wanglab/gogpt-training-data huggingface dataset:
Protein: Intraflagellar transport protein 74 (Intraflagellar transport protein 71) (IFT-71) (Intraflagellar transport protein 72) (IFT74/72) (Q6RCE1)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the intraflagellar transport (IFT) complex B: together with IFT81, forms a tubulin-binding module that specifically mediates transport of tubulin within the cilium. Binds beta-tubulin via its basic region. Required for ciliogenesis.
Subcellular location: Cell projection, cilium {ECO:0000305|PubMed:23990561}.
Interaction partners:
Sequence:
MDRPSSRGALALGAGGLGKAPTGGAVQQPDRPMTGQRGAAPAGPMRAPAGASIIGAGPPGTAMRGGPGPAGGPPGTAYKRMGTASQRPGTGQQAAAAAAAARAGQQLQVENRPITNHGVSGMKTAAAGVGRQVLDKNYFMNELRQKRMEIAQVTSNMKSDLEALERKQAQYNSMDKRASDLSKEVKILQEALADYNTVLDKVGSQAPVYVIQQEFAALKDRNEQQRKRVDEVLTERLNLESKAKQAESKMSEIQASMDQRLNSMPPSQRNEYTTLVAEQQQLQADSKRFEEVLDELDKALQASEGELARNPFKQRSLQLQEQIRALTEKKYELTEEERQSKRSPEELRADLMAKIKRDNTEVEQMTQQIRELQDQIKKMEERVKSLGGATSGAAAAEEKANREKFEELLAKERDLNNFMDGFPSRKAAKMQEKQQKEDGIVGVLEKMVKMQGIIGSNLPSQKKYKEMQDELEYKKMQLENTQTTQERLKEELTMRRTELEKIDTLEDKIKLELTQLAERQEAMEKEMGEFGSVEDIQRKANAARERMEGLRSVLLKRKDLLRSIVAERGLKFQAKRAQLQDHNLQVQLEKMEAKLKNLSAGVFEMDEFIKAKESETNYRQLASNIAALVDDLNVHVKKAVV
Protein: Cysteine and glycine-rich protein 3 (Cardiac LIM protein) (cDNA, FLJ93801, Homo sapiens cysteine and glycine-rich protein 3 (cardiac LIMprotein) (CSRP3), mRNA) (A2TDB8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPNWGGGAKCGACEKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGYGQGAGCLSTDTGEHLGLQFQQSPKPARSVTTSNPSKFTAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTQQVEKKE
Protein: Methyl-CpG-binding domain protein 1 (CXXC-type zinc finger protein 3) (Methyl-CpG-binding protein MBD1) (Protein containing methyl-CpG-binding domain 1) (Q9UIS9)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binding is abolished by the presence of 7-mG that is produced by DNA damage by methylmethanesulfonate (MMS). Acts as transcriptional repressor and plays a role in gene silencing by recruiting ATF7IP, which in turn recruits factors such as the histone methyltransferase SETDB1. Probably forms a complex with SETDB1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Isoform 1 and isoform 2 can also repress transcription from unmethylated promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14610093}. Nucleus matrix {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624}. Nucleus speckle {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624}. Chromosome {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624, ECO:0000269|PubMed:12711603, ECO:0000269|PubMed:14555760}. Note=Nuclear, in a punctate pattern (PubMed:12711603). Associated with euchromatic regions of the chromosomes, with pericentromeric regions on chromosome 1 and with telomeric regions from several chromosomes (PubMed:10454587, PubMed:10648624). {ECO:0000269|PubMed:10454587, ECO:0000269|PubMed:10648624, ECO:0000269|PubMed:12711603}.
Interaction partners:
- Activating transcription factor 7-interacting protein 1
- Histone-lysine N-methyltransferase SETDB1
- Chromobox protein homolog 5
- Cilia- and flagella-associated protein 53
- Chromatin assembly factor 1 subunit A
- Histone-lysine N-methyltransferase SUV39H1
- E3 SUMO-protein ligase PIAS1
- Small ubiquitin-related modifier 1
Sequence:
MAEDWLDCPALGPGWKRREVFRKSGATCGRSDTYYQSPTGDRIRSKVELTRYLGPACDLTLFDFKQGILCYPAPKAHPVAVASKKRKKPSRPAKTRKRQVGPