wanglab/gogpt-training-data huggingface dataset:
Protein: Spore wall protein 7 (B3STP1)
Organism: Nosema bombycis (strain CQ1 / CVCC 102059) (Microsporidian parasite) (Pebrine of silkworm)
Function: Involved in adherence of spores to the host cell surface and in infection efficiency.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25605761}. Spore wall {ECO:0000269|PubMed:18563739, ECO:0000269|PubMed:25605761}. Spore polar tube {ECO:0000269|PubMed:25605761}. Note=Localized to the cytoplasm of sporonts and sporoblasts and to the spore wall and polar tube of mature spores. {ECO:0000269|PubMed:25605761}.
Interaction partners:
Sequence:
MIKGLIYLFLFRCLEGRLADYEEESSDLGDYSLNGQTDEEYGKFPSHVLTEKETGPMDEIRCTNDDYTYNIKLNVHLQNYAIQAIADAAKPKLGMNLKERDAILSYFGTIANELNADLARLGAQIVIGLKHYKAEDFIDTNSFDTSCEIRDPVMDRLDSTFKQLKDVYQDSMGLRLFVWTCPQLTSSFETMKIMSNLNCGRIMGVLWQGADATRTSIKSTILEAISGVSELYLDGALPVDRVFSNVCRFCSKCVGVEPGVIGWKHPDVVKLIHAIPEEDTHEHGYDH
Protein: Transcriptional repressor OPI1 (Negative regulator of phospholipid biosynthesis) (Overproducer of inositol protein 1) (P21957)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulator of the transcriptional complex INO2-INO4 in response to phospholipid precursor availability. When precursors become limiting, OPI1 is retained at the endoplasmic reticulum (ER) and INO2-INO4 activates INO1 and other genes required for phospholipid biosynthesis, whereas abundant precursor availability results in targeting of OPI1 to the nucleus to repress transcription of these genes. Binds directly to phosphatidic acid, which is required for ER targeting and may act as sensing mechanism for precursor availability, as phosphatidic acid becomes rapidly depleted upon phospholipid biosynthesis.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:15192221}. Nucleus {ECO:0000269|PubMed:15192221}. Note=Maintained at the endoplasmic reticulum by SCS2 (PubMed:12727870). In response to elevated inositol levels, translocates to the nucleus (PubMed:15192221).
Interaction partners:
- Protein INO2
- Vesicle-associated membrane protein-associated protein SCS2
- Protein INO4
- Inositol-3-phosphate synthase
- Phosphatidic acid phosphohydrolase 1
- Transcriptional regulatory protein SIN3
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Acetyl-CoA carboxylase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidylethanolamine N-methyltransferase
Sequence:
MSENQRLGLSEEEVEAAEVLGVLKQSCRQKSQPSEDVSQADKMPASESSTTPLNILDRVSNKIISNVVTFYDEINTNKRPLKSIGRLLDDDDDEHDDYDYNDDEFFTNKRQKLSRAIAKGKDNLKEYKLNMSIESKKRLVTCLHLLKLANKQLSDKISCLQDLVEKEQVHPLHKQDGNARTTTGAGEDETSSDEDDDDEEFFDASEQVNASEQSIVVKMEVVGTVKKVYSLISKFTANSLPEPARSQVRESLLNLPTNWFDSVHSTSLPHHASFHYANCEEQKVEQQQQQQQQQQQQQLLQQQLLQQQQQKRNKDGDDSASPSSSVTANGKVLILAKESLEMVRNVMGVVDSTLGKAEEWVKQKQEVKEMIRERFLQQQQQYRQQQQKDGNYVKPSQDNVDSKD
Protein: G-protein coupled receptor family C group 5 member C (Retinoic acid-induced gene 3 protein) (RAIG-3) (Q8K3J9)
Organism: Mus musculus (Mouse)
Function: This retinoic acid-inducible G-protein coupled receptor provide evidence for a possible interaction between retinoid and G-protein signaling pathways.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MATHRTLLMCLGLPLFFPGALAQNHAPPGCSPDLDPLYYNLCDRSGAWGIVSEAVAGAGIITTFVLTIILVASLPFVQDTKKRSLLGTQVFFLLGTLGLFCLVFACVVKPDFSTCASRRFLFGVLFAICFSCLVAHVLSLNFLTRKNHGPRGWVIFTVALLLTLVEVIINTEWLIITLVRGGGQVSPLGNVSADSTMTSPCAIANMDFVMALIYVMLLLLTAFLGAWPTLCGRFKRWRKHGVFVLLTTVISIAIWVVWIVMYTYGNEQHHSPTWDDPTLAIALAANAWTFVLFYVIPEVSQVTKPSPEQSYQGDMYPTRGVGYETILKEQTGQSMFVENKAFSMDEPASAKRPVSPYSGYNGQLLTSVYQPTEMALMHKGPSEGAYDVILPRATANSQVMGSANSTLRAEDMYMVQSHQVATPPKDGKISQVFRNPYVWD
Protein: At3g57630 (Exostosin family protein) (Glycosyltransferase) (Q6NKR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Glycosyltransferase-pyrophosphoryl-undecaprenol N-acetylglucosamine transferase)
- Uncharacterized protein At4g19900
- Glycosyltransferase
- Glycosyltransferase
- At1g19710
- Arabinosyltransferase XEG113
- dolichyl-phosphate beta-glucosyltransferase
- Pentatricopeptide repeat-containing protein At5g03800
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-D-xylose:L-fucose alpha-1,3-D-xylosyltransferase 1
Sequence:
MFSHQKWKFSWSQIATVASVIVLVSLVHLFLGPVVPSFDSITVRQAQNLCGPSNESISQVTKNSSQSLVVVAFDRRFPADSHGAVVYRNASWKAEIGQWLSSCDAVAKEVDIIEPIGGRKCMSDCSGQGVCNHEFGLCRCFHGFTGEDCSQKLRLDCNYEKTPEMPYGKWVVSICSRHCDTTRAMCFCGEGTKYPNRPVPESCGFQINSPTNPDEPKMTDWSKPDLDILTTNSSKQGWCNVDPEDAYAMKVKIKEECDCKYDCLWGRFCEIPVQCTCVNQCSGHGKCRGGFCQCDKGWFGTDCSIPSTLSTVGEWPQWLRPAHLEVPSEKNVPGNLINLSAVVKKKRPLIYIYDLPPDFNSLLIEGRHFKFECVNRIYDERNATVWTDYLYGSQMAFYENILATAHRTMNGEEADFFFVPVLDSCIINRADDAPHINMQNHTGLRSSLTLEFYKRAYEHIVEKYPYWNRSAGRDHIWFFSWDEGACYAPKEIWNSMMLVHWGNTNSKHNHSTTAYFGDNWDDISDERRGDHPCFDPRKDLVIPAWKVPDPYSMRKNYWERPREKRKTLFYFNGNLGPAYEKGRPEDSYSMGIRQKLAEEFGSSPNKEGKLGKQHAEDVIVTPLRSDNYHKDIANSIFCGAFPGDGWSGRMEDSILQGCVPVIIQDGIYLPYENMLNYESFAVRVNEDDIPNLINTLRGFSEAEIQFRLGNVKELWQRFLFRDSILLEAERQKATYGHEEDWAVQFSKLKHDDIFATIIQTLHFKLHNDPWRREQAVNRTKDYGLPQECLHKTS
Protein: Berberine bridge enzyme-like 26 (AtBBE-like 26) (EC 1.1.1.-) (Q9FKU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:O64743}.
Interaction partners:
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Proline-rich family protein
- Endo-1,4-beta-xylanase 5
- UPF0496 protein At3g28300
- Probable pectate lyase 18
- UPF0496 protein At3g28290
- Proline-rich extensin-like family protein
- Proline-rich extensin-like family protein
- Pectin acetylesterase 7
- Transcription factor MYB87
Sequence:
MGISKPLPLFSILVLYFSLYTITPTSSLASLQDQFINCVQRNTHVYFPLEKTFFAPTKNVSMFSQVLESTAQNLRFLKKSMPKPGFIFSPIHESHVQASIICSKKLRMHLRVRSGGHDYEGLSYVSQIDKPFILMDLSKMRQVNINIQDNSAWVQSGATVGELYYRIAEKSKVHGFPAGLCSSLGIGGHITGGAYGSMMRKYGLGADNVLDAKIVDANGKLLDRAAMGEDTFWAIRGGAGGSFGIILAWKIKLVPVPKTVTVFTVTKTLQQDVGNKIISKWQRVADKLVEELFIRVLFNVAGTGGNKTVTTSYNALFLGGKGTLMNVMKKSFPELGLTFKDCIEMSWLESIAYISGFPTHTPTNVLLQGKSPFPKVSFKAKSDFVKTPIPESGLQGIFKKLLKEDIPLMIWNPYGGMMAKIPESQIPFPHRKGVLFKVQYVTSWLDSDKRPSRHINWIRDLYSYMTPYVSSNPREAYVNYRDLDLGRNTKDVKTCIKQAQVWGANYFKNNFNRLMMIKAKVDPENFFRHEQSIPPMM
Protein: Cation channel sperm-associated protein 4 (CatSper4) (Q8BVN3)
Organism: Mus musculus (Mouse)
Function: Voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertilization. Activated by intracellular alkalinization.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:16107607, ECO:0000269|PubMed:17227845}; Multi-pass membrane protein {ECO:0000269|PubMed:34225353}. Note=Specifically located in the principal piece of the sperm tail. {ECO:0000269|PubMed:17227845, ECO:0000269|PubMed:34225353}.
Interaction partners:
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated protein 3
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated auxiliary subunit gamma 2
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated auxiliary subunit zeta
- Cation channel sperm-associated auxiliary subunit TMEM249
Sequence:
MSEKHKWWQQVENIDITHLGPKRKAYELLGRHEEQVLINRRDVMEKKDAWDVQEFITQMYIKQLLRHPAFQLLLAFLLLSNAITIALRTNSYLGQKHYELFSTIDDIVLTILICEVLLGWLNGFWIFWKDGWNILNFAIVFILFMGFFIKQLDMVAITYPLRVLRLVHVCMAVEPLARIIKVILQSMPDLANVMALILFFMLVFSVFGVTLFGAFVPKHFQNMGVALYTLFICITQDGWLDIYTDFQMDEREYAMEVGGAIYFAVFITLGAFIGLNLFVVVVTTNLEQMMKTGEEEGHLNIKFTETEEDEDWTDELPLVHCTEARKDTSTVPKEPLVGGPLSNLTEKTCDNFCLVLEAIQENLMEYKEIREELNMIVEEVSSIRFNQEQQNVILHKYTSKSATFLSEPPEGANKQDLITALVSREKVSDSNINMVNKHKFSH
Protein: Circadian clock oscillator protein KaiA (Q79V62)
Organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Function: Key component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. KaiA binding to the KaiC CII domain during the subjective day yields KaiA(2-4):KaiC(6) complexes which stimulate KaiC autophosphorylation. Phospho-Ser-431 KaiC accumulation triggers binding of KaiB during the subjective night to form the KaiB(6):KaiC(6) complex, leading to changes in the output regulators CikA and SasA. KaiB(6):KaiC(6) formation exposes a site for KaiA binding on KaiB that sequesters KaiA from KaiC's CII domain, making the KaiC(6):KaiB(6):KaiA(12) complex resulting in KaiC autodephosphorylation. Complete dephosphorylation of KaiC leads to dissociation of KaiA(2):KaiB(1), completing 1 cycle of the Kai oscillator (By similarity). Formation of the KaiB:KaiC complex is promoted by KaiA, helping switch KaiC from its autophosphorylation to autodephosphatase function.
