wanglab/gogpt-training-data huggingface dataset:
Protein: IP13286p (Zinc transporter 33D, isoform C) (Q4V528)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSKKSLKRQDEHTKDNDCEEEDEEELQAAIREMVKIPDIDIIPRKSSESVREKESTGNVLKKNHDERGSQTGDGKDTTSKTRQKKLESDDSWAALLRKRFAWTKDNKTDAVNQNIPNTKGSSKDFTENKGSGNKHSTVTSNEKLIRSEYYENSQTKSDAIKSLSNNQLSEESPEFLNKLRRIEEASKPKTWKRPTPVVLKSNQNYSANKNSENALDAKPQTATNTEETHGCINILKVPFQSNLYYVPEKPSRQDKGSGTSDFQPGAPETPIVENSAVDSDRKAVEIMPENVKNSEEKKIDNSDSTKTVTITGHSHITAKWDGHCHFKERETGVDKAARRVLIIACILCTIFLILEVIGGILSNSLAIATDAAHLLTDLASFLISISALHLAGRPSSERLNYGWHRAEVIGAMVSIFFIWVVTGERHPRVHGHNAMG
Protein: 5'-nucleotidase (5'-NT) (EC 3.1.3.35) (EC 3.1.3.5) (EC 3.1.3.89) (EC 3.1.3.91) (EC 3.1.3.99) (5'-deoxynucleotidase) (Ecto-5'-nucleotidase) (IMP-specific 5'-nucleotidase) (Thymidylate 5'-phosphatase) (CD antigen CD73) (Q61503)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of nucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside. Hydrolyzes IMP. Shows a preference for ribonucleotide monophosphates over their equivalent deoxyribose forms (By similarity). Although AMP is the preferred substrate can also hydrolyze UMP, GMP, CMP, dAMP, dCMP, dTMP, NAD and NMN (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P21589}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P21589}.
Interaction partners:
- Ectonucleoside triphosphate diphosphohydrolase 1
- Adenosine deaminase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Endoglin
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
Sequence:
MRPAAAKVPKWLLLALSALLPQWPAASAWELTILHTNDVHSRLEQTSDDSTKCLNASLCVGGVARLFTKVQQIRKEEPNVLFLDAGDQYQGTIWFTVYKGLEVAHFMNILGYDAMALGNHEFDNGVEGLIDPLLRNVKFPILSANIKARGPLAHQISGLFLPSKVLSVGGEVVGIVGYTSKETPFLSNPGTNLVFEDEISALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDIVVGGHSNTFLYTGNPPSKEVPAGKYPFIVTADDGRQVPVVQAYAFGKYLGYLKVEFDDKGNVITSYGNPILLNSSIPEDATIKADINQWRIKLDNYSTQELGRTIVYLDGSTQTCRFRECNMGNLICDAMINNNLRHPDEMFWNHVSMCIVNGGGIRSPIDEKNNGTITWENLAAVLPFGGTFDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDINRKPWNRVVQLEVLCTKCRVPIYEPLEMDKVYKVTLPSYLANGGDGFQMIKDELLKHDSGDQDISVVSEYISKMKVVYPAVEGRIKFSAASHYQGSFPLVILSFWAMILILYQ
Protein: Protein LATERAL ORGAN BOUNDARIES (ASYMMETRIC LEAVES 2-like protein 4) (AS2-like protein 4) (Q9FML4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not known; ectopic expression of LOB leads to alterations in the size and shape of leaves and floral organs and causes male and female sterility.
Interaction partners:
- Transcription factor AS1
- Homeobox protein knotted-1-like 2
- Homeobox protein knotted-1-like 6
- Floral homeotic protein APETALA 2
- Basic leucine zipper 8
- Auxin transporter protein 1
- Auxin response factor 4
- Auxin response factor 3
- Probable transcription factor KAN2
- Transcription repressor KAN1
Sequence:
MASSSNSYNSPCAACKFLRRKCMPGCIFAPYFPPEEPHKFANVHKIFGASNVTKLLNELLPHQREDAVNSLAYEAEARVRDPVYGCVGAISYLQRQVHRLQKELDAANADLAHYGLSTSAAGAPGNVVDLVFQPQPLPSQQLPPLNPVYRLSGASPVMNQMPRGTGGSYGTFLPWNNGHDQQGGNM
Protein: BRCA1 associated protein (J3KNN7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDEEIKKTTLASAVACLEGKSPGEKVAIIHQHLGRREMTDVIIETMKSNPDELKTTVEERKSSEASPTAQRSKDHSKECINAAPDSPSKQLPDQISFFSGNPSVEIVHGIMHLYKTNKMTSLKEDVRRSAMLCILTVPAAMTSHDLMKFVAPFNEVIEQMKIIRDSTPNQYMVLIKFRAQADADSFYMTCNGRQFNSIEDDVCQLVYVERAEVLKSEDGASLPVMDLTELPKCTVCLERMDESVNGILTTLCNHSFHSQCLQRWDDTTCPVCRYCQTPEPVEENKCFECGVQENLWICLICGHIGCGRYVSRHAYKHFEETQHTYAMQLTNHRVWDYAGDNYVHRLVASKTDGKIVQYECEGDTCQEEKIDALQLEYSYLLTSQLESQRIYWENKIVRIEKDTAEEINNMKTKFKETIEKCDNLEHKLNDLLKEKQSVERKCTQLNTKVAKLTNELKEEQEMNKCLRANQVLLQNKLKEEERVLKETCDQKDLQITEIQEQLRDVMFYLETQQKINHLPAETRQEIQEGQINIAMASASSPASSGGSGKLPSRKGRSKRGK
Protein: V-type proton ATPase subunit d 1 (V-ATPase subunit d 1) (P39) (Physophilin) (V-ATPase 40 kDa accessory protein) (V-ATPase AC39 subunit) (Vacuolar proton pump subunit d 1) (P51863)
Organism: Mus musculus (Mouse)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in coupling of proton transport and ATP hydrolysis. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P61421}; Peripheral membrane protein {ECO:0000250|UniProtKB:P61421}; Cytoplasmic side {ECO:0000250|UniProtKB:P61421}. Lysosome membrane {ECO:0000250|UniProtKB:P61421}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P61420}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium. {ECO:0000250|UniProtKB:Q6PGV1}.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase 21 kDa proteolipid subunit c''
- Renin receptor
- V-type proton ATPase subunit D
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit E 1
- V-type proton ATPase catalytic subunit A
Sequence:
MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDKLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: Translationally-controlled tumor protein (TCTP) (21 kDa polypeptide) (p21) (p23) (P63028)
Organism: Mus musculus (Mouse)
Function: Involved in calcium binding and microtubule stabilization.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13693}.
Interaction partners:
- Elongation factor 1-beta
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS3
- Elongation factor 1-gamma
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein eL31
Sequence:
MIIYRDLISHDELFSDIYKIREIADGLCLEVEGKMVSRTEGAIDDSLIGGNASAEGPEGEGTESTVVTGVDIVMNHHLQETSFTKEAYKKYIKDYMKSLKGKLEEQKPERVKPFMTGAAEQIKHILANFNNYQFFIGENMNPDGMVALLDYREDGVTPFMIFFKDGLEMEKC
Protein: Aspartate-beta-hydroxylase (A0A096MIY8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
Interaction partners:
Sequence:
MAEDKEAKHGGHKNGRRGGISGGSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGVYDADGDGDFDVDDAKVLLEGPGGLAKRKTKAKGLKERSTSERTFPPEEAETQAELEEQAPEGADLEADGPAGEPQSEVEDFLTATDSDDRFEALEPGTVHEDTEDSYHVEETASQNHPNDAEEVMSEQESSDHGEAVTDDGLQQHAEEVRHEDYDEPVYEPSENERIEISDNAIDDSNIISEEINVASVEEQQDTPPDT
Protein: FAM3 metabolism regulating signaling molecule C (C9JP35)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDASLGNLFARSALDTAARSTKPPRYKCGISKACPEKHFAFKMASGAANVVGPKICLEDNVLMSGVKNNVGRGINVALANGKTGEVLDTKYFDMWGGDVAPFIEFLKAI
Protein: Nucleoporin NUP42 (NLP-1) (Nucleoporin-like protein 2) (Q8CIC2)
Organism: Mus musculus (Mouse)
Function: Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15504}. Nucleus membrane {ECO:0000250|UniProtKB:O15504}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15504}; Cytoplasmic side {ECO:0000250|UniProtKB:O15504}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:O15504}.
Interaction partners:
- mRNA export factor GLE1
- Nuclear pore complex protein Nup214
- Aladin
- Exportin-1
- Nuclear RNA export factor 1
- Nuclear pore complex protein Nup88
- E3 SUMO-protein ligase RanBP2
- Tip-associated protein
- Nucleoporin SEH1
- Tip-associated protein
Sequence:
MTICQFFLQGRCRFGDRCWNEHPGARGAGGARQPPPQQQPPSGNNRRGWNASSQRYSNVIQPSSFPKSTPWGGSRDQDKPPFGSFDSGASTSRGFGSSQNPFASPLSDEQKDEKKLLEGIVKDVEVWESSGQWMFSVYSPVRKKPNISGFTDISPEELRLEYHNFLTSNNLQSYLNSVQQLVSQWRNRINELKNLTMSTKGALLSDVKDGVSQAVPAFGFGSKQAGSFGSPGFPVNNSSSSTVQNFSFKTSPGLATPPSGSTSVFGSHPAFGAGPSAGSSISSSTPAFGLGKPEATSAASFSFKSPEASSFASPGFSGFPASMAASPSGSTTAPPLRSGSSVVGFGSPSPHSQAVFAKPSTDVFGGSGISTSVLASGAADNALFTPRDQLMKEELEQFQSQRFTLGKIPLKPPPVELLTV
Protein: rRNA methyltransferase 1, mitochondrial (EC 2.1.1.-) (16S rRNA (guanosine(1145)-2'-O)-methyltransferase) (16S rRNA [Gm1145] 2'-O-methyltransferase) (Q6IN84)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1145 (Gm1145) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:24036117, ECO:0000269|PubMed:25009282, ECO:0000269|PubMed:27184847}.
Interaction partners:
- rRNA methyltransferase 2, mitochondrial
- Mitochondrial ribosome-associated GTPase 1
- Mitochondrial assembly of ribosomal large subunit protein 1
- rRNA methyltransferase 3, mitochondrial
- Pseudouridylate synthase RPUSD4, mitochondrial
- Large ribosomal subunit protein uL29m
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- GTP-binding protein 8
- Large ribosomal subunit protein bL21m
- Mitochondrial ribosome-associated GTPase 2
Sequence:
MALLSTVRGATWGRLVTRHFSHAARHGERPGGEELSRLLLDDLVPTSRLELLFGMTPCLLALQAARRSVARLLLQAGKAGLQGKRAELLRMAEARDIPVLRPRRQKLDTMCRYQVHQGVCMEVSPLRPRPWREAGEASPGDDPQQLWLVLDGIQDPRNFGAVLRSAHFLGVDKVITSRRNSCPLTPVVSKSSAGAMEVMDVFSTDDLTGFLQTKAQQGWLVAGTVGCPSTEDPQSSEIPIMSCLEFLWERPTLLVLGNEGSGLSQEVQASCQLLLTILPRRQLPPGLESLNVSVAAGILLHSICSQRKGFPTEGERRQLLQDPQEPSARSEGLSMAQHPGLSSGPEKERQNEG
Protein: TATA element modulatory factor 1 TATA binding domain-containing protein (Q385X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLGSWLNEIQKTLDNVSGLAGKLEEFEGIEEKEGHGSDDVVHLSGSELNEVEGGVISMQLATKQKETHQEDSSTHGVAPSAIGMGDCCEVEASDRLLPPAVLQTRSSDVSCELGQKFDTTEREQGKTAVTGTKQTPVTFLSKPGERGGGEGIFKGASSGVVSEEGDNRSLVTSEDHTHDSRNLQEGQGGGTVSSSDPNATDGQLLRFQALLAEEMETSQRLNDENKRLTQSILSLQKEVNSLRNLKRSTVDKEKMASLEREGVELSEQLGRERERSKQLLERKAEAEDRVVSLERQLRQGAADYNELQNIAAARQTQCEATQRQVNELTIQLEEKNRRVQELQGEVSRYVSELNHRCDTANDVVESLKREKEVFVSSLHRNQMEYELHIQQLEKKLLQAEHRADRAETRLVEHERGSLNPLRELRAALDDTERQKKQLLEEAALAAEECAALKRDHVVVVESYKQQLAGVQNELRAAVDERTASIQELLQWKGRHTQVQKELGDALIRAAQAEALNKQIKQPADAVCTGIQPRSGSRCSSSIAAAEPSFVPSQPLTPVDVCANNTCLALLHFHTDGPTSHFSRGGRERMEKELVRQAVEIESLRRYKDEVEELRKKLAALAAQHDLLMQMYGQLQEETQQQTKSQS
Protein: Diguanylate cyclase DosC (DGC) (EC 2.7.7.65) (Direct oxygen-sensing cyclase) (P0AA89)
Organism: Escherichia coli (strain K12)
Function: Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Is involved in the modulation of intracellular c-di-GMP levels, in association with DosP which catalyzes the degradation of c-di-GMP (PDE activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. DosC regulates biofilm formation through the oxygen-dependent activation of the csgBAC operon, which encodes curli structural subunits, while not affecting the expression of the regulatory operon csgDEFG. DosC, but not the other DGCs in E.coli, also promotes the production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through up-regulation of the expression of the PNAG biosynthetic pgaABCD operon, independently of CsrA.
Interaction partners:
- Oxygen sensor protein DosP
- Cyclic di-GMP phosphodiesterase PdeL
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeB
- Probable cyclic di-GMP phosphodiesterase PdeD
- Probable cyclic di-GMP phosphodiesterase PdeC
- Cyclic di-GMP phosphodiesterase PdeH
- Cyclic di-GMP phosphodiesterase PdeF
- Probable cyclic di-GMP phosphodiesterase PdeI
Sequence:
MEMYFKRMKDEWTGLVEQADPPIRAKAAEIAVAHAHYLSIEFYRIVRIDPHAEEFLSNEQVERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILYPVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEEEKERQIASILSWEIDIIYKILLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISRLIQDFDGIFNQTMRNTRNLNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVLTKLLNRRFLPTIFKREIAHANRTGTPLSVLIIDVDKFKEINDTWGHNTGDEILRKVSQAFYDNVRSSDYVFRYGGDEFIIVLTEASENETLRTAERIRSRVEKTKLKAANGEDIALSLSIGAAMFNGHPDYERLIQIADEALYIAKRRGRNRVELWKASL
Protein: Epididymis luminal protein 46 (Golgi phosphoprotein 2, isoform CRA_a) (cDNA FLJ14811 fis, clone NT2RP4001975, highly similar to Golgi phosphoprotein 2) (cDNA PSEC0257 fis, clone NT2RP3003642, highly similar to golgi phosphoprotein 2) (B3KNK9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MMGLGNGRRSMKSPPLVLAALVACIIVLGFNYWIASSRSVDLQTRIMELEGRVRRAAAERGAVELKKNEFQGELEKQREQLDKIQSSHNFQLESVNKLYQDEKAVLVNNITTGERLIRVLQDQLKTLQRNYGRLQQDVLQFQKNQTNLERKFSYDLSQCINQMKEVKEQCEERIEEVTKKGNEAVASRDLSENNDQRQQLQALSEPQPRLQAAGLPHTEVPQGKGNVLGNSKSQTPAPSSEVVLDSKRQVEKEETNEIQVVNEEPQRDRLPQEPGREQVVEDRPVGGRGFGGAGELGQTPQVQAALSVSQENPEMEGPERDQLVIPDGQEEEQEAAGEGRNQQKLRGEDDYNMDENEAESETDKQAALAGNDRNIDVFNVEDQKRDTINLLDQREKRNHTL
Protein: Cell division cycle 25C (D6RJC2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQ
Protein: Early nodulin-like protein 1 (Phytocyanin-like arabinogalactan-protein) (A7J385)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Protein TIME FOR COFFEE-like
- Classical arabinogalactan protein 5
Sequence:
MAAKAFSRSITPLVLLFIFLSFAQGKEIMVGGKTGAWKIPSSESDSLNKWAEKARFQIGDSLVWKYDGGKDSVLQVSKEDYTSCNTSNPIAEYKDGNTKVKLEKSGPYFFMSGAKGHCEQGQKMIVVVMSQKHRYIGISPAPSPVDFEGPAVAPTSGVAGLKAGLLVTVGVLGLF
Protein: Zgc:112180 (Q502I5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNIPPPNILEDQDDDIEKEKQASAGDGASAGSGASGGVSASLTPAIWEKTIPYDGETFHLEYMDLDEFLLENGIPVSLEEELSRGLEAERRDGETQASSENSEEPAAVPEMPEQMQTEQDEDLSDSQTAEQELSEETTAEPSSVPERATPSPVSPEDIEVNVSFQPDPTDLVLSSVPGGELFNPRKHRFSEDELKPQPMIKKAKKVFVPEDAKDDKYWSRRKKNNVAAKRSRDARRLKENQIAVRASFLERENAALRQQVAELRKDCGRCQKIMALYEAKYGLL
Protein: Syntaxin binding protein 1 (A0A1B0GTP9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPTKFLMDLRHPDFRESSRVSFEDQAPTME
Protein: Probable beta-1,4-xylosyltransferase IRX9H (EC 2.4.2.-) (Protein IRREGULAR XYLEM 9 homolog) (Xylan xylosyltransferase IRX9H) (Q9SXC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the elongation of glucuronoxylan xylosyl backbone.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:20335400}; Single-pass type II membrane protein {ECO:0000305|PubMed:20335400}.
Interaction partners:
- Probable beta-1,4-xylosyltransferase IRX10L
- Probable beta-1,4-xylosyltransferase IRX10
- Probable glucuronoxylan glucuronosyltransferase F8H
- Probable galacturonosyltransferase 12
- Probable glucuronoxylan glucuronosyltransferase IRX7
- Probable galacturonosyltransferase-like 1
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 2
- Beta-1,2-xylosyltransferase
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Putative UDP-glucuronate:xylan alpha-glucuronosyltransferase 4
Sequence:
MASIRRTLSPMYHDRSHENGGSHKGFTIGGSSSKHNSSQFLSYLTKLLGVTSDPKSSRRGPWRRPFYQFLVFFLLGFVLGLTPFGKMEDVNGSDRFSFEIKQPYVEERLENRKREEAAVDAVSFVAETENGKKEVNFVPKKLLIVVTPTYNRAMQAYYLNRVAQTLRLVESPVLWIVVEGNVASFETSEILRKTGVMYRHLVCKRNMTSIKDRGVHQRNTALEHIELHKLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAQSKNKAILEGPVCNGSQVIGWHTNEKSKRLRRFHVDMSGFAFNSTILWDPKRWRRPFSHPTRQLDTVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHLDALDVPYPQGWAIQKNLQALITMK
Protein: Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE) (P17183)
Organism: Mus musculus (Mouse)
Function: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase 1
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Phosphoglycerate mutase 2
- Glucose-6-phosphate isomerase
- Bisphosphoglycerate mutase
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Phosphoglycerate kinase 1
- Phosphoenolpyruvate carboxykinase, cytosolic
- Triosephosphate isomerase
Sequence:
MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALISSGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL
Protein: Alpha-mannosidase (EC 3.2.1.-) (F7FG85)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGTGSLAPGVRAGGGNTGWLWMSSCNLGLPVLSISFLIWLLLAAPGAQAAGYKTCPTTKPGMLNVHLLPHTHDDVGWLKTVDQYYYGMDPHLLTFMPIVMSDVQHASVQYILDSVIYSLLNDPTRRFIYVEMAFFSRWWKQQTNVTQDAVRNLVRQGRLEFVNGGWVMNDEAATHYGAIVDQMTLGLRFLQDTFGSDGLPRVAWHIDPFGHSREQASLFAQMGFDGFFLGRIDYQDKFNRKRKLKMEELWRASASLKPPAADLFTGVLPNNYNPPKDLCWDVLCTDPPVVDDPTSPEFNANKLVDYFLNLASSQKKYYRTNHTVMTMGSDFQYENANMWFKNMDKLIRLVNEQQANGSKVHVLYSTPSCYLWELNKANLTWTVKEDDFFPYADGPHMFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGPEAKVGPYGSGDSAPLNEAMAVLQHHDAVTGTARQNVVNDYAKQLAAGWGPCEVLVSNALARLSLYKQNFSFCREINISICPASQTSEHFRVIIYNPVGRKVDLMVRLPVSEGIFLVKDPNDRRISSNVVMVPSAYSKTYQWELLFPASVPALGFSIYSVNKMSGHNHQAHNLTARPKKSKSRVLVIENKYIRATFDSDTGLLRKIENLEQNISLPVRQGFFWYNASAGDEESPQASGAYIFRPSHRKPLPVSHWAQVTLVKTNLVQEVHQNFSAWCSQVIRLYEGQRHLELEWTVGPIPVKDDWGKEVISRFNTPMRTRGQFFTDSNGREILKRRDDFRPTWTLNQTEPVAGNYYPVNTRIYITDGHMQLTVLTDRSQGGSSLLDGSLELMVHRRLLVDDERGVAEPLLETDTGDKVRGRHLVILSSVSDAAARHRLLAEQEVLAPQVVLAHGGSSPYHSQAPKMQFSALRRELPPQVHLLTLARWGPKMLLLRLEHQFAVKEDSNRNLSSPVTLNLQNLFKTFTINYLQETTLAANQPLSRVSRLKWMTDTGPISYPAPSRLDPTSITLQPMQIRTFLASVQWQRLI
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 (Ribophorin I) (RPN-I) (Ribophorin-1) (E2RQ08)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12887896, ECO:0000269|PubMed:29519914}; Single-pass type I membrane protein {ECO:0000269|PubMed:29519914}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Tumor suppressor candidate 3.
- Malectin.
- Protein transport protein Sec61 subunit alpha isoform 1.
- Protein transport protein Sec61 subunit alpha isoform 1
- Mannosyl-oligosaccharide glucosidase.
Sequence:
MEVPTARLLLLLLLGAWAPAPESASPEAPLLVNEDVKRTVDLSSHLAKVTAEVVLAHPGGGSTARAASFLLALEPELEARLAHLGVQVKGEDEEENNLEVRETKIKGKSGRFFTVKLPVALDPGAKVSVVVETVYTHVLQPYPTQITQSEKQFVVFEGNHYFYSPYPTKTQTMRVKLASRNVESYTKLGNPTRSEDLLDYGPFRDIPAYSQDTFKVHYENNSPFLTITSMTRVIEVSHWGNIAVEENVDLKHTGAVLKGPFSRYDYQRQPDSGIASIRSFKTILPAAAQDVYYRDEIGNVSTSHLLILDDSVEMEIRPRFPLFGGWKTHYIVGYNLPSYEYLYNLGDQYALKMRFVDHVFDEQVIDSLTVKIILPEGAKNIQVDSPYEISRAPDELHYTYLDTFGRPVIVAYKKNLVEQHIQDIVVHYTFNKVLMLQEPLLVVAAFYILFFTVIIYVRLDFSITKDPAAEARMKVACITEQVLTLVNKRIGLYRHFDETINRYKQSRDVSTLNSGKKSLETEHKALTSEIASLQSRLKTEGSDLCDKVSEMQKLDAQVKELVLKSAVEAERLVAGKLKKDTYIENEKLISGKRQELVTKIDHILDAL
Protein: Type 3 secretion system needle filament protein (T3SS needle filament protein) (Pseudomonas secretion protein F) (Type III needle protein PscF) (P95434)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Major component of the type III secretion needle structure that plays an essential role in translocation of effector toxins into host cells, facilitating the establishment and dissemination of infection.
Subcellular location: Secreted {ECO:0000269|PubMed:16115870}. Cell surface {ECO:0000269|PubMed:31001211}. Note=Secreted via type III secretion system (T3SS).
Interaction partners:
- Type 3 secretion system chaperone PscE
- Type 3 secretion system chaperone PscG
- Type III inner-rod protein PscI
- Type III secretion protein PcrV
- Type 3 secretion system secretin
- Lipoprotein
- Translocator outer membrane protein PopD
- Type III export protein PscH
- Translocator protein PopB
- Type III export apparatus protein
Sequence:
MAQIFNPNPGNTLDTVANALKEQANAANKDVNDAIKALQGTDNADNPALLAELQHKINKWSVIYNINSTVTRALRDLMQGILQKI