wanglab/gogpt-training-data huggingface dataset:
Protein: Caspase 4 (E9PSM0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Gasdermin D
- NLR family CARD domain-containing protein 4
- Apoptosis-associated speck-like protein containing a CARD
- Absent in melanoma 2
- NACHT, LRR and PYD domains-containing protein 3
- NACHT, LRR and PYD domains-containing protein 6
- NLR family, pyrin domain-containing 1A.
- Caspase-1
- NLR family, apoptosis inhibitory protein 6
- Caspase-12
Sequence:
MLMKCPSNFQFILRSSLQGAKELRLFLMAENNHPDKPLKVLEELGKEFLTEYLEKLVQSNVLKLKEEEKQKFNNAERSDKRWVFVDVLKRKHNQVGKMLLQTFLNVDSGSHHGEANLEMEEPEESVDTLKLCSSEEFTRLCREKKQEIYPIKETNGRTRKALIICNTEFKHLSLRYGANIDISGMKGLLEELGYDVVVKEELTAEGMESEMKDFAALSEHQTSDSTFLVLMSHGTLQGLCGTMHSEATPDVLLYDTIYQIFNNCHCPGLRDKPKVIIVQACRGGNPGEVWIRESSGAHSYRAVDLPRNMEADAVRMSHVEKDFIALYSTTPHHLSYRDKTRGSYFISKLISCFRIHACSCHLFDIFLKVQQSFEKASINSQMPTIDRATLTRYFYLFPGN
Protein: Glucose-6-phosphatase 2 (G-6-Pase 2) (G6Pase 2) (EC 3.1.3.9) (Islet-specific glucose-6-phosphatase catalytic subunit-related protein) (Q9NQR9)
Organism: Homo sapiens (Human)
Function: May hydrolyze glucose-6-phosphate to glucose in the endoplasmic reticulum. May be responsible for glucose production through glycogenolysis and gluconeogenesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15044018}; Multi-pass membrane protein {ECO:0000269|PubMed:15044018}.
Interaction partners:
- Hexokinase-4
- Hexokinase-3
- GDH/6PGL endoplasmic bifunctional protein
- Hexokinase-1
- Hexokinase HKDC1
- Glucose-6-phosphate 1-dehydrogenase
- Hexokinase-2
- Glucose-6-phosphate isomerase
- Glucose-6-phosphatase 3
- Insulin
Sequence:
MDFLHRNGVLIIQHLQKDYRAYYTFLNFMSNVGDPRNIFFIYFPLCFQFNQTVGTKMIWVAVIGDWLNLIFKWILFGHRPYWWVQETQIYPNHSSPCLEQFPTTCETGPGSPSGHAMGASCVWYVMVTAALSHTVCGMDKFSITLHRLTWSFLWSVFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAFEHTPGIQTASLGTYLKTNLFLFLFAVGFYLLLRVLNIDLLWSVPIAKKWCANPDWIHIDTTPFAGLVRNLGVLFGLGFAINSEMFLLSCRGGNNYTLSFRLLCALTSLTILQLYHFLQIPTHEEHLFYVLSFCKSASIPLTVVAFIPYSVHMLMKQSGKKSQ
Protein: Coiled-coil domain-containing protein 137 (Q6PK04)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000269|PubMed:20813266}.
Interaction partners:
- Nucleolar protein 12
Sequence:
MAGAGRGAAVSRVQAGPGSPRRARGRQQVQPLGKQRPAPWPGLRSKEKKKVNCKPKNQDEQEIPFRLREIMRSRQEMKNPISNKKRKKAAQVTFRKTLEKEAKGEEPDIAVPKFKQRKGESDGAYIHRMQQEAQHVLFLSKNQAIRQPEVQAAPKEKSEQKKAKKAFQKRRLDKVRRKKEEKAADRLEQELLRDTVKFGEVVLQPPELTARPQRSVSKDQPGRRSQMLRMLLSPGGVSQPLTASLARQRIVEEERERAVQAYRALKQRQQQLHGERPHLTSRKKPEPQL
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q7KTC6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLTSEANQLSVEKVLVSIALFDLMKLPLTILPMLSVDIAETQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQGLCNYGAAISLFTATLHASSRVFHRLFNNIMHCPSEFFDTTPKGRILDRCSSDVNCLDLVMPLNIRMVMSTAFQVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: RH73277p (SD13345p) (Q9VL68)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dodecenoyl-CoA delta-isomerase
- Enoyl-CoA delta isomerase 1, mitochondrial
- Enoyl-CoA delta isomerase 1, mitochondrial
- acetyl-CoA C-acyltransferase
- HL08109p)
- LP03547p
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase 1, isoform A)
- Hydroxysteroid dehydrogenase-like protein 2
- Sterol carrier protein 2
Sequence:
MMRSKVLSLVARAGSNRMMSTATKLTTVEVNDKTGIATLTMNRPPVNGLNLELLQDLKSSIDEIESNKSRGLILTSSSSTIFSAGLDILEMYKPDKDRIRAFWTQLQDTWLALYGSSVPTAAAINGHSPAGGCLLATSCEYRVMVPNFTIGLNETQLGIVAPQWFMASFLSVLPQRIAERALNQGRMFTTEEALKVGLIDETANNKEEAIEKCVAFIGTFAKVNPLARSLTKQQFRAADLQQLQNGRKEDLEKFLFFVNQPAVQKGLGIYLEGLKKKAKKQ
Protein: Homeobox protein ceh-33 (Q94166)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein phosphatase eya-1
- HABP4_PAI-RBP1 domain-containing protein
- Dachshund homolog dac-1
Sequence:
MQLNSSSFHPHHFTCDTTRYSEEQVACICEALSNDARKLSQFVWTVLERDEMRNNQYILKAQAFLAFHSNNFKELYRIIESHHFASEHHLPLQEWWLNAHYHEAEKIRGRQLGAVGKYRIRRKYPLPRTIWDGEETSYCFRDKSRVLLRDWYCRNSYPSPREKRELAEKTHLTVTQVSNWFKNRRQRDRAGVPEPKDCLKDISEEEDLKLIRKTASKLSNSFHNPSDLSSYSAAAAAATFPGFYMNYNDMMIGAGTSYQSL
Protein: Malate dehydrogenase (EC 1.1.1.37) (P9WK13)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Interaction partners:
- Putative citrate synthase 2
- Citrate synthase 1
- 2-methylcitrate synthase
- Fumarate hydratase class II
- Putative malate oxidoreductase
- Pyruvate carboxylase
- Probable malate:quinone oxidoreductase
- Malate synthase G
- Phosphoenolpyruvate carboxykinase
- Glutamate synthase large chain
Sequence:
MSASPLKVAVTGAAGQIGYSLLFRLASGSLLGPDRPIELRLLEIEPALQALEGVVMELDDCAFPLLSGVEIGSDPQKIFDGVSLALLVGARPRGAGMERSDLLEANGAIFTAQGKALNAVAADDVRVGVTGNPANTNALIAMTNAPDIPRERFSALTRLDHNRAISQLAAKTGAAVTDIKKMTIWGNHSATQYPDLFHAEVAGKNAAEVVNDQAWIEDEFIPTVAKRGAAIIDARGASSAASAASATIDAARDWLLGTPADDWVSMAVVSDGSYGVPEGLISSFPVTTKGGNWTIVSGLEIDEFSRGRIDKSTAELADERSAVTELGLI
Protein: Influenza virus NS1A-binding protein homolog (NS1-BP) (NS1-binding protein homolog) (Kelch family protein Nd1-L) (ND1-L2) (Nd1-S) (Q920Q8)
Organism: Mus musculus (Mouse)
Function: Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (By similarity). In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (By similarity). Inhibits pre-mRNA splicing (in vitro) (By similarity).
Subcellular location: [Isoform 1]: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12213805}. Note=Associated with actin filaments. {ECO:0000269|PubMed:12213805}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:15684717}. Note=Not associated with actin filaments. {ECO:0000269|PubMed:15684717}.
Interaction partners:
- Phosphoribosyl pyrophosphate synthase-associated protein 1
- Krev interaction trapped protein 1
Sequence:
MIPNGYLMFEDENFIESSVAKLNALRKSGQFCDVRLQVCGHEMLAHRAVLACCSPYLFEIFNSDSDPHGVSHVKLDDLNPEAVEVLLNYAYTAQLKADKELVKDVYSAAKKLKMDRVKQVCGDYLLSRMDVTSCISYRNFASCMGDSRLLNKVDAYIQEHLLQISEEEEFLKLPRLKLEVMLEDNVCLPSNGKLYTKVINWVQRSIWENGDSLEELMEEVQTLYYSADHKLLDGNPLDGQAEVFGSDDDHIQFVQKKPPRENGHKQISGSSTGCLSSPNASMQSPKHEWKIVASEKTSNNTYLCLAVLDSTFCVIFLHGRNSPQSSPTSTPKLSKSLSFEMQPDELLEKPMSPMQYARSGLGTAEMNGKLIAAGGYNREECLRTVECYDPHTDHWSFLAPMRTPRARFQMAVLMGQLYVVGGSNGHSDDLSCGEMYDPNIDDWTPVPELRTNRCNAGVCALNGKLYIVGGSDPYGQKGLKNCDVFDPVTKSWTSCAPLNIRRHQSAVCELGGYLYIIGGAESWNCLNTVERYNPENNTWTLIAPMNVARRGAGVAVLDGKLFVGGGFDGSHAISCVEMYDPTRNEWKMMGNMTSPRSNAGITTVGNTIYAVGGFDGNEFLNTVEVYNPQSNEWSPYTKIFQF
Protein: Heat shock protein, mitochondrial, putative (Q386P5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Phosphatase-like protein, putative
- CS domain-containing protein
- CS domain-containing protein
- Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein
- Ankyrin repeat protein
- Serine/threonine-protein phosphatase T
- Serine/threonine-protein phosphatase
- Heat shock protein 70
- Hsp70 protein
Sequence:
MMRRVCQRVNRQALTSTVVARCTATTASVSLRGICPPVSTDGNRNAGIGPMQGSVRFCSTQAGEKVPEAADNADEDIVIDPVPDLKGNAGESADEGSAGGVKANEDSEKVVGSAEEMGFKTETRQLLDIVACSLYTEKEVFIRELVSNASDALEKRHLMELSKPEEYPREEGDEAPIISITCNQSKSRFVIRDTGIGMTREELAENLGTIAGSGSKAFVRELQSQGESSSGAAEKIIGQFGVGFYAAFMVARNVKVYSRSVKKGSKGYVWESDGTGTFKIAECEGVDKGTKIVLDVKDTELSFCTPQVCERVLKRYSNFVSYEITLNGGKVNTVEALWMKDKNSVTNEEHIDFYKFISGAYDSPMFRLHYAVDAPLSIRALLYVPQSHTEKYGGGRMESGVNLYCRRVLIQSKAKGILPEWLRFIKGAVDTESIPLNVSREHTQDGSMMRRLSTVLTKRVIRWMEEEAKQDRQKYERFIKEYGPFLKEGVCTDQVHKMELAKLLRFETTKSDIDYPYVSLDEYRDRMVANQTHIYYINAPSKEMALESPYYEQYKEHDLEVLVCTEPIDDFVMQHLDTYAKHKLQNIELFDASLDGSVQNKLKLEGDKGEVKVEKQLTEAQVKALSDFISKRLVGRVGVVKSTTRLRDSPAVIADHESAQMRKIYRITGQMAGAPPKYNMHFNPKHTIVRKLYTLSISPNSEEVETAGLLVEQMFDNAVIAAGLLEDPRSIVSRLNTIMTRMVENVEEPTADK
Protein: Hyaluronan synthase (EC 2.4.1.212) (Hyaluronate synthase) (Hyaluronic acid synthase) (HA synthase) (P0C0H0)
Organism: Streptococcus pyogenes
Function: Glycosaminoglycan synthesis. The hyaluronic acid capsule is involved in the pathogenicity of group A Streptococci; it may be the major virulence determinant.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- UDP-glucose 6-dehydrogenase
- UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Transcriptional regulatory protein DltR
- Thiol-activated cytolysin
- Signal transduction histidine-protein kinase ArlS
- Streptopain
- Sensor histidine kinase
- Streptokinase
- ADP-ribosyl cyclase / cyclic ADP-ribose hydrolase
Sequence:
MPIFKKTLIVLSFIFLISILIYLNMYLFGTSTVGIYGVILITYLVIKLGLSFLYEPFKGKPHDYKVAAVIPSYNEDAESLLETLKSVLAQTYPLSEIYIVDDGSSNTDAIQLIEEYVNREVDICRNVIVHRSLVNKGKRHAQAWAFERSDADVFLTVDSDTYIYPNALEELLKSFNDETVYAATGHLNARNRQTNLLTRLTDIRYDNAFGVERAAQSLTGNILVCSGPLSIYRREVIIPNLERYKNQTFLGLPVSIGDDRCLTNYAIDLGRTVYQSTARCDTDVPFQLKSYLKQQNRWNKSFFRESIISVKKILSNPIVALWTIFEVVMFMMLIVAIGNLLFNQAIQLDLIKLFAFLSIIFIVALCRNVHYMVKHPASFLLSPLYGILHLFVLQPLKLYSLCTIKNTEWGTRKKVTIFK
Protein: Inactive pancreatic lipase-related protein 1 (PL-RP1) (P54315)
Organism: Homo sapiens (Human)
Function: May function as inhibitor of dietary triglyceride digestion. Lacks detectable lipase activity towards triglycerides, diglycerides, phosphatidylcholine, galactolipids or cholesterol esters (in vitro) (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:1379598, ECO:0000269|PubMed:19824014}.
Interaction partners:
- Colipase
- Gastric triacylglycerol lipase
- Pancreatic triacylglycerol lipase
- Bile salt-activated lipase
- Hepatic triacylglycerol lipase
- Lipoprotein lipase
- Monoglyceride lipase
- 1-acylglycerol-3-phosphate O-acyltransferase PNPLA3
- Patatin-like phospholipase domain-containing protein 2
- Endothelial lipase
Sequence:
MLIFWTITLFLLGAAKGKEVCYEDLGCFSDTEPWGGTAIRPLKILPWSPEKIGTRFLLYTNENPNNFQILLLSDPSTIEASNFQMDRKTRFIIHGFIDKGDESWVTDMCKKLFEVEEVNCICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPPSKVHLIGHSLGAHVAGEAGSKTPGLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQQMGHLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRDFVACNHLRSYKYYLESILNPDGFAAYPCTSYKSFESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNFARWRYGVSITLSGRTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLWNNNVINPTLPKVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC
Protein: RE38148p (Q86P34)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVYGRSIAVGFCLMTVVLLLAAVIFYLSLGPCPAASFACDNGTLCVPRRQMCDSRNDCADSSDENPVECGLLYGSKEIADKIVRNAIEKKQQRLISAVSNASGADSTTSMVPRNQSLTLNMTCDIVTYPKACQCGQGTILYCGRYAKLRRFPRLSSEVTNLIIIRNNLTLRDNIFANFTRLQKLTLKYNNISRVPLGSFSGLFHLEHLELSHNNVSHLPHGVFLGLHSLQWLFLVNNHLHHLPVEQLRFFRRLEWLVLSRNRLTLRNVQLPKIPTLYEVYLDFNRIEYIGEETFSQLDNLHLLDLQHNLITHIHGRAFANLTNMRDIRLVGNPIKELSGETFLHNTRLEALSLALMPIHISSSLMEPLNISFLNLTGIRYDHIDFEAINSMRNLTYIIYDRFFYCSMTPRVRMCKPSTDGVSSFQDLLSKPVLRYSAWVMATLTIAGNVLVLWGRFIYRDENVAVTMVIRNLALADMLMGFYLVTIGVQDYRYRNEYYKVVLDWITSWQCTLIGTLAVSSSEVSILILAFMSLERFLLIADPFRGHRSIGNRVMWLALICIWITGVGLAVAPVLLWRTSTLPYYGSYSGTCFPLHIHEAFPMGWLYSAFVFLGVNLLLLVMIAMLYTALLISIWRTRSATPLTLLDCEFAVRFFFIVLTDFLCWVPIIVMKIWVFFNYNISDDIYAWLVVFVLPLNSAVNPLLYTFTTPKYRNQIFLRGWKKITSRKRAEAGNGNVATTTTGTATGSSQHPDDFTIFAKAAMRCH
Protein: AP-1 complex subunit mu-2 (AP-mu chain family member mu1B) (Adaptor protein complex AP-1 subunit mu-2) (Adaptor-related protein complex 1 subunit mu-2) (Clathrin assembly protein complex 1 mu-2 medium chain 2) (Golgi adaptor HA1/AP1 adaptin mu-2 subunit) (Mu-adaptin 2) (Mu1B-adaptin) (Q9Y6Q5)
Organism: Homo sapiens (Human)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Interaction partners:
- AP-1 complex subunit sigma-2
- AP-1 complex subunit sigma-1A
- AP-1 complex subunit gamma-1
- AP-1 complex subunit gamma-like 2
- AP-1 complex subunit beta-1
- AP-1 complex subunit sigma-3
- AP-2 complex subunit beta
- AP-1 complex subunit mu-1
- Aftiphilin
- AP-4 complex subunit beta-1
Sequence:
MSASAVFILDVKGKPLISRNYKGDVAMSKIEHFMPLLVQREEEGALAPLLSHGQVHFLWIKHSNLYLVATTSKNANASLVYSFLYKTIEVFCEYFKELEEESIRDNFVIVYELLDELMDFGFPQTTDSKILQEYITQQSNKLETGKSRVPPTVTNAVSWRSEGIKYKKNEVFIDVIESVNLLVNANGSVLLSEIVGTIKLKVFLSGMPELRLGLNDRVLFELTGRSKNKSVELEDVKFHQCVRLSRFDNDRTISFIPPDGDFELMSYRLSTQVKPLIWIESVIEKFSHSRVEIMVKAKGQFKKQSVANGVEISVPVPSDADSPRFKTSVGSAKYVPERNVVIWSIKSFPGGKEYLMRAHFGLPSVEKEEVEGRPPIGVKFEIPYFTVSGIQVRYMKIIEKSGYQALPWVRYITQSGDYQLRTS
Protein: Succinylornithine transaminase/acetylornithine aminotransferase (ACOAT) (SOAT) (Succinylornithine aminotransferase) (EC 2.6.1.11) (EC 2.6.1.81) (O30508)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Transaminates both N(2)-acetylornithine and N(2)-succinylornithine.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- N-succinylglutamate 5-semialdehyde dehydrogenase
- N-succinylarginine dihydrolase
- Arginine N-succinyltransferase subunit beta
- Arginine N-succinyltransferase subunit alpha
- Succinylglutamate desuccinylase
- Arginine biosynthesis bifunctional protein ArgJ
- N-acetyl-gamma-glutamyl-phosphate reductase
- Amino-acid acetyltransferase
- Acetylglutamate kinase
- Argininosuccinate synthase
Sequence:
MSAPHAQVERADFDRYMVPNYAPAAFIPVRGEGSRVWDQSGRELIDFAGGIAVTSLGHAHPALVKALTEQAQRIWHVSNVFTNEPALRLARKLVDATFAERVFLANSGAEANEAAFKLARRYANDVYGPQKYEIIAASNSFHGRTLFTVNVGGQPKYSDGFGPKFEGITHVPYNDLEALKAAISDKTCAVVLEPIQGEGGVLPAQQAYLEGARKLCDEHNALLVFDEVQSGMGRVGELFAYMHYGVVPDILSSAKSLGGGFPIGAMLTTGEIAKHLSVGTHGTTYGGNPLASAVAEAALDVINTPEVLDGVKAKHERFKSRLQKIGQEYGIFDEIRGMGLLIGAALTDEWKGKARDVLNAAEKEAVMVLQASPDVVRFAPSLVIDDAEIDEGLERFERAVAKLVRG
Protein: Grunge, isoform F (M9NDL9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASTQGEIRVGPGHQVNDVYAKLPDYNPISSFPIDKETDERELEESRWSPGVVADGDLLMFLRAARSMAAFQGMCDGGLEDGCLAASRDDTTINALDVLHDSGYDPGKALQALVKCPVSKGIDKKWTEDETKKFIKGLRQFGKNFFRIHKDLLPHKDTPELVEFYYLWKKTPGANNNRPHRRRRQSALRRNRVTRANNSNSNTPPKKEDTPEPQTATTATAAATAASETASRSSPAVSKEENSSLTEDDASECDSDSSLTHKRDESPSRMRTRNKQQNNNSSTSSGNNTAGNGGGNATSISSGSTGGGAAGGNSSSKDQSANAVANGKRPKRGSETPDVSGGASVDSPKTPTKAVAESSANKRKGGKQDTPNKKKRTEQESNEPSAHEENAIKEKRKRPDSPVESMNSDSRPDSVLDDGESNTTDTTTAEQQSTKDSKETVSCKEEREMVTNDLEAKAEEKAIKAEALAEDSKDSAIKNMDEETNIQAPSSADTSLVDGPNPNALPSPVAAPITMKVPTIATVEALNASVDRKEAIEKMESCDSDPEMLKKLATIKQEVSPQQQQHMQQQSQQQMQQQLAPVGIPQPPSCPPSESVYIKKEPMEDSMDATCNQNSNEPQDLKVKIEIKNEDALKHSAGGLPPSGPCAPPSALHPLSGAPVESGQEPLHLQHMPHGQVTTQPPPGYLIDGQLKYGPSGQGVPPQPPQLHSDAAGGVSGAPPGAPTTPQKYPPEMEMKFAPQDLKYPPPPPLDALKYSQEMQAAAAAAAAAGKYDMKYMMEQQGKYNVELSAAHQPPSKPGYQDSLKIPDIKPGFGHLPHNVGSPLDAAHKYGPPPTSQESQQQQPQPPAHQVPPGATPPPGIAMPKPHYQHDVQTPPLGRPFEPTGLMLKYGDPLAAKYGPPQDLKYPMPPVSQAGPADVKPYGGENLIKSSPYGPPPESPIDASARSTPGQDSQGSNSNSQPPSMPPQPQQFQSPHPSPHMPSPAGGGLPPGMHPQNLIHGPPPGAAGGSGPQPPPPPTSLHQPTPTSAGPPSLQHGLHPGHQHSQLSVASSIPPSSIGIPPTLSTMAPSHMHPHLHPHAHLQGLHRPHDLPPSMHPHAPMPLSLQGHPQHGHGLPPSHTSQQQQQQQQQQQPGGPAGTVRTPSPAQQPPRSMHDPQSSREPPTSQPSTTMAGSSGPGGPPPQQSPHAHRTSPLPGLAGSGPPPPGLIGHPMAIHPHLAHLPPGHPAHAALAHPGHHLLSHSIAGLGPGGGPIALLAGPGGLGGIPESALSRRTPPSHLPHSHASSAPLTAHSVASMTSTSMSLTTSTVPSSAFSRASPSVQISSSGGGPSGPGSVGPGGMPNSSAAAAAAAAAHRAASPASSVSSLSRQSPLHPVPQSPLSHHPSSSALSAAAAAVAERDRHALMRQQSPHMTPPPVSNASLMASPLSKMYAPQPGQRGLGTSPPPHLRPGASPPVIRHPQMPLPLPLIAPGGGIPQIGVHPGQSPYPHPLLHPSVFYSPHHHPFNSPYGYAPYGPGFPAYMKPPPQPGQLDPAAVMAAHHAGLQGPPPQQMRQDEQNAAAAAAQAAAEKQHQAAAAAAAQQHKAPQQQQPGGMPPNKPPTPKTPQGPGGGMPPGMGGPGTPTGLPPGAYPGSHMPGYPQGPPHGSPFAPQDGQPHGLKPTSHMDALRAHAHSANSAGMGGGHHPTEPLPIDIEPDPEPEIPSPTHNIPRGPSPEAKPDDTECHRSQSAIFVRHIDRGDYNSCTRTDLIFKPVADSKLARKREERDRKLAEKERERRQQQQQQQQQQQQQQAAAAQQAAQQAKMKAELKPPYADTPALRQLSEYARPHVAFRELEEIKNAQAAAASQSRLDPHWMEYYRRGIHPSQFPLYANPAISQMERERLGIPPPHHVGLDPGEHMIRLTREYHAHSHTHLHLPLHPQPQPPEAGFQLPPNVGQYPRPNMLIPREPHSDVLLRMSYADQLQYLQAAEFQRQSLHDQYFRQRPR
Protein: Odorant receptor coreceptor (A0A026W182)
Organism: Ooceraea biroi (Clonal raider ant) (Cerapachys biroi)
Function: Odorant coreceptor which complexes with conventional odorant receptors (ORs) to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). Obligate coreceptor of all odorant receptors (By similarity). Orco is a universal and integral part of the functional odorant receptor, involved in the dendritic localization of other olfactory receptors. Can form functional ion channels in the absence of an odor-binding odorant receptor (By similarity). Plays a central role in the perception of olfactory stimuli in ants and is essential for ant social organization. Required for pheromone sensing. Also required for the development and maintenance of odorant receptor neurons (ORNs) and of antennal lobe glomeruli.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MMKMKQQGLVADLLPNIRVMKTFGHFVFNYYNDNSSKYLHKVYCCVNLFMLLLQFGLCAVNLIVESADVDDLTANTITLLFFTHSIVKICYFAIRSKYFYRTWAIWNNPNSHPLFAESNARYHAIALKKMRLLLFLVGGTTMLAAVAWTVLTFFEHPIRKIVDPVTNETEIIELPQLLIRSFYPFDAGKGITHVLVLVYQFYWVLFMLIDANSLDVLFCSWLLFACEQLQHLKQIMKPLMELSATLDTVVPNSSELFKAGSADHLRDGDNPPPPPPPQSDNMLDLDLRNIYSNRQDFTATFRPTAGMTFNGGVGPNGLTKKQEALVRSAIKYWVERHKHIVRLVTAVGDAYGFALLLHMLTTTITLTLLAYQATKVNGINVYAASTIGYILYTFGQVFLFCIFGNRLIEESTSVMEAAYSCHWYDGSEEAKTFVQIVCQQCQKAMSISGAKFFTVSLDLFASVLGAVVTYFMVLVQLK
Protein: Sodium-dependent dopamine transporter (DA transporter) (DAT) (Solute carrier family 6 member 3) (Q61327)
Organism: Mus musculus (Mouse)
Function: Mediates sodium- and chloride-dependent transport of dopamine. Also mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (By similarity). Regulator of light-dependent retinal hyaloid vessel regression, downstream of OPN5 signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12606774}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01959}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P23977}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Note=Localizes to neurite tips in neuronal cells (By similarity). Colocalizes with SEPTIN4 at axon terminals, especially at the varicosities (PubMed:17296554). {ECO:0000250|UniProtKB:P23977, ECO:0000269|PubMed:17296554}.
Interaction partners:
- D
- Syntaxin-1A
- Alpha-synuclein
- Synaptic vesicular amine transporter
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Protein kinase C alpha type
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
- Protein kinase C beta type
- Protein kinase C gamma type
- Tyrosine 3-monooxygenase
Sequence:
MSKSKCSVGPMSSVVAPAKEPNAVGPREVELILVKEQNGVQLTNSTLINPPQTPVEVQERETWSKKIDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYLLFMVIAGMPLFYMELALGQFNREGAAGVWKICPVLKGVGFTVILISFYVGFFYNVIIAWALHYFFSSFTMDLPWIHCNNTWNSPNCSDAHSSNSSDGLGLNDTFGTTPAAEYFERGVLHLHQSRGIDDLGPPRWQLTACLVLVIVLLYFSLWKGVKTSGKVVWITATMPYVVLTALLLRGVTLPGAMDGIRAYLSVDFYRLCEASVWIDAATQVCFSLGVGFGVLIAFSSYNKFTNNCYRDAIITTSINSLTSFSSGFVVFSFLGYMAQKHNVPIRDVATDGPGLIFIIYPEAIATLPLSSAWAAVFFLMLLTLGIDSAMGGMESVITGLVDEFQLLHRHRELFTLGIVLATFLLSLFCVTNGGIYVFTLLDHFAAGTSILFGVLIEAIGVAWFYGVQQFSDDIKQMTGQRPNLYWRLCWKLVSPCFLLYVVVVSIVTFRPPHYGAYIFPDWANALGWIIATSSMAMVPIYATYKFCSLPGSFREKLAYAITPEKDRQLVDRGEVRQFTLRHWLLV
Protein: Condensin complex subunit 2 (Barren homolog protein 1) (Chromosome-associated protein H) (mCAP-H) (Non-SMC condensin I complex subunit H) (XCAP-H homolog) (Q8C156)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. Early in neurogenesis, may play an essential role to ensure accurate mitotic chromosome condensation in neuron stem cells, ultimately affecting neuron pool and cortex size.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}.
Interaction partners:
- Structural maintenance of chromosomes protein 4
- Non-SMC condensin I complex, subunit G
- Condensin complex subunit 1
- Structural maintenance of chromosomes protein 2
- Condensin-2 complex subunit D3
- Condensin-2 complex subunit G2
- Condensin-2 complex subunit H2
- Aurora kinase B
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Chromosome-associated kinesin KIF4
Sequence:
MRIPRSETMNSSFLKARGQQDVLSSPLERVPPASRPGKAPLGTPKTPVLEDFPQNDDEKERMQRRRSRVFDLQFSTDSIHLASPNRNIDVSTTISKFTNTQITEHYSTCIKLSSENKITTKNAFGLHLIDFMSEILKQKDAEPTNFKVAAGTLDASTKIYAVRVDAVHADVYRVLGGLGKDTPPQGEESHSGDGSTLETERTKKPAKPKKKQSCKTIEQNLSNINVSEADGKCAVDPMFQKTAASFDECSTTGVFLSTLHCQDYRSELLFPSDMQTLSSGEPLELPDLGFVDMTDLEASLQQCVEDRPLCPSLAGFQFTKWDSETHNESVSALVDKFKKNDQVFDINAEAEDDEEDVPDGPLVEDFVDNDEPDLSAAGDHEEFRSWKELCQVQSNQEEVISLEDRDIQVMCSFLSMKPGEYSYFSPRTMKMWAGPDHWRFRPRPKQDATSCTEHKKKSAKKDFEINFDDDIDFDAYFQKTKAATILTKSTLENQNWKATTLPTDFHYETDNLIQLHLKPGKRSLKMDQDQKAKTEHYEEIEDYDYNNPNDTSNYCPGLQAADSDYEEADDLFADPVGTLDLESDPKTTQENGHISPENQGVDITTYQELNLVAEPQKVNKIEIHYAKTAKKMDMKKLKQSMWSLLTKFSRKEADTEANHTESGQEGAPEEVADEKKLSGLTKDLQTRLPPLMAQNLSIPLAFACLLHLANEKNLKLEGTEDLSDVLVMQGD