wanglab/gogpt-training-data huggingface dataset:
Protein: Nitrate/nitrite response regulator protein NarL (P0AF28)
Organism: Escherichia coli (strain K12)
Function: This protein activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal transmitted by either the NarX or NarQ proteins.
Interaction partners:
- Nitrate/nitrite sensor protein NarX
- Nitrate/nitrite sensor protein NarQ
- Nitrate/nitrite antiporter NarK
- Respiratory nitrate reductase 1 alpha chain
- DNA-binding transcriptional dual regulator CRP
- DNA-binding transcriptional regulator NtrC)
- Signal transduction histidine-protein kinase/phosphatase UhpB
- DNA-binding transcriptional dual regulator ModE
- Beta-galactosidase
- DNA-binding protein Fis
Sequence:
MSNQEPATILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALHQAAAGEMVLSEALTPVLAASLRANRATTERDVNQLTPRERDILKLIAQGLPNKMIARRLDITESTVKVHVKHMLKKMKLKSRVEAAVWVHQERIF
Protein: Nup98 protein (Q6DCP4)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MFNKTFGSPFGTGNGAFGATSTFGQTTGFGTTPAAAFGSAGFGTNTTTGGLFGNTQTKPGSLFGANTFNQPATSSASSGFGFGASTGTTNSLFGSTNTGSSLFSTPSNAFAQTKPASFGNFGTSTSTGGLFGNTNTANPFSGTSASLFGASTFSSAPTGTTIKFNPQSGTDTMAKGGVTTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNPVGAPAGTGLFGTSAATSSAPTGIFGSTAANSFSFAGNKTTFGAAGTGAFAANTGGLFGQPTNPPAASLFNKPFGNAATTQSTGFSFGNTSTLGQAQTSTMGLFGANQATQAGGLFGATTNTNAAGAFGAGSSLFGQPNPAPFGGGSTLFGNKPAGFGTTTTTAPAFGTTTGGLFGNKATLTLGTNTNTSNFGFGANAAGTSLFGNKPATGTIGPSLGTSFGTALNPGQTSLFGGNQPKLTGTLGTGAFGGTGFNSTSTGLGFGAPQPAMATLTDPNASAAQQMFLQQQYNALRYSPFPDSPLFRNPISDPKKKEELLKPTNPAAQKAVLTPTHYKLTPRPAARVRPKALQNSGAAKSQLFDALDDDEPVLSSGVFMPKKSIKKLDLKYLKNSSSLFAQESKDVNEVVPPTPETQDRSVENHHADEKKKK
Protein: Chromobox protein homolog 7 (P60889)
Organism: Rattus norvegicus (Rat)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to histone H3 trimethylated 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3). May possibly also bind trimethylated lysine residues in other proteins (in vitro). Binds non-coding, single-stranded and double-stranded RNA. Plays a role in the timely repression of differentiation-specific genes in pluripotent embryonic stem cells to maintain the undifferentiated state. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8VDS3}. Chromosome {ECO:0000250|UniProtKB:Q8VDS3}. Note=Requires trimethylation at 'Lys-27' (H3K27me3) for the localization to chromatin. Localizes to facultative heterochromatin and to the inactivated X chromosome in females. {ECO:0000250|UniProtKB:Q8VDS3}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- BMI1 proto-oncogene, polycomb ring finger.
- SUZ12 polycomb repressive complex 2 subunit
- Polycomb group ring finger 2
- Histone-lysine N-methyltransferase EZH2
- Chromobox homolog 8
- Polycomb group RING finger protein 1
- Polyhomeotic homolog 1
- Polycomb protein EED
Sequence:
MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEEKDRASGYRKRGPKPKRLLLQESAAPDVLQATGDWEPVEQPPEEEAEADLTNGPPPWTPMLPSSEVTVTDITANSVTVTFREAQAAEGFFRDRSGKL
Protein: UspA1 (Q8GH87)
Organism: Moraxella catarrhalis (Branhamella catarrhalis)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442}. Cell surface {ECO:0000256|ARBA:ARBA00004241}.
Interaction partners:
Sequence:
MNKIYKVKKNAAGHLVACSEFAKGHTKKAVLGSLLIVGILGMATTASAQAINTGQGTVVDQNGNEAIGNYSTASGGDYNQAKGNYSTASGGSGNTAEGNYSTASGGLGNTAEGNYSTASGGLGNTAKGKYSTVAGGANNQAKGDYSTASGGSGNTAEGNYSTVAGGKNNQATGLNSTVAGGSDNQATGTGSFAAGVGNKANAENAVALGNKNTIEGENSVAIGSNNTVETGKENVFILGSGTTGVTSNSVLLGNKTAGKEATAVNDATVNGLTLKNFAGVSKTGNGTVSVGSENHERQIVNVGAGKISADSTDAVNGSQLHALATVVAKNKSDITKNQAETLVNRVNIKELERKQENDIKEVVEMQNAIAEQADKNKNHIQDLAKAQLAGVTVMEELNKHVEDLYEATNDNLDKISQLDGAVFNNTQNIAKNSNHIKTLENNVEEELLNLSGRLLDQKADIDNNINNIYELAQQQDQHSSDIKTLKNNVEEGLLDLSGRLIDQKADLTKDIKALENNVEEGLLDLSGRLIDQKADIAKNQADIAQNQTDIQDLAAYNELQDAYAKQQTEAIDALNKASSANTDRIATAELGIAENKKDAQIAKAQANENKDGIAKNQADIQLHDKKITNLGILHSMVARAVGNNTQGVATNKADIAKNQADIANNIKNIYELAQQQDQHSSDIKTLAKVSAANTDRIAKNKAEADASFETLTKNQNTLIEQGEALVEQNKAINQELEGFAAHADVQDKQILQNQADITTNKTAIEQNINRTVANGFEIEKNKAGIATNKQELILQNDRLNRINETNNRQDQKIDQLGYALKEQGQHFNNRISAVERQTAGGIANAIAIATLPSPSRAGEHHVLFGSGYHNGQAAVSLGAAGLSDTGKSTYKIGLSWSDAGGLSGGVGGSYRWK
Protein: Mitochondrial fission 1 protein (A0A2R8Q8G0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004572}.
Interaction partners:
- TBC1 domain family, member 15.
- Mitochondrial fission factor homolog B
- Mitofusin 2
- Mitofusin 1
- Mitofusin 1b
- Mitochondrial fission factor homolog A
- Dynamin-1-like protein
- Dynamin-1-like protein
- Ganglioside-induced differentiation-associated protein 1.
- Dynamin-like GTPase OPA1, mitochondrial
Sequence:
MEAVVSDIVAPEDLKKFEKKYNAELVKGPVSRDTTFEYAWCLIRSKYTNDIVKGIQLLEELVHTSKKDDQRDFLFYLAVANYRLKEYERALKYIRTLLKNEPDNKQALELEKLIKDALKKDGLVGMAIVGGIGLGVAGLAGLIGLAVSKGAKS
Protein: Ras-related protein Rab-27A (EC 3.6.5.2) (Q9ERI2)
Organism: Mus musculus (Mouse)
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 cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P51159}; Lipid-anchor {ECO:0000250|UniProtKB:P51159}. Melanosome {ECO:0000250|UniProtKB:P51159}. Late endosome {ECO:0000250|UniProtKB:P51159}. Lysosome {ECO:0000250|UniProtKB:P51159}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Localizes to endosomal exocytic vesicles. {ECO:0000250|UniProtKB:P51159}.
Interaction partners:
- Melanophilin
- Unconventional myosin-Va
- Rab effector MyRIP
- Synaptotagmin-like protein 2
- Synaptotagmin-like protein 4
- Protein unc-13 homolog D
- Synaptotagmin-like protein 1
- Rabphilin-3A
- Exophilin-5
- Synaptotagmin-like protein 5
Sequence:
MSDGDYDYLIKFLALGDSGVGKTSVLYQYTDGKFNSKFITTVGIDFREKRVVYRANGPDGAVGRGQRIHLQLWDTAGQERFRSLTTAFFRDAMGFLLLFDLTNEQSFLNVRNWISQLQMHAYCENPDIVLCGNKSDLEDQRAVKEEEARELAEKYGIPYFETSAANGTNISHAIEMLLDLIMKRMERCVDKSWIPEGVVRSNGHTSADQLSEEKEKGLCGC
Protein: 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase (EC 5.3.1.17) (5-keto-4-deoxyuronate isomerase) (DKI isomerase) (Q46938)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the isomerization of 5-dehydro-4-deoxy-D-glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate (By similarity). Plays a role in the catabolism of hexuronates under osmotic stress conditions, likely substituting for the regular hexuronate degrading enzyme UxaC whose expression is repressed in these conditions.
Interaction partners:
- 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
- Uncharacterized protein YaeQ
- Uronate isomerase
- DNA topoisomerase 4 subunit A
- Mannonate dehydratase
- HTH-type transcriptional regulator RcdA
- Elongation factor Tu 1
- Elongation factor Tu 2
- Uncharacterized protein YciQ
- Protease 7
Sequence:
MDVRQSIHSAHAKTLDTQGLRNEFLVEKVFVADEYTMVYSHIDRIIVGGIMPITKTVSVGGEVGKQLGVSYFLERRELGVINIGGAGTITVDGQCYEIGHRDALYVGKGAKEVVFASIDTGTPAKFYYNCAPAHTTYPTKKVTPDEVSPVTLGDNLTSNRRTINKYFVPDVLETCQLSMGLTELAPGNLWNTMPCHTHERRMEVYFYFNMDDDACVFHMMGQPQETRHIVMHNEQAVISPSWSIHSGVGTKAYTFIWGMVGENQVFDDMDHVAVKDLR
Protein: Keratin-associated protein 12-2 (High sulfur keratin-associated protein 12.2) (Keratin-associated protein 12.2) (P59991)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MCHTSCSSGCQPACCAPSPCQPACCVPSSCQASCCVPVGCQSSVCVPVSFKPAVCLPVSCQSSVCVPMSFKSAVCVPVSCQSSVCVPVSCRPIVCAAPSCQSSLCVPVSCRPVVYAAPSCQSSGCCQPSCTSVLCRPISYSISSCC
Protein: Histone acetyltransferase Rtt109 (EC 2.3.1.48) (PcRTT109) (D3G9N3)
Organism: Pneumocystis carinii
Function: Histone chaperone-dependent acetylase that modifies 'Lys-56' of histone H3 (H3K56ac). Histone H3 'Lys-56' acetylation may be required for S-phase-linked DNA damage tolerance (By similarity). Also acetylates 'Lys-9' of histone H3 (H3K9ac) (By similarity). Autoacetylates.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q07794}.
Interaction partners:
Sequence:
MDNLYTGISKSIESLPPEITFSYGYIFTNFKKLKWPWLNKRKIDNVYLSNHFFFILQEDAMAYAIEVLIFFSSELSVFYISKADSTGFFNRHGSPSPLKAVISTFLSYLIRRFSRKNIPSRISLFSRSQPQYLFPSSSLNPSKHILDDRELVRWWLKVLDSVNGSQCPKKYVLIPGMDPRETLKYTPQHVDTDLNWICGHPYESMGQSAGEIIPRFPDDPKTRFLDQLDRDGEVVSIDKFWELMAFRQECIHGRIVGFFSLEFPGNDQDGTNNTITEDLDLQNGIQINEKIYRMVYEKLLRSDFETLEKSKGATLDLINDINNSKDIKDSVDWIKKVSGKKTSEDKKRKAIDISEQLKPVNILNESLIRKKSKKK
Protein: Cell division protein FtsZ (V6F5E5)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity (By similarity). Mild overexpression impairs cell division, leading to very elongated cells. Isolated protein forms filaments and bundles in the presence of GTP.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:24272781}. Note=Assembles at midcell at the inner surface of the cytoplasmic membrane (Probable). Upon mild overexpression during extended growth additional foci appear, which are probably blocked division sites. Foci colocalize with FtsZ-like protein (also called FtsZm) (PubMed:24272781). {ECO:0000269|PubMed:24272781, ECO:0000305|PubMed:24272781}.
Interaction partners:
- Cell division protein FtsA
- Cell shape-determining protein MreB
- Actin-like protein MamK
- Chromosome partitioning protein
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylmuramate--L-alanine ligase
- Cell division protein FtsQ
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- Magnetosome-associated protein MamJ
Sequence:
MLNFLPGNPQDLKPKITVIGVGGAGGNAVNNMIASRLEGVEFIVANTDAQAINQSRTERRVQLGTTVAQGLGAGSRPEIGRAAAEESLEEVIGQIAGANMVFITAGMGGGTGSGAAPVIARAARDHGILTVGVVTKPFHFEGAHRMRTAEGAIEELSQYVDTLIIIPNQNLFRVATERTTFADAFKMADDVLYSGVRGVTDLMIMPGLINLDFADIRTVMSEMGKAMMGTGEAEGDKRAIEAAEAAISNPLLDDTSMKGAKGVLINITGGMDMTLFEVDEAANRIRDEVDPEANIIFGSTFDEKLNGKMRVSVVATGIASEAAAQPKPTVVSLNTPQAQPQPRVAAGGTAGAGFRPAVVTAQAAPAAAVAVAQAQPQMEARTVAQPAPQPAHQPVVTAQVRVQPAAARPAQQPMAETFRPDPQLRLDPVLERPVPATTSLQADFRADPDMGHLSQAVSHIAETAQAAPQPQRQPEIQRQQAPQPQRQPEPEARRSGGLFGLLRRPAAAQPAPQPQRHEPAPMAQQPRQEPARMGNMATRSEPSVARAGEDLDIPAFLRRQAN
Protein: Pto-interacting protein 1 (Pti1) (EC 2.7.11.1) (Pto kinase interactor 1) (Q41328)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: A serine-threonine kinase involved in the hypersensitive response (HR)-mediated signaling cascade.
Interaction partners:
- Pto kinase
- non-specific protein-tyrosine kinase
- non-specific serine/threonine protein kinase
Sequence:
MSCFSCCDDDDMHRATDNGPFMAHNSAGNNGGQRATESAQRETQTVNIQPIAVPSIAVDELKDITDNFGSKALIGEGSYGRVYHGVLKSGRAAAIKKLDSSKQPDREFLAQVSMVSRLKDENVVELLGYCVDGGFRVLAYEYAPNGSLHDILHGRKGVKGAQPGPVLSWAQRVKIAVGAAKGLEYLHEKAQPHIIHRDIKSSNILLFDDDVAKIADFDLSNQAPDMAARLHSTRVLGTFGYHAPEYAMTGQLSSKSDVYSFGVVLLELLTGRKPVDHTLPRGQQSLVTWATPRLSEDKVKQCVDARLNTDYPPKAIAKMAAVAALCVQYEADFRPNMSIVVKALQPLLPRPVPS
Protein: NAD-specific glutamate dehydrogenase (NAD-GDH) (EC 1.4.1.2) (NAD(+)-dependent glutamate dehydrogenase) (Q9HZE0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in arginine catabolism by converting L-glutamate, into 2-oxoglutarate, which is then channeled into the tricarboxylic acid cycle. Can also utilize other amino acids of the glutamate family.
Interaction partners:
- Citrate synthase
- Succinylglutamate desuccinylase
- Bifunctional protein PutA
- Glutamate synthase large chain
- Glutaminase-asparaginase
- Glutamate dehydrogenase
- Glutamine synthetase
- GS catalytic domain-containing protein
- Probable glutamine synthetase
- Probable glutamine synthetase
Sequence:
MAFFTAASKADFQHQLQTALAQHLGDKALPQVTLFAEQFFSLISLDELTQRRLSDLVGCTLSAWRLLERFDRDQPEVRVYNPDYEKHGWQSTHTAVEVLHPDLPFLVDSVRMELNRRGYSIHTLQTNVLSVRRSAKGELKEILPKGSQGKDVSQESLMYLEIDRCAHAGELRALEKAILEVLGEVRVTVADFEPMKAKARELLTWLGKAKLKVPAEELKEVRSYLEWLLDNHFTFLGYEEFSVADEADGGRMVYDEKSFLGLTRLLRAGLSKDDLHIEDYAVAYLREPVLLSFAKAAHPSRVHRPAYPDYVSIRELDGKGRVIRECRFMGLFTSSVYNESVNDIPFIRGKVAEVMRRSGFDTKAHLGKELAQVLEVLPRDDLFQTPVDELFSTALAIVRIQERNKIRVFLRKDPYGRFCYCLAYVPRDVYSTETRLKIQQVLMERLQASDCEFWTFFSESVLARVQFILRVDPKSRIDIDPARLEEEVIQACRSWQDDYSSLVVENLGEAKGTNVLADFPKGFPAGYRERFAPHFAVVDLQHLLSLSEQRPLVMSFYQPLAQGEQQLHCKLYHADTPLALSDVLPILENLGLRVLGEFPYRLRHQNGREYWIHDFAFTYAEGLDVDIQQLNEILQDAFVHIVSGDAENDAFNRLVLTANLPWRDVALLRAYARYLKQIRLGFDLGYIASALNAHTDIARELVRLFKTRFYLARKLTAEDLEDKQQKLEQAILGALDEVQVLNEDRILRRYLDLIKATLRTNFYQPDGNGQNKSYFSFKFNPKAIPELPRPVPKYEIFVYSPRVEGVHLRGGKVARGGLRWSDREEDFRTEVLGLVKAQQVKNAVIVPVGAKGGFVPRRLPLGGSRDEIQAEAIACYRIFISGLLDITDNLKEGEVVPPANVVRHDEDDPYLVVAADKGTATFSDIANGIAAEYGFWLGDAFASGGSAGYDHKGMGITAKGAWVSVQRHFRERGIDVQKDNISVIGIGDMAGDVFGNGLLMSDKLQLVAAFNHMHIFIDPNPDAASSFVERQRLFNLPRSSWADYDAKLISAGGGIFLRSAKSIAITPEMKARFDIQADRLAPTELIHALLKAPVDLLWNGGIGTYVKSSKETHADVGDKANDGLRVDGRELRAKVVGEGGNLGMTQLARVEFGLHGGANNTDFIDNAGGVDCSDHEVNIKILLNEVVQAGDMTEKQRNALLVKMTDAVGALVLGNNYKQTQALSLAQRRARERIAEYKRLMGDLEARGKLDRALEFLPSDEELAERISAGQGLTRAELSVLISYSKIDLKESLLKSLVPDDDYLTRDMETAFPALLAEKFGDAMRRHRLKREIVSTQIANDLVNHMGITFVQRLKESTGMSAANVAGAYVIVRDVFHLPHWFRQIENLDYQVPADIQLTLMDELMRLGRRATRWFLRSRRNELDAARDVAHFGPRIAALGLKLNELLEGPTRELWQARYQTYVDAGVPELLARMVAGTSHLYTLLPIIEASDVTGQDTAEVAKAYFAVGSALDLTWYLQQITNLPVENNWQALAREAFRDDLDWQQRAITVSVLQMQDGPKEVEARVGLWLEQHLPLVERWRAMLVELRAASGTDYAMYAVANRELMDLAQSSQHGVCIP
Protein: SCART2 splice variant A (Scavenger receptor family member expressed on T cells 2) (B3F5L4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAFSFLRLWPLLLLTCWTLVPDLALENFVSFLGGDNKCEGQVRLRNGGQWGLMCADGLGMQEASVICRELGCGSVKFMPRYVLTPEEMRQPWLYDAQCHGNESTFLECRLGSWGTISGCKCQCVAVITCSGGTTLQMGLVDGGSPCAGTAQATGASNFALRCDLHEKEAGVVCRQLECGTALQWSRAHDGTNGNQEQKYLTCQGTETNILQCLINVNVLEQCDLLTYTQVVCTESTRSLETETGTCSDRVSLGNCTPKEIWHGTVLSWAVAFDATLLEPSSWEQQRVVSAPGVLCMLLQDEEWSKTHQGSQEQKFVSCQGTEADIFYCKINVNFAEQCDLQSYTQVVCTGHVEARLLGGVHPCEGRLEVLRGLTWGTVCHDDLDLPMAHVVCRELGCGTAVSILGSSHFGYGSGPLWTEAFRCMGNESLLFHCLREPGHQCGHDQDAALICSGEKFRLVNGSSRCEGRVELLVQDAWQPLCAANWDLADATVLCHQLNCGYAVATPQGGHFGNVEGPIRTDVFHCVGTEPHLLSCPTSTLGAQACALGNSASALCSGLQDALRLREGQSHCDGRVEVFLDGTWGRVLDSAWDLRDAAVVCRQLGCGEAQLAYDAPAPGHKTIPVGLSLVHCLGSETHLTQCNVSASLLVHAGTLRDAGVVCSGSLHIRLAAGKNRCAGRVEVFYQGTWGTVCDDAWDLQDAHVVCRQLGCGHALSAPRAAHFGAGTGRIWMDELGCMGEEAALWECQSGGWGQQDCGHKEDAGVICSEFIDVRLQEHSQPCTGRLEVFYNGTWGGVCQSLNAASLRVLCEHLGCGSQGQLLARPRGSSTIETVWLKSIQCRDKHDMSLWQCPSEPWNRHSCLRGEEAWLACAEKTEVSQDMEQIANCSSTLSCPEEGALRVLGGENGCSGRVELWHGGSWGTVCDDSWDLADAEVVCRQLGCGPAIAALQNAAFGPGSGPVWLDEVGCRGSELSLGACQAEPWGYGDCSHKEDAGVRCLGIPGTMASGNSSAPPPVPEFWTMPEIACLVLGCLLGIVFLVLAVQWCHSRAIGLGSGAVAELPSEVVYECIETVPMDEKEEPAASQSPVQDEDYDDAEEPKDSPGEDMEAGHH
Protein: ORC1-type DNA replication protein 1 (Q980N4)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and strongly inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Stimulates the DNA-binding activity of Cdc6-3.
Interaction partners:
- Minichromosome maintenance protein MCM
- DNA primase large subunit PriL
- ORC1-type DNA replication protein 3
- DNA primase small subunit PriS
- DNA polymerase 1
- UPF0215 protein SSO0256
- Single-stranded DNA binding protein Ssb
- Flap endonuclease 1
- DNA primase DnaG
Sequence:
MSDIIDEVISSFKTSSIFINREYLLPDYIPDELPHREDQIRKIASILAPLYREEKPNNIFIYGLTGTGKTAVVKFVLSKLHKKFLGKFKHVYINTRQIDTPYRVLADLLESLDVKVPFTGLSIAELYRRLVKAVRDYGSQVVIVLDEIDAFVKKYNDDILYKLSRINSEVNKSKISFIGITNDVKFVDLLDPRVKSSLSEEEIIFPPYNAEELEDILTKRAQMAFKPGVLPDNVIKLCAALAAREHGDARRALDLLRVSGEIAERMKDTKVKEEYVYMAKEEIERDRVRDIILTLPFHSKLVLMAVVSISSEENVVSTTGAVYETYLNICKKLGVEAVTQRRVSDIINELDMVGILTAKVVNRGRYGKTKEIGLAVDKNIIVRSLIESDSRFADLWS
Protein: Probable clathrin heavy chain (Q10161)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic face of coated pits and vesicles. {ECO:0000250}.
Interaction partners:
- Clathrin light chain
- UBA domain-containing protein 7
- Epsin-1
- AP-1 complex subunit gamma-1
- AP-2 complex subunit alpha
- Endocytosis protein end4
- Uncharacterized calcium-binding protein C800.10c
- AP-1 complex subunit beta-1
- AP-2 complex subunit beta
- AP-2 complex subunit mu
Sequence:
MAQQLPIRFSEVLQLASVGIQPSSFGFANVTLESDKYVCVRDNPNGVNQVVIVDLEDPSNVLRRPISADSVILHPKKKIIALKAQRQLQVFDLEAKAKINSYVMNQDVVYWTWISDSVIGMVTDTSVFHWTVSGSDPVKMFDRHSSLNGTQIISYKSNYNEEWFTLIGISSRDNRIAGNLQLYSKKRKVSQPLESHASAFAVIQPEGVDHEVQVLALASRLPTGSKLSIVEVDRNPNNPAFATKTVDLFFPPEAVNDFPIAIEIGSTYNVAYVVTKYGFIHVYDLETAKCIYMNRVSGESIFVTTAHKSVNGLMAINRKGQVLSVSINPETIIPYILSNLNDPGLAVRMASHANLPGADNLYMQQFQQLMAQGNYSEAAKVAASSPRGILRTSQVIDQFKLIQAAPGQIAPILQYFGTLLDKGPLNEHETIELARPVLAQNRIQLLEKWYGENKLACTEALGDLVKPYNTPFALKIYETANVPNKVVMCLSELGDFGKLATYTSQQNITPDYVSLLQNLVRVNPDQAAEFATQMFNSNPSINLEKIVDIFMSQNLVQQATAFLLDALKDDNPEHSHLQTRLLEINLINAPQVADAILGNQMFTHFDRAVIASLCERAGLVQRALELYDKPADIKRVIVHSNLLNPEWLMNYFSRFSPDEVYDYLREMLRSNLRQNLQIVVQIATRYSDLVGAQRIIEMFEKFKTFEGLYYYLGSIVNITEDPEVVYKYIQAACLMNQFTEVERICRDNNVYNPEKVKNLLKEAKLADQLPLILVCDRYDFVNDLVFYLFRNNMFQFIEIYVQRINPSKTPQVVGALLDIDCDEELVQNLLMSVVGQVPVDELVEEVERRNRLKLLLPYLESLLQSGSQDRAIYDALAKIYIDSNNNPEVFLKENNFYDTLTVGKYCEKRDPYLAFIAYEKGGNDTEIINLCNENSMFKQLARYLLKRSDSNLWSEVLQDSAYRRPLLDQVIATAVPESSDPEAVSIVVKALMEVDLPSQLIELLEKIVLQPSSFSENANLQNLLFLTAIKADKSRVMEYIDKLDKYDVDEIAEIAIENGLYEEAFRIYKIHNKHEQAMKVLVEDIVSLDRAQDYAETVEQPEVWSRLAKAQLDGIRIPDAIESYLKADDPSNYSEVIELASRAGKYEELIKYLLMARSKMHEPDVDSALLIAYAKTNQLTEMETFLIGSNVADVKAVGDECFESKNYEAAKLMYSSISNWSMLATTLVYLGEYQGAVDCARKANSIKVWKQVGTACIDKREFRLAQICGLNLIVHAEELPGLIRLYEERGYFEEVISLMEAGLGLERAHMAFYTELAILYAKYKPERMMEHLKLFWGRLNMAKVIRACDQMHLWNEAVFLYVHDQSYDNAAAVMMEQPEAFDHQSFKDIIVHVANLELYYRALNFYLEQHPMLLTDLLAALTPRIDHPRVIRIFEKSENTPLILNFMVAIQHLNIQAVNHAYNDLLIEMEDYQSLQDSIENYDHFDAIALARRLEKHSLLEFRRIAAYIYRKNKRWTQSIELSKQDRFYKDAIITARDSDQTTIAEDLMKYFVEIGNYECFAAILYTCYHLLRNDLVMEISWRKGLQDYAYPYFINFQCEMFSKVLNLEKDLKDRQAVKSEEESASTIGAGILGNTLMLTQGPMANNNDQFDSFQQASPMPRLGNF
Protein: Caffeoyl-CoA O-methyltransferase 3 (PhCCoAOMT3) (EC 2.1.1.104) (5-hydroxyferuloyl-CoA O-methyltransferase 1) (EC 2.1.1.-) (A0A0S2UWA5)
Organism: Petunia hybrida (Petunia)
Function: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0A0S2UWC9}.
Interaction partners:
Sequence:
MAENGASQETTQVAKHQEVGHKSLLQSDALYQYILETSVYPREPEPMKELREITAKHPWNLMTTSADEGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPDDGKILAMDINRENYEIGLPVIQKAGVAHKIDFREGPALPVLDLMVEDKSNHGTYDFIFVDADKDNYINYHKRIIELVKVGGVIGYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRVS
Protein: Nucleolar protein 56 (Ribosome biosynthesis protein SIK1) (Suppressor of I kappa b protein 1) (Q12460)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for 60S ribosomal subunit synthesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:9372940}.
Interaction partners:
- Ribosome biogenesis protein ENP2
- U3 small nucleolar RNA-associated protein 16
- rRNA-processing protein FCF1
- 13 kDa ribonucleoprotein-associated protein
- NET1-associated nuclear protein 1
- Protein SOF1
- Periodic tryptophan protein 2
- H/ACA ribonucleoprotein complex subunit NHP2
- U3 small nucleolar RNA-associated protein MPP10
- RNA cytidine acetyltransferase
Sequence:
MAPIEYLLFEEPTGYAVFKVKLQQDDIGSRLKEVQEQINDFGAFTKLIELVSFAPFKGAAEALENANDISEGLVSESLKAILDLNLPKASSKKKNITLAISDKNLGPSIKEEFPYVDCISNELAQDLIRGVRLHGEKLFKGLQSGDLERAQLGLGHAYSRAKVKFSVQKNDNHIIQAIALLDQLDKDINTFAMRVKEWYGWHFPELAKLVPDNYTFAKLVLFIKDKASLNDDSLHDLAALLNEDSGIAQRVIDNARISMGQDISETDMENVCVFAQRVASLADYRRQLYDYLCEKMHTVAPNLSELIGEVIGARLISHAGSLTNLSKQAASTVQILGAEKALFRALKTKGNTPKYGLIYHSGFISKASAKNKGRISRYLANKCSMASRIDNYSEEPSNVFGSVLKKQVEQRLEFYNTGKPTLKNELAIQEAMELYNKDKPAAEVEETKEKESSKKRKLEDDDEEKKEKKEKKSKKEKKEKKEKKDKKEKKDKKEKKDKKKKSKD
Protein: Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial [Includes: NAD-dependent methylenetetrahydrofolate dehydrogenase (EC 1.5.1.15); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9)] (P13995)
Organism: Homo sapiens (Human)
Function: Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency.
Subcellular location: Mitochondrion.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Thymidylate synthase
- Methylenetetrahydrofolate reductase
- Bifunctional purine biosynthesis protein ATIC
- Formimidoyltransferase-cyclodeaminase
- Aminomethyltransferase, mitochondrial
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
Sequence:
MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN