESSILYRALKEELKREQKMNSLLKEQLAQLNGTATLRSPRKSAAVNGDSDAPKQRPVSIAALPRSPQKQQQPLKRTTSQVELKTTAEKPTKVTIENQAHHRFELALQESKVDAVNCVVCEKAVVAGSPFWKCKECKDVTHRKCRSNVQSHCGSTKPTAPSADDLSSIQSVSSLTLDSVDVAGGTTSGGEYIGSLVYSSDGAEDQARKEIEVNCAFEVAEQQILLLGCNTGLYAYHLDSQRLVHISGLESVSCMSICKRLAKAIMVGTVGEKLYQCDYRQLESRCQSSSSCHKPVLETSAIELPFANRTPSEKWKLVLISDEAENALDSVAIAATSTRIVILKYDLKLHMFKPVRALDTATPVTSIFFTRHSAIVSSDKFYEIDLDNYAAEEFVDLSDKSMESTAKCQPLTAVRISRQEYLLCFAEYGVFVDEFGCRSRPYDLNWVYAPTGFVYRDPFLFISHYQSVQIVRLHRSFSKEMASGDNASENSESPELQRVYLPHYMSTLLANSGDVNLYAVAIDQRPCNGTQKIYHLDTMQAFKQKFNISMETLSSVATSVTLGSTVTGNSI
Protein: Sterol 14alpha-demethylase (EC 1.14.15.36) (CYPLI) (Cytochrome P450 51) (Cytochrome P450-14DM) (Cytochrome P450-LIA1) (Sterol 14-alpha demethylase) (P9WPP9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sterol 14alpha-demethylase whose physiological substrate is not known. Accepts electrons from the iron-sulfur ferredoxin Fdx encoded by an adjacent gene. In vitro, catalyzes C14-demethylation of lanosterol, 24,25-dihydrolanosterol and obtusifoliol, to produce the 8,14-dienes stereoselectively.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Putative cytochrome P450 123
- Nuclear transport factor 2 family protein
- Ferredoxin Fdx
- Probable oxidoreductase
- Uncharacterized HTH-type transcriptional regulator Rv0767c
- Uncharacterized oxidoreductase Rv0770
- Possible 4-carboxymuconolactone decarboxylase
- Polyketide synthase Pks13
- Probable aldehyde dehydrogenase NAD dependent AldA
- Cytochrome P450 130
Sequence:
MSAVALPRVSGGHDEHGHLEEFRTDPIGLMQRVRDECGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSACLIGKKFRDQLDGRFAKLYHELERGTDPLAYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRNDHSKMVVQLAQPACVRYRRRTGV
Protein: Mitochondrial carnitine carrier (Q12289)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transports carnitine, acetylcarnitine, propionylcarnitine and to a much lower extent medium- and long-chain acylcarnitines.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Carnitine O-acetyltransferase, mitochondrial
- Putative mitochondrial carnitine O-acetyltransferase
- Carnitine O-acetyltransferase YAT2
- Mitochondrial pyruvate carrier 3
- Acetyl-coenzyme A synthetase 1
- Citrate/oxoglutarate carrier protein
Sequence:
MSSDTSLSESSLLKEESGSLTKSRPPIKSNPVRENIKSFVAGGVGGVCAVFTGHPFDLIKVRCQNGQANSTVHAITNIIKEAKTQVKGTLFTNSVKGFYKGVIPPLLGVTPIFAVSFWGYDVGKKLVTFNNKQGGSNELTMGQMAAAGFISAIPTTLVTAPTERVKVVLQTSSKGSFIQAAKTIVKEGGIASLFKGSLATLARDGPGSALYFASYEISKNYLNSRQPRQDAGKDEPVNILNVCLAGGIAGMSMWLAVFPIDTIKTKLQASSTRQNMLSATKEIYLQRGGIKGFFPGLGPALLRSFPANAATFLGVEMTHSLFKKYGI
Protein: Protocadherin 1 (E0CXD4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPLRPSPGPGGQRLLLPPLLLALLLLLAPSASHTTQVVYKVPEEQPPNTLIGSLAADYGLPDVGHLYKLEVGAPYLRVDGKTGDIFTTETSIDREGLRECQNQIPGNPCILEFEVSITDLVQNGSPRLLEGQIEVQDINDNTPNFASPVITLAIPENTNIGSLFPIPLATDRDAGPNGVASYELQAGPEAQELFGLQVAEDQEEKQPQLIVMGNLDRERWDSYDLTIKVQDGGNPPRASSALLRVTVLDTNDNAPKFERPTYEAELSENSPIGHSVIQLPHRRVTFSATSQAQELQDPSQHSYYDSGLEESETPSSKSSSGPRLGPLALPEDHYERTTPDGSIGEMEHPENEPAGRSRP
Protein: Nuclear pore complex protein Nup153 (153 kDa nucleoporin) (Nucleoporin Nup153) (Q640Z6)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. May be involved in the retention of unspliced mRNAs in the nucleus. Probably mediates tpr anchoring to the nuclear membrane at NPC. Possible DNA-binding subunit of the nuclear pore complex (NPC) (By similarity).
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:9531546}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:9531546}. Note=Localized to the nucleoplasmic side of the nuclear pore complex (NPC) core structure, forming a fibrous structure called the nuclear basket. Colocalizes with tpr at the nuclear pore complex.
Interaction partners:
Sequence:
MAAAGGGGPGGPGTGGKIRSRRYHLSSGRTPYSKSRQQQQGIISRVTDTVKSIVPGWLQKYFNKQEEEHDRVHSASEVIVNDTEARENNAEHHIYVVDDDDDEEGNSPTDGRVTPEPIINVDEEVPSTSQSAINNTDALTRPSLHRASLNFNIFDSPALNCQPSTSSAFPIGTSGFSLIKEIKDSTSQHDDDNISTTSGFSSRASDKDLAVSKNVSVPPLWSPEVDRSQSLSHNSSMTSKKPTFNLSAFGSLSPSLGNASILNRQLGDSPFYPGKTTYQGAAAVRSSRVRATPYQAPLRRQVKAKPAAHSQQCGVTSSAARRILQSLEKMSSPLADAKRIPSNSSLSHTPEKNVMDIPENPSKRKKVESPFPPVQRLVTPKSISVSANRSLYIKPSLTPSAVSNTNSRRIQPDKHNESRKNNLQTTSQSHSFSYPKFSTPASNGLSSGTGGGKMMREKGSHYSTKPANEELDGPVLPEIPLPLSTAALPSFQFSTLSGSATSPISVTKPANSTTCRLTSSSPSFTFSSPIVKSTESNAQSPGSSVDFTFSVPAAKASSATSDESKVSAVSRAAKTHAAVSSAKNTDDEQLGFCKPAKTLKEGSVLDMLRSPGFSSSPSLLTSASSLNRSTPTLSKTVGNTFSPANVSLGVGSKQAFGLWQCSACFHENMSSDSNCISCSALKPRPTETSKKLPASPPSSNTKSTVPLSSTPGLGDIFKKPAGMWDCDTCLVQNKAEVTKCVACETPKPGTGMKATLLIPSTTKSTNPATNTLAFASCSASIPNEEMFKKPMGSWECTVCHMQNKTEDNTCVGCKAEKPGTVKSVPTAAPSGLLGLLDQFKKPTGSWDCDVCLIQNKPEANKCIACESAKPGTKAELKGTFDTVKNSVSVAPLSSGQLGLLDQFKKSAGSWDCDVCLVENKPEATKCVACETSKPGTKAELKGFGTSTFSSGTAAPTFKFGVQSSDSTAELKSGASTSGFAKSIGNFKFGLASASTTTEETGKKSFTFGSSTTNEVSAGFKFGIAGSAQTKPDTLSQSTTSGFTFGSVSNTVSLAPTATSSGSTGLQVAAVIADSNLATTATLKSAEEKKAEAPTITPFSFGKTDQNKETASTSFVFGKKDEKTDSAPTGSSFAFGLKKDGEESKQFLFGKPEPTKVDGSAASAGFAFGVTNPTEKKDIEQPGKSVFAFGAQTSITDAGASKQPFSFLTNVSSTAASSSTCGVSSSVFGSVTQSSTPATPSNVFGSAISANAPAPSSGVFGNLTPSNAPAASSTLFGNVAPSSTPSGSSGLFGTAAASSTPATSTSLFGSAAKLSAPASSGGVFNSAAPAAPASTASSVFGSVASSTNTSANSANIFGSSGGAATAPGAFVFGQPASTASTVFGNSSESKSTFVFSGQENKPVTSASTSVTPFLFGAVSASTTPAAPGFNFGRTITSNTTGTSSSPFIFGAGASGSASSSITAQANPVPAFGQSSNPSTAPAFGSSTSVPVFPAGNSQQVPAFGSSSAQPPVFGQQATQPSFGSPAAPSAGSGFPFGNNANFNFNSTNSSGGVFTFNANSGSTTQPPPPGYMFNAAAPGFNMGTNGRTTPASTISTRKIKTARRRK
Protein: Uncharacterized protein (Q57ZE2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Transmembrane protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Letm1 RBD domain-containing protein
- Uncharacterized protein
Sequence:
MVLFSTYRSSRLVSKEFLHGPVMRFRALGEYYFQRAWNGTLNWALPGEYRLYAVMIPFIYFYHRWHNDHTLDRDHVEKAMIMRWGGTLEDVRKLSAKDQLRVRCFTDIEKLYSAYGPKDTYLQPPGDTLPGKDFYRKAGGAQAHH
Protein: Serine/threonine-protein kinase Nek8 (EC 2.7.11.1) (Never in mitosis A-related kinase 8) (NimA-related protein kinase 8) (Q90XC2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for renal tubular integrity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q91ZR4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91ZR4}. Cell projection, cilium {ECO:0000250|UniProtKB:Q91ZR4}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q86SG6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q86SG6}. Note=Predominantly cytoplasmic. Localizes to the proximal region of the primary cilium and is not observed in dividing cells (By similarity). {ECO:0000250|UniProtKB:Q91ZR4}.
Interaction partners:
- Nephrocystin-3
- Inversin
- Ankyrin repeat and sterile alpha motif domain-containing 3.
- Si:dkey-202c5.1 protein.
- Nephronophthisis 1.
- Centrosomal protein of 290 kDa
- RPGR-interacting protein 1.
- Meckelin isoform X1
- IQ calmodulin-binding motif-containing protein 1
- Zinc finger protein 423.
Sequence:
MEKYEKTKVVGRGAFGIVHLCRRRTDSALVILKEIPVEQMTRDERLAAQNECQVLKLLSHPNIIEYYENFLEDKALMIAMEYAPGGTLADYIQKRCNSLLDEDTILHSFVQILLALYHVHNKLILHRDLKTQNILLDKHQMIVKIGDFGISKILVSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMSGTFAPISDRYSPELRQLILNMLNLDPSKRPQLNEIMAHAICIRPLLNLYTDIGNVKMRRIEKPLSNVQAGPHGRPGGWITSTRTRGGLSSLTSSKMMHPLPLFSVYTWGSGISTPLRLPMLNTEVIQVSLGRTQKMGVTKSGRLITWEAPSVGSGEPTLPGAVEQMQPQFISRFLEGQSGVTIKSVSCGDLFTTCLTDRGIIMTFGSGSNGCLGHGNFNDVTQPKIVEALLGYELVQVSCGASHVLAVTNEREVFSWGRGDNGRLGLATQDSHNCPQQVSLPADFEAQRVLCGVDCSMIMSTQHQILACGNNRFNKLGLDKVSGTEEPSSFCQVEEVHLFQLVQSAPLNTEKIVYIDIGTAHSVAVTEKGQCFTFGSNQHGQLGCSHRRSSRVPYQVSGLQGITMAACGDAFTLAIGAEGEVYTWGKGARGRLGRKEEDFGIPKPVQLDESHAFTVTSVACCHGNTLLAVKPFFEEPGPK
Protein: Probable thiamine biosynthetic bifunctional enzyme [Includes: Thiamine-phosphate synthase (TP synthase) (TPS) (EC 2.5.1.3) (Thiamine-phosphate pyrophosphorylase) (TMP pyrophosphorylase) (TMP-PPase); Hydroxyethylthiazole kinase (EC 2.7.1.50) (4-methyl-5-beta-hydroxyethylthiazole kinase) (TH kinase) (THZ kinase)] (P40386)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
Interaction partners:
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1
- Thiamine-repressible acid phosphatase pho4
- Thiamine thiazole synthase
- 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase
- Alkaline phosphatase
- Acid phosphatase
- Thiamine-repressible acid phosphatase SPBC21H7.03c
- Low molecular weight phosphotyrosine protein phosphatase
Sequence:
MKRQIDYSLYLVTSSSLIAPGSTIERQVEEGILGGVTLVQHREKDISTKCFVERAKRLSEICKKYDVPFLINDRIDVALAVGADGVHIGQDDMDCALARKILGDDAIIGVSTNNIEEIEKAAADGADYVGIGSIYETNTKDVKDRLIGITGLRKILEHVSKMHCQLGTVAIAGLNSSNIQRVIYLSEANGKRIDGIALVSAIMCSITPRETAKELRNLIATPPCFAQARSSLTTPKDLLNQIPAALQKLKDFTPLIHHLTNAVAKNFSANVTLAAYGSPTMGESYDEVADFAKAPGALVLNIGILENTKTYIHAAQVNNDLARPVILDPVAVGATTARSKVINTLLNYAYYDIIKGNEGEIMNLAGEQGLMRGVDSISQHTLAARITAVHRLAVERRCVVAMSGAVDVISDGNSTYVIKNGNPLLGQITASGCSLGSVMGVTASICQNDKLLAAITATLLYNIASELAVEAKNSCGDLLVQGPGTFIPIFVDKLHQLINETIKGNVDWIERAKLEKAE
Protein: Pentatricopeptide repeat-containing protein 2, mitochondrial (Q8WV60)
Organism: Homo sapiens (Human)
Function: Involved in mitochondrial RNA maturation and mitochondrial respiratory chain function.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18729827}.
Interaction partners:
- Pentatricopeptide repeat-containing protein 1
- Small ribosomal subunit protein mS39
Sequence:
MVRDSMAAAFRPSNRVLLQALQILVYPGVGGSGSVSCRCPLGAKRYLLTDNVVKLKEFQQKKVAVACNLSGTKETYFRNLKKKLTQNKLILKGELITLLHLCESRDHVELAKNVIYRYHAENKNFTLGEYKFGPLFVRLCYELDLEESAVELMKDQHLRGFFSDSTSFNILMDMLFIKGKYKSALQVLIEMKNQDVKFTKDTYVLAFAICYKLNSPESFKICTTLREEALLKGEILSRRASCFAVALALNQNEMAKAVSIFSQIMNPESIACINLNIIIHIQSNMLENLIKTLKNAAEGNLSKFVKRHVFSEEVLAKVREKVKDVPALVAKFDEIYGTLHITGQVTTDSLDAVLCHTPRDRKSHTLLLNKRMVSRRTFQPLSQSLLAE
Protein: Gamma-soluble NSF attachment protein (N-ethylmaleimide-sensitive factor attachment protein gamma) (A0A0G2K350)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170, ECO:0000256|RuleBase:RU367013}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170, ECO:0000256|RuleBase:RU367013}.
Interaction partners:
- Alpha-soluble NSF attachment protein
- Beta-soluble NSF attachment protein
- Vesicle-fusing ATPase
- Golgi SNAP receptor complex member 1
- Syntaxin-7
- Syntaxin-8
- Syntaxin-12
- NBAS subunit of NRZ tethering complex
- Vesicle-associated membrane protein 4
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MAAQKINEGLEHLAKAEKYLKTGFLKWKPDYDSAASEYGKAAVAFKNAKQFEQAKDACLREAVAHESNRALFHAAKAYEQAGMMLKEMQKLPEAVQLIEKASMMYLENGTPDTAAMALERAGKLIENVDPEKAVQLYQQTANVFENEERLRQAVELLGKASRLLVRGRRFDEAALSIQKEKNIYKEIENYPTCYKKTIAQVLVHLHRNDYVAAERCVRESYSIPGFNGSEDCAALEQLLEGYDQQDQDQVSEVCNSPLFKYMDNDYAKLGLSLVVPGGGIKKKSPATPQAKPEGAAGAAAEEEEDEYSGGLC
Protein: Parathyroid hormone-related protein (PTH-rP) (PTHrP) [Cleaved into: Osteostatin] (Q7YRI2)
Organism: Cervus elaphus (Red deer)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368098}. Nucleus {ECO:0000256|RuleBase:RU368098}. Secreted {ECO:0000256|RuleBase:RU368098}.
Interaction partners:
Sequence:
QWSVXVFLXSYSVPSCGRSVEELGRRLKRAVFEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPAPNTKNHPVRFGSDDEGKYLTQETNKVETYKEQPLKTPGKKKKSKPGKRKEQEKKKRRTRSTLLTSGVAGTGLEEDYLCDISATSLELDSRRH
Protein: La-related protein 1A (AtLARP1a) (Q940X9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for acclimation and survival during thermal stress. Heat-specific cofactor of XRN4 required for its targeting to polysomes and subsequent rapid degradation of seedling transcriptome during the early steps of the heat stress response.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:24332370}. Cytoplasm, cytosol {ECO:0000269|PubMed:24332370}. Note=Translocates from cytosol to P-bodies upon heat stress.
