wanglab/gogpt-training-data huggingface dataset:
Protein: Dynamin-like protein A (EC 3.6.5.5) (Q55F94)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in cytokinesis. May hydrolyze GTP.
Subcellular location: Cytoplasm {ECO:0000305}. Cleavage furrow {ECO:0000269|PubMed:18809930}. Note=During cytokinesis, found in the cleavage furrow.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Dynamin N-terminal domain-containing protein
- Guanylate-binding protein
- Dynactin subunit 2
Sequence:
MSVFKKKDKSDDKKKKHDEETPQGTFQPASQSTSNTNLNSLASSVNNGASVGSTNGSTPNNSNGSTPTYNHNNSAEELEKQKKEEDEKRKKSELEAAAAVVAKKKEDEEKQRKEQVELERKRRDEEIRRTNAAAANAANKELNEQVEISSLEQMGKLDPSSTIHDMFSFFPNEVYNSYEKLQYFSRDLNTAVSHPEIVFVGPRSSGKSSLIEAFIGRALNIVGGGNIVGVGGSNANGCSKRVLYLQFTNNIDFEVPKVTIKKDNTIKEFDHDIIVSIEQLNENLAKRNQLTNDYIEEPIYVSIESRTTLNLTLIDSPGLLFDQSQAESNKIESIVSSLLRPSHRLIIAVESCSQDWKSMSMGQYLKKIDPELSRSTFVFTKFHHTVRGFSSTRDINKYLSGTVPDIKGFFVTLPNHQVRASYSEANRFQEKIYQAHKRDMHALEQLQYDKRYERTIGVAPLRRYILNIVWKSYQDTIPRILKHLRSKRQTAEATLNELQKQSSSLDSTKLRSIASNYTVTFLQITEKLLSGTSEGNPSANGQTLDEEKSQQGDCGEWVDAYKEAIYIDPEEWNIPYWSSKLYGGQQLERLMAEFKAVCDNSKISEVKMDDIATASGINKLNNIPNYAWAASDLTSLISRDTFVPLIEQLCERAMYIMKRLTDIADKVIDSRRKSRCIGSSPFGGNGLNNINSGGNNGININDRLSNTDMDSLDQYPFFTHHVKNLYYDFVHRAAKGCKEKCMDEFYSSRTIYWELTEHPDSSLPSIRNDHHETKTAVCQLATKLFDSIRQRITKNVLLKLYNFFLVPMQTDLWNEIQAQITCLSNEQLEQLFEVQATREQLKQEEKKQQQILEKYSQIDEQFLKAASLFCRPLSNPTPSA
Protein: Amun, isoform A (Amun, isoform B) (Amun, isoform E) (Amun, isoform F) (Amun, isoform G) (Amun, isoform H) (Amun, isoform I) (Amun, isoform K) (Amun, isoform L) (GH02702p) (Q9VYV4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- F-actin-capping protein subunit beta
- Dynactin subunit 2
- Actin-related protein 10, isoform A
- Dynactin subunit 4
- Twinfilin
- Leucine-rich repeat, isoform F
- CIN85 and CD2AP related, isoform J
Sequence:
MSNGKATVSFFETGSTKQFEYCYQLYPQVLKLKAEKRCKKPQELIRLDQWYQNELPKLIKARGKDAHMVYDELVQSMKWKQSRGKFYPQLSYLVKVNTPRAVIQETKKAFRKLPNLEQAITALSNLKGVGTTMASALLAAAAPDSAPFMADECLMAIPEIEGIDYTTKEYLNFVNHIQATVERLNAEVGGDTPHWSPHRVELALWSHYVANDLSPEMLDDMPPPGSGASTGTGSLSTNGNSSKVLDGDDTNDGVGVDLDDESQGAGGRNTATESETENENTNPAALTPLQSGEAKNNAAAVGAALQDGDSNFVSNDSTSQEPIIDDNDGTTQTTATTSTEDGEPIALDIGIGIGSSGTPLASDSESNQEAPPKTNSLPILTPTQHSSQNQNQKQSPSQPHKTNNSITNNGQPAPLAEEEAVTAAPQPASKATAAPANGNGNGNGVLGDEDEDEAEDEEEDELDEEEDNEAELEADESNSSNGIVRDSKLQQLAANKAVDAVSPVAAGADSAPAIGQKRTALHCDMELKNAGGVGVGVGEKSPDLKKLRSE
Protein: NAC domain-containing protein 92 (ANAC092) (AtNAC2) (AtNAC6) (Protein ORESARA 1) (Q9FKA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds to DNA in promoters of target genes on a specific bipartite motif 5'-[ACG][CA]GT[AG](5-6n)[CT]AC[AG]-3'. Promotes lateral root development. Triggers the expression of senescence-associated genes during age-, salt- and dark-induced senescence through a regulatory network that may involve cross-talk with salt- and H(2)O(2)-dependent signaling pathways. Regulates also genes during seed germination. Regulates positively aging-induced cell death. Involved in age-related resistance (ARR) against Pseudomonas syringae pv. tomato and Hyaloperonospora arabidopsidis. Antagonizes GLK1 and GLK2 transcriptional activity, shifting the balance from chloroplast maintenance towards deterioration during leaf senescence. Promotes the expression of senescence-associated genes, including ENDO1/BFN1, SWEET15/SAG29 and SINA1/At3g13672, during senescence onset.
Subcellular location: Nucleus {ECO:0000269|PubMed:16359384, ECO:0000269|PubMed:23459204, ECO:0000269|PubMed:30374089}. Note=Localizes in the nucleus, where it interacts with NLA. {ECO:0000269|PubMed:30374089}.
Interaction partners:
- Senescence-specific cysteine protease SAG12
- Magnesium dechelatase SGR1, chloroplastic
- Ethylene-insensitive protein 2
- Transcription activator GLK2
- Transcription activator GLK1
- Protein ETHYLENE INSENSITIVE 3
- Probable chlorophyll
- Senescence-associated protein 13
- Bidirectional sugar transporter SWEET15
- E3 ubiquitin-protein ligase NLA
Sequence:
MDYEASRIVEMVEDEEHIDLPPGFRFHPTDEELITHYLKPKVFNTFFSATAIGEVDLNKIEPWDLPWKAKMGEKEWYFFCVRDRKYPTGLRTNRATEAGYWKATGKDKEIFKGKSLVGMKKTLVFYKGRAPKGVKTNWVMHEYRLEGKYCIENLPQTAKNEWVICRVFQKRADGTKVPMSMLDPHINRMEPAGLPSLMDCSQRDSFTGSSSHVTCFSDQETEDKRLVHESKDGFGSLFYSDPLFLQDNYSLMKLLLDGQETQFSGKPFDGRDSSGTEELDCVWNF
Protein: Translation initiation factor IF-3, mitochondrial (IF-3(Mt)) (IF-3Mt) (IF3(mt)) (IF3mt) (Q32KZ1)
Organism: Bos taurus (Bovine)
Function: IF-3 binds to the 28S ribosomal subunit and shifts the equilibrum between 55S ribosomes and their 39S and 28S subunits in favor of the free subunits, thus enhancing the availability of 28S subunits on which protein synthesis initiation begins.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Translation initiation factor IF-2, mitochondrial
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS22
- Alpha-ketoglutarate dehydrogenase component 4
- Ribosome binding factor A
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein mS35
Sequence:
MAALFLKKLTLQTVKTENYCIRRCLGKYILQGPAPTQQPPRPSCLIHAKAFSTEDTQDEMTKKKKNETAFSSVGRKINERIIHVLDEQGNDLGHMHRANVIRLMAERDLRLVKRDASAEPPQYQLLTGAQIHQERLRLREAERAAPKPGPTLTKELTFSSNIGQHDLDTKSKQIQQWIEKKYKVQITVKKGKSADEPEDKMEEMCNRIVQTMSGIATFSSRPQPIRGGKAVMCVLRPLSKKEEAAWKAAPDTPRRDALNGGDGKDGASGVLPQ
Protein: RNA 2'-O-methyltransferase FBLL1 (EC 2.1.1.-) (Fibrillarin like 1) (Q80WS3)
Organism: Mus musculus (Mouse)
Function: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Also acts as a protein methyltransferase by mediating methylation of glutamine residues (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:A6NHQ2}.
Interaction partners:
- Nucleolar protein 56
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit DKC1
- NHP2-like protein 1
- Periodic tryptophan protein 2 homolog
- Nucleolar protein 6
- H/ACA ribonucleoprotein complex subunit 1
- U3 small nucleolar RNA-interacting protein 2
- WD repeat domain 36
- WD repeat-containing protein 46
Sequence:
MKPAGGRGGWGWGGGKGGSKGGDTGSGTKGGFGARTRGSSGGGRGRGRGGGGGGGGGGGDRQRRGGPGKNKNRRKKGITVSVEPHRHEGVFIYRGAEDALVTLNMVPGVSVYGEKRVTVMENGEKQEYRTWNPFRSKLAAAILGGVDQIHIKPKSKVLYLGAASGTTVSHVSDIIGPDGLVYAVEFSHRAGRDLVNVAKKRTNIIPVLEDARHPLKYRMLIGMVDVIFADVAQPDQSRIVALNAHTFLRNGGHFLISIKANCIDSTASAEAVFASEVRKLQQENLKPQEQLTLEPYERDHAVVVGVYRPPPKSK
Protein: Membrane protein insertase YidC (Foldase YidC) (Membrane integrase YidC) (Membrane protein YidC) (P9WIT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Putative membrane protein insertion efficiency factor
- Ribonuclease P protein component
- Protein translocase subunit SecY
- Conserved protein similar to jag protein
- Probable protein-export membrane protein SecG
- Protein translocase subunit SecE
- Protein translocase subunit SecA 1
- Protein translocase subunit SecD
- Signal recognition particle protein
- Protein translocase subunit SecA 2
Sequence:
MSLLFDFFSLDFIYYPVSWIMWVWYRLFAFVLGPSNFFAWALSVMFLVFTLRALLYKPFVRQIRTTRQMQELQPQIKALQKKYGKDRQRMALEMQKLQREHGFNPILGCLPMLAQIPVFLGLYHVLRSFNRTTGGFGQPHLSVIENRLTGNYVFSPVDVGHFLDANLFGAPIGAYMTQRSGLDAFVDFSRPALIAVGVPVMILAGIATYFNSRASIARQSAEAAANPQTAMMNKLALYVFPLGVVVGGPFLPLAIILYWFSNNIWTFGQQHYVFGMIEKEEEAKKQEAVRRRAANAPAPGAKPKRSPKTAPATNAAAPTEAGDTDDGAESDASTERPADTSNPARRNSGPSARTPRPGVRPKKRKR
Protein: Calcium release-activated calcium channel protein 1 (Protein orai-1) (Transmembrane protein 142A) (Q8BWG9)
Organism: Mus musculus (Mouse)
Function: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit which mediates Ca(2+) influx following depletion of intracellular Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1. CRAC channels are the main pathway for Ca(2+) influx in T-cells and promote the immune response to pathogens by activating the transcription factor NFAT (By similarity). Plays a prominent role in Ca(2+) influx at the basolateral membrane of mammary epithelial cells independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May mediate transepithelial transport of large quantities of Ca(2+) for milk secretion (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96D31}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96D31}. Basolateral cell membrane {ECO:0000269|PubMed:23840669}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96D31}. Note=Colocalizes with STIM1 in membrane punctate structures at ER-PM junctions. {ECO:0000250|UniProtKB:Q96D31}.
Interaction partners:
- Stromal interaction molecule 1
- Stromal interaction molecule 2
- Protein orai-2
- Protein orai-3
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Short transient receptor potential channel 1
Sequence:
MHPEPAPPPSHSNPELPVSGGSSTSGSRRSRRRSGDGEPSGAPPLPPPPPAVSYPDWIGQSYSEVMSLNEHSMQALSWRKLYLSRAKLKASSRTSALLSGFAMVAMVEVQLDTDHDYPPGLLIVFSACTTVLVAVHLFALMISTCILPNIEAVSNVHNLNSVKESPHERMHRHIELAWAFSTVIGTLLFLAEVVLLCWVKFLPLKRQAGQPSPTKPPAESVIVANHSDSSGITPGEAAAIASTAIMVPCGLVFIVFAVHFYRSLVSHKTDRQFQELNELAEFARLQDQLDHRGDHSLTPGTHYA
Protein: Lupeol synthase (GgLUS1) (EC 5.4.99.41) (Q764T8)
Organism: Glycyrrhiza glabra (Licorice)
Function: Oxidosqualene cyclase involved in the biosynthesis of lupeol. Required for the production of betulinic acid.
Interaction partners:
Sequence:
MWKLKIGEGGAGLISVNNFIGRQHWEFDPNAGTPQEHAEIERLRREFTKNRFSIKQSADLLMRMQLRKENHYGTNNNIPAAVKLSDAENITVEALVTTITRAISFYSSIQAHDGHWPAESAGPLFFLQPLVMALYITGSLDDVLGPEHKKEIVRYLYNHQNEDGGWGFHIEGHSTMFGSALSYVALRILGEGPQDKAMAKGRKWILDHGGLVAIPSWGKFWVTVLGAYEWSGCNPLPPELWLLPKFAPFHPGKMLCYCRLVYMPMSYLYGKKFVGPITALIRSLREELYNEPYNQINWNTARNTVAKEDLYYPHPLIQDMLWGFLYHVGERFLNCWPFSMLRRKALEIAINHVHYEDENSRYLCIGSVEKVLCLIARWVEDPNSEAYKLHLARIPDYFWLAEDGLKIQSFGCQMWDAAFAIQAILACNVSEEYGPTLRKAHHFVKASQVRENPSGDFNAMYRHISKGAWTFSMHDHGWQVSDCTAEGLKAALLLSEMPSELVGGKMETERFYDAVNVILSLQSSNGGFPAWEPQKAYRWLEKFNPTEFFEDTMIEREYVECTGSAMQGLALFRKQFPQHRSKEIDRCIAKAIRYIENMQNPDGSWYGCWGICYTYGTWFAVEGLTACGKNCHNSLSLRKACQFLLSKQLPNAGWGESYLSSQNKVYTNLEGNRANLVQSSWALLSLTHAGQAEIDPTPIHRGMKLLINSQMEDGDFPQQEITGVFMRNCTLNYSSYRNIFPIWAMGEYRRQVLCAHSY
Protein: Cysteine desulfurase IscS (PfIscS) (EC 2.8.1.7) (Q8IBI5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24086138}.
Interaction partners:
- Iron-sulfur cluster assembly protein IscU
- Rhodanese like protein, putative
- Probable molybdopterin-synthase adenylyltransferase
- Adrenodoxin-type ferredoxin, putative
- Protein Isd11
- NifU-like protein, putative
- NifU-like scaffold protein
- Chaperone, putative
- NADH-cytochrome b5 reductase, putative
Sequence:
MKFLQIIKHLKLQNKKNALDNFVNCRTYEHISNINKLFLNNFSSTKEHSEHGQVKHENFLNSTLKYEENSQNGSTNNLKNGKYNMYVSEGNVNINEEKYKDNNISSNNTQYNNNSSNSGSLNDEGPLWKEHIDDVVNENKKKKMNRFYLDSQATTMIDPRVLDKMLPYMTYIYGNAHSRNHFFGWESEKAVEDARTNLLNLINGKNNKEIIFTSGATESNNLALIGICTYYNKLNKQKNHIITSQIEHKCILQTCRFLQTKGFEVTYLKPDTNGLVKLDDIKNSIKDNTIMASFIFVNNEIGVIQDIENIGNLCKEKNILFHTDASQAAGKVPIDVQKMNIDLMSMSGHKLYGPKGIGALYIKRKKPNIRLNALIHGGGQERGLRSGTLPTHLIVGFGEAAKVCSLEMNRDEKKVRYFFNYVKDYLTKHLDYIVFNGCQINRYYGNMNISFLFVEGESLLMSLNEIALSSGSACTSSTLEPSYVLRSIGISEDIAHTSIRIGFNRFTTFFEVQQLCINLVKSVERLRSISPLYEMELEKKNPSNDDIPKFIWT
Protein: Dynein light chain Tctex-type protein 2B (Tctex1 domain-containing protein 2) (Q8WW35)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. Required for proper retrograde ciliary transport.
Subcellular location: Dynein axonemal particle {ECO:0000305}.
Interaction partners:
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 2
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain Tctex-type 1
- Dynein light chain roadblock-type 1
- Dynein light chain roadblock-type 2
- Cytoplasmic dynein 2 heavy chain 1
- Dynein light chain Tctex-type 3
- Dynein light chain 1, cytoplasmic
- Dynein light chain 2, cytoplasmic
Sequence:
MATSIGVSFSVGDGVPEAEKNAGEPENTYILRPVFQQRFRPSVVKDCIHAVLKEELANAEYSPEEMPQLTKHLSENIKDKLKEMGFDRYKMVVQVVIGEQRGEGVFMASRCFWDADTDNYTHDVFMNDSLFCVVAAFGCFYY
Protein: Opsin-5 (G-protein coupled receptor 136) (G-protein coupled receptor PGR12) (Neuropsin) (Transmembrane protein 13) (Q6U736)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor which selectively activates G(i) type G proteins via ultraviolet A (UVA) light-mediated activation in the retina (By similarity). Preferentially binds the chromophore 11-cis retinal and is a bistable protein that displays emission peaks at 380 nm (UVA light) and 470 nm (blue light). Required for the light-response in the inner plexiform layer, and contributes to the regulation of the light-response in the nerve fiber layer, via phosphorylated DAT/SLC6A3 dopamine uptake (By similarity). Involved in local corneal and retinal circadian rhythm photoentrainment via modulation of the UVA light-induced phase-shift of the retina clock (By similarity). Acts as a circadian photoreceptor in the outer ear, via modulation of circadian clock-gene expression in response to violet light during the light-to-dark transition phase and night phase of the circadian cycle (By similarity). Required in the retina to negatively regulate hyaloid vessel regression during postnatal development via light-dependent OPN5-SLC32A1-DRD2-VEGFR2 signaling (By similarity). Involved in the light-dependent regulation of retina and vitreous compartment dopamine levels (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase
- Guanine nucleotide-binding protein G
Sequence:
MALNHTALPQDERLPHYLRDGDPFASKLSWEADLVAGFYLTIIGILSTFGNGYVLYMSSRRKKKLRPAEIMTINLAVCDLGISVVGKPFTIISCFCHRWVFGWIGCRWYGWAGFFFGCGSLITMTAVSLDRYLKICYLSYGVWLKRKHAYICLAAIWAYASFWTTMPLVGLGDYVPEPFGTSCTLDWWLAQASVGGQVFILNILFFCLLLPTAVIVFSYVKIIAKVKSSSKEVAHFDSRIHSSHVLEMKLTKVAMLICAGFLIAWIPYAVVSVWSAFGRPDSIPIQLSVVPTLLAKSAAMYNPIIYQVIDYKFACCQTGGLKATKKKSLEGFRLHTVTTVRKSSAVLEIHEEWE
Protein: Formin-binding protein 4 (Formin-binding protein 30) (Q8N3X1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKKSRAVPGRRPILQLSPPGPRGSTPGRDPEPEPDTEPDSTAAVPSQPAPSAATTTTTAVTAAAASDDSPSEDEQEAVQEVPRVVQNPPKPVMTTRPTAVKATGGLCLLGAYADSDDDDNDVSEKLAQSKETNGNQSTDIDSTLANFLAEIDAITAPQPAAPVGASAPPPTPPRPEPKEAATSTLSSSTSNGTDSTQTSGWQYDTQCSLAGVGIEMGDWQEVWDENTGCYYYWNTQTNEVTWELPQYLATQVQGLQHYQPSSVPGAETSFVVNTDIYSKEKTISVSSSKSGPVIAKREVKKEVNEGIQALSNSEEEKKGVAASLLAPLLPEGIKEEEERWRRKVICKEEPVSEVKETSTTVEEATTIVKPQEIMLDNIEDPSQEDLCSVVQSGESEEEEEQDTLELELVLERKKAELRALEEGDGSVSGSSPRSDISQPASQDGMRRLMSKRGKWKMFVRATSPESTSRSSSKTGRDTPENGETAIGAENSEKIDENSDKEMEVEESPEKIKVQTTPKVEEEQDLKFQIGELANTLTSKFEFLGINRQSISNFHVLLLQTETRIADWREGALNGNYLKRKLQDAAEQLKQYEINATPKGWSCHWDRDHRRYFYVNEQSGESQWEFPDGEEEEEESQAQENRDETLAKQTLKDKTGTDSNSTESSETSTGSLCKESFSGQVSSSSLMPLTPFWTLLQSNVPVLQPPLPLEMPPPPPPPPESPPPPPPPPPPAEDGEIQEVEMEDEGSEEPPAPGTEEDTPLKPSAQTTVVTSQSSVDSTISSSSSTKGIKRKATEISTAVVQRSATIGSSPVLYSQSAIATGHQAAGIGNQATGIGHQTIPVSLPAAGMGHQARGMSLQSNYLGLAAAPAIMSYAECSVPIGVTAPSLQPVQARGAVPTATIIEPPPPPPPPPPPPPPAPKMPPPEKTKKGRKDKAKKSKTKMPSLVKKWQSIQRELDEEDNSSSSEEDRESTAQKRIEEWKQQQLVSGMAERNANFEALPEDWRARLKRRKMAPNT
Protein: Probable CAAX prenyl protease 2 (EC 3.4.26.1) (Prenyl protein-specific endoprotease 2) (PPSEP 2) (O94448)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Proteolytically removes the C-terminal three residues of farnesylated proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q03530}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable CAAX prenyl protease 1
- Protein-S-isoprenylcysteine O-methyltransferase
- Protein farnesyltransferase subunit beta
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Acyl-protein thioesterase 1
- Pheromone-processing carboxypeptidase kex1
Sequence:
MRVYLISFFFTAIYVVSLYTFPVARPRPSLNRNDPKVITARCISVLLASSVCCILTRLIIGPSLNVFTFPTDQVLKSLLHAATIFIGPLYEVWIVDKEYRLFFIHLKDCLSNAIAWRNIIIGPLSEELTFRCCIVPICEAAGWSRLKIIFVAPLLFGMAHIHHTYEFLLAYPNAYIAAALQTVVQFSYTTVFGWYTTHLFLSTHSLFPSFLVHAFCNSMGLPTLYGKIGNRNQTRIYYTLLLLGVLIFYMTWGITDFNNHQDFEPRLVPLN
Protein: Golgi pH regulator conserved domain-containing protein (Q580H0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Pyroglutamyl-peptidase I
Sequence:
MLLKLGAVLLLLVLYHVGSLFSRLVFVYTIQQGTTKFCFRFVFALSTYAFILLLLDASQVSERIKSNFSIQTLRCVLAVDLVLIALFCPFLVVRSLLPNVRLYYFFLVLLACGLVKMLFGASVAAWSWTLSSTQGIPTLFSWDVVSVAVSTTGVVVVGLLSGYAAVTTPLAFVEPLFEHGSGDQARLAVGVLAKRQKHLLELWMLKRQQIARAYGAVSRADGGRDGSNRGSIAAGRRMWNWVANSIYSSVRASGADIAAMETESDGIRAVSMAVFLQMSEMDTLVRSAGSGETWRRRFNALFGLILFTHALVKFLSTVISLLRWGVLAAENAAPHREDTATKVMNFLEAYGLATPHGDGAEQRVVWVSIALNAWMIASAIRGFFLLVFRLTTHIAFISLDTTVTILTAGMGAFFVGQLVLLRLTPSLERESVLYTALREQLPQHGAYCHLNDLVFVVAAALVAMMRRCMFSSSATALCAAAD
Protein: Hypoxanthine phosphoribosyltransferase (HPRT) (EC 2.4.2.8) (6-oxopurine phosphoribosyltransferase) (6-oxopurine PRTase) (P0A9M2)
Organism: Escherichia coli (strain K12)
Function: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine.
Subcellular location: Cytoplasm.
Interaction partners:
- Xanthine-guanine phosphoribosyltransferase
- Adenine phosphoribosyltransferase
- Adenylosuccinate synthetase
- GMP synthase
- Guanylate kinase
- Guanosine-inosine kinase
- Inosine-5'-monophosphate dehydrogenase
- Adenylate kinase
- Bifunctional purine biosynthesis protein PurH
- Purine nucleoside phosphorylase DeoD-type
Sequence:
MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVGLLRGSFMFMADLCREVQVSHEVDFMTASSYGSGMSTTRDVKILKDLDEDIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLLDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRHLPYIGKVILLDE
Protein: Probable ubiquitin receptor RAD23a (AtRAD23a) (Putative DNA repair protein RAD23-2) (RAD23-like protein 2) (AtRAD23-2) (Q84L32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in nucleotide excision repair (By similarity). Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-48'-linked ubiquitin chains. Acts as a ubiquitin receptor that associates with the 26S proteasomal docking subunit RPN10 for the indirect recognition of ubiquitinated substrates of ubiquitin/26S proteasome-mediated proteolysis (UPP) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20086187}. Cytoplasm {ECO:0000269|PubMed:20086187}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- DNA repair protein RAD4
- Peptide-N
- Probable ubiquitin conjugation factor E4
- 26S proteasome regulatory subunit RPN13
- Ubiquitin domain-containing protein DSK2b
- Protein NBR1 homolog
- Protein DNA-DAMAGE INDUCIBLE 1
- Calcium-binding protein CML19
- Ubiquitin domain-containing protein DSK2a
Sequence:
MKLTVKTLKGSHFEIRVLPTDTIMAVKKNIEDSQSKDNYPCGQQLLIHNGKVLKDETTLVENKVTEEGFLVVMLSKSKTASSAGPSSTQPTSTTTSTISSTTLAAPSTTQSIAVPASNSTPVQEQPTAQSDTYGQAASTLVSGSSIEQMVQQIMEMGGGSWDKETVTRALRAAYNNPERAVDYLYSGIPETVTIPATNLSGVGSGRELTAPPPSGGPNSSPLDLFPQEAVSDAAGGDLGTLEFLRGNDQFQQLRSMVNSNPQILQPMLQELGKQNPQLLRLIQENQAEFLQLLNEPYEGSDGDVDIFDQPDQEMPHSVNVTPEEQESIERLEAMGFDRAIVIEAFLSCDRNEELAANYLLEHSADFED
Protein: DNA damage-binding protein 1 (Q586I3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein
- Cullin family profile domain-containing protein
- Cullin 4B, putative
- DNA excision repair protein, putative
- Protein artemis
- Telomerase-associated protein, putative
- COP9 signalosome complex subunit 5
- PCI domain-containing protein
- DNA-directed RNA polymerase subunit beta
- RING-type domain-containing protein
Sequence:
MPFLASTTKPPTAVSGAVTGNFLGDGEKLVLLSRLNIVSLFRADDHSFEHVADFSLFASLRFVESLPLFDNRGCGRHVVFFLSVKQEVSVVAFERRNNGLIGMVTLFHGDVETYFHQGKINDASLCCSGVYRSTTGNLLPIVIFSIYRGGVIGFDVAAAISGYSRDSKTAAAALNALFPSDYVQGVLKKTKRRSNFAHGNFAAAEIDVRSIALDHRDGIDGAVSLLVLYADLTGKTHVSEYLVNFWRNADQRRVPKTQGRSRIPEALNILPGGDIIQRKGLLSTSVETNACLLHVVPDGFFILGPQLLNFCSWKSSGVQSGSSKNVTTLEVPRLGAYVEPVCCATLPGQELLILFEDGSYLKVSVRDDCEGLNSGKSMLSQSSGAPLRTIPKCVAVVGECCVVGSHMDHTLWMRWLTGESGVLVYNCGPVFDVTVAADGSRTSVIAGTGVGLNGGLSFVRSAVSVRQDIRVTGLQNVRQISVSEDTIIFSLPGYSRVCRYCVGETMVLEEIHNTFFGTEETLLLEYNNERNVFLQVTTAGLRNVWPDRGEYVIRVINNDIGHAHASEGLLVFSNPANLYVFCMKTLTPVATLCLADAISCLLVFSSSSLLVGTWGSCAVHLYELHDGMIQSKVILQCSATPCSMCVVFHSGGHRLLVGLHNGYVADVPISGANVCGEMVETMLTTQPVRLFNLESHAAVLCLGEIPLILIVTNTGFQLTGIDFRDVSACAIMPKMRSPSRYIFFSKSECALILGSITSVQKLNTDYVGLKATATCVKYMPWWNVLVLSIRRIEKDQVVSTMGHEVSNLSVLLDEPNSFELLENERCAFIDCVALGQANEWGSCGEVASDAGVVLIGTTFVFPDEQLSRSSRFMWCTVEVAKLRTEKTLLRLQGSKDVEGALQCCCIVPNYAGRVALGIGGCVVLYSWNAADATFVAEETIQIGTLIVRLIPVMQKEVSYIVASDARHSCFFVRIDTIQGSLNIVARDPELRGVMDCAILQYESRHDVCLGDDLFNFFCVSHVEPLANSSGVSAPAMPTKKLQTTAQYHMGDLITVMHQGSFAPCSVLNDVVPIPATLVRGVCGPQIVYGTSHGAFGAITPISSETFILLKGLEVSVASVVPPLGGFTHASFREVLRVGQERGASRNASFQVTNPQATELFNRRRRRCVPRGVCCGDVVEMFLTLSGGDQLRVVQEANQHVRRWFAYAWPTLEEYAMSDLDDFSSNQGDELAPDRIVDAEINSLLLRQALPTLSLTVEAVTAFIQTIQRIH
Protein: K Homology domain-containing protein (Q9W2D0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- K Homology domain-containing protein
Sequence:
MEKMENPSEITEEQPTTTHEYQPRLNEIAQKFLADLDEERQRLSAEFPLCALLIDEARDRVYATGRIPGKELYADVYRQKPMKIIQKVFVPVNQYPKFNFAGKILGPKGNSLRRLQEETQCKIALKGRSSMRDRNKEEELRSDPRYAHLQKNLFLEVSTVAIPAECHSRIAYALAEIRKYLIPDNNDEVSHEQLRELMEIDPESAKNFKGLNLEAYRSVRDSNGASKYINLIKRVAENPSKVADMEQVDYDYDEHHMPPIHLPTGYEYSIQRPSKIVAKFKRPYPYPTDMKPVREPPIKFYKPNPGIGTYVMKSMLGAQ
Protein: FI01201p (Jim zinc finger protein) (Jim, isoform C) (Jim, isoform D) (Jim, isoform H) (Q7KAH0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAINFSASFAACIAAGLKVPRQIMYCITQDTGQPYVLYKDSQDAERNPGAIGATPAQWGSEMYPNIQQQAQQHLTAQQQQQQQQQNAAQAAAQAAAVAAAAGQPQSPPGGGQEARDNGSGDGRQQQVSPSSSPYPSVQQQQRANGAGDEDPMNHQLANQQNPAPNQNQSSNDPQHSGSNAGESGNPHVQQNGGPQNDPGNSFRTPDYYDPRHAAPQGGMLAPPGFPPLHYLNKGVLPMEQSGGGGGAGGGEAYALPEMLPAQQNGQQNAGPANTNANEGGAGANGSGGVGGATGASVGVGSVGVTSGGRTGNGPGRPHKNKPHSDLRLFKCLTCGKDFKQKSTLLQHDRIHTDARPFPCSECGKRFRQQSHLTQHLRIHANEKPFTCPYCSRSFRQRAILNQHIRIHSGEKPFACPECGKHFRQKAILNQHVRTHQDVSPHLIFKNGPHPTLWPSDVPFPGEDNDTKGDIAGTGGGYHDEDSQGTPDGSGGMHYPSYFKDGKGQKILPEVLQHIGVRPANMPLYVRCPICDKEFKQKTTLLQHGCIHIESRPYPCPECGKRFRQQSHLTQHLRIHTNEKPFGCMYCPRFFRQRTILNQHLRIHTGEKPYKCGQCGKDFRQKAILDQHTRTHQGDRPFCCPMPNCRRRFATENEVTKHIDNHMNPNTTKVRRQQQQQHQQQQQQQQQQQQQQQQQNNNAVAQVANHLMNDAKSLAAQQFLNNNNPSAVDNKANILPVRSIASNAAAAAVVQQSVVKNELYFPQCYGPPFQHPFQAQQQQAQQPSVAHANGGPTPPVTVTVANSVASGVVVQQNASASVVAQ