wanglab/gogpt-training-data huggingface dataset:
Protein: Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC 2.4.1.265) (Asparagine-linked glycosylation protein 8) (Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase) (Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase) (Q10479)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adds the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Glc:Glc
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Man:Man
- Probable Dol-P-Man:Man
- UDP-N-acetylglucosamine transferase subunit alg13
- GDP-Man:Man
- UDP-N-acetylglucosamine transferase subunit alg14
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Alpha-1,2-mannosyltransferase alg9
Sequence:
MGKLSMLYNAAIASTFVKVFLFPSYRSTDFEVHRNWLAITHSLPISEWYKSSISEWTLDYPPFFAYMECVLSWIAYFFGFDKAMLDPYNLNYVSPSTVVFQRGSVIVLELVLLFALREYVLSSNVKDQRNALLTAIDIFLSPGLLIIDHIHFQYNGFLFGLLLWSIVLAKPEKNMLLSAAIFSALICFKHIFLYVAPAYFVYLLRVYCFTPNFRPQFLNILKLGSTVISIFLLAFGPWIYMKQIPQLLSRLFPFSRGLCHAYWAPNFWALYSFVDRVAFAVLPRFGYALNQGTSINAPTRGLVGESSFAVLPNIPPALTFYICLGLQITVLIKLFIKPTWRVFVGAVTLCGWISFLFGWHVHEKAILMVILPFSILSLIDRRYLEAFRPLAVSGYLSLLPLLFTLNEAPIKYLFTGAWIAMLLTFDKCAPVPVKRVFLLNRVNIAYISGFVPLFIYNCFIHKLVMGDKFEFLPLMLLSTYAAWGIFWSFVSLLWLYFTDLK
Protein: Conserved secreted protein (O16267)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRSQLRNSLNVVAVIILLLPTATWQNHLEINDWELIGSRTYSWKGNEVLRCKHWDKVAIRWHLSTCTEHGVCDGGTNVDYATRAQNWTEMPVWRNAFTYVQIPGQLQKTKFLRLGLTGYDSRKTQLEAFSPLKIDVDWRWQVTRDGCNNFVVRMSAMSMINEKMRPKLERFCRLFDKDHFVDCTNL
Protein: RAB30, member RAS oncogene family (E9PRF7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYASNK
Protein: Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase) (h-FKBP-12) (P68106)
Organism: Homo sapiens (Human)
Function: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Ryanodine receptor 2
- Ryanodine receptor 1
- Calmodulin-1
- Triadin
- Activin receptor type-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Ryanodine receptor 3
- Aspartyl/asparaginyl beta-hydroxylase
- Calmodulin-like protein 4
Sequence:
MGVEIETISPGDGRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE
Protein: Ribonuclease, putative (Q38AC8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP-dependent RNA helicase
- ATP-dependent RNA helicase
- ATP-dependent RNA helicase
Sequence:
MDVDKYNCSVVFDDFKVSIEQCDFYALDQEMTGVDNGERPQSGTMSLTELYQVSRDVVNRYIAFQLGVTVFKRVDGGYEVKPYNFYLLKSVGDFVVNIESLKFLADNHMDFQRWLVTGMPYCGKVDTGLRGDEGGSVSSLRRGLSEYLVSRIKKWYNSPLARDGECITFKTVICEEIERLTLSKLKEEQVFVSFEYDKSRCIGSPVSLTVHRGTSHFASGQGKEKATPDLEPIKVCGFQHFWKCLTDCKKPIVGHNFWLDIMFMVQMHEGPLPEDYDTYKRLVHQLFPCVYDTKTLGREVIINNLSESFCLKDLYDRCLASRLKLGGAPEFFFPPGFGRYDPDSLESECKAHEAGYDSYMTGVAFSICRDLYCSGENSTLDKWRNIVSVYGSNYYMNVNGKDSLRRSATFVVEFREEIEYPFGELLLCRDDAFTNVDRDVELLPRDCIISYDNKGLCRTIIVVFEDDISEDEVQTRIANSARRWSEVTKEANAYNIVFPEILSVYRLSG
Protein: Uncharacterized protein FLJ34048 (A4D1I3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDWGKTLSSEQPKAADLAFLPPVSRPTQVKAAKQRQRSPGAWFRPGQQVGGPDWGPGTEEGRPARTGVQGPGFRVPGLEEVAGSPPFQRLEIGWTRPEDPLGLDPDFRSA
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (EC 1.18.1.6) (J3QQX3)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|PIRNR:PIRNR000362}.
Interaction partners:
Sequence:
MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKQHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVPELQEAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH
Protein: Guanine nucleotide exchange factor for Rab-3A (Rab-3A-interacting-like protein 1) (Rab3A-interacting-like protein 1) (Rabin3-like 1) (Q8TBN0)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) which may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. May also activate RAB8A and RAB8B.
Interaction partners:
- Ras-related protein Rab-8A
- Alpha-2-macroglobulin
- Ras-related protein Rab-11A
- Rab-3A-interacting protein
- Inositol hexakisphosphate kinase 1
- Ras-related protein Rab-3A
- Ras-related protein Rab-8B
- Transmembrane protein 102
Sequence:
MWSGPPQPDQGLPPPLAAVPVPWKSTDPCQGHRESPGALVETSAGEEAQGQEGPAAAQLDVLRLRSSSMEIREKGSEFLKEELHRAQKELKLKDEECERLSKVREQLEQELEELTASLFEEAHKMVREANMKQAASEKQLKEARGKIDMLQAEVTALKTLVITSTPASPNRELHPQLLSPTKAGPRKGHSRHKSTSSTLCPAVCPAAGHTLTPDREGKEVDTILFAEFQAWRESPTLDKTCPFLERVYREDVGPCLDFTMQELSVLVRAAVEDNTLTIEPVASQTLPTVKVAEVDCSSTNTCALSGLTRTCRHRIRLGDSKSHYYISPSSRARITAVCNFFTYIRYIQQGLVRQDAEPMFWEIMRLRKEMSLAKLGFFPQEA
Protein: Synaptonemal complex protein 1 (SCP-1) (Q03410)
Organism: Rattus norvegicus (Rat)
Function: Major component of the transverse filaments of synaptonemal complexes, formed between homologous chromosomes during meiotic prophase. Required for normal assembly of the central element of the synaptonemal complexes. Required for normal centromere pairing during meiosis. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q62209}. Chromosome {ECO:0000269|PubMed:1464329}. Chromosome, centromere {ECO:0000250|UniProtKB:Q62209}. Note=In tripartite segments of synaptonemal complexes, between lateral elements in the nucleus. Its N-terminus is found towards the center of the synaptonemal complex while the C-terminus extends well into the lateral domain of the synaptonemal complex (PubMed:1464329). Only rarely detected at centromeres during leptotene and zygotene. Detected at centromeres during mid-diplotene, when it is no longer present along chromosome arms. No longer detected at centromeres at later stages of meiosis (By similarity). {ECO:0000250|UniProtKB:Q62209, ECO:0000269|PubMed:1464329}.
Interaction partners:
- Synaptonemal complex central element protein 1
- Synaptonemal complex protein 3
- Phenylalanyl-tRNA synthetase subunit alpha
- Testis expressed 12
- Synaptonemal complex central element protein 3
- Probable E3 SUMO-protein ligase RNF212
- HORMA domain-containing protein 1
- Meiotic recombination protein REC8 homolog
- Six6 opposite strand transcript 1
- HORMA domain containing 2
Sequence:
MEKQKPFTLFVPPRLSSSQVSAVKPQTAGGDSNYFKTVNKCTEGDFGVPLTMSSLSKNRENIDTDPAFQKLSILPMLEQVANSGSCHYQEGVNDSDFENSEPMSRLYSKLYKEAEKIKKWKVSIESELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHWCNLLKETCARSAEKTSKYEYEREETRQVYVDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYQKEVNNKENQVSLLLIQSTEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELNEKKDHLTSELEDIKMSMQRSMSTQKTLEEDLQIATKTIYQLTEEKEAQMEELNKAKTTHSLVVTELKATTCTLEELLRTEQQRLENNEDQLKLITMELQKKSSELEEMTKFKNNKEVELEELKTILAEDQKLLDEKKQVEKLAEELQGKEQELTFLLQTREKEIHDLEVQVTVTKTSEEHYLKQVEEMKTELEKEKLKNIELTANSDMLLLENKKLVQEASDMVLELKKHQEDIINCKKQEERMLKQIETLEEKEMNLRDELESVRKEFIQQGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKSKNIEELHQENKALKKKSSAENKQLNAYEIKVNKLELELASTKQKFEEMINNYQKEIEIKKISEEKLLGEVEKAKATVDEAVKLQKEIDLRCQHKIAEMVALMEKHKHQYDKIVEERDSELGLYKNREQEQSSAKVALETELSNIRNELVSLKKQLEVEKEEKEKLKMEQENTAILTDKKDKKIQASLLESPEATSWKFDSKTTPSQNISRLSSSMDSGKSKDNRDSLRASAKSILSTTVTKEYTVKTPTKKSIYQRENKYLPTGGSNKKRKTVFEFDVNSDSSETTDLLSLVSEEDISNRIYNNNTPDSHLLVKTPKQTPLSLSTPASFTKFGSLKKMREDRWATIAKIDRKRRLKEAEKLFT
Protein: Cytochrome P450 93G2 (EC 1.14.14.162) (Flavanone 2-hydroxylase) (OsF2H) (Q5VRI5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as flavanone 2-hydroxylase that catalyzes the direct conversion of flavanones to 2-hydroxyflavanones. In vitro, can convert naringenin and eriodictyol to the corresponding 2-hydroxyflavanones. Generates 2-hydroxyflavanone substrates for C-glycosylflavone biosynthesis by the glycosyltransferase CGT.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Flavanone 4-reductase
- Flavanone 3-dioxygenase 1
- Chalcone--flavanone isomerase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Naringenin 7-O-methyltransferase
- Flavonoid 3'-monooxygenase CYP75B4
- Flavonoid 3'-monooxygenase CYP75B3
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
Sequence:
MEEGVVGGGGAAVLVALLVTVVLAVMRSAGSRSSKRGRLPPSPMALPIIGHLHLIRPPPHRAFDRILARHGPLVYLRLGPSTHCVVIGSADVARDFLKFEASIPERPPTAVTRQLAYGKAGFAFAPYGAYWRFVKRLCMSELLGPRTVELLRPVRAAELADVLRAAQSAAERGEGVDMSHELVRMANNSIMRMVASALPGEMAEAARDCAKQVAELVGAFNAEDFVAVCRGWDLQGIGRRTNEVHARFDALLETIIEAKEEARRRSLRLGRRESSSKDLLDMLMDAAEDDTAEVKLTRDNIKAFVLDIFTAGSDTTATTVEWMLAELVNHPECMAKLRGELDAVVGRSRLVGEQDVARLPYLQAVLKETLRLRPPAVFAQRVTVEPVQVRGYTIPTDTQVFFNIFSIGRDATYWDQPLHFRPDRFLPDGAGATVDPKGQHPQLMPFGSGRRACPGMGLAMQAVPAFLAALVQCFDWAPPPSQPLPLDMEEAAGLVSARKHPLLLLPTPRIQPLPSFYS
Protein: Membrane protein BRI3 (Brain protein I3) (pRGR2) (O95415)
Organism: Homo sapiens (Human)
Function: Participates in tumor necrosis factor-alpha (TNF)-induced cell death. May be a target of Wnt/beta-catenin signaling in the liver.
Subcellular location: Lysosome membrane {ECO:0000305|PubMed:14592447}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30983867}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000269|PubMed:30983867}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:30983867}. Nucleus {ECO:0000269|PubMed:30983867}. Note=Diffuse localization in the cytoplasm and nucleus. {ECO:0000269|PubMed:30983867}.
Interaction partners:
- Olfactory receptor 6A2
Sequence:
MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPAAPPPPPYPYLVTGIPTHHPRVYNIHSRTVTRYPANSIVVVGGCPVCRVGVLEDCFTFLGIFLAIILFPFGFICCFALRKRRCPNCGATFA
Protein: Coatomer subunit epsilon (Q381U5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}.
Interaction partners:
- Coatomer subunit alpha
- Coatomer subunit beta
- Coatomer subunit beta'
- Coatomer subunit delta
- Coatomer subunit gamma
- Coatomer subunit zeta
- ER lumen protein-retaining receptor
- Vesicle-associated membrane protein, putative
- ADP-ribosylation factor GTPase activating protein 1, putative
- SEC7 domain-containing protein
Sequence:
MADPFYDARNALALGNYHQAVAEASGTKTDARKAEDIAAFHAEKEVLLALAQTGLGQGDAVVAQLKAATCPILVAVREWAVFCSAMKNLSGDIQSDPVICMQLKKLTEAAEVIDPARTQIAVLAAAALLAVGDNAGALKLSKEWLNDQRHSRENSLLRLHMELRVIVVEALLRMGRTEMARSEVKAMEQADEESMLTVLCSGITNLYEGIKTKEAYQTALRRFKELTMSCGQSVLASNLTALAQIQLGEYTEAERTLLDVLAMKSGDSDTTANLAVISAHSGKGLDSTGLYTRQAVATSGPWSRSFSAASAALDAAIEEFTASA
Protein: Alpha-2B adrenergic receptor (Alpha-2B adrenoreceptor) (A0A060XV00)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ig-like domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Endothelin-3
- Neuropeptide Y
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit alpha-13
Sequence:
MASPLDSACSVELGNTNSSTSGSSLPCNQSVSSLQLAPYSPEATALFATAITLMIVFTIVGNIFVIIAVLTSRALRGPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFKSLWCEIYLALDVLFCTSSIAHLCAISLDRYLSISRVTYSRQRTPMRIKASIVVVWLISAIISFPPLLSLNKSEPGGEGSERGPQCQLNDERWYILYSTVGSFFAPCLIMILVYMRIYQIAKQRTQNPPGEPRKDGVGSIPHKTSSIRPPTLAITPSLSPDQANETPPSSPTPNNLLHPPDPSLAPTPTTTSPPTSPMGPSHSSAKPKDGEKKGKKGKKGKNSDSDMEHEGGGRRGVNTPSMAGSPGIHSPATIQKYRDMIATSKGARLVAGRRSKPDTTPGAARRKAMVNREKRFTFVLAVVIGVFVVCWFPFFFSYSLQAICPETCALPDPLFKFFFWIGYCNSCLNPVIYTIFNQDFRKAFKKILCKNTKGTFF
Protein: Ubiquitin-conjugating enzyme family protein (Q9C8I1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Developmentally-regulated G-protein 1
- Developmentally-regulated G-protein 2
- Developmentally-regulated G-protein 3
- Ubiquitin-ribosomal protein eS31y fusion protein
- E3 ubiquitin-protein ligase UPL2
- Protein ILITYHIA
- CRIB domain-containing protein RIC5
- Probable pectinesterase/pectinesterase inhibitor 23
- Ubiquitin-activating enzyme E1 1
- Cullin-associated NEDD8-dissociated protein 1
Sequence:
MTEYKQEQEMEIEALEAILMDEFKEIHSSESGLNTSNRCFQITVTPQDDELEELAIPPVQLALVFSHTENYPDEAPLLDVKSIRGIHVSDLTILKEKLEQEASENLGMAMIYTLVSSAKDWLSEHYGQDDAAEFAEVEAAKEDEVIVPHGEPVTLETFLAWRERYEAELALERAKLMPESALTAPKEKKLTGRQWFESGRGRGTVVIADEEDEEEDEEDIDFEDEDFEDDEEDMLEHYLAEKSDSSAPPTRT
Protein: Putative aldo-keto reductase family 1 member C8 (Aldo-keto reductase family 1 member C-like protein 1) (EC 1.1.1.-) (Q5T2L2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MMTDLKQSHSVRLNDGPFMPVLGFGTYAPDHTPKSQAAEATKVAIDVGFRHIDSAYLYQNEEEVGQAIWEKIADGTVKREEIFYTIKLWATFFRAELVHPALERSLKKLGPDYVDLFIIHVPFAMKGSS
Protein: Cullin, a subunit of E3 ubiquitin ligase (O69681)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- IscS-like cysteine desulfurase
- Lipid II isoglutaminyl synthase subunit MurT
- Lipid II isoglutaminyl synthase subunit GatD
- Alpha-keto-acid decarboxylase
- DNA repair protein RadA
- DNA integrity scanning protein DisA
Sequence:
MLISRMSVRSASMSVMGDVFIGSEAITAGRLTRHELQRWYQPMFRGVYVSRRSVPTLWDRTVGAWLATRRHGVIAGNAASALHGAQWVDVDVAIELISPTTRPQHGLVIRRETLCDDEITRVVGLPVTTLARTAYDLGRHLSRGEAVARLDALMRATPFSRDDVLLLAKRHAGARGVRRLRDVLPLVDGGAASPKETWLRLLLIDAGLPVPTTQIPVVHRWRNVGVLDMGWEKYMVAAEYDGDQHRSDRGRYVKDQRRLRKLAELGWIVIRVIAEDNPDDVVNRVRAALLARGWRP
Protein: E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (RING-type E3 ubiquitin transferase CHIP) (Q86DT8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LKRWELCCQDSRRALDIDGNLLKGHFFLGQGLMEIDNFDEAIKHLQRAYDLSKEQKQNFGDDITLQLRLARKKRWNVMEEKRIQQEIELQSYLNGLIKGDMESRLANLKLNGNVHDEQLKDKQQEIEQECDDHIKELNNIFSKVDERRKKREVPDFLCGKISFEILTDPVITPSGITYERKDIEEHLQRVGHFDPVTRVKLTQDQLIPNFSMKEVVDSFIA
Protein: 4-hydroxybenzoate 3-monooxygenase (NAD(P)H) (EC 1.14.13.33) (4-hydroxybenzoate 3-hydroxylase) (4HB 3-hydroxylase) (C4TP09)
Organism: Paenibacillus sp
Function: Involved in the degradation of 4-hydroxybenzoate (4HB) via the protocatechuate (PCA) 2,3-cleavage pathway. Catalyzes the conversion of 4HB into 2-hydroxypenta-2,4-dienoate (HPD). It is highly specific for 4-hydroxybenzoate, and is able to utilize both NADH and NADPH as electron donors at approximately equal rates.
Interaction partners:
Sequence:
MRTQVGIIGAGPAGLLLSHLLYLQGIESIIIENRTREEIEGTIRAGVLEQGTVDLMNQMGVGARMMKEGHFHEGFELRFNGRGHRINVHELTGGKYVTVYAQHEVIKDLVAARLQTGGQIHFNVGDVSLHDVDTSSPKIRFRPNKDGELQEIECDFIAGCDGFRGPSRPAIPQSVRKEYQKVYPFSWLGILVEAPPSAHELIYANHERGFALVSTRSPQIQRLYLQVDAQDHIDNWSDDRIWSELHARLETRDGFKLLEGPIFQKGIVSMRSFVCDPMQHGRLFLAGDAAHIVPPTGAKGLNLAAADVQVLARGLEAYYKAGKMEILNRCTEICLRRIWKAERFSWFMTTMLHRDQGHTPFERGIQLAELDYVTSSRAASTSLAENYIGLPMEF
Protein: Cytochrome c, somatic (P62898)
Organism: Rattus norvegicus (Rat)
Function: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Subcellular location: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane.
Interaction partners:
- Apoptotic protease-activating factor 1
- Caspase-9
- Bcl-2-like protein 1
- Caspase-3
- Apoptosis regulator Bcl-2
- Non-selective voltage-gated ion channel VDAC2
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Heat shock protein beta-1
Sequence:
MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITWGEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
Protein: Nuclear transcription factor Y subunit A-7 (AtNF-YA-7) (Q84JP1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit B-3
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit C-4
- Nuclear transcription factor Y subunit B-2
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit B-7
- Nuclear transcription factor Y subunit C-6
- Nuclear transcription factor Y subunit B-5
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit B-1
Sequence:
MTSSIHELSDNIGSHEKQEQRDSHFQPPIPSARNYESIVTSLVYSDPGTTNSMAPGQYPYPDPYYRSIFAPPPQPYTGVHLQLMGVQQQGVPLPSDAVEEPVFVNAKQYHGILRRRQSRARLESQNKVIKSRKPYLHESRHLHAIRRPRGCGGRFLNAKKEDEHHEDSSHEEKSNLSAGKSAMAASSGTS
Protein: SD05277p (Q86NP0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPLADSQKDLRQQPQQQQQQQHVSSTSSSNNAEQQCSSSGLGLQLRQRMQITSSGCSSLAVTPMEHTPTEDDESGGGNSGVTSSVTTVTSSQRRQQLQQVQQQSALQAALEQHHISPTADLDSARKRPTHRTLCPPPELMELSDSESQGGVETGGRREGATGRSAPDLEDTEPLYETENEFELKEVIKEGHDKADPSQFELLRVLGEGSFGKVFLVRKIIGKDAGTLYAMKVLKKATLKVKDRVRSTNERKILADVGHAFIVRLHYAFQTPGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALAMNHLHTLGIIYRDLKPENILLDEHGHIALTDFGLSKQPLDGSKTYSFCGTVEYMAPEIVNRKGHDFAADWWSFGVLMYEMLTGNLPFHGQTRQETMNQILRSKLGMPENLSPEAQSLLRALFKRNPQNRLGAGAQGILDIKAHCFFATIDWVRLERKQVRPPFIPAVSRDDAFYFDVEYTSKSPRDSPGGPISASAHEIFRGFSFVAPVLLEGQCAGSNMCSTSASPLHSIAPIPAAPVGAPRTLPGVLPGNFHAEYNLLQELGRGTFSVCRLCEHRASKKHYAVKVIEKAAVAAASTSTSADCWEEVEIMLRYGNHPNIVTLYSVYEDAGSAYLVMELLKGGELLDRILAVGQMCESEASAVLRTIASAVAYLHEHGVVHRDLKPSNMIYASMRQTPETLKLCDLGFAKQLRADNGLLMTPCYTANFVAPEVLKRQGYDLACDIWSLGVLLYIMLSGRTPFASTPNDSPDVILKRIGSGQIDFTSSRWALISVPAKELLRQMLHIVPENRPTAARILEHDWLREQFAGGVQLTEYAVAPGSQLSLGAQQQQQNHISMALRGAVDATFRAIAIPQAANVGP
Protein: Sentrin-specific protease 6 (EC 3.4.22.-) (SUMO-1-specific protease 1) (Sentrin/SUMO-specific protease SENP6) (Q9GZR1)
Organism: Homo sapiens (Human)
Function: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional activation. Involved in chromosome alignment and spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML and CENPI, protecting them from degradation by the ubiquitin ligase RNF4, which targets polysumoylated proteins for proteasomal degradation. Desumoylates also RPA1, thus preventing recruitment of RAD51 to the DNA damage foci to initiate DNA repair through homologous recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875}.
Interaction partners:
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 1
- Sodium/potassium-transporting ATPase subunit beta-1-interacting protein 2
- Ran GTPase-activating protein 1
- Pre-mRNA-processing factor 19
- DBF4-type zinc finger-containing protein 2
- SUMO-conjugating enzyme UBC9
- Small ubiquitin-related modifier 4
- SUMO-activating enzyme subunit 2
- SUMO-activating enzyme subunit 1
Sequence:
MAAGKSGGSAGEITFLEALARSESKRDGGFKNNWSFDHEEESEGDTDKDGTNLLSVDEDEDSETSKGKKLNRRSEIVANSSGEFILKTYVRRNKSESFKTLKGNPIGLNMLSNNKKLSENTQNTSLCSGTVVHGRRFHHAHAQIPVVKTAAQSSLDRKERKEYPPHVQKVEINPVRLSRLQGVERIMKKTEESESQVEPEIKRKVQQKRHCSTYQPTPPLSPASKKCLTHLEDLQRNCRQAITLNESTGPLLRTSIHQNSGGQKSQNTGLTTKKFYGNNVEKVPIDIIVNCDDSKHTYLQTNGKVILPGAKIPKITNLKERKTSLSDLNDPIILSSDDDDDNDRTNRRESISPQPADSACSSPAPSTGKVEAALNENTCRAERELRSIPEDSELNTVTLPRKARMKDQFGNSIINTPLKRRKVFSQEPPDALALSCQSSFDSVILNCRSIRVGTLFRLLIEPVIFCLDFIKIQLDEPDHDPVEIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSIQLQMNKEDKVWNDCKGVNKLTNLEEQYIILIFQNGLDPPANMVFESIINEIGIKNNISNFFAKIPFEEANGRLVACTRTYEESIKGSCGQKENKIKTVSFESKIQLRSKQEFQFFDEEEETGENHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLNEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNHETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVIQKCSTVEDSCISSSASEMESCSQNSSAKPVIKKMLNKKHCIAVIDSNPGQEESDPRYKRNICSVKYSVKKINHTASENEEFNKGESTSQKVADRTKSENGLQNESLSSTHHTDGLSKIRLNYSDESPEAGKMLEDELVDFSEDQDNQDDSSDDGFLADDNCSSEIGQWHLKPTICKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPILSFELPMNLANWFPPPRMRTKREEIRNIILKLQEDQSKEKRKHKDTYSTEAPLGEGTEQYVNSISD
Protein: Flagellar transcriptional regulator FlhD (A0A0F6B2Q9)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00725}.
Interaction partners:
Sequence:
MGTMHTSELLKHIYDINLSYLLLAQRLIVQDKASAMFRLGINEEMANTLGALTLPQMVKLAETNQLVCHFRFDDHQTITRLTQDSRVDDLQQIHTGIMLSTRLLNEVDDTARKKRA
Protein: Uncharacterized protein, isoform B (A0A0B4JDC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKDCVEIFEGEFEVLRVTPPLYDEVEELLVNISINYEFGCVIAKLKDSPLAIAELVHPNQNTKRKTSYYDICAQIKSPNMIKYMELWDAVDASFNVNEHCQVDSTGDVEYMATLPEFRRRGLGHILCQQSIQFASLLAQRKLPLEILNQLPEEMRIERPQAIVAITTSQSSQIMGRQLGMKTMHKWHFSELRSLCGAMAESNGAAQAFEYAELQVVKF
Protein: HTH-type transcriptional regulator TrpI (TrpBA operon transcriptional activator) (P11720)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Activates the expression of the trpBA genes, which encode the two tryptophan synthase subunits, and represses initiation at its own promoter. Acts by binding to two adjacent sites in the intergenic region. In the absence of the inducer indoleglycerol phosphate (InGP), TrpI binds to site I. In the presence of InGP, TrpI binds to site I and site II. Binding to site II is site I dependent. InGP strongly stimulates binding to site II and is required for maximal activation of trpBA.
Interaction partners:
- Tryptophan synthase beta chain
- Tryptophan synthase alpha chain
Sequence:
MSRDLPSLNALRAFEAAARLHSISLAAEELHVTHGAVSRQVRLLEDDLGVALFGKDGRGVKLTDSGVRLRDACGDAFERLRGVCAELRRQTAEAPFVLGVPGSLLARWFIPRLDQLNRALPDLRLQLSTSEGEFDPRRPGLDAMLWFAEPPWPADMQVFELAPERMGPVVSPRLAQETGLAQAPAARLLQEPLLHTASRPQAWPAWAASQGLAAEALRYGQGFEHLYYLLEAAVAGLGVAIAPEPLVRDDLAAGRLAAPWGFIETDARLALWVPARLHDPRAGRLAQWLREQLAG