Interaction partners:
- Eukaryotic translation initiation factor isoform 4G-2
- Pumilio homolog 4
- Eukaryotic translation initiation factor 4G
- Serine-threonine kinase receptor-associated protein
- Serine-threonine kinase receptor-associated protein
- At1g17330
- Eukaryotic translation initiation factor isoform 4G-1
- Pumilio homolog 2
- Regulatory-associated protein of TOR 2
- Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1
Sequence:
MMAETEGSVADDRELITREGGIGTKSPWKTTTSPVETIDAPVMGAHSWPALADAAQQPRPKNPPAPAPAPPSKNIPTSIPIPTPAVTGQAKSKGGGKANPGHKNPSGRHSKPGPRSNQNGPPPPPYLVHAVPYHPPPFPPMVPLPHAAGPDFPYAPYPPYPVPVPPVTESGNEKQVQASPLPPVLPAPQGDPGKPWPHQRGFDPRNMPQGAGPRNFGRPPFMGPAPGFLVGPGPGFPGPVYYLPGPPPGAIRGPYPPRFAPYPVNQGPPILSPEKLDLRDRVLKQVEYYFSDENLENDHYLISLMDEEGWVPTKIIAGFKRVKAMTMDVDFIVYALGFSNSVEVQGDQIRKRDKWSDWIPASKKSTSAETIGDGDKDSPKSITSGDNFGNPSKGSSKPTVSDFSSEGAQSSRTNNYKSGNLKSSADEKRNVEDLSNDFSNTFLLDEELDLEHRSPRKSGLSMSKSIEYEDDDMAVDDQDIQKLVIVTQNSGKSDGAGIGGTEAKNIPKELASTINDGLYYFEQELKKKRSGRRKNNSHLDTKDGKIKSGEGLNTKLGENSAANDGGEEHGIITSRRKQNKGTHKHHTAHARRFFSSNIRNNGNISESPPSSSIGFFFGSTPPDSHGPRLSKLSSSPQCTLSGSSPPVGSLPKSFPPFQHPSHQLLEENGFKQEKYLKYRKRCLNERKKLGSGCSEEMNHLYRFWSYFLRDTFVLSMYDDFQKFALEDAAGNYDYGLECLFRFYSYGLEKHFDEDLYKDFEKLSLDFYHKGNLYGLEKYWAFHHYRGKEEPITKHPELEKLLKEEFRSIDDFRAKETITNQKENKSH
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FPS5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- quinol--cytochrome-c reductase
- Candida glabrata strain CBS138 chromosome J complete sequence
- Cytochrome b-c1 complex subunit 7
- Complex III subunit 9
Sequence:
MGPLRVAIVGANGKIGHLLTAKLKNSKASFATPVAIVRNEEQVKHFQDEMGVDASLASIESATVPELQKAFTGCDAVVFTAGAGGKGVERIFTVDLEGCAKVVEACEKSGISRFVIVSAIKAEDRDFWWGLEGLRNYYIAKKAADQYVRNSKLDWTILQPGFLDTNSGTGKLVPQDQLESKKDDNYRIQREDVAEFIVQSLLHPAETKLKTISLANGDVPIADFIKSL
Protein: Transketolase (EC 2.2.1.1) (Q5A750)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transaldolase
- Glucose-6-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Ribulose-phosphate 3-epimerase
- Fructose-bisphosphate aldolase
- fructose-bisphosphatase
- Glyceraldehyde-3-phosphate dehydrogenase
- Ribose-5-phosphate isomerase
- Enolase 1
- Triosephosphate isomerase
Sequence:
MPSLDELTISTIRGLSVDAVSAANSGHPGAPLGLAPAAHVVWQKMKFNPKDPNWINRDRFVLSNGHACALLYSLLVLYKFELTVDDLKQFRQLGSKTPGHPEATDTAGVEVTTGPLGQGISNAVGIAIAQKQFAATYNKPDITLSDSYVYTFVGDGCLMEGVSSETSSLAGHLQLNNLIAFWDDNRISIDGDTAVSFTENVPDRYRAYGWNVLEVPDANTNIEAIAAAVDEAKKSTDKPTLIRLVTTIGYGSLKQGSHDVHGSPLKPDDIKQLKKSWGFKEDVDFFIPEEVSEYLAKHVSENQKVQKEWEAKLAEYKKKYPTEGAEIQRRLDGKLPEGWKEYLPKYTPADKPLATRKLSENVINALHGKIPEFIGGSADLTGSNLTRAEGSVDFQPPSTGLGNYDGVYIRYGVREHGMGAIMNGIAAFGANYKNYDGTFLNFVSYAAGALRLSALSHHPVIWVATHDSIGLGEDGPTHQPIETLAHFRAIPNLSVWRPADGNEVSAAYAAAIESTSHPSVIALTRQNLPQLEGSSIENALKGGYTLVKKDNPDVIIVSSGSEVSISVAASEELAKQGVKANVVSLPDFFTFDQQSDEYRLSVLPDGVPILSVEVMSTFGWSKYSHEQFGLNRFGASGKAADLYKYFEFTPEGIAERAQKTIKYYEGKQLLSPLDRAF
