wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-tubulin complex component 5 (GCP-5) (Q96RT8)
Organism: Homo sapiens (Human)
Function: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}.
Interaction partners:
- Gamma-tubulin complex component 3
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 2
- Gamma-tubulin complex component 6
- Mitotic-spindle organizing protein 1
- Gamma-tubulin complex component 4
- Magnesium transporter NIPA2
- Magnesium transporter NIPA1
- Mitotic spindle organizing protein 2B
- Cytoplasmic FMR1-interacting protein 1
Sequence:
MARHGPPWSRLDAQQERDVRELVRGVAGLQDEADPNFQLALNFAWSNFRFHRFLDVNSHKIEKTIEGIYEKFVIHSDLSKAASWKRLTEEFLNAPLPSIKEIKTDAHYSILSLLLCLSDSPSNSSYVETPRNKEVEKKDDFDWGKYLMEDEEMDIGPYMDTPNWSEESEEENDQQPLSREDSGIQVDRTPLEEQDQNRKLDPCISWKDEPDDRSWLEHHVVHQYWTARPSQFPHSLHLHSNLAAVWDQHLYSSDPLYVPDDRVLVTETQVIRETLWLLSGVKKLFIFQLIDGKVTVRNNIIVTHLTHSCLRSVLEQIAAYGQVVFRLQEFIDEVMGHSSESMLPGSGSVPKKSTEAPFRTYQAFMWALYKYFISFKEELAEIEKCIINNDTTITLAIVVDKLAPRLSQLKVLHKVFSTGVAEVPPDTRNVVRASHLLNTLYKAILEYDNVGEASEQTVSLLFSLWVETVRPYLQTVDEWIVHGHLWDGAREFIIQRNKNVPVNHRDFWYATYTLYSVSEKTENEEKMSDNASASSGSDQGPSSRQHTMVSFLKPVLKQIIMAGKSMQLLKNLQCAESTTCQAGARDAERKSLYTLFLESVQSRLRHGEDSTPQVLTEQQATKENLMKMQSIAESHLELDDVHDPLLAINFARMYLEQSDFHEKFAGGDVCVDRSSESVTCQTFELTLRSCLYPHIDKQYLDCCGNLMQTLKKDYRLVEYLQAMRNFFLMEGGDTMYDFYTSIFDKIREKETWQNVSFLNVQLQEAVGQRYPEDSSRLSISFENVDTAKKKLPVHILDGLTLSYKVPWPVDIVISLECQKIYNQVFLLLLQIKWAKYSLDVLLFGELVSTAEKPRLKEGLIHEQDTVAQFGPQKEPVRQQIHRMFLLRVKLMHFVNSLHNYIMTRILHSTGLEFQHQVEEAKDLDQLIKIHYRYLSTIHDRCLLREKVSFVKEAIMKVLNLALMFADGWQAGLGTWRMESIEKMESDFKNCHMFLVTILNKAVCRGSFPHLESLALSLMAGMEQS
Protein: Receptor expression enhancing protein A, isoform J (A0A0B4JD87)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISSLFSRLIILFCGTLYPAYASYKAVRTKDVKEYVKWMMYWIVFAFFTCIETFTDIFISWLPFYYEVKVALVFWLLSPATKGSSTLYRKFVHPMLTRHEQEIDEYVNQAKERGYSAVLQLGSKGVNYATNVLMQTAIKGGGNLVQTIKRSYSLSDLSEPDMHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNEQLLEEMRDEVYLDNQLYFQGVQRKSSVPEAEELKIVESSESIQSQELEKVLKEENIDAEDEAFFETLPLIEEHINEVVANYGRDEKLLPQERKHNSIEEEQFEDALFEEPQKCVSDEVDAKNIEEILTDRSQNQTPNGSAETTDSGTPSQNKPYVHPPIDPFLLVLSASASAPDPFMPERPRPMSPREMRETLEEIKHSFRAQLEAEPSVSASPSPSLRPKANHGKGRAPPPPLPPKKHSLSPQPDAISQTSTGSVERKSGIGQLFKNIKANVLRNKANPSQQQPEDEQLAAKETQI
Protein: Poly(3-hydroxyalkanoate) polymerase subunit PhaC (PHA polymerase) (EC 2.3.1.-) (PHB synthase subunit PhaC) (Poly(3-hydroxybutyrate) polymerase subunit PhaC) (PHB polymerase) (Poly(hydroxyalkanoic acid) synthase subunit PhaC) (PHA synthase) (Polyhydroxyalkanoic acid synthase subunit PhaC) (P73390)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: When expressed in E.coli with Synechocystis PhaE and C.necator PhaA and PhaB, confers the ability to synthesize up to 13% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all 4 genes are necessary for PHB production. Cell-free in vitro coexpression with PhaE gives a heterodimer able to polymerize 3-hydroxybutyrate-CoA.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Poly
- Acetoacetyl-CoA reductase
- Acetyl-CoA acetyltransferase
- Slr0060 protein
- Renin-binding protein
- Slr0058 protein
Sequence:
MFLLFFIVHWLKIMLPFFAQVGLEENLHETLDFTEKFLSGLENLQGLNEDDIQVGFTPKEAVYQEDKVILYRFQPVVENPLPIPVLIVYALVNRPYMVDLQEGRSLVANLLKLGLDVYLIDWGYPSRGDRWLTLEDYLSGYLNNCVDIICQRSQQEKITLLGVCQGGTFSLCYASLFPDKVKNLVVMVAPVDFEQPGTLLNARGGCTLGAEAVDIDLMVDAMGNIPGDYLNLEFLMLKPLQLGYQKYLDVPDIMGDEAKLLNFLRMEKWIFDSPDQAGETYRQFLKDFYQQNKLIKGEVMIGDRLVDLHNLTMPILNLYAEKDHLVAPASSLALGDYLPENCDYTVQSFPVGHIGMYVSGKVQRDLPPAIAHWLSERQ
Protein: Arginine kinase (AK) (EC 2.7.3.3) (A0A286R7K5)
Organism: Polybetes pythagoricus (South American huntsman spider) (Ocypete pythagorica)
Function: Catalyzes the reversible transfer of high energy ATP gamma-phosphate group to L-arginine.
Interaction partners:
Sequence:
MVDQATLDKLEAGFKKLQDATDCKSLLKKYLNREVFDQCKSLKTALGATLLDCIQSGVENLDSGVGIYAPDAEAYTLFAPIFNPIIEDYHEGFKPTDKHPPTDFGDINTIVNVDPSGKYVVSTHVRCGRSLKGYPFNPCLTEANYKEMEDKVSAIFGTFEGELKGKYYPLTGMDKATQQQLIDDHFLFKEGDRFLQAANACRYWPTGRGIYHNDAKTFLVWVNEEDHLRIISMQKGGDLKTIFQRLVNAVNTIESKLPFSRDDRLGFLTFCPTNLGTTIRASVHIALPKLAKDKKQLEAIAAKFNLQVRGTRGEHTESEGGVYDISNKRRMGLTEYQAVKEMQDGILEMIKMEEAAP
Protein: UDP-glycosyltransferase CGT (EC 2.4.1.360) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase) (OsCGT) (C3W7B0)
Organism: Oryza sativa subsp. indica (Rice)
Function: UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of 2-hydroxyflavanones. Acts preferentially on the dibenzoylmethane tautomers formed in equilibrium with 2-hydroxyflavanones. No activity with naringenin or naringenin chalcone.
Interaction partners:
Sequence:
MPSSGDAAGRRPHVVLIPSAGMGHLVPFGRLAVALSSGHGCDVSLVTVLPTVSTAESKHLDALFDAFPAVRRLDFELAPFDASEFPGADPFFLRFEAMRRSAPLLGPLLTGAGASALATDIALTSVVIPVAKEQGLPCHILFTASAAMLSLCAYFPTYLDANAGGGGGVGDVDIPGVYRIPKASIPQALHDPNHLFTRQFVANGRSLTSAAGILVNTFDALEPEAVAALQQGKVASGFPPVFAVGPLLPASNQAKDPQANYMEWLDAQPARSVVYVSFGSRKAISREQLRELAAGLEGSGHRFLWVVKSTVVDRDDAAELGELLDEGFLERVEKRGLVTKAWVDQEEVLKHESVALFVSHCGWNSVTEAAASGVPVLALPRFGDQRVNSGVVARAGLGVWADTWSWEGEAGVIGAEEISEKVKAAMADEALRMKAASLAEAAAKAVAGGGSSHRCLAEFARLCQGGTCRTN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F6RJM5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASNQNSPIRTFGLNLSSDSSALGAVASDSEQSKTEEERESRSLFPGSLKPKLGKRDYLEKAGELIKLALKKEEEDDYEAASDFYRKGVDLLLEGVQGESSPTRREAVKRRTAEYLMRAESISSLYGKPQLDDVSQPPGSLSSRPLWNLRSPAEELKAFRVLGVIDKVLLVMDTRTEQTFILKGLRKSSEYSRNRKTIIPRCVPNMVCLHKYIISEESVFLVLQHAEGGKLWSYISKFLNRSPEESFDIKEVKKPTLAKVHLQQPTSSPQDSSSFESRGSDGGSMLKALPLKSSLTPSSQDDSNQEDDGQDSSPKWPDSGSSSEEECTTSYLTLCNEYGQEKIEPGSLNEEPFMKTEGNGVDTKAIKSFPAHLAADSDSPSTQLRAHELKFFPNDDPEAVSSPRTSDSLSRSKNSPMEFFRIDSKDSASELLGLDFGEKLYSLKSEPLKPFFTLPDGDSASRSFNTSESKVEFKAQDTISRGSDDSVPVISFKDAAFDDVSGTDEGRPDLLVNLPGELESTREAAAMGPTKFTQTNIGIIENKLLEAPDVLCLRLSTEQCQAHEEKGIEELSDPSGPKSYSITEKHYAQEDPRMLFVAAVDHSSSGDMSLLPSSDPKFQGLGVVESAVTANNTEESLFRICSPLSGANEYIASTDTLKTEEVLLFTDQTDDLAKEEPTSLFQRDSETKGESGLVLEGDKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFFTPVDWAELMR
Protein: Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (Q9ER34)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16341586}.
Interaction partners:
- Citrate synthase, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- ATP-citrate synthase
- 2-oxoglutarate dehydrogenase complex component E1
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MAPYSLLVTRLQKALGVRQYHVASALCQRAKVAMSHFEPSEYIRYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGTLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAEEFKDHLVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHPVADVGTVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGSEQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRNDANPETHAFVTSPEIVTALAIAGTLKFNPETDFLTGKDGKKFKLEAPDADELPRSDFDPGQDTYQHPPKDSSGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAAGPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVIGDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNKIHPVDKLTIQGLKDFAPGKPLNCIIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ
Protein: Vacuolar protein sorting-associated protein 26 (VPS26 protein homolog) (Q9W552)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the retromer complex which acts in conjunction with wingless (wg) and clathrin-mediated endocytosis to sustain a wntless (wls) traffic loop. This loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, thereby enabling wls to direct wg secretion. The hh and dpp signaling pathways do not require the retromer complex suggesting that it does not play a general role in exocytosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18193032}. Membrane {ECO:0000269|PubMed:18193032}; Peripheral membrane protein {ECO:0000269|PubMed:18193032}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- FI18122p1
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-3
- Sorting nexin 6, isoform B
- LD13361p
- Sorting nexin
- GH10459p
- Vacuolar protein sorting-associated protein 26C
- WASH complex subunit 2
Sequence:
MNFLGFGQSADIEIVFDGAEHKTAEVKGEDGKVEKMLLFYDGETVSGKVNVTLKKPGSKLEHQGIKIEFIGQIELYYDRGNHHEFKCLAKALARPGDLIQNNSYPFDFPKVEKQFEVYAGSNVRLRYFLRATIVRRISDITKEVDIAVHTLCSYPEMNNPIKMEVGIEDCLHIEFEYNKSKYHLRDTIIGKIYFLLVRIKIKHMEIAIIKKESTGTGPTMFNENETIAKYEIMDGAPVKGESIPIRVFLAGYNLTPTMRDINKKFSVKYFLNLVLMDTEDRRYFKQQEITLWRKADKPRYHGAQQHQQQQHQHVPLHAPPHLVSGPAAPTVAHSLISSSTDSGEVGGAPTAPGTAGSESKMGLFTRESPNQEFSQQQMDSPPLTPTPSTASVAVAVPTAASSVSEPAPERGIGDGAAAATTSASPVAMLSSSPPPLLPVSPLSRSETEASEQVQPEDEDLDAITPNTKKTGATPLATD
Protein: RNA-splicing ligase RtcB homolog (EC 6.5.1.8) (3'-phosphate/5'-hydroxy nucleic acid ligase) (Q9VIW7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs.
Interaction partners:
- Protein archease-like
- ATP-dependent RNA helicase Ddx1
- RNA 3'-terminal phosphate cyclase
- RE59232p
- 2'-phosphotransferase
- Protein CLP1 homolog
- Probable RNA 3'-terminal phosphate cyclase-like protein
- FI17904p1
- X-box-binding protein 1
- Eukaryotic peptide chain release factor subunit 1
Sequence:
MVVRPYNDELRYLEKVSDHCWRIKKGFQPNMNVEGCFYVNSRLERLMLEELKNSCRPGAVGGFLPGVKQIANVAALPGIVGRSIGLPDIHSGYGFAIGNMAAFDMNDPLSVVSPGGVGFDINCGVRLLRTNLYEKDVQPVKEQLAQSLFDHIPVGVGSKGIIPMNARDLEEALEMGMDWSLREGYVWAEDKEHCEEYGRMLNADPAKVSMRAKKRGLPQLGTLGAGNHYAEIQVVDEIYDKWSASKMGIEEKGQVVVMIHSGSRGFGHQVATDALVQMEKAMKRDKIETNDRQLACARINSVEGQDYLKAMAAAANFAWVNRSSMTFLTRQAFAKMFNTTPDDLDMHVIYDVSHNIAKVENHMVDGKERKLLVHRKGSTRAFPPHHPLIPVDYQLTGQPVLVGGTMGTCSYVLTGTEQGMQETFGSTCHGAGRALSRAKSRRNLDYKDVLDKLDQLGIAIRVASPKLVMEEAPESYKDVTDVVDTCHAAGISKKCIKMRPIAVIKG
Protein: ATP synthase regulation protein NCA2 (Q386P2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004225}.
Interaction partners:
- Rab GDP dissociation inhibitor
- Uncharacterized protein
- Exocyst complex component EXOC6/Sec15 N-terminal domain-containing protein
- Geranylgeranyl transferase type-2 subunit beta
- Exocyst complex component Sec3 coiled-coil domain-containing protein
Sequence:
MEVAYGSTCHMIVQCMCSFPPSFFLFFFFLFLHSFQRFLFYATVTSRHLCLLLFLGLLVCAFIRPSLPSFFSFSVRMCVCVCVFGGGGGKAYEHVTQLSLFYELALFFFFFSDLYFSFSFSLSFVLSLYLFFSSSSVSCDMFCEDGSQLGWSFTVTDLLARKRRNFPSSFATALASRSREALLHISRNPTVTKLLTERPGILSELEAPAKQLRSLEDLVLLLRELNTSPVGDRLRFLNGASPTLVEVFGEENVKDPQAIAERELIAWLQLSVWVRYCTVIVMQRLVALHECISAYAQYWVWAEKHSARASFHLSLSGWQWLRQQCYGILYTGWGRYMLQIALMANTHGAFLHRMMRSVVCGIGTLHNILDRANSSIAAVGNDDSWFPVLTDAQHEEARQRVLSRVRTAVTRAVWQLKGSLHVLVPPEDVSGGSARDPQSFPEGGATSLHEVLNLFYVTAYSLQLNVSKLEEGADKGHMPPRGRRWRPVAFFIFVVIPSVAWLAAGGARKLLQVCSSARATLRWMVSNYVVWPLQEVRRSLLGSRPGVLERRRALEEEMKSVANIISDYCKDCSPDMSDANHLEQLHRDTLQSLRMGVMTDDEGYLTINRDFESAIKRPIRSVLFGNLPRLILVQLACKQLEVNRVINVTGEILEENDLNFRVMAMIPVITFLGGILQLSLQNRRVKRRPVILHLKLCWWAVHHLVTFPEMGEISGANCEHPHHNYRDHYVKDVQLKLPEFRRDESPVSTNLEEVSLVNPSRYYHSTYLSDYDQGMLLLLTHHMRRIAMEYYPRYHHLKQYLEDLDRLESVWSTRQQRLSTLDRMWHAFHFLSQHALAG
Protein: Ankyrin repeat and SOCS box protein 4 (ASB-4) (Q9WV71)
Organism: Mus musculus (Mouse)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes differentiation and maturation of the vascular lineage by an oxygen-dependent mechanism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17276034}.
Interaction partners:
- Cullin-2
- von Hippel-Lindau disease tumor suppressor
- Cullin-5
- Elongin-B
- Elongin-C
- RING-box protein 2
- COMM domain-containing protein 1
- E3 ubiquitin-protein ligase RBX1
- Insulin receptor substrate 4
- Amyloid protein-binding protein 2
Sequence:
MDGITAPISKAGAAKLVKKDFLEALKTNDFGKLKAILIERQIDVDTVFEVEDENMILASYKQGYWLPSYKLKSSWATGLHLSVLLGHVECLMVLLDHNATINCRPNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLVLRGANVNMKTNNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIATYWALRFKEQEYSREHHLICRTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAIQYVLKVTSVRPAAQPEICYQLLLNHGAARIYPPQFHKVIQACHSCPKAIEVVVNAYEHIRWNIKWRRAIPDDDLEKHWDFYHSLFKVCCNTPRTLMHLSRCAIRKALHNRCHKAIPMLSLPLPLKKYLLLEPEGIIY
Protein: Hyaluronan synthase 2 (EC 2.4.1.212) (Hyaluronate synthase 2) (Hyaluronic acid synthase 2) (Q9DG41)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Vesicle {ECO:0000256|ARBA:ARBA00004373}.
Interaction partners:
- UDP-glucose 6-dehydrogenase
- Versican core protein
- T-box transcription factor TBX2b
- Bone morphogenetic protein 4.
- Hyaluronidase.
Sequence:
MRCDKAVSYLRIVGTTLFGISLLVGISTAYIMGYKLVTTPGNYLSFGLYGAILVIHLIIQSVFALLEHRNMKRSLETPIKLNKSLALCIAAYQEDPNYLRKCLISVKRLTYPGIKVIMVIDGNNDDDCYMMEIFREIMGRDKAATYIWKSNYHHRGPEETEESYATSLQHVSHLVLNNKCVCIMQKWGGKREVMYTAFKALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPNVGGVGGDVQILNKYESWVSFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFLEDWYDQTFMGSHCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPITYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYEAVITGFFPFFLIATAIQLFYQGRIWNILLFLLIVQVVALIKSSFASCLRGNIVMVFMSFYSVLYMSSLLPAKMFAIATINKSGWGTSGRKTVVVNFIGLIPISIWFTILFVGIIYTIIQETRKPFPESEKVVLIIGAIVYISYWVVFLTLYAVLIMKCGKRKKGQQYDMVLDV
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1 (EC 2.4.1.15) (UDP-glucose-glucosephosphate glucosyltransferase) (Q4WLM9)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process. The disaccharide trehalose serves as a storage carbohydrate that is mobilized during conidial germination. Regulates the level of trehalose as a protectant for cell integrity during thermal and oxidative stress.
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase subunit Tps2, putative
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen [starch] synthase
- Alpha,alpha-trehalose phosphate synthase subunit TPS3, putative
- Alpha-glucosidase
- glycogenin glucosyltransferase
- 1,3-beta-glucan synthase
- Alpha,alpha-trehalose phosphate synthase subunit, putative
- Trehalase
- alpha,alpha-trehalase
Sequence:
MPSLENSTQNEARLLLVSNRLPITIKRSEDGKYDFSMSSGGLVSGLSGLSKSTTFQWYGWPGLEVPEEEIPVVKQRLKDEYGAIPVFIDDELADRHYNGFSNSILWPLFHYHPGEITFDESAWEAYKEANRLFAKAVAKEVQDGDLIWVHDYHLMLLPEMLREEIGDSKENVKIGFFLHTPFPSSEIYRILPVRNELLLGVLHCDLIGFHTYDYTRHFLSACSRLLGLATTPNGIEFQGKVIACGAFPIGIDPEKFQEGLKKEKVQKRIAQLEQKFQGVKLMVGVDRLDYIKGVPQKLHALEVFLSDHPEWVGKVVLVQVAVPSRQDVEEYQNLRAVVNELVGRINGKFGTVEFMPIHFLHKSVNFDELIALYAVSDACIVSSTRDGMNLVAYEYIASQQKRHGVLVLSEFAGAAQSLNGSIIINPWNTEELAGAYQEAVTMSDEQRALNFSKLDKYVNKYTSAFWGQSFVTELNRISAHSAGKFQSRKAKLPESADAEKPMNGSGESEESQTTQ
Protein: Transcription factor AmrZ (Alginate and motility regulator Z) (G3XCY4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Functions as both a transcriptional activator and repressor of multiple genes encoding virulence factors as well as genes involved in environmental adaptation. Plays a role in alginate production via the activation of AlgD which is the first gene in the alginate biosynthetic operon. Regulates also the transcription of genes responsible for type IV pili localization and twitching motility. Mediates transition of P.aeruginosa biofilm infections from colonizing to chronic biofilms through repression of the psl operon. Represses also its own transcription by binding to two sites on amrZ promoter, amrZ1 and amrZ2.
Interaction partners:
- RNA polymerase sigma-H factor
- Transcriptional regulator FleQ
- Positive alginate biosynthesis regulatory protein
- Alginate biosynthesis transcriptional regulatory protein AlgB
- GDP-mannose 6-dehydrogenase
- Alginate biosynthesis protein AlgZ/FimS
- Sigma factor AlgU negative regulatory protein
- Negative regulator of flagellin synthesis
- Phosphomannomutase/phosphoglucomutase
Sequence:
MRPLKQATPTYSSRTADKFVVRLPEGMREQIAEVARSHHRSMNSEIIARLEQSLLQEGALQDNLGVRLDSPELSLHERELLQRFRQLTHRQQNALVALIAHDAELAQA
Protein: Tumor susceptibility gene 101 protein (ESCRT-I complex subunit TSG101) (Q99816)
Organism: Homo sapiens (Human)
Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan. It may also play a role in the extracellular release of microvesicles that differ from the exosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17853893}. Early endosome membrane {ECO:0000269|PubMed:23166352}; Peripheral membrane protein {ECO:0000305|PubMed:23166352}; Cytoplasmic side {ECO:0000305|PubMed:23166352}. Late endosome membrane {ECO:0000269|PubMed:11916981, ECO:0000269|PubMed:17229889}; Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17853893}. Midbody, Midbody ring {ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}. Nucleus {ECO:0000269|PubMed:17229889}. Note=Mainly cytoplasmic. Membrane-associated when active and soluble when inactive. Nuclear localization is cell cycle-dependent. Interaction with CEP55 is required for localization to the midbody during cytokinesis. {ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}.
Interaction partners:
- Multivesicular body subunit 12A
- Vacuolar protein sorting-associated protein 28 homolog
- Ubiquitin-associated protein 1
- Centrosomal protein of 55 kDa
- Multivesicular body subunit 12B
- Vacuolar protein sorting-associated protein 37B
- Vacuolar protein sorting-associated protein 37C
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Vacuolar protein sorting-associated protein 37A
- Programmed cell death 6-interacting protein
Sequence:
MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFSRPISASYPPYQATGPPNTSYMPGMPGGISPYPSGYPPNPSGYPGCPYPPGGPYPATTSSQYPSQPPVTTVGPSRDGTISEDTIRASLISAVSDKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLSRKQFQLRALMQKARKTAGLSDLY
Protein: B2 bradykinin receptor (B2R) (BK-2 receptor) (Q9GLX8)
Organism: Sus scrofa (Pig)
Function: Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30411}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Adenosine receptor A1
- Endothelin-1 receptor
- Endothelin receptor type B
- Endothelin-1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha
- G protein subunit alpha i3
Sequence:
MLNLTSQVPEPALNGTLPQSSSCFHSDWWNWLNTIQAPFLWVLFLLAALENIFVLSVFCLHKNSCTVAEIYLGNLAMADLILALGLPFWAITIANHFDWLFGEVLCRVVNTMIYMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWGCTLLLSSPMLAFRTMHEYAAEGHNVTACIIKYPSRSWMVFTNILLNSVGFLLPLSIITYCTVQILQVLRNNEMQKFKEIQTERKATVLVLAVLLLFVVCWLPFQISTFLDTLLRLGVLSGCWDEHAVDVITQISSYVAYSNSGLNPLVYVIVGKRFRKKSREVYRVLCQKGGCMGEPVQMENSMGTLRTSISVERQIHKLQDWAGKKQ
Protein: Putative histone deacetylase 2 (EC 3.5.1.98) (Q09440)
Organism: Caenorhabditis elegans
Function: Probably responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). As a likely component of a histone deacetylase complex, together with saeg-1 and hda-2, functions downstream of the cAMP-dependent kinase egl-4 to regulate the expression of genes required for egg-laying and forgaging.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear receptor corepressor 1
- Suppressor of hairless protein homolog
- Histone deacetylase
- Histone deacetylase 1
- C-terminal-binding protein 1
- Paired amphipathic helix protein sin-3
- Suppressor of activated egl-4 protein 2
- histone acetyltransferase
- Probable histone-binding protein rba-1
- CBF1-interacting co-repressor CIR N-terminal domain-containing protein
Sequence:
MSSDKFKLDTLFDDNDEIIEPDGADVKKRNVAYYYHKDVGHFHYGQLHPMKPQRLVVCNDLVVSYEMPKYMTVVESPKLDAADISVFHTEDYVNFLQTVTPKLGLTMPDDVLRQFNIGEDCPIFAGLWDYCTLYAGGSVEGARRLNHKMNDIVINWPGGLHHAKKSEASGFCYVNDIVLGILELLKYHKRVLYIDIDIHHGDGVQEAFNNSDRVMTVSFHRFGQYFPGSGSIMDKGVGPGKYFAINVPLMAAIRDEPYLKLFESVISGVEENFNPEAIVLQCGSDSLCEDRLGQFALSFNAHARAVKYVKSLGKPLMVLGGGGYTLRNVARCWALETGVILGLRMDDEIPGTSLYSHYFTPRLLRPNLVPKMNDANSAAYLASIEKETLACLRMIRGAPSVQMQNIVGIRLDEIEQIEENERLQKSSKSSIEYEVGKVSEKMEEECFVEEDSKPPSFPPGQDPRRIGQYWGYDRSGLAPPRSHSDVIEEAKYEDRDRRKDLNIPGIP