wanglab/gogpt-training-data huggingface dataset:
Protein: Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide-nucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1) (Q9HAN9)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. Also acts as a cofactor for glutamate and aspartate ADP-ribosylation by directing PARP1 catalytic activity to glutamate and aspartate residues on histones (By similarity). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following mechanical or toxic insults (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11248244, ECO:0000269|PubMed:12574164, ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:22842230}.
Interaction partners:
- Nicotinamide phosphoribosyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Glutamine-dependent NAD
- Nicotinate phosphoribosyltransferase
- NAD-dependent protein deacetylase sirtuin-1
- Nicotinamide riboside kinase 1
- 5'-nucleotidase
- Nicotinamide riboside kinase 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- NAD-dependent protein deacetylase sirtuin-3, mitochondrial
Sequence:
MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGLIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTLERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVANYGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT
Protein: Ras-related protein Rab-27B (EC 3.6.5.2) (C25KG) (O00194)
Organism: Homo sapiens (Human)
Function: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion. Plays a role in NTRK2/TRKB axonal anterograde transport by facilitating the association of NTRK2/TRKB with KLC1. May be involved in targeting uroplakins to urothelial apical membranes (By similarity).
Subcellular location: Membrane; Lipid-anchor. Late endosome {ECO:0000269|PubMed:30771381}.
Interaction partners:
- Melanophilin
- Synaptotagmin-like protein 1
- Rab effector MyRIP
- Synaptotagmin-like protein 2
- Synaptotagmin-like protein 4
- Synaptotagmin-like protein 5
- Ras-related protein Rab-27A
- Protein unc-13 homolog D
- Unconventional myosin-Va
- CD63 antigen
Sequence:
MTDGDYDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVVYNAQGPNGSSGKAFKVHLQLWDTAGQERFRSLTTAFFRDAMGFLLMFDLTSQQSFLNVRNWMSQLQANAYCENPDIVLIGNKADLPDQREVNERQARELADKYGIPYFETSAATGQNVEKAVETLLDLIMKRMEQCVEKTQIPDTVNGGNSGNLDGEKPPEKKCIC
Protein: Nucleolar RNA binding protein, putative (Q38F23)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- HEAT repeat-containing protein 1
- H/ACA ribonucleoprotein complex subunit 2
- Uncharacterized protein
- BING4 C-terminal domain-containing protein
- KRR1 small subunit processome component
- Bms1-type G domain-containing protein
- U3 small nuclear ribonucleoprotein
- 40S ribosomal protein S13, putative
- U3 small nucleolar RNA-associated protein 6 N-terminal domain-containing protein
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
Sequence:
MSGAILVYIMLHTAYKTISSPTRVVMEKLNLGCRTTCDIRACHCSPVAECMFLPLLSLSTFLSIVCAALCFLRKMVFALLELPAGVGLFKVDGDKQKLKALLSFKSTADALATTTQVVNGELAKPVRKFLKKNFVEKQITEELAVADAKLAKAIKDALAIQCVHGDDTLATFRALRANLDDLLEDVSTEQLNQTALGLAHNLNRYKLKFSPDKVDMMVVQAVALLEDLDKEINKYAMRAREWYGWHFPELAKIVNDNILYAKIVLAAKTRFNVRDTDFSDFLEEELEQKVKDAAMVSMGTEIAEEDIENICRLCSEVVAASKYRESLAAYLSSRMQTIAPNLTTMVGEQIGARLIQKAGSLLSLAKYPSSTLQILGAEKALFRALKQRQATPKYGILYNAQVVAKAAATHKGAMSRVLAAKASLSARIDSFGEGDNSAALEYRGKVEERLRQFEEGVTYGRTGNVRGRGGGMQLQQKRGPPNGNGGGAPFKRQRLDGGGFR
Protein: Midkine (MK) (Q9R1S9)
Organism: Rattus norvegicus (Rat)
Function: Developmentally regulated, secreted growth factor homologous to pleiotrophin (PTN), which has heparin binding activity. Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation. Involved in neointima formation after arterial injury, possibly by mediating leukocyte recruitment. Also involved in early fetal adrenal gland development (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Tyrosine-protein kinase receptor
- Receptor-type tyrosine-protein phosphatase zeta
- Nucleolin
- Hepatoma-derived growth factor
- Pleiotrophin
Sequence:
MQHRSFFLLALVALLAVTTAVAKKKDKVKKGSECSEWTWGPCTPSSKDCGMGFREGTCGAQTQRIHCKVPCNWKKEFGADCKYKFESWGACDGSTGTKARQGTLKKARYNAQCQETIRVTKPCTSKTKSKAKAKKGKGKD
Protein: Sodium chloride cotransporter 69, isoform E (M9PI37)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase Wnk
- GH09711p
- GH08941p
Sequence:
MSDTISFELGSAADRPPNRFQVNPVNGNSRKSQGADGPGSGSGAGAGAGAGAGEDGPHEVYRRLTNAEGELLEDDTFDATQMLNQRQPRQQRQSIKSSFRDKDKPSRFKDLQTTTRFQVDPQNEESDESNDSQEERELLDNEYDTKYGKSFRHFTREALPRLDNYRNMMSIQAAYRPTLDELHNATLVGKNTHSLTRNQDPESGILNGVLKFGWIKGVLVRCLLNIWGVMLFLRLSWVVGQAGVIEGFVLILTTTAVTTITALSMSAISTNGVIKGGGTYYMISRSLGPEFGGSIGLIFSLANAVACAMYVVGFCESMLAMMTTFGWEIIDGGVQDVRIIGCITILLLLIIVVVGMEWEAKAQIGLLIILLVAIGDFVIGSFIGPKSDAEMAKGFLGYNATLFKNNLFADYRPEKGGIQHDFFSVFAIFFPAATGILAGANISGDLKDPQKSIPKGTILAIVITTGTYLIMVLQCGATVARDATGNLSDVVNGTFAFLDCQPGECNYGLQNSFQVIELVSAFGPLIYAGCYAATLSSALASLVSAPKVFQALCKDELYPKIVWFAKGYGKNNEPVRGYVLTFIIACAFILIGELNLIAPLISNFFLAAYMLINFSTFHASLAKPVGWRPTFKYYNMWLSLLGAILCVAVMFLISWATALITFAAVLALYLIVAYRKPDVNWGSTTQAQTYKNALMSVQQLNNVEEHVKNYRPQILVLSGLPNTRPVLVDLAYMLTKNLSLLVCGHVLKGSSSQKYRTYLQERAGNWFRKHRVKGFYALVDGEDFESGTRALMQATGIGKLKPNIILMGYKTDWQTCDHKELDQYFNVMHKALDMYLSVAILRVPQGLDCSQVLGSQDGWKTVSDVPRTLQPNESSGDLQAVDSSVRNGLSGSIDSLSRNVSQEDRNRNQLVHSEQNSLKIVKLRFKQGLRRMRSWPGAASSTSDLSFIAGNQSKDVSGMPDPLDAKSANLVSNSLRKSKLKHDDPASLYKGPGGAELPKEVLADLTQFTRKRSHAVIDVWWLYDDGGLTLLLPYIISTRRTWQSCKLRVYALANKNSELEFEQRSMASLLSKFRIDYSDLTLIPDITKKPQETSTQFFNELIKDFVVTEKDGENGTSSRATLNEDDALITDDDLLAVQDKTNRYLRLREYLREQSTKSDLVVMTLPMPRKNIVSAPLYMAWLESLSRDMPPFLFVRGNQTSVLTFYS
Protein: Iroquois-class homeodomain protein IRX-2 (Homeodomain protein IRXA2) (Iroquois homeobox protein 2) (Iroquois-class homeobox protein Irx6) (P81066)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Iroquois-class homeodomain protein IRX-1
Sequence:
MSYPQGYLYQAPGSLALYSCPAYGASALAAPRSEELARSASGSAFSPYPGSAAFTAQAATGFGSPLQYSADAAAAAAAGFPSYVGSPYDTHTTGMTGAISYHPYGSAAYPYQLNDPAYRKNATRDATATLKAWLNEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWAPRNKSEDEDEDEGDASRSKEESSDKAQDGTETSAEDEGISLHVDSLTDHSCSAESDGEKLPCRAGDALCESGSECKDKFEDLEDEEDEEDECERDLAPPKPVTSSPLTGVEAPLLSPAPEAAPRGGSGGKTPLGSRTSPGAPPPASKPKLWSLAEIATSDLKQPSLGPGCGPPGLPAAAAPASTGAPPGGSPYSASPLLGRHLYYTSPFYGNYTNYGNLNAALQGQGLLRYNTAASSPGETLHAMPKAASDTGKAGSHSLESHYRPPGGGYEPKKDTSEGCAVVGAGVQTYL
Protein: Protein spire (Q9U1K1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10744979}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10744979}. Cell membrane {ECO:0000269|PubMed:21730168}; Peripheral membrane protein {ECO:0000269|PubMed:21730168}; Cytoplasmic side {ECO:0000269|PubMed:21730168}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21730168}; Peripheral membrane protein {ECO:0000269|PubMed:21730168}; Cytoplasmic side {ECO:0000269|PubMed:21730168}. Note=Punctate spots in perinuclear region and cytoplasm. {ECO:0000269|PubMed:10744979}.
Interaction partners:
- Protein cappuccino
- Actin-5C
- DNA-binding protein K10
- Formin 3, isoform B
- Protein MON2 homolog
- Growth factor receptor-bound protein 2
- Dilute class unconventional myosin, isoform C
Sequence:
MTEHQAEEQADTPPTKVKATPTPTPSGKFKDAKEDAFLSTSPDSANGDAQHKLPADQLAMSSSAHPQQAGQARPLILQAFHRCSSPEQCVTLHDILDSFKAPLSEDQAWALIHQFAGLYHQVAVQAHTCAADYEAALPTGFELHFHRDGSVHFSGPDQLTPKEQLQQEQIPLPPQHDVIVDQPDHSASSSGDSSVINRAFDNSNHHHHHQHHHPPLVVSHRKIISELAEIVYTALDYNLPEDEECQVSQELENLFNFMTADETDDDCIDEGIDEGDKRWDDESEEERNDTKELEHIIETCRNHIKTTLPENHYRAVCRALVTETIELRVFLQQVLNNEAGAEKLIKASESSATTQQELAKLGFNDWARFWVQVIDELRRGVRLKKSNHERTPIEYELTPYEILMGDIRAKKYQLRKVMVNGDIPPRVKKDAHAMILEFIRSRPPLKKASDRQLGPPRMCEPSPREQLMESIRKGKELKQITPPEAPTLRERVLPSANSTLSRSRQRLIKVDFSKFQDDDLFYDENSISSSHSTAATHQHHPHFAEMHRCSQPKMPPYPFGGYMVPSQARQDCRETASLMRPRRTMEPAKQVPPPEEPSFTKDEYHKFYDTALESYDLATQCESRRASLRRHTIVGCQSNLDETHSMPPTRPESRQSDDVSKETPKRSPAEQTHPSDEGSSTSSLGPWNKSFMDKQTWMERGDDRLSVTLAEIVHIRSVMTKAELEGLPMDVRVKEDVEKRRVCFLCLRTRFSFFGPWGIQCKLCQRTVCAKCYTKMRIPSEHFRNVPLVLISPSLLSSPASSSTPSPSHHAQQAHSSSTGNIMDDQFPKSLIERLLRSESDRKTRSTVGSAPSSPKHQRSNMSTPGISVGPGASSSSAAATGQAVEALHDQATMSSSYSAAMRPSGVHQQQKQHYNNAMSRSMEGPRSLPVHSPAYRPLSNNSTLERKSRFSRGFNLFSSGSHLAQTQEQKENLRGEQVTVCNDCQGLVNEITSSVKQKRSSARNRTIQNLTLDLTPVWK
Protein: Flagellar protein FliT (P0ABY2)
Organism: Escherichia coli (strain K12)
Function: Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 2
- Flagella synthesis protein FlgN
- Negative regulator of flagellin synthesis
- Flagellum-specific ATP synthase
- Flagellar FliJ protein
- Flagellin
- Regulator of sigma S factor FliZ
- Flagellar biosynthetic protein FlhB
- Flagellar motor switch protein FliM
Sequence:
MNHAPHLYFAWQQLVEKSQLMLRLATEEQWDELIASEMAYVNAVQEIAHLTEEVDPSTTMQEQLRPMLRLILDNESKVKQLLQIRMDELAKLVGQSSVQKSVLSAYGDQGGFVLAPQDNLF
Protein: Exostosin family protein (Glycosyltransferase) (Q9LFL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MSGKQQNHRSTSSRPRSKTLILIGSLFTVSLLVILYTSSSSSRASISNPNPSDRPETSFVTSLEHFLIYKAPKLSLPVRDDTVRGESDDDVRKLDEMVFERENRWLNEDPGYPVEFPIKVYVYEMPKKFTFDLLWLFHNTYKETSNATSNGSPVHRLIEQHSIDYWLWADLISPESERRLKSVVRVQKQQDADFFYVPFFTTISFFLLEKQQCKALYREALKWVTDQPAWKRSEGRDHIFPIHHPWSFKSVRKFVKNAIWLLPDMDSTGNWYKPGQVSLEKDLILPYVPNVDICDTKCLSESAPMRTTLLFFRGRLKRNAGGKIRAKLGAELSGIKDIIISEGTAGEGGKLAAQRGMRRSLFCLCPAGDTPSSARLFDAIVSGCIPVIVSDELEFPFEGILDYKKVAVLVSSSDAIQPGWLVNHLRSLTPFQVKGLQNNLAQYSRHFLYSSPAQPLGPEDLTWRMIAGKLVNIKLHTRRSQRVVKGSRSICRCDCWRSNSTASNSLSSLLS
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q38AV2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TAP42-like protein
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MGFFSFKSNEKLKSGADGRNATGSGSIKPSGPTDGDGGFSGSSGRPVALTAEEHHEGVDPLGYMSHLPVTDIIELYTSFRNSLQECPDLVQKRYFVSTVKTLSSQMKLRDFSEKSISTHDGTKLPIVKRVLREVPSVRSRLALALQNFCHVTDWELENEEIECGTGLLATLRGESSRLRSGHEVDEGESAARLIPRMDSFDPTHIYNLVSTTDKLPSMQEMAELIRRTNELLLQEVNVVLVSAPCVVVGDIHGQKKDLIDNVLAAGGPIAPCGTDAVPEGKPDDGAAKPAGRNYLFLGDIVDRGPESLGCLALLFAAKLMAPKSVHLLRGNHESSETNRNYGFLRECWERYPINSPGGGGPTACTGGNTAMDCVWELQSHPLWVLANETFRSLPLCAVVTGEAASPSALPNCGKHREGDRQGGLTLCAMHGGLSPFIAESLDGILAVNRFRDIVDGPLADLTWADPVSALALFSPGNVAAAATTAGNVGSELSDTNNGAPPQQQEGRFQHHRMAVQRSEPVPTTSATVGHVLSSRGRGHNFGEDVTLRFLRKNKMDFIVRAHQCVMEGYEWQHQRRLLTLFSAPNYCGCGNKGAILIVHERGDPELVQFEAAGIQICGAIAAVSPKPSPVPPKEFCS
Protein: Membrane protein of ER body-like protein (Q8LPT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not essential for the accumulation of ER body components, including PYK10.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MGSAAELTEPTTGTEKLHQPIEVEEDDEQIVDLERKTFRHGKGHDTSVDSSTITNTSSSSSSSFSGDGGTEETPDFHSNGDGEHTDLVNLEVPELETEIVFHQEHDDGKNCIVFFDGEQGSESAGAIPDAHEESQTADLNGEQTQLEPENGSTSEDNERSREIEEVLDGDVSKDLDAVDPLAGEVIEEEVDFEDVEYHDVENMMDKQETHDLYCPNCDSCITKKVILKRRKRKIRRHELGDSKRPHLTEPLFHSEDNLPSLDGGENSANESFVFKCLSCFTIFIPKGVSSKPIPPRQGVEGLKIQPNPQVEATGDSNWFSSIFGLNKKESAIQQGGASSSVLEANPPPRESIVPVVNPSRGNLSPMRKDTTGSAVVQPDAATSIQVAKSNDTSEIVNNGAIVGDGQKFLAPMVEEQTQQKIDNDDSSTADGNHTSDKGRLSPIQPSHGMSILNTVTNGPDGLKVETTIHEEGAPLLFEGKDTPDTSTADFGLTKVTGVMDTGDRGVITGPANPEIDISAGNLLEEGSLREPLMRRVVVQGRKLEILKSIVYGGLLEAITSLGVISSAAGSGASMLNILVLGLANLLGGLILIIHNLQELREEEPIRTTTEDNQTNGREEEEGRYKRLLGRRENFTLHATVAILSFIITGILPPVVYYFSFSEKHNKDYKVASVFGASLFCIVLLAIAKAHVRYPRGSYLKSILYYGSIAVSVSGISYVVGNFLEQLLEKHGWSDGSETPVGQMMLSSLMGRKAGFGYSSSY
Protein: CLAVATA3/ESR (CLE)-related protein 40 [Cleaved into: CLE40p] (Q9LXU0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide secreted by differentiated root cells that regulates root cell fate. Acts with ACR4 as a ligand-receptor pair in a signal transduction pathway, coordinating movement of the root tip and organization of cell divisions in the root meristem. Promotes cell differentiation in the distal root meristem in a dose-dependent manner, especially the transition from columella stem cells (CSC) daughters into columella cells (CCs). Induces ACR4 expression in root quiescent center (QC). Involved in WUX5 QC-specific expression pattern regulation. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular location: [CLE40p]: Secreted, extracellular space {ECO:0000269|PubMed:12602871}.
Interaction partners:
- Serine/threonine-protein kinase-like protein ACR4
- Receptor protein kinase CLAVATA1
- WUSCHEL-related homeobox 5
- Protein CLAVATA 3
- CLAVATA3/ESR
- Receptor-like protein CLAVATA2
- CLAVATA3/ESR
- CLAVATA3/ESR
- Protein WUSCHEL
- CLAVATA3/ESR
Sequence:
MAAMKYKGSVFIILVILLLSSSLLAHSSSTKSFFWLGETQDTKAMKKEKKIDGGTANEVEERQVPTGSDPLHHKHIPFTP
Protein: Tubulin-folding cofactor E (AtTFCE) (Protein PFIFFERLING) (Q8GRL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential tubulin-folding protein involved in the tubulin folding pathway. Not essential for cell viability. Probably involved in the binding of alpha-tubulin in the multimeric supercomplex.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Tubulin-folding cofactor B
- Tubulin-folding cofactor D
- ADP-ribosylation factor-like protein 2
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 1
- SNARE associated Golgi protein family
- HEAT repeat-containing protein
- Glycine-rich protein
- Subtilisin-like protease SBT2.3
- At4g22860
Sequence:
MKAESSNESFIIGQRVHSLNDSRRVGTVKYVGDVEGYSGTWIGVDWDQDGDGKHNGSVNGVFYFNGRSQSSASFVRSQNLSRGITLLQALELRYRTISTKDEEDEMYVLSAGNRRVSIQLLGGDKIQDKLSRFEELTSASLSYLGVSSLGVSSDLGSILPNLKLLDLTGNLISDWEEIGALCEQLPALTTLNLSCNSLSSDIKSLPQLKNIRVLVLNNSGLSWTQVEILRRSLPGIEELHLMGNMISTITSTSSSDDQAFNSLRLLNLDDNCISDWSEVLKLSQLPCLEQLYLNKNKLSRIFQSVNGTESSEKGSDPFPSLSCLLLGANNIGDLASVDALNGFPQLVDIRLSENPISDPVRGGVPRFVLVARLTKVQVLNGSEVRAREKKDSEIRYVRMVMSKLNDKSGEIELLHPRFYELKKLHGIEDERASAENSGPKNIASGLISITLKCVGPSMGEKPHLTKKLPGSITVGKLKILSENFFKLKSIKPRLFLQEEGSPFPTALDDETATLLDVGICDGSTLLVDEES
Protein: Acetaldehyde dehydrogenase (EC 1.2.1.10) (Acetaldehyde dehydrogenase [acetylating]) (P77580)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE.
Interaction partners:
- 4-hydroxy-2-oxovalerate aldolase
- 2-keto-4-pentenoate hydratase
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Acetaldehyde dehydrogenase
- Aldehyde dehydrogenase B
- Formate acetyltransferase 1
- Phosphate acetyltransferase
- 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
- 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase
- Phosphate acetyltransferase EutD
Sequence:
MSKRKVAIIGSGNIGTDLMIKILRHGQHLEMAVMVGIDPQSDGLARARRMGVATTHEGVIGLMNMPEFADIDIVFDATSAGAHVKNDAALREAKPDIRLIDLTPAAIGPYCVPVVNLEANVDQLNVNMVTCGGQATIPMVAAVSRVARVHYAEIIASIASKSAGPGTRANIDEFTETTSRAIEVVGGAAKGKAIIVLNPAEPPLMMRDTVYVLSDEASQDDIEASINEMAEAVQAYVPGYRLKQRVQFEVIPQDKPVNLPGVGQFSGLKTAVWLEVEGAAHYLPAYAGNLDIMTSSALATAEKMAQSLARKAGEAA
Protein: NADPH--cytochrome P450 reductase 1 (CPR 1) (P450R 1) (EC 1.6.2.4) (A0A2U1LIM9)
Organism: Artemisia annua (Sweet wormwood)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes (By similarity). It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity). Involved in the biosynthesis of the antimalarial endoperoxide artemisinin. Acts as a redox partner for CYP71AV1 which catalyzes the conversion of amorphadiene to more oxygenated products.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- adenylyl-sulfate reductase
- adenylyl-sulfate reductase
- APS reductase 3
- assimilatory sulfite reductase
- assimilatory sulfite reductase
- Uncharacterized protein
- Ferredoxin--nitrite reductase, chloroplastic
- nitrate reductase
- Nitrate reductase
- Nitrate reductase
Sequence:
MQSTTSVKLSPFDLMTALLNGKVSFDTSNTSDTNIPLAVFMENRELLMILTTSVAVLIGCVVVLVWRRSSSAAKKAAESPVIVVPKKVTEDEVDDGRKKVTVFFGTQTGTAEGFAKALVEEAKARYEKAVFKVIDLDDYAAEDDEYEEKLKKESLAFFFLATYGDGEPTDNAARFYKWFTEGEEKGEWLEKLQYAVFGLGNRQYEHFNKIAKVVDEKLVEQGAKRLVPVGMGDDDQCIEDDFTAWKELVWPELDQLLRDEDDTSVATPYTAAVAEYRVVFHDKPETYDQDQLTNGHAVHDAQHPCRSNVAVKKELHSPLSDRSCTHLEFDISNTGLSYETGDHVGVYVENLSEVVDEAEKLIGLPPHTYFSVHTDNEDGTPLGGASLPPPFPPCTLRKALASYADVLSSPKKSALLALAAHATDSTEADRLKFLASPAGKDEYAQWIVASHRSLLEVMEAFPSAKPPLGVFFASVAPRLQPRYYSISSSPKFAPNRIHVTCALVYEQTPSGRVHKGVCSTWMKNAVPMTESQDCSWAPIYVRTSNFRLPSDPKVPVIMIGPGTGLAPFRGFLQERLAQKEAGTELGTAILFFGCRNRKVDFIYEDELNNFVETGALSELVTAFSREGATKEYVQHKMTQKASDIWNLLSEGAYLYVCGDAKGMAKDVHRTLHTIVQEQGSLDSSKAELYVKNLQMAGRYLRDVW
Protein: Regulation of enolase protein 1 (P40893)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the galactose metabolic pathway via the GAL83 protein and that it may control the level of ENO1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Putative acetyltransferase YJL218W
- Putative cystathionine beta-lyase
- Copper transport protein CTR3
- Catalase T
Sequence:
MVESKNTELSQGTWLNKPKSVFQEAGKVTLETDEKTDFWRETFYGFTRDSGHFLGVETGSAFTAQVRVQGSYESLYDQAGIMVRIDDGHWLKAGIEISDGHAMLSSVLTNGKSDWSTAVYGGNARDFWLRVTVEKGVLRIQVSSDKKTWPLVRLAPFPTSDHYLVGPMACTPERGGLKVTFSEWSLTAPLGKALHDLS
Protein: Carnitine operon protein CaiE (P39206)
Organism: Escherichia coli (strain K12)
Function: Overproduction of CaiE stimulates the activity of CaiB and CaiD.
Interaction partners:
- Carnitinyl-CoA dehydratase
- L-carnitine CoA-transferase
- Crotonobetaine/carnitine--CoA ligase
- Crotonobetainyl-CoA reductase
- L-carnitine/gamma-butyrobetaine antiporter
Sequence:
MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANIQDGCIMHGYCDTDTIVGENGHIGHGAILHGCLIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFRGEKRQLLMGTPARAVRNVSDDELHWKRLNTKEYQDLVGRCHVSLHETQPLRQMEENRPRLQGTTDVTPKR
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q6F3C9)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- FMRFamide-like neuropeptide 18
- FMRFamide-like neuropeptide 21
- G protein-coupled receptor EGL-6 isoform b
- FMRF-Like Peptide
- Neuropeptide-like protein 1
- G-protein coupled receptors family 1 profile domain-containing protein
Sequence:
MVSSAATISTISTTTTPSTISNVITSHSNNGSCIQIAEAIAAQGIDDITVDFYIRSIFTFLYGFLFVLGIFGNGGVLWAVARNKRLQSARNVFLLNLIFTDLILVFTAIPVTPWYAMTKDWAFGSVMCHLVPLSNSCSVFVTSWSLTAISLDKFLHINDPTKQPVSIRQALAITFLIWIVSTLINLPYLMSFEHVDGSFYVQPGETPYCGHFCDEANWQSENSRKIYGTTVMLLQFVVPMAVITYCYFKILQKVSKDMIIQNAQFCQSLTQKQRSDATSRKKKVNYILIAMVVTFIGCWLPLTLLNLVKDFKKEPEWLKRQPFFWAINAHVIAMSLVVWNPLLFFWLTRKQKRSGLSKILNSTEIVSSFASRVSNSIRRSTFRRNNIDRVRKKQVVLDCEGSSYTTSSRPLLIRTDVQATLSNGSTSTTREML
Protein: Rhombotin-1 (Cysteine-rich protein TTG-1) (LIM domain only protein 1) (LMO-1) (T-cell translocation protein 1) (Q924W9)
Organism: Mus musculus (Mouse)
Function: May be involved in gene regulation within neural lineage cells potentially by direct DNA binding or by binding to other transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:1703797}.
Interaction partners:
- LIM domain-binding protein 1
- T-cell acute lymphocytic leukemia protein 1 homolog
- Transcription factor E2-alpha
- T-cell acute lymphocytic leukemia protein 2 homolog
- Endothelial transcription factor GATA-2
- Erythroid transcription factor
- Helix-loop-helix protein 1
- Trans-acting T-cell-specific transcription factor GATA-3
- T-cell leukemia homeobox protein 1
- Protein lyl-1
Sequence:
MMVLDKEDGVPMLSVQPKGKQKGCAGCNRKIKDRYLLKALDKYWHEDCLKCACCDCRLGEVGSTLYTKANLILCRRDYLRLFGTTGNCAACSKLIPAFEMVMRARDNVYHLDCFACQLCNQRFCVGDKFFLKNNMILCQVDYEEGHLNGTFESQVQ
Protein: Mediator of RNA polymerase II transcription subunit 17 (Mediator complex subunit 17) (D4ABU0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364140}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 22
- Mediator complex subunit 12
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
Sequence:
MSGVRAVRISIESACEKQVQEVGLDGTETYLQPLSMSQNLARLAQRIDFSQGSGSEEEEAAGPDGDAPDWAGAGADQDDEEGLVKFQPSLWPWDSVRNNLRSALTEMCVLYDVLSIVRDKKFMTLDPVSQDALPPKQSPQTLQLISKKKSLAGAAQILLKGAERLTKSVTENQENKLQRDFNSELLRLRQHWKLRKVGDKILGDLSYRSAGSLFPHHGTFEVIKNTDIDLDKKIPEDYCPLDVQIPSDLEGSAYIKVSIQKQAPDIGDLGTVNLFKRPLPKSKPGSPHWQTKLEAAQNVLLCKEIFAQLSREAVQIKSQIPHIVVKNQIISQPFPSLQLSISLCHSSDDKKSQKCAPEKPGQEGHLYVLEHNLHLLIREFHKQTLSSIVMPHPASAPFGHKRMRLSGPQAFDKNEINSIQSTEGLLEKIIKQAKHIFLRSRTAATIDSLASRIEDPQIQAHWSNINDVYESSVKVLITSQGYEQICKSIQLQLNIGVEQVRVVHRDGRVITLSHQEQELQDFLLSQMSQHQVHAVQQLAKVMGWQVLSFSNHVGLGPIESIGNASAITVASPSGDYAISVRNGPESGSKIMVQFPRNQCKDLPKSDVLQDSKWSHLRGPFKEVQWNKMEGRNFVYKMELLMSALSPCLL