Protein: Stau1 protein (Q9ESY8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MYKPVDPHSRMQSTYSYGMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKMRPPVKHDATARALRTLQSEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTRVSVGEFVGEGEGKSKKISKKNAARAVLEQLRRLPPLPAVERVKPRIKKKSQPTCKLQTAPDYGQGMNPISRLAQIQQAKKEKEPEYMLLTERGLPRRREFVMQVKVGHHTAEGAGTNKKVAKRNAAENMLEILGFKVPQAQPAKPALKSEEKTPVKKPGDGRKVTFFEPSPGDENGTSNKEDEFRMPYLSHQQLPAGILPMVPEVAQAVGVSQGHHTKDFARAAPNPAKATVTAMIARELLYGGTSPTAETILKSNISSGHVPHGPRTRPSEQLYYLSRAQGFQVEYKDFPKNNKNECVSLINCSSQPPLVSHGIGKDVESCHDMAALNILKLLSELDQQSTEMPRTGNGPVSACGRC
Protein: Processive diacylglycerol beta-glucosyltransferase (EC 2.4.1.315) (Beta-diglucosyldiacylglycerol synthase) (Beta-DGS) (DGlcDAG synthase) (Glc2-DAG synthase) (Beta-gentiobiosyldiacylglycerol synthase) (Beta-monoglucosyldiacylglycerol synthase) (Beta-MGS) (MGlcDAG synthase) (Beta-triglucosyldiacylglycerol synthase) (TGlcDAG synthase) (Diglucosyl diacylglycerol synthase (1,6-linking)) (Glucosyl-beta-1,6-glucosyldiacylglycerol synthase) (UDP glucosyltransferase) (UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase) (P54166)
Organism: Bacillus subtilis (strain 168)
Function: Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). Also seems to be able to form beta-tetraglucosyl-DAG, although this glycolipid has not been found in B.subtilis membrane. UgtP can only use UDP-glucose as sugar donor.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01280}. Note=Localized in both septal membrane. {ECO:0000269|PubMed:15743965}.
Interaction partners:
- Cell division protein FtsZ
- Lipoteichoic acid synthase 1
- Lipoteichoic acid synthase 2
- Diacylglycerol kinase
- UTP--glucose-1-phosphate uridylyltransferase
- Lipase EstA
- Extracellular esterase EstB
- Phosphatidylglycerol lysyltransferase
- Phosphoglucomutase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
Sequence:
MNTNKRVLILTANYGNGHVQVAKTLYEQCVRLGFQHVTVSNLYQESNPIVSEVTQYLYLKSFSIGKQFYRLFYYGVDKIYNKRKFNIYFKMGNKRLGELVDEHQPDIIINTFPMIVVPEYRRRTGRVIPTFNVMTDFCLHKIWVHENVDKYYVATDYVKEKLLEIGTHPSNVKITGIPIRPQFEESMPVGPIYKKYNLSPNKKVLLIMAGAHGVLKNVKELCENLVKDDQVQVVVVCGKNTALKESLSALEAENGDKLKVLGYVERIDELFRITDCMITKPGGITLTEATAIGVPVILYKPVPGQEKENANFFEDRGAAIVVNRHEEILESVTSLLADEDTLHRMKKNIKDLHLANSSEVILEDILKESEMMTAKQKAKVLS