wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P-448) (Cytochrome P-450d) (Cytochrome P450-D) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (P04799)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}. Microsome membrane {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05177}.
Interaction partners:
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase 2B1
- Cytochrome P450 3A1
- UDP-glucuronosyltransferase
- Cytochrome P450 2B3
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 2B37
- Cytochrome P450 2E1
- Cytochrome P450 3A18
Sequence:
MAFSQYISLAPELLLATAIFCLVFWVLRGTRTQVPKGLKSPPGPWGLPFIGHMLTLGKNPHLSLTKLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVKQGDDFKGRPDLYSFTLITNGKSMTFNPDSGPVWAARRRLAQDALKSFSIASDPTSVSSCYLEEHVSKEANHLISKFQKLMAEVGHFEPVNQVVESVANVIGAMCFGKNFPRKSEEMLNLVKSSKDFVENVTSGNAVDFFPVLRYLPNPALKRFKNFNDNFVLFLQKTVQEHYQDFNKNSIQDITGALFKHSENYKDNGGLIPQEKIVNIVNDIFGAGFETVTTAIFWSILLLVTEPKVQRKIHEELDTVIGRDRQPRLSDRPQLPYLEAFILEIYRYTSFVPFTIPHSTTRDTSLNGFHIPKECCIFINQWQVNHDEKQWKDPFVFRPERFLTNDNTAIDKTLSEKVMLFGLGKRRCIGEIPAKWEVFLFLAILLHQLEFTVPPGVKVDLTPSYGLTMKPRTCEHVQAWPRFSK
Protein: Diacylglycerol kinase (DAG kinase) (EC 2.7.1.107) (Q58AU4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAAEGHNVDANLVDMRPNHGHYFVKKTFGKPAYCHHCCDKIWGMLTTGYSCEMCNFVCHEKCLRTVVSYCSSVALQLIKNPVAHTWSAPCLIKRKYCCVCRKRTDDALSVECEVCEYYVHVDCSDLAVSDCKEAATYVANMESANTVQYHHMREGNLPKESKCIVCRKTCFSTECLAGMRCEWCGQTAHAVCYRQMDKECDFGVLRKIMLPPMCLTIPRTELPMEQLLNISSHDQPQSRKGQIFHYPISRNIVVAKHVSVQQVRDAALRRFHINDTPERYYITQVVGEVEEEILEDPVPLRNVKRPEGKRAQIFIRYYDDPDKDEVKVYGGWLRKVPVTFCAISVSKDTVVQDLVTDALYHFGLDGSCWNRYNLIEVSLDRGVAERTCNPQENVLQLVRNLRKDSLRRYHVVRFYVQEKEDPHDHAVFVGNLPVSLAQRQYERILLKLLGAKEKPFTAIGPIYFEYGSLIITFNTPKAATAAVQKLQSAIYEEKKLIVLCLPNVQPQMIPKDVEPLLVLVNVKSGGCQGTELIQSFRKLLNPFQVFDVLNGGPLVGLYVFRNIPKYKILACGGDGTIGWVLQCLDIAKQDAACFSPPCGIVPLGTGNDLARVLRWGGGYTGEENPMDILKDVIEADTVKLDRWAVVFHEEERNQPTSSGNQTEMNEQTMNNPEDQTSMIIMNNYFGIGIDADVCLKFHNKRDANPEKFQSRLFNKTQYAKIGLQKMFFERTCKDLWKRIELEVDGRIIELPNIEGIVVLNLLSWGSGANPWGTSKEEGNFSKPTHYDGLLEVVGISDVSRLGLIQSKLAAGIRIAQGGSIRITTHEEWPVQVDGEPHIQPPGTITILKSALKAQMLKKAKKSRRGGATNATSLTHPHPETSESMSGPLGVPSTLGDPNHGKTTPDNTAADSDEEGDAFL
Protein: Fanconi anemia group J protein homolog (EC 5.6.2.3) (BRCA1-associated C-terminal helicase 1) (BRCA1-interacting protein C-terminal helicase 1) (BRCA1-interacting protein 1) (DNA 5'-3' helicase FANCJ) (Q5SXJ3)
Organism: Mus musculus (Mouse)
Function: DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the 'Fanconi anemia' pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BX63}. Cytoplasm {ECO:0000250|UniProtKB:Q9BX63}.
Interaction partners:
- DNA topoisomerase 2-binding protein 1
- Breast cancer type 1 susceptibility protein homolog
- DNA mismatch repair protein Mlh1
- BRCA1-associated RING domain protein 1
- Breast cancer type 2 susceptibility protein homolog
- Partner and localizer of BRCA2
- Nibrin
- Double-strand break repair protein MRE11
- Mismatch repair endonuclease PMS2
- Fanconi anemia group D2 protein homolog
Sequence:
MSSVLSDYTIGGVKIHFPCRAYPAQLAMMNSIVRGLNSSQHCLLESPTGSGKSLALLCSALAWQQSLSEKPVDEGLNKKPEAPPSCSCACHSKNFTYSDTNLDTSPHFNSPSKPSSGRNGVSTPCQDSPEKNTLAAKLSAKKQASIHRDEDDDFQVEKKRIRPLETTQQIRKRHCLEKDVHHVDARLASEKRVKPESPIGKSFSDRKDSFQNVDGLCSRCCCSAKQGNNQEPANTVKKDHGGQCKRPKIYFGTRTHKQIAQITRELRKTAYSGVPMTILSSRDHSCVHPEVVGNFNRKEKCMELLDGKHGKSCYFYHGVHKISNQQTLQHLQGMSRAWDIEELVSLGRKLKACPYYTARELIEDADIVFCPYNYLLDSQIRETMDIKLKGQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSLINGNIRKKSHEPLRDVCYNLINWLETNSKHLVERGYESSCKIWSGNEMLLNLYRMGITTATFPVLQRHLSAVLQKEEKVTPIHGKEEAIQIPIISASTQVVLKGLFMVLDYLFRENSRFADDYKVAIQQTYSWTNQIAIFDKTGVLAVPKNKKHSRQKIGVNALNFWCLNPAVAFSDINDKVRTIVLTSGTLSPLKSFSSELGVTFSIQLEANHVISNSQVWVGTVGSGPKGRNLCATFQHTETFEFQDEVGMLLLSVCQTVSQGILCFLPSYKLLEKLRERWIFTGLWHSLESVKTVIAEPQGGEKTDFDELLQVYYDAIKFKGEKDGALLIAVCRGKVSEGLDFSDDNARAVITVGIPFPNVKDLQVELKRQYNDHHSKSRGLLPGRQWYEIQAYRALNQALGRCIRHKNDWGALILVDDRFNNNPNRYISGLSKWVRQQIQHHSSFASALESLTEFSRRHQKVTNRSKKDEKCTKDNEPTLEVACLEDSTFTSVSESSHQSPENSTEEAEVCVQELQCPQVATKSPSVASHGVSRRKKSDPGLRGESLQTMKTEKNEISRSSSPTFGKQTEPVNWPIFNSLRRHFNSKVKNCTPVLKSSKNRAPGSSTFNKTALPLTGNCVPSNETADTSLGPCLQSEVIISPVKIEATPATNYSKQVFCCEKDLLPDTELSPGTEEAKCPSSNKAAETEVDDDSECFTPELFDPVDTNEENGELVETDRSSHSSDCFSAEELFETATGFGQK
Protein: Small acidic protein 1 (Q9T0H2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D). Not involved in the response to indole-3-acetic acid (IAA). Interacts with RUB modification-related components and may regulate the cullin-ring ubiquitin E3 ligase complex (CRL) activity.
Interaction partners:
- Small acidic protein 2
- Defective in cullin neddylation protein AAR3
Sequence:
MRPMQLDMLSEMDDAGSSMAMDVDDLEAMEILNEGGLVSDNKLADADFFNKFDDDFDDTDIN
Protein: Nucleoporin NUP84 (Nuclear pore protein NUP84) (P52891)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA export, in NPC assembly and distribution, as well as in nuclear envelope organization.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Nucleoporin NUP120
- Nucleoporin NUP133
- Protein transport protein SEC13
- Nucleoporin NUP170
- Nucleoporin NUP159
- Nucleoporin SEH1
- Nucleoporin NUP85
- Nucleoporin NSP1
- Nucleoporin NUP145
- Nucleoporin NIC96
Sequence:
MELSPTYQTERFTKFSDTLKEFKIEQNNEQNPIDPFNIIREFRSAAGQLALDLANSGDESNVISSKDWELEARFWHLVELLLVFRNADLDLDEMELHPYNSRGLFEKKLMQDNKQLYQIWIVMVWLKENTYVMERPKNVPTSKWLNSITSGGLKSCDLDFPLRENTNVLDVKDKEEDHIFFKYIYELILAGAIDEALEEAKLSDNISICMILCGIQEYLNPVIDTQIANEFNTQQGIKKHSLWRRTVYSLSQQAGLDPYERAIYSYLSGAIPNQEVLQYSDWESDLHIHLNQILQTEIENYLLENNQVGTDELILPLPSHALTVQEVLNRVASRHPSESEHPIRVLMASVILDSLPSVIHSSVEMLLDVVKGTEASNDIIDKPYLLRIVTHLAICLDIINPGSVEEVDKSKLITTYISLLKLQGLYENIPIYATFLNESDCLEACSFILSSLEDPQVRKKQIETINFLRLPASNILRRTTQRVFDETEQEYSPSNEISISFDVNNIDMHLIYGVEWLIEGKLYVDAVHSIIALSRRFLLNGRVKALEQFMERNNIGEICKNYELEKIADNISKDENEDQFLEEITQYEHLIKGIREYEEWQKSVSLLSSESNIPTLIEKLQGFSKDTFELIKTFLVDLTSSNFADSADYEILYEIRALYTPFLLMELHKKLVEAAKLLKIPKFISEALAFTSLVANENDKIYLLFQSSGKLKEYLDLVARTATLSN
Protein: VIN3-like protein 3 (Vernalization5/VIN3-like protein 2) (Q5BPT4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in both the vernalization and photoperiod pathways by regulating gene expression.
Subcellular location: Nucleus {ECO:0000250}. Note=Probably DNA-associated. {ECO:0000250}.
Interaction partners:
- Ketose-bisphosphate aldolase class-II family protein
- Afadin/alpha-actinin-binding protein
- VEFS-Box of polycomb protein
- Acetyl-CoA acetyltransferase 2
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- Acetyl-CoA acetyltransferase 1
- Histone-lysine N-methyltransferase EZA1
- AGAMOUS-like 79
Sequence:
MASFHKGAAGDSMGSSKMSFDQRRQLVLKLSKESEREFKEVLKDWSCNEIRELLRAESKKDIKYTGLTKDEIITRLFNIVSKKNTRDHEVEEIIPSPKRQKRDLVTPLAKAKGKGKMYCQNLACQNKLREEATFCKRCSCCICFKYDDNKDPSLWLTCNSDSQFDGESCGLSCHLNCAFDSEKSGLKEDTPSSDIDGCFNCVSCGKTNSKIECLKKQLIIANEERRVGVFCYRILLAHKLLKGTKKYIIVSEEVEKAVMHLKNEFGVPISCLPSKMSRGLVNRLCCAEKVKKHCSSALKELDGLPLPSTIQGSMKIRIESVLATSVTFDIEAEESFSWGDTNHYRMVYRKVSEKHSSKDLTRELFSTSSHQRFTVMELTPATEYWFKIVSFSGVEELSVDEFIVSTKTLQDEEVAAVLLNMSNCNNANKMEKSGSCSFGFEECVNLIRQLECSGQVKSDFRKKFLTWYCLKATDKEKHVVEIFVDTFKDDKEALAKQLIDTFSDCITRKHPEIGGGSESAGVSLILLQD
Protein: Xylanase (EC 3.2.1.-) (E0SCM6)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Endoglucanase Z
- Xylosidase/arabinosidase
- Mannan endo-1,4-beta-mannosidase
- Pectate lyase L
- Arabinogalactan endo-beta-1,4-galactanase
- Pectate lyase C
- Pectate lyase
- Pectate lyase B
Sequence:
MNGNVTCWVRHCLSAAIVVSVTAGAFSAYADTVKIDAKVNYQTIQGFGGMNGAGWINDLTTEQINTAFGNDAGQIGLSIMRIRIDPDSNKWNIQVPSARKAVSLGAKLMATPWTPPAYMKSNNSLINGGRLLPAHYSAYTSHLLDFSKYMQTNSAPIYAISIQNEPDWKPDYESCEWSGDEFKNYLKSQGSKFGSLKVIVAESLGFNPALTDPVLKDSDASKYVSIIGGHLYGTTPKPYPLAQNAGKQLWMTEHYVDSKQSANNWTSALDVGTELNASMVSNYSAYVWWYIRRSYGLLTEDGKVSKRGYVMSQYARFVRPGALRIQATENPQSNVHLTAYKNSDGKMVIVAVNTNDSDQMLSLNISNANVGKFEKYSTSEVLNVEYGGSYQVDDSGKATVWLNPLSVTTFVGK
Protein: Ataxin-1-like (Brother of ataxin-1) (Brother of ATXN1) (P0C7T5)
Organism: Homo sapiens (Human)
Function: Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Can suppress ATXN1 cytotoxicity in spinocerebellar ataxia type 1 (SCA1). In concert with CIC and ATXN1, involved in brain development (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16121196}. Cell projection, dendrite {ECO:0000269|PubMed:16121196}. Note=Forms nuclear foci. Colocalizes with NCOR2 and HDAC3. Distributed beyond the nucleus into the cell body and dendrites in Purkinje cells and in inferior olive cells.
Interaction partners:
- Ataxin-1
- Recombining binding protein suppressor of hairless
- Histone acetyltransferase KAT5
- Pumilio homolog 2
- Recombining binding protein suppressor of hairless-like protein
- Angiotensin-converting enzyme 2
- Protein capicua homolog
- Nuclear receptor corepressor 2
- Splicing factor 45
Sequence:
MKPVHERSQECLPPKKRDLPVTSEDMGRTTSCSTNHTPSSDASEWSRGVVVAGQSQAGARVSLGGDGAEAITGLTVDQYGMLYKVAVPPATFSPTGLPSVVNMSPLPPTFNVASSLIQHPGIHYPPLHYAQLPSTSLQFIGSPYSLPYAVPPNFLPSPLLSPSANLATSHLPHFVPYASLLAEGATPPPQAPSPAHSFNKAPSATSPSGQLPHHSSTQPLDLAPGRMPIYYQMSRLPAGYTLHETPPAGASPVLTPQESQSALEAAAANGGQRPRERNLVRRESEALDSPNSKGEGQGLVPVVECVVDGQLFSGSQTPRVEVAAPAHRGTPDTDLEVQRVVGALASQDYRVVAAQRKEEPSPLNLSHHTPDHQGEGRGSARNPAELAEKSQARGFYPQSHQEPVKHRPLPKAMVVANGNLVPTGTDSGLLPVGSEILVASSLDVQARATFPDKEPTPPPITSSHLPSHFMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGGLKIDSSTVVDIQESQWPGFVMLHFVVGEQQSKVSIEVPPEHPFFVYGQGWSSCSPGRTTQLFSLPCHRLQVGDVCISISLQSLNSNSVSQASCAPPSQLGPPRERPERTVLGSRELCDSEGKSQPAGEGSRVVEPSQPESGAQACWPAPSFQRYSMQGEEARAALLRPSFIPQEVKLSIEGRSNAGK
Protein: Myosin IEb (Zgc:64042) (Q6PFT4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGSKEKYHWQTQNVKVSGVDDMVLLSKITEDAITDNLKKRYMDDYIFTYIGPVLISVNPFKQLPYFTDREIELYQGAAQYENPPHIYALADNMYRNMMIDSENQCVIISGESGAGKTVAAKYIMSYISKVSGGGPKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSRGGEPDGGKISNFLLEKSRVVSQNNGERNFHIYYQLLKGATKEQRENLGVTTPDYYFYLNQSDTYTVEDVNDKKEFEDTMNAMSVVGLSMDAQDSVLQIVAGILHLGNIAFREEGNYAVVESEDFLAFPSYLLGINQDGLKSKLTSRIMDSKWGGKTETISVTLNTEQASFTRDALSKALYSRLFDYLVDAINKAMQKDREELNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGISWTPIEYFNNKVVCDLIESKLNPPGIMSILDDVCATMHAKGEGADQTLLQKLQSQIGTHEHFNSWNKGFVVHHYAGKVSYDVSGFCERNRDVLFSDIIELMQSSEFAFIKGLFPENIEAEKRGRPTTAGSKIKKQANTLVQTLMKCTPHYIRCIKPNETKKSRDWEESRVKHQVEYLGLRENIRVRRAGYAFRRIFKKFLHRYAILTRETWPQWRGDEKQGVLHLLKSVNMDSDQYQLGKTKIFIKAPESLFLLEEMRERKYNGYARVIQQAWRKHIAVRKYVRMREEASDLLLNKKERRKNSLNRNFVGDYIGTDNHPEIRQFVGRRERIDFADVVVKYDRRFKSVKRDLILTPKFLYLIGREKVKQGPEKGQIREVLKRKIEVEKIQSVSLSTLQDDIFILHEDQYDSVLQSVFKTEFLSLLYKRFEEKTKKKLPLKFNNLLEFKVKKGGWGPFASAGSRQIQFQMGQGDDAVLKPSSKILTVSIGSGLPKNTRPTRRDNRKSSFMGNQNRSAGQYSREAPKSAGRGRGQPAVRHSLLRQQSTMDQPTLPRLQGSVRSQRESQVYTDMGFMKVPDQGVAGMHRRRSKEYKPLPGSGRPKPSPKPVPRTPRCKALYAYDAQDTDELSFQPDDIIEILSEDPSGWWQGRLRGKEGMFPGNYVEKI
Protein: Conserved protein (O86340)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MTPTFSDLAEAQYLLLTTFTKDGRPKPVPIWAALDTDRGDRLLVITEKKSWKVKRIRNTPRVTLATCTLRGRPTSEAVEATAAILDESQTGAVYDAIVKRYGIQGKLFTFVSKLRGGMRNNIGLELKVAESETG
Protein: T-box transcription factor TBX6 (T-box protein 6) (T-box transcription factor TBX24) (T-box protein 24) (Q8JIS6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: T-box transcription factor involved in the development of paraxial mesoderm.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- Mesoderm posterior ab.
- Protein ripply1
- Mesogenin-1
- Homeobox protein MOX-1
- Hairy-related 1.
- Fibroblast growth factor 8
- Mesoderm posterior ba.
- Protein ripply2
- Paired box 3a
- Homeobox protein unc-4 homolog
Sequence:
MLGVEMYPGLALGPQRLSDCYYRDRDVPLYPSTCEMAARALPPALLKPHANTDSPATPQDSVRMELENAGLWKQFSTVGTEMIVTKKGRRMFPQLRVKLSGLNPSLRYILLLDIVPVDSSRYRFQDNSWQVVGGAEARLPDRVFIHPDSPATGEHWQNRTISFHRAKLTNNTLDAQGYIILHSLHRYQPRVHVIEARDVLMWGRTQHSFTFPETQFITVTAYQNNKITELKINSNPFAKGFRENGMNCKKQREARLKRKITSSQEECLDIESCDPCDSTELLPQSVDLPSSALTIMNTALPITDSGFHTEVSSHPDQTDSDQTLVLEQAFLTSEMPSSMESQQQTTSETNVNNALMDETGQMMDLSGYTSSFPTPQLSSHTSVPQSSSMYSVVSSTQSSDLELPQASSISSPHSMPAYSSIPSAEYPGVNSSTAMPASTTSLSDSYPSISHSTSSHLLQSSSYHSLLPTDQSQDNLSPHTPTNPPFQSIPACQGTRLTIDSGQNQVDDGGLSSANATTPAVPNPTQTAFPFPPVQPNNDPDPTSPSCQSLPQSALPYQQVSQCNQIPTPSDPNTTPTAFPFPPSEQSTPNSIMVSSNPNTTAFPFPPVQQQLNLSTSGPSSFPVSQSSGLNAIPNPVHPTTGSFSFPSTSAIHQGPMQSVPNTLHPSTAYTFPSSLPKHTGPLPNPAPTSYPFPTPIPPGPHPLQSLTLPSSCSIPNTSQIQSTFPQSYHNPSFSHIPPQMANHSQITSQSFPPLQTSSAPQLLSQSSTHPQCPPPSNAYPAVAPTEIGTFPQLNSAAPYLPDVVLHPSILPSLDPSLSSSAPPSLYNPFPSYSLRLCQDPRSSLHLPLRHIYRQPQHAHGQGSYFDLGGRTVF
Protein: Hexitol phosphatase B (2-deoxyglucose-6-phosphate phosphatase) (EC 3.1.3.68) (Mannitol-1-phosphatase) (EC 3.1.3.22) (Sorbitol-6-phosphatase) (EC 3.1.3.50) (Sugar-phosphatase) (EC 3.1.3.23) (P77247)
Organism: Escherichia coli (strain K12)
Function: Sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate. Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important activity in vivo since it contributes to the elimination of this toxic compound and plays an important role in the resistance of E.coli to 2-deoxyglucose. To a lesser extent, is also able to dephosphorylate mannose 6-phosphate (Man6P), erythrose-4-phosphate, 2-deoxyribose-5-phosphate (2dRib5P), ribose-5-phosphate (Rib5P) and glucose-6-phosphate (Glu6P) in vitro.
Interaction partners:
- Mannitol-1-phosphate 5-dehydrogenase
- Hexitol phosphatase A
- PTS system mannitol-specific EIICBA component
- PTS system mannitol-specific cryptic EIICB component
- Mannitol-specific cryptic phosphotransferase enzyme IIA component
- Sugar phosphatase YbiV
- Probable electron transfer flavoprotein-quinone oxidoreductase YdiS
- Sugar phosphatase YidA
- Kojibiose phosphorylase
- 6-phosphogluconate phosphatase
Sequence:
MSTPRQILAAIFDMDGLLIDSEPLWDRAELDVMASLGVDISRRNELPDTLGLRIDMVVDLWYARQPWNGPSRQEVVERVIARAISLVEETRPLLPGVREAVALCKEQGLLVGLASASPLHMLEKVLTMFDLRDSFDALASAEKLPYSKPHPQVYLDCAAKLGVDPLTCVALEDSVNGMIASKAARMRSIVVPAPEAQNDPRFVLADVKLSSLTELTAKDLLG
Protein: Photosystem II extrinsic protein V (PsbV) (Cytochrome c-550) (Cytochrome c549) (Cytochrome c550) (Low-potential cytochrome c) (Q55013)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Required for normal function or stabilization of PSII. Extrinsic protein associated with PSII that enhances oxygen evolution.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Lumenal side {ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:7896839}. Note=Associated with photosystem II at the lumenal side of the thylakoid membrane (PubMed:34937700). CyanoQ (PsbQ) binds to the large lumenal domain of PsbC (CP43) between PsbO and PsbV (PubMed:34937700). {ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:7896839}.
Interaction partners:
- Photosystem II reaction center protein K
- Photosystem II reaction center protein M
- Photosystem II CP43 reaction center protein
- Photosystem II extrinsic protein U
- Photosystem II protein D1 2
- Photosystem II reaction center protein X
- Photosystem II D2 protein
- Cytochrome b559 subunit beta
- Photosystem II reaction center protein I
- Cytochrome b559 subunit alpha
Sequence:
MKRFFLVAIASVLFFFNTMVGSANAVELTESTRTIPLDEAGGTTTLTARQFTNGQKIFVDTCTQCHLQGKTKTNNNVSLGLADLAGAEPRRDNVLALVEFLKNPKSYDGEDDYSELHPNISRPDIYPEMRNYTEDDIFDVAGYTLIAPKLDERWGGTIYF
Protein: Ben, isoform B (Q9VXZ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSRRIALVLLIGIIVSFSGHDALTYPERFDRLPTWGGHSQIGGPLLDTAHRENREKRENRVDLCRHCFCIHLKAICDYKLNKTLPNEFNDKLLVPLNIKYIEVRLTVGTQFVMYENFFQDNQVNYFGVIGVGKDDQVEITSNAFSHNKGGFPNIEIRNVLRVFLREKFLTGADYKLLVEDVTQLSVFSNALQMTNLDCSLKRIKELNLMKNAFNPGVAKYGINLRIEDSNINQLGIFGVSMGKVSLLRCHIDMIMSNAFDVTSIKELIIEGCNIEVIESQALTNKLHSDKVAIVDTVIGTIEGQAISQSGITTMIMFGNTITKIRSNAIQIVAVSLFIRNNSMSHVEPNWLSVSQADQVEIANNRFEDYGRCELNIGSSNCSFRNNILQNPQSGSLNFTCRVHQVRVGTECSCNKSWLSELTDHDLESEIMCQVAKRDANCFNATNTDVRRYVNEACGSNVTRYCMGGQWVTKAVSDHSSDSSKLTIGMIALEIVILTLLLVAIVCVLAKNCGSGSCAPAGGQSTDNCLIEEDIRNSLRQLALHSESNKTRKAILKLINGHLSKGECNDRILFIVDNMPQNQAIESLLFRHISQSHMEPSDSEAYASTALTANATAPPLPPSTDSSEPIYQELDQQRLIIDDKYSLPLNSDEDPPYSEPSNMMSEYGNDYNYNGTNESYTSEQSNPSPNRPLLPIPNRL
Protein: Tubulin beta chain (G3V2A3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSLRFPGQLNADLRKLAVNMVPFP
Protein: PAX-interacting protein 1 (PAX transactivation activation domain-interacting protein) (Q9W061)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADVSLFFGGLPAILLKADTIYRIGRQKGLEISIADESMELAHATACILRRGVVRLAALVGKIFVNDQEETVVDIGMENAVAGKVKLRFGNVEARLEFGEDHDEVHDSSGFGECLKNGLNNTTLDSMDVPETQPPSANTSVNTTADSLFIPETQAVLCERPSTGQRVSLGDDFMIPETQDMLADLPPEPPVFKPPVIPVVDKPGPTIDSDEESSQGSIIRMCTQDYNEDAIDDFDTSQVLCDVLLPLPPPTAPIEGLENQDTKRDQLDTTDMEMSALNWSASNSKCCALSSTKADDILPRGDACITPDLTAPSVDRNICTPDLFDLIMGGDRRRDGSSSPDPFVRPADNTNTATPQFGGVKQLVVATIETPTATPDTNSQEKNQDMIATQRFPRHKLLESDEEDNGQNNQDFVATQAFNLGRPQAPQENEANQDLIATQAFNLAPPQKVDSPKPSTANDASNQDFIETQAFNLGIPQANMASPENNEISNQDLIATQAFPAKINSSRCQDFVATQPFHVVNQHSVSLQDKENIPLDDSVKVASGTVATSPVSPNEESIPFFEPCVIKDKNHYQKICQIEGVFSNVSNRSRGRTDGTGFGRLKRVAKSESPPETPIRKDRRRSEGSERPGSNSRERLNNLVDKKSEALNKSVIREHGIDSIPEEITKEDKSDSEEKGDCFNNVVNQWRSRKRRIQSRPGTPGSSSERNEVNADVVDKPNEEPPTKNIRARKAKKAEKADSSKDIPKPTTRTRRQTSDEDVRTPDLGKGRKAKNTASSKADTSKNIAKGSKRVTRQNSADDAELLEEDSSVQTESGKRVKKVKSSKGETSKDIPKAKPRTRRQTADEDAMTPKAEKERQIQGEETKDMSKPAARTRRKASAEETESAAQAVKPKRGGKGKKNETTKAEATVEKPMVRTRRMTIAEDSSTLTEVKTGGALIKRAVVRISRVSIEQLESSTSAGNNARVTGAAQSRSTTPSIEEPSSSSAAAKEPNVSTATTRRRAKRLTSGEEPTSSSDVPTKKPKMSVDEEVLKNRSGATTTRFSQPDADPLRAINLYVRKAKTTTGKIKVAFTMCNRPALETVLKSLKHVVEITEDPLQCDLLVMDKGERTYKFLTVIASNKPVLSTNWLHSVKKTRSIDIKADHLFSDPTFEETYKFKPSSVLEHPRLLYGLHFMLGKDIVPKANEMKVIIHSAGGKVHAQPPSLAISVDLYVVTTSKDTKSKRRLNNYEKVHFIKTEAVMQALVQHNIEMLQEHTLKL
Protein: Protein phosphatase 2A scaffold subunit (Protein phosphatase 2A 65 kDa regulatory subunit) (Protein phosphatase 2A A subunit) (Serine/threonine-protein phosphatase 2A regulatory subunit pppA) (Q54QR9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Scaffolding molecule which may coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay. The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells where it regulates F-actin dynamics and signal relay by controlling the activation of rasC and the downstream target of rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18673380}. Cell membrane {ECO:0000269|PubMed:20493808}. Note=The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells (PubMed:20493808). Membrane localization of the Sca1 complex is regulated by scaA phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit A
- Serine/threonine-protein phosphatase 2A regulatory subunit psrA
- Protein phosphatase 2A catalytic subunit B
- Serine/threonine-protein phosphatase 2A regulatory subunit phr2AB
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
- EF-hand domain-containing protein
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Ras guanine nucleotide exchange factor H
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Ras guanine nucleotide exchange factor A
Sequence:
MASINTESDDYHPIVILIDELKNEDIQLRLNSIKKLQSIAKALGPERTRTELIPYLQDSVLEDEDEVLVVLSEELGNLIEFVGGAEHAVCLLPPLQILAGAEELVVREKAVESLCKIAKEIPTSSFEESFLPLLFSLSKADWFTSRTSACGLFTVSYPRANAEMKKSLRKTFGGLCHDDTPMVKRAAATNLGSFAKQIEKESVKSEILPLFQSLSTDEQDSVRLLGVENCALLGSMLTNEENIQFILPTIKASSLDKSWRVRYMVARLLKELCESMGTEITKTELIGAFVKLLKDTEAEVRTEASLRIADVCSLLTKEMNIKTILPCVKDLVSDSSQHVRAALAQVIMSLAPIYGKEDTLTHLLELFLHLLKDDFPDVRLNIISKLDQVSKVIGIEMLSQSLLPAIVELAEDHQWRVRLAIIDYIPLLASQLGVEFFDEKLGNLCMTWLGDPVFSIREAATNNLKKLTEVFGVDWAKNNIIPKVLSLHSHPNYLYRMTTLFSISTLSTVVGGDVISSSMVPLLAKMVSDKVPNIRFNVAKTFQTIIPLLDSTIVQSRVKPLLVKLHEDTDKDVKFYASQALQLC
Protein: Bile salt hydrolase (I3QNT3)
Organism: Bifidobacterium catenulatum
Interaction partners:
Sequence:
SDNEGNMYFGRNLDWSFSYGETILVTPRGYQYDYVYGTEGKNEPNAVIGVGVVMADRPMYFDCANEHGLAIAGLNFPGYASFAHEPVEGTENVATFEFPLWVARNFDSVDEVEEALKNVTLVSQVVPGQQESLLHWFIGDGTRSIVVEQMSDGMHVHHDDV