wanglab/gogpt-training-data huggingface dataset:
Protein: B cell-specific coactivator of octamer binding factors (POU domain class 2-associating factor 1) (A1YKC3)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
- B-cell antigen receptor complex-associated protein alpha chain
Sequence:
MHMGKSLSEQAASKPYQGVRVKDPVKELLRRKRGNTAKTLPPTAVVIPNNTLPSYTHVGPSGFPGSSQSALNESAVDVGALCPGWVAQPSSTATFQPLGHWAPPEYFQHEQSISTLPSLTSDMYVQPVCPSYAVVGPSSVLTLAHAPLFTNLGTISSSTSGLPQIDVQDGSLAYIPWAPPLSPCPQNVAPQLLPMPVPVSHPEPQQEEPAPSSEGTLALEKLLEEEEEDQKEPYACSPSLFTQDI
Protein: SET domain-containing protein (Q57XB8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- SET domain-containing protein
Sequence:
MATVTEAPLKSPQDRLVERVCSSEEDDSGRYVIAKDDISPGEIVLLAAPYAVALNPNEAVSAMYVAANVEEWEDASMGELAGRRVGQRVKKSGNIPTDGGEYVALSPCVTFCSCCLRRIPTGTPFLNCETIEVLSHLIAVEHVESENAKWEKERESHQRTGSDAGDAADLGDRMHIKKEKKLQKPARSAKMRSKGYLSLKQRLLEAATAQRESAMYEAQKFGGALGDSSRNISWPERVVEKHVLEEDLLVRGACGCAGCGVAIYCSKSCWQSFNELHRATGACRVLRDVYSPLMRIFLSRITKGNKGGSAEIFCIDSWSPKHWLRRTTDEKAWEMLQLLLAALLVGRCAKEGYANNMREEEKERQHPAENVDDYYSEEEDRVWGTMGDEESASPRDCDHLQVSNTPTTGTKIEEDGGRDVSITVNSAIPREAEVIRLVRSRMGTAVEVLDSRVNECGKCPPSVGRIPMSLCVSIKDHIVLGIRADGSETHAIQCPQWPEAAALVTNLSVLRKESRSVFRRYYRRFCLSVLPWLNCSEGTDEPLSVSSSFFDRLCGAVQCNNFGLFDPKEDCIGVSVIPEASYFNHSCLPNLCRVMCDGGIAAFYALREIRKGEPLTICYVDVQEVSTAERRRTLLTSYRFFCQCKRCNGSSVVDDKTDADAAKLRLCGACAARGYLRPLPPTDAAILCRWTMDSIATGECTVCHNRAPWGGTS
Protein: E3 ubiquitin-protein ligase MIB1 (EC 2.3.2.27) (DAPK-interacting protein 1) (DIP-1) (Mind bomb homolog 1) (RING-type E3 ubiquitin transferase MIB1) (Q80SY4)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation (By similarity). Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Cytoplasm. Cell membrane. Note=Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock (By similarity). Localizes to the plasma membrane. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase NEURL1B
- Protein jagged-1
- Death-associated protein kinase 1
- Delta-like protein 1
- E3 ubiquitin-protein ligase NEURL1
- Delta-like protein 4
Sequence:
MSNSRNNRVMVEGVGARVVRGPDWKWGKQDGGEGHVGTVRSFESPEEVVVVWDNGTAANYRCSGAYDLRILDSAPTGIKHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRITTPGSERVLLESRRKSKKITARGIFAGARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCVQDAKGGSFYRDHCPVLGEQNGNRNPGGLQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPSGNRWTFNPAVLTKANIVRSGDAAQGAEGGTSQFQVGDLVQVCYDLERIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEVCGTSWTYNPAAVSKVAPAGSAISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRPDVDVNGQCAGHTAMQAASQNGHVDILKLLLKQNVDVEAEDKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQDMQDVGKVDAAWEPSKNTLIMGLGTQGAEKKSAASIACFLAANGADLSIRNKKGQSPLDLCPDPSLCKALAKCHKEKVSGQVGSRSPSMISNDSETLEECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTKIEECVVCSDKKAAVLFQPCGHMCACENCASLMKKCVQCRAVVERRVPFITCCGGKSSEDPSDEISSGNIPVLQKDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY
Protein: Complement C1q subcomponent subunit A (P31720)
Organism: Rattus norvegicus (Rat)
Function: C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.
Subcellular location: Secreted.
Interaction partners:
- Complement C1q subcomponent subunit B
- Complement C1q subcomponent subunit C
- Complement C1s subcomponent
- Complement C1r subcomponent
- Complement C4
- Plasma protease C1 inhibitor
- Complement C2
- V-set and immunoglobulin domain containing 4
- Complement C4A
- Calreticulin
Sequence:
METSQGWLVACVLAVTLVWTVAEDVCRAPNGKDGVAGIPGRPGRPGLKGERGEPGAAGIRTGIRGLKGDMGESGPPGKPGNVGFPGPTGPLGNSGPQGLKGVKGNPGNIRDQPRPAFSAIRQNPPTYGNVVVFDKVLTNQENPYQNRTGHFICAVPGFYYFTFQVISKWDLCLSIVSSSRGQPRNSLGFCDTNSKGLFQVLAGGTVLQLQRGDEVWIEKDPAKGRIYQGTEADSIFSGFLIFPSA
Protein: Flavohemoprotein (EC 1.14.12.17) (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (Q9URY5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Peroxisomal membrane protein pex32
- Glutathione reductase
Sequence:
MSSVEVNRENADVANTNRQANLAEGYEIKELNESQKQYIRSSIPILESSGVNLTKAFYQKMLGNYPEVLPYFNKAHQISLSQPRILAFALLNYAKNIDDLTSLSAFMDQIVVKHVGLQIKAEHYPIVGHCLLSTMQELLPSDVATPAFLEAWTTAYGNLAKILIDSEKKVYQSQPWNGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYKRSEENVNRPLLCFAGGIGITPLIPIIETALLDGRKVNFCYSSRNYVSRPFKQWLEQLKLKYKENLKLKEFFSEESSVTKEQIVDEVMTRIINEEDLEKLDLSECDIYMLGPNNYMRFVKQELVKLGVEPNKVQSEFFGPYIP
Protein: L-saccharopine oxidase (EC 1.5.3.18) (Q9UTM9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Secreted {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Sphingolipid delta
Sequence:
MSRTIVIVGCGVFGLSTAVELAKNHSFDNIIAIDAEPVPSSMSAANDINKIVRPEYADLKYMKLALEAMEKWRNDPELSSVYFECGRLSTISKDPYRARFDEVAQRNLRKLLGDSALINLSSSEEIRKKYPSLFSNSPLRSDMQAVVNEHAGYANSAASLKLLELKARELGVEFVFGKAGKFKKFVVNHSETDIDKNDNHVSVQTEDGTIYHADTILLAVGAYLNAYLNTSHRVCAKGLPVAHIQLTDEEFKTYKNMPIIFDPDCAYAFPPYPVTKLIKLASTGYEYVCNVETDYDENSKVVSIPHSGPSKSSLPKYAIIQMRRFLDTFLPDLADRSLINTKMCWISDTEDANFLIDKVPQFDNVFVANGDSGHAFKFLPNIGRYIAQRILGDLSEEWKDAWRWREDDKASELKWRCVRSLIDYKDAEFTYDK
Protein: Glutamate receptor-interacting protein 1 (GRIP-1) (AMPA receptor-interacting protein GRIP1) (P97879)
Organism: Rattus norvegicus (Rat)
Function: May play a role as a localized scaffold for the assembly of a multiprotein signaling complex and as mediator of the trafficking of its binding partners at specific subcellular location in neurons. Through complex formation with NSG1, GRIA2 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:10436050}. Perikaryon {ECO:0000269|PubMed:10436050}. Cell projection, dendrite {ECO:0000269|PubMed:10436050}. Cytoplasm {ECO:0000269|PubMed:10436050}. Endomembrane system; Peripheral membrane protein. Postsynaptic cell membrane {ECO:0000269|PubMed:10436050}. Postsynaptic density {ECO:0000269|PubMed:10436050, ECO:0000269|PubMed:15226318}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:10436050}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated with vesicles, peri-Golgi complexes and endoplasmic reticulum. Enriched in postsynaptic plasma membrane and postsynaptic densities. {ECO:0000269|PubMed:10436050}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 3
- PRKCA-binding protein
- Glutamate receptor 1
- GRIP1-associated protein 1
- Glutamate receptor 4
- Ephrin B2
- Chondroitin sulfate proteoglycan 4
- Disks large homolog 4
- FRAS1-related extracellular matrix protein 2
Sequence:
MIAVSFKCRCQILRRLTKDESPYTKSASQTKPPDGALAVRRQSIPEEFKGSTVVELMKKEGTTLGLTVSGGIDKDGKPRVSNLRQGGIAARSDQLDVGDYIKAVNGINLAKFRHDEIISLLKNVGERVVLEVEYELPPVSIQGSSVMFRTVEVTLHKEGNTFGFVIRGGAHDDRNKSRPVVITCVRPGGPADREGTIKPGDRLLSVDGIRLLGTTHAEAMSILKQCGQEATLLIEYDVSVMDSVATASGPLLVEVAKTPGASLGVALTTSVCCNKQVIVIDKIKSASIADRCGALHVGDHILSIDGTSMEYCTLAEATQFLANTTDQVKLEILPHHQTRLALKGPDHVKIQRSDRQLPWDPWASSQCSVHTNHHHNPHHPDHCRVPALGFPKALTPNSPPAMVSSSSPTSMSAYSLSSLNMGTLPRSLYSTSPRGTMMRRRLKKKDFKSSLSLASSTVGLAGQVVHTETTEVVLTADPVTGFGIQLQGSVFATETLSSPPLISYIEADSPAERCGVLQIGDRVMAINGIPTEDSTFEEANQLLRDSSITSKVTLEIEFDVAESVIPSSGTFHVKLPKKHSVELGITISSPSSRKPGDPLVISDIKKGSVAHRTGTLELGDKLLAIDNIRLDSCSMEDAVQILQQCEDLVKLKIRKDEDNSDEQESSGAIIYTVELKRYGGPLGITISGTEEPFDPIIISSLTKGGLAERTGAIHIGDRILAINSSSLKGKPLSEAIHLLQMAGETVTLKIKKQTDAQPASSPKKLPIPSHSSDLGDGEEDPSPIQRPGKLSDVYPSTVPSVDSAVDSWDGSGIDARYGSQGTTFQTSGYNFNTYDWRSPKKRASLSPVPKPRSQTYPDVGLSNEDWDRSTASGFAGASDSADAEQEENFWSQALEDLETCGQSGILRELEATIMSGSTMSLNHEAPTARSQLGRQASFQERSNSRPHYSQTTRSNTLPSDVGRKSVTLRKMKQEIKEIMSPTPVELHKVTLYKDSGMEDFGFSVADGLLEKGVYVKNIRPAGPGDLGGLKPYDRLLQVNHVRTRDFDCCLVVPLIAESGNKLDLVISRNPLASQKSIEQPALPSDWSEQNSAFFQQPSHGGNLETREPTNTL
Protein: Prokaryotic ubiquitin-like protein Pup (Bacterial ubiquitin-like modifier) (P9WHN5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Among the identified substrates are the FabD, PanB and Mpa proteins.
Interaction partners:
- Proteasome subunit beta
- Proteasome subunit alpha
- Proteasome-associated ATPase
- Pup deamidase/depupylase
- Pup--protein ligase
Sequence:
MAQEQTKRGGGGGDDDDIAGSTAAGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ
Protein: Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (EC 2.7.1.93) (80 kDa diacylglycerol kinase) (Diglyceride kinase alpha) (DGK-alpha) (P51556)
Organism: Rattus norvegicus (Rat)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group (By similarity). Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22627129}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- RAS guanyl-releasing protein 1
- Phospholipase D2
- Phosphoinositide phospholipase C
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Phospholipase D1
- Diacylglycerol O-acyltransferase 1
Sequence:
MAKDKGLISPEDFAQLQKYIDYSTKSVSDVLKVFEMNKYCQGDEIGYLGFEQFLKMYLEVEEVPHHLCWTLFWSFHSSQDLDEETESKANVICLSDVYCYFTLLEGGSPEDKLEFTFKLYDMDRNGILDSTEVEKIILQMMRVAEYLDWDVSELRPILQEMMKEMDRDGSGCVSLAEWVRAGATTVPLLVLLGIDMTMKDDGHHIWRPKRFSRPVYCNLCELSIGLGKQGLSCNLCKYIVHDHCAMKAQPCEVSTYAKSRKDIGVQPHVWVRGGCHSGRCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGPECDCGLLRDHILPPCSIYPRVLVSGQECKQKTTDVTSLCTPEAFRIEPVSNTHPLLVFINPKSGGKQGQSVLWKFQYILNPRQVFNLKDGPEPGLRFFKDVPQFRVLVCGGDGTVGWILETIDKANFPIVPPVAVLPLGTGNDLARCLRWGRGYEGENLRKILKDIEISKVVYLDRWLLEVIPQQNGEKSDPVPSQIINNYFSIGVDASIAHRFHLMREKYPEKFNSRMKNKLWYLEFATSESIFSTCKKLEESVTVEICGKLLDLSDLSLEGIAVLNIPSMHGGSNLWGDTKRPHGDTCGINQALGSVAKIITDPDILKTCVPDMSDKRLEVVGIEGVIEMGQIYTRLKSAGHRLAKCSEITFQTTKTLPMQVDGEPWMQAPCTIKITHKNQMPMLMGPAPSSSNFFGFWS
Protein: Plant/protein (DUF789) (Q8LF98)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVNVKGSTKKSNLDRFLHCITPLVPPQSLPKTEIRTLNRLWHPWERQKVEFFRLSDLWDCYDEWSAYGASVPIHVTNGESLVQYYVPYLSAIQIFTSHSSLIRLREESEDGECEGRDPFSDSGSDESVSEEGLENNTLLHPSDRLGYLYLQYFERSAPYTRVPLMDKINELAQRYPGLMSLRSVDLSPASWMSVAWYPIYHIPMGRTIKDLSTCFLTYHTLSSSFQDMEPEENGGDKERVRREGEDITLLPFGMATYKMQGDVWLSQDHDDQERLASLYSVADSWLKQLRVQHHDFNYFCNMSMTHRG
Protein: Mitoguardin 1 (A0A2R8YDC7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MSEETVSESQFSLKTAALRVFDLPLTWYYSLSQIKFSPVAKKLFVVTAVSAISVIFLAHHFKRKRGKKKGKILPWEPEHLILEYTKRAASDKGSSCSSSRQNLTLSLSSTKDKGSQVCNYANGGLFSKYSGSAQSLASVQSVNSCHSCACGNSNSWDKADEDDIKLVNIPVTTPENLYLMGMELFEEALRRWEQALTFRNRQAEDEACGSIKLGAGDAIAEENVDDIISTEFIHKLEALLQRAYRLQEEFEATLGASDPNSLADDIDKDTDITMKGNVEDFGLRDTLSIASTDSFASAAELAEHREVRHTYSLESLCHCPFYEEAMHLVEEGKIYSRVLRTEMLECLGDSDFLAKLHCIRQAFQVILSESANRIFLAESGRKILSALIVKARKNPKKFEDVFDEMIYFLEQTDHWGSTEMELAARGVKNLNFYDVVLDFILMDSFEDLENPPTSIQNVVNNRWLNSSFKETAVASSCWSVLKQKRQQMKTESHSVAQAGVQWHDLSSLQPLPPRFKRFFCLSLSSSWDYRRLPPCPANLYIFGKDGVSSCWPG
Protein: Serine/threonine-protein kinase ppk30 (EC 2.7.11.1) (O43066)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inner kinetochore subunit fta6
- Serine/threonine-protein kinase ppk15
- Inner kinetochore subunit fta1
- Inner kinetochore subunit cnl2
Sequence:
MTEVYSKAPATVGQVKLSNNGTSNKAYSVPKSPAPVRTDLFSKIPAGTKIQVGSHSVIIQRYLSEGGFSHVYLALLENEKPFVLKRIYVPDKTALQLVHGEIETMKRLKGHRHIVNYIDSSALYSKSENRYEVYLLMEFCAGGGLIDFMNTRLQHRLTEGEILKILADVCDAVAAMHYLDPPLIHRDLKIENVLLVAPNSYKLCDFGSACEPLAPATTPDTIMFLEQNIAAYTTPQYRAPEMIDINRRQGIDEKSDIWAIGVLAYKLCYYTTPFEQVGNSAILKASFSFPPFPRYSDRMKRFIATCLQEQPSHRPNIYQTLKEIMEMQGTPLKLPDVYGGVNASTYNPPRAPLQRTPSGSLTPLSSRPAHTSLPPIPTVQTTSSNVPPVNRPSLKSKSPSVSNILSNQLSPISSANNDVMARLQPKSPIPATKSYSATIQTPRSPSLRRADSTSHIIKVPHLPDTSVKTAKTGASEIDVLSRYPSVEEIDKITDKIEVSKPLRNSGPLAFKPFEKISANKQTDLLQNKPEALLDLENRFLPKPSPKPSEFSSSVGSKQNLSMDIPSVQNVSTKQKSTNDTDNSKLKINKPLTGGYAPLPSRPNRMNHSVLNEKSNKEFVRGPRVLPPIEVSSSKMAGLDIRKEPFTPAVPSAKSGLKKDQSSEVANKDVVSKNKDNIAILADREARPQLLLDDNNDSSSSSSEHLISFNNHTGNKILSRQTTSSSIDSNNVQSNIEFLKGLNATHARSTSQVSHTQRLQQSISTSLERVKSNTKKESNSPRQVSKLKRPIGASNKILSGKFGEAFKKFEFGGEKMSRRRKSETKKNLVSILPDTEVDEYPKASNEWIVESEELPQVHETINQYRKSCETQRSRKSHEGSNDLERQPSSPDTVHPGIKRSHFIRERVKQLLSDANKHHQSPSDSETDRTPDSSSIHLPHIERLNLFHTKSESLE
Protein: Cleft palate-related protein 1 (cDNA sequence AY074887) (Q8R5F9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKHPRRIWLPRVRRTARGRGGAGGRGSSPSAGAGSVCPRGLCRSTTSALAAVCIRGGLEGGGKRLYRGEWNQIPPTLCTPLSFSLLYHSNGGQSSNCIDKSNRLLFQSCPLTVFPLFFLLASFSPFSDPTL
Protein: NADH-quinone oxidoreductase subunit N (EC 7.1.1.-) (NADH dehydrogenase I subunit N) (NDH-1 subunit N) (Q9I0I9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00445}.
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit C/D
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit I
Sequence:
MTFTIQHFIALLPLLITSATLVVVMLAVAWKRNHSFTATLSVIGLNLALLSLLPVLGVTPIEVTPLVLVDNYACFYMALVLVSALACVTLAHAYMESYPGNREELYLLLLLATAGGLVLVSAQHLASLFIGLELLSVPVYGMVAYAFFNKRSLEAGIKYTVLSAAGSAFLLFGMALLYAESGTLGFAGLGAKVAEHVLSGPLVSVGVGMMLVGLGFKLSLVPFHLWTPDVYEGAPAPVSAFLATASKVAVFAVLLRLFQIAPAALDNQLLNISLSVIAVASILFGNLLALTQSNIKRLLGYSSIAHLGYLLVALIASKGMAVEAVGVYLATYVLTSLGAFGVITLMSTPYSGRDADALFEYRGLFWRRPVLTAVMTVMMLSLAGIPLTAGFIGKFYVIAVGVESHLWWLIGALVLGSAIGLYYYLRVMVTLFLVEPGIRQHDAPFNWGQRAGGIMLVAIALLAFFLGVYPQPLLEILQHSGLALAG
Protein: Irregular chiasm C-roughest protein (Protein IRREC) (Q08180)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for correct axonal pathway formation in the optic lobe and for programmed cell death in the developing retina.
Subcellular location: Membrane {ECO:0000269|PubMed:7503814}; Single-pass type I membrane protein {ECO:0000269|PubMed:7503814}.
Interaction partners:
- Sticks and stones, isoform B
- Hibris, isoform B
- CIN85 and CD2AP related, isoform J
Sequence:
MLHTMQLLLLATIVGMVRSSPYTSYQNQRFAMEPQDQTAVVGARVTLPCRVINKQGTLQWTKDDFGLGTSRDLSGFERYAMVGSDEEGDYSLDIYPVMLDDDARYQCQVSPGPEGQPAIRSTFAGLTVLVPPEAPKITQGDVIYATEDRKVEIECVSVGGKPAAEITWIDGLGNVLTDNIEYTVIPLPDQRRFTAKSVLRLTPKKEHHNTNFSCQAQNTADRTYRSAKIRVEVKYAPKVKVNVMGSLPGGAGGSVGGAGGGSVHMSTGSRIVEHSQVRLECRADANPSDVRYRWFINDEPIIGGQKTEMVIRNVTRKFHDAIVKCEVQNSVGKSEDSETLDISYAPSFRQRPQSMEADVGSVVSLTCEVDSNPQPEIVWIQHPSDRVVGTSTNLTFSVSNETAGRYYCKANVPGYAEISADAYVYLKGSPAIGSQRTQYGLVGDTARIECFASSVPRARHVSWTFNGQEISSESGHDYSILVDAVPGGVKSTLIIRDSQAYHYGKYNCTVVNDYGNDVAEIQLQAKKSVSLLMTIVGGISVVAFLLVLTILVVVYIKCKKRTKLPPADVISEHQITKNGGVSCKLEPGDRTSNYSDLKVDISGGYVPYGDYSTHYSPPPQYLTTCSTKSNGSSTIMQNNHQNQLQLQQQQQQSHHQHHTQTTTLPMTFLTNSSGGSLTGSIIGSREIRQDNGLPSLQSTTASVVSSSPNGSCSNQSTTAATTTTTHVVVPSSMALSVDPRYSAIYGNPYLRSSNSSLLPPPTAV
Protein: T-complex protein 1 subunit theta (TCP-1-theta) (CCT-theta) (Q3ZCI9)
Organism: Bos taurus (Bovine)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P50990}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P42932}.
Interaction partners:
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- Uncharacterized protein
- T-complex protein 1 subunit zeta-2
- Molecular chaperone MKKS
Sequence:
MALHVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRLGLSVSEVIEGYEIACKKAHEILPDLVCCSAKNLRDVDEVSSLLHTSVMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGVHSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVLIKSAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGRVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLNPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGVLDTYLGKYWAIKLATNAAVTVLRVDQIIMAKPAGGPKPPSGKKDWDEDQND
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O76222)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
SVAAVQVIVGIFSLEVLSPGCLVSFYGEVISSIQKQARVQVRKREEILVHLISLVRILKGHLRPHLKEITSTVDSFISVTDLSVLRQVLALLKELCCSLRRRFRPYMSSLLGPIIVLVEENVEETSEIVLDFFSAMGSLLEDHLHTVLPVVCNIIVDTSVPSRCRIVAVKTLICFTKRLPDLCFHASRCVHCLCRVLRESDGGDGVGDEGRLGCSAMEALCTLAGSLGKNFENFVLVVLPAVADRYGETSGEYCRFCHDIYEAIDGKRAPEVSSNGVGKAGGGGAPSLPFTAGTSASPLKDRADAYASLRFHLRKRDQASDEDWNHWLPQLAVNLLRSSSSPSHGRALTLAELHEPFARQMLHSAFAACYADMDEHTQREVIGLLTEVLRGLRVPSEVMQELLNLSEHMERQGIRLSAGGKASIKHSSNFCPFDRQVLMESSANCNLYSKALHYAEIEFLETVREYERSILRGCPKPLPVEDWQNLIKLCEKSIYFCNLLGQRESANGILKFIRQNLPLLTGKKVTELSQMMDAHLFDKLRWWSQSLQAYERRLQQEPNKVSNMVGLLRALDALGEYPRVLEMWRQFSKRVSKREVSKLASMGAHAAWLLRRWDDMEHITSFMSDEDYTGTTALFYKATLAARKKRFREAEKLIDMCRKRVDSKLSALVAESYDRAYDLFVGIQQLSELEELAMATSDPQSAMHWRQLWERRLSVMAYEGWPGTLANHTLLVPPSSEIDMWLRFVSLSRAHGQGSVSTEVLRELLGNQSIESAIENGIPTPAVAMGSFQHLYETNQRDSAIARLQLYVSKVEGSGAQHVSREREDMAVCHAKLAEWLVHQKKAHRTEDELQKIFHHLRRATELDKSNGSIWRTLARVHREAATKPADGSDSSGASGHIMEALSAYLRSVSLSEELEDALGFLSLWFMYGPLLAVQVGSTLKEEIEEVNPTVWLKVIPQIIARISSSNGTVADSVYNLLVLVARRHPQAILYSLNVAHSSYQGKGTADGVEPLKGSHRVLARIAEIHQNGKAMVEDSALVCRELVRCAVLWPELWFNELGRALYQWERQRSAENLLLAMGPLLEQLKRPETMAEAQFAAELRQPLENACCHVERAVSSRHEQFMEEARRIFVSIERRIREQISGMSSLALQLVSPKLHQNGRNLSLVVPGQYREDGNYPLIASFQNVLKVLNSKQRPRRIYINGSNGEIYKFLLKGHEDLRLDERVMQLLGFVNTILEKHSVPKRHDCLIQTYSVTPLSDNAGLVGWVDHCDTLNKIIEDYRVNPRCIRMELDLMRSMCDNLYYLTAIQRVEPFEFPLERTEGVDLVRSFWVKAPSAETWLERRTTYVCSLATMSMVGHILGLGDRHPSNLMIHAFSGRVVHIDFGDCFEVAQQRSIHPEKVPFRLTRMLVKAMEMGGIEGLFRHGCHTVMNVLREEGGSLLALLEAFVHDPLVSWWRDEAEGFSGNGQAASSVQTISVIGSMTNVAEEGSVGSLQLSQLSVQRRATTQQRVNANIEKDTSQTRKPKSVVKRIKRKLRGLEFPQSQEGKSSDGFTVEEQVSRLIEEATSNENLCVHFLGWCPFW
Protein: Growth-regulating factor 3 (AtGRF3) (Transcription activator GRF3) (Q9SJR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues. Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation. microRNA396-GRF1/GRF3 regulatory module acts as a developmental regulator in the reprogramming of root cells during cyst nematode infection, leading to the formation of the syncytium.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU01002}.
Interaction partners:
- GRF1-interacting factor 1
- Transmembrane protein
Sequence:
MDLQLKQWRSQQQQQHQTESEEQPSAAKIPKHVFDQIHSHTATSTALPLFTPEPTSSKLSSLSPDSSSRFPKMGSFFSWAQWQELELQALIYRYMLAGAAVPQELLLPIKKSLLHLSPSYFLHHPLQHLPHYQPAWYLGRAAMDPEPGRCRRTDGKKWRCSRDVFAGHKYCERHMHRGRNRSRKPVETPTTVNATATSMASSVAAAATTTTATTTSTFAFGGGGGSEEVVGQGGSFFFSGSSNSSSELLHLSQSCSEMKQESNNMNNKRPYESHIGFSNNRSDGGHILRPFFDDWPRSSLQEADNSSSPMSSATCLSISMPGNSSSDVSLKLSTGNEEGARSNNNGRDQQNMSWWSGGGSNHHHHNMGGPLAEALRSSSSSSPTSVLHQLGVSTQAFH
Protein: UDP-arabinopyranose mutase 3 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 3) (AtRGP3) (UDP-L-arabinose mutase 3) (O22666)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides. Catalyzes the interconvertion of UDP-L-arabinopyranose (UDP-Arap) and UDP-L-arabinofuranose (UDP-Araf). Preferentially catalyzes the formation of UDP-Arap from UDP-Araf. At thermodynamic equilibrium in vitro the ratio of the pyranose form over the furanose form is 95:5. Is not active on other UDP-sugars (UDP-Gal, UDP-Xyl, UDP-Glc, GDP-Man and GDP-Fuc). Is probably active as heteromer in vivo.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21478444}. Golgi apparatus {ECO:0000269|PubMed:21478444}. Note=Soluble and membrane-associated.
Interaction partners:
- UDP-sugar pyrophosphorylase
- Endo-1,4-beta-xylanase 4
- Actin-related protein 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- F-actin-capping protein subunit beta
- Actin-related protein 9
- UDP-glucuronic acid decarboxylase 1
- Chromatin structure-remodeling complex protein SYD
- Actin-related protein 2/3 complex subunit 2A
Sequence:
MAQLYSSVKPTPMLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVINIPVGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGKEINALEQHIKNLLSPSTPHFFNTLYDPYRDGADFVRGYPFSMREGAITAVSHGLWLNIPDYDAPTQLVKPLEKNSRYVDAVMTIPKGTLFPMCGMNLAFDRELIGPAMYFGLMGDGQPIGRYDDMWAGWCVKVICDHMGWGVKTGLPYIWHSKASNPFVNLKKEYNGIFWQEEAIPFFQSVTLPKECTSVQQCYLELAKLVREKLGKVDPYFITLATGMVTWIEAWEELNSAEGTEAEAPKGKN