Interaction partners:
- Circadian clock oscillator protein KaiC
- Circadian clock oscillator protein KaiB
- Circadian oscillation regulator
- Amidophosphoribosyltransferase
- Thiamine-phosphate synthase
- CpmA protein
- Protein RecA
- Cell division protein FtsZ
- Glutathione S-transferase
- Tlr0341 protein
Sequence:
MAQSTALTICGLVYSPAIGQELVRLHTSDIDELVYFSSEREFCNYLEARRNSIACLILEWGEGTPQIITYLHHSATLLPAILIFPAAPAPPPAGPHYHIAEVILTTDQLDQLNRQIEEAITGFVKLCPGCAVPPHVLFRLPALKESSNVDPQHRLSQKLKERLGYLGVYYKRDTAFFFRRMSPADKRKLLDELRSIYRTIVLEYFNTDAKVNERIDEFVSKAFFADISVSQVLEIHVELMDTFSKQLKLEGRSEDILLDYRLTLIDVIAHLCEMYRRSIPREV
Protein: Peroxisome biogenesis factor 2 (EC 2.3.2.36) (Peroxin-2) (Q7K1R0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004585}.
Interaction partners:
Sequence:
RKGRVHINKKYINGQLTKGKNINKIMEKNKYVPRVNQIDAIYLNKDIARLIRDNLLENLQAISPVLFIKIQPELDLIIQSAIWFGSVGKRCSTFGQQLLVLAYDAEKLTVSRLVLHFILTVLPGYVKSWEERRLTRRVEWFSEAIMWVENSALILNILNYFRFLKTGRKPTLVDYLLGLDYISLRNNQRRDIGYKYLTRELLWGGFMEILGLVLPIINFRKLQRVLKSWTFSGRRLEDRDGPAFLAPQMTLSTTCTFCGERPTLPHHMGCGHIYCYYCLNANVLTDASFCCPNCGSACPESGIQSV
Protein: Fos-related antigen 1 (FRA-1) (P15407)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51145}.
Interaction partners:
- Transcription factor JunD
- Transcription factor Jun
- Transcription factor JunB
- Protein FosB
- Fos-related antigen 2
- Protein c-Fos
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Cyclic AMP-dependent transcription factor ATF-3
- Transcription factor p65
Sequence:
MFRDFGEPGPSSGNGGGYGGPAQPPAAAQAAQQKFHLVPSINTMSGSQELQWMVQPHFLGPSSYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEGAKEGDTGSTSGTSSPPAPCRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCASAHRKSSSSSGDPSSDPLGSPTLLAL
Protein: H/ACA ribonucleoprotein complex subunit DKC1 (EC 5.4.99.-) (Dyskerin) (Nopp140-associated protein of 57 kDa) (Nucleolar protein NAP57) (Nucleolar protein family A member 4) (snoRNP protein DKC1) (P40615)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (By similarity). Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs (By similarity). Required for ribosome biogenesis and telomere maintenance (By similarity). Also required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:7798307}. Nucleus, Cajal body {ECO:0000269|PubMed:7798307}.
Interaction partners:
- Ribonucloprotein
- H/ACA ribonucleoprotein complex subunit 1
- Nucleolar protein 58
- Telomerase Cajal body protein 1
- Protein SHQ1 homolog
- Nucleolar protein 56
- Telomerase reverse transcriptase
- H/ACA ribonucleoprotein complex subunit 3
- Nucleolar and coiled-body phosphoprotein 1
- Ribonucloprotein
Sequence:
MADAEAAMTFPKKHKKKKERKPLPEADVAEIQHAEDFLIKPESKAAQLDTSQWPLLLKNFDRLNVRTTHYTPIPCGSNPLKREIGEYVRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGVVRLHNAIEGTAQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESRVVEYDPERRLGVFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVVGERDHMVTMHDVLDAQYLYDHHRDESYLRRVVFPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGLLRYEDGIEVNQEVVVITTKGEAVCVAIALMTTAVISTCDHGVVAKIKRVIMERDTYPRKWGLGPKASQKKQLIKQGLLDKHGRPTDGTPASWTRDYVDYSDSSKKATAAEATPGPGVTADAASIVKRKRDSDSDADEATPTTTPRVKKEKKKKKEKADGGEEAAEDGDGDATRKKKKKKARAAEELSG
Protein: Uncharacterized protein C2G11.04 (Q09806)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43
- U3 small nucleolar RNA-associated protein 22
- rRNA biogenesis protein rrp36
- U3 small nucleolar RNA-associated protein 6
- ATP-dependent RNA helicase dbp4
- Uncharacterized protein C13G1.09
- Suppressor of glycerol defect protein 1
- KRR1 small subunit processome component homolog
- U3 small nucleolar ribonucleoprotein protein imp3
- Probable nucleolar complex protein 14
Sequence:
MGFMLYEGIDSKSIEEITEESEKTKTDLQKANTPNKTEAVHSLNNTCSEQNSGTKDYLNSLQFLPSNFRPKTHKKKKSVSSYLSSTIQKNANENIPHVQCRNDSQSTVTTRNPTPFKIEVGIYPSKPNNLNKEPPASTVHSDNLGDAVEHEWVELYDPLFPTSYSVFKESDYANLCETNWSHYVNQVPSLSIEAKLSNIVNASKSGIGPPPSLLSHATLARPSESMVLSNNIAAEDLDFFKKSPPVPAISKKENVALKMLQRCGWKEGQGLGQHNQGIINPLHVEISGFVTETKHSKINDK
Protein: DUF155 domain-containing protein (Q386E2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MITSAAHFAWCYSNCFSSLRHCSRSKLKIDMTDSESDAGFIQLRNRLLELLYSSNSSFSVDQIARILAVDESKIVNELKHVAHNDVAYDEAKGIVQVRADMWKPRSMKAGDVVIDTAATTTPAAVADVAPGSVAVEAYGGGTSGGGVERRNINAGGPLTPSPVLGSPLNPMFKAYPKYGSHNYYPNRGMRVLAPKGALRKTKYRRTGDAETLGKGGGMRDEGTSPTGRVGYVCVADEFRLSEMESYYCAQGYYAKFAFDVLHIRFSDREMKAKDPRGDGLGAGGSGCQDGSGNNLDNSSTNPAGGEKVTDRTTSSAFTKLSRSAGFDLFVFGYGAVVWWGFDQRFFKIVENDFMLSSSPISNLMVNRYATHLVNANYPVWCTYNLARKESLEPDEHFREQLRFDHFLIPCGRGDFSTGNVCMLCVSHALAQSAKIDYLELKVQELAERCSPLPRELRENGRVTIAERRLLQLRGEVLSYRLMLKSGSNLMDEPDFFWENAYLKPVFQATKEYFEIAERVEALDNKLDAANEILSMIAEEFSQRHGARLEWIVIWLVFVEVILGVLELIINIKPWVERGK
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC (EC 3.2.1.113) (HMIC) (Mannosidase alpha class 1C member 1) (Processing alpha-1,2-mannosidase IC) (Alpha-1,2-mannosidase IC) (Q9NR34)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
- Alpha-mannosidase 2x
- Alpha-mannosidase 2
Sequence:
MLMRKVPGFVPASPWGLRLPQKFLFLLFLSGLVTLCFGALFLLPHSSRLKRLFLAPRTQQPGLEVVAEIAGHAPAREQEPPPNPAPAAPAPGEDDPSSWASPRRRKGGLRRTRPTGPREEATAARGNSIPASRPGDEGVPFRFDFNAFRSRLRHPVLGTRADESQEPQSQVRAQREKIKEMMQFAWQSYKRYAMGKNELRPLTKDGYEGNMFGGLSGATVIDSLDTLYLMELKEEFQEAKAWVGESFHLNVSGEASLFEVNIRYIGGLLSAFYLTGEEVFRIKAIRLGEKLLPAFNTPTGIPKGVVSFKSGNWGWATAGSSSILAEFGSLHLEFLHLTELSGNQVFAEKVRNIRKVLRKIEKPFGLYPNFLSPVSGNWVQHHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNVSPGGLTYIAEWRGGILDHKMGHLACFSGGMIALGAEDAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYMYLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDWVFNTEAHPLPVNHSDSSGRAWGRH
Protein: Polycomb protein SUZ12 (Chromatin precipitated E2F target 9 protein) (ChET 9 protein) (Joined to JAZF1 protein) (Suppressor of zeste 12 protein homolog) (Q15022)
Organism: Homo sapiens (Human)
Function: Polycomb group (PcG) protein. Component of the PRC2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The PRC2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.
Subcellular location: Nucleus {ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}. Note=Localizes to chromatin as part of the PRC2 complex. {ECO:0000269|PubMed:29499137, ECO:0000269|PubMed:31959557}.
Interaction partners:
- Polycomb protein EED
- E3 ubiquitin-protein ligase RING2
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- Histone-lysine N-methyltransferase EZH2
- Metal-response element-binding transcription factor 2
- Zinc finger protein AEBP2
- Histone-lysine N-methyltransferase EZH1
- Protein Jumonji
- PHD finger protein 19
Sequence:
MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAVAAATASGGKSGGGSCGGGGSYSASSSSSAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESASPANEEITEEQNGTANGFSEINSKEKALETDSVSGVSKQSKKQKL
Protein: Nicotianamine aminotransferase A (EC 2.6.1.80) (Nicotianamine aminotransferase III) (NAAT-III) (Q9ST02)
Organism: Hordeum vulgare (Barley)
Function: Involved in biosynthesis of mugineic acid family phytosiderophores.
Interaction partners:
Sequence:
MVHQSNGHGEAAAAAANGKSNGHAAAANGKSNGHAAAAAVEWNFARGKDGILATTGAKNSIRAIRYKISASVEESGPRPVLPLAHGDPSVFPAFRTAVEAEDAVAAALRTGQFNCYAAGVGLPAARSAVAEHLSQGVPYKLSADDVFLTAGGTQAIEVIIPVLAQTAGANILLPRPGYPNYEARAAFNKLEVRHFDLIPDKGWEIDIDSLESIADKNTTAMVIINPNNPCGSVYSYDHLAKVAEVARKLGILVIADEVYGKLVLGSAPFIPMGVFGHIAPVLSIGSLSKSWIVPGWRLGWVAVYDPTKILEKTKISTSITNYLNVSTDPATFVQEALPKILENTKADFFKRIIGLLKESSEICYREIKENKYITCPHKPEGSMFVMVKLNLHLLEEIHDDIDFCCKLAKEESVILCPGSVLGMENWVRITFACVPSSLQDGLERVKSFCQRNKKKNSINGC
Protein: Endoglucanase gh5 (EC 3.2.1.4) (Glyoside hydrolase family 5 endoglucanase) (C0HLV0)
Organism: Fomes meliae (Fomitopsis meliae)
Function: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose.
Interaction partners:
Sequence:
QAVLSETGGGDTASCDEYLYQELAYVK
Protein: Vomeronasal 2 receptor o (Q3LHH5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PHSKIPGFKKFIQTVHPSNYSKDTSLARLWWLYFNCSLPSHCKTLKNCSTKILLEWLSRHQFEVSMSEPSYNLYNAVYAVAYALHEMLIQHTEHWQKDIGKELEFYSWKVAPFLENNKFIIPSEYQYRRGKLDTEYDILYAMDLLPALGLNVKIGKFSQHFLHFQQLYIAEDMIDWTIDIRQTLQSVCSVPCSVGFRKFIQKGKAVCCFDCTPCPENE
Protein: adenylate cyclase (EC 4.6.1.1) (Q9VK51)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ras-like protein 1
- cAMP-dependent protein kinase catalytic subunit 1
- IP06402p
- Bis
- Inosine triphosphate pyrophosphatase
- LD28489p
- cAMP-dependent protein kinase catalytic subunit 2
- Molybdenum cofactor biosynthesis protein 1
- GTP cyclohydrolase 1
- GEO12020p1
Sequence:
MNKKNTYKTPYRERFRRCNLEYTNERLWEQSYLKARCKELHLEEEYMKYKIRLMISSLTVFVPMLILLIVALQVIIWSFTEYTKYIYINAIFDLGSLILVTGLLSINFFEDFVIRHRWVMTFTSTLSAYVVVLGDIAFNTYYYYKSNWPLNTLYDVFVLCMIYMFLPIPSSKAAALLAISVSLTYVIYFIHFMAFNEHNVAKYVHGLDIVSIDFFHYLGFNMMGIFFRIMNDTMVRSSFLDRYQFITEEIWLRQARRQESLLLDSILPPQIAKPIQKSIKEKIIQPDNDFYHLGTSRTAENFMSIQIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIANIKEVSVNRSLNIGMRIGVHSGTLFAGVIGKAKLQYDIWGADVNIASRLEATGSPGYVHVSGRTLSSLNAEEYNIYPGTESAQKDPVLQKHPMSTYLLTAIPSLDSDKTISIVEGVPNLDLQTVGSNRKSQILKPNLLSHEMREEFRKMPVGGFKFQFPWSRRERNLKNEKVERDLGIFCVAFKDKSVEWNYLHQPDYIFKYSVALGWGIGCCLIYIQSVNNSDIFYTGVVINIIAFFVLTFLLFICWYKKVCWWHSGQNEHRSYGKLSCAIFHLFEKIQHSFVLRLTVYMMIILCYYMVISLILMSCEKDQYELDIIESKLYNYDMDPFTCFHPWAYTNMMALILGMSYTFARIPFALKTFIGCAEAVVFVLVVCFQYAFIFEHSVTTSPYLKAEIAHSCRVCMMLITMYAKERQSEFNTKMNYKLNLDLQNKQKSADVTNQSIIILLNNILPSHVVEVYLSSIAKHELYYENYRMVSVMFAMLTNFQMDLPSLRVLNDIITAFDRLLSAYKQYYVVEKIKVVGCTYMAACGLDFSLIENLDSNSNFGSTSLSSELEQVRSRLESSIKEKNHDEVAFIMATFALDLMRVLSVCNKAYAGEPFDRALSTGEIRIGISTGQIMAGVVGASQPHYDIWGNPVNMASRMESTGLSGHIQVTKETAQTLEEFDVMCYYRGLTFVKGRGEIPTYFVGIDKDLKFMSKKIDRLSENPSNPDLNHDLDGS
Protein: Neuropeptide Y receptor type 2 (NPY-Y2 receptor) (E7F951)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Peptide YY-A
- Pro-neuropeptide Y
- Peptide YYb
Sequence:
MDSLSLINGSSGSKDLSIGEDSSDLTLNHPLLELGDSTKLLGVQVVLILAYSTIILLGVVGNSLVIYVVYKFKTLRTVTNFFIANLAVADLLVNTLCLPFTLAYTLLREWKFGQVLCFTLPYAQGLAVHVSTITLNVIALDRHRCIVYHLDTRMSKDTCFLVIAITWVVSAVLASPLAIFREYGIVDLSPDNSIEVCGEKWPDSSTDSTLYSISTLLLQYVLPLAIISFAYIRIWSKLRNHVSPVGRNDRHHRRRKTTKMLVTMVVVFAVSWLPFHAFQLAIDIDHSVLDMKDFRLLYTVFHIVAMCSTFANPLLYGWMNRNYRSAFVAVFRCKERLDSLHTEGQPAATVRSKPKKALEAQDMVTTHLNATDV
Protein: Polyphosphate glucokinase (Poly(P) glucokinase) (EC 2.7.1.63) (ATP-dependent glucokinase) (EC 2.7.1.2) (Polyphosphate--glucose phosphotransferase) (P9WIN1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in M.tuberculosis (By similarity).
Interaction partners:
- Possible sugar kinase
- Glucose-6-phosphate isomerase
- Probable phosphoglucomutase PgmA
- Transaldolase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate 1-dehydrogenase 1
- Transketolase
- Glucose-6-phosphate 1-dehydrogenase 2
- Deoxyribose-phosphate aldolase
- RNA polymerase sigma factor SigA
Sequence:
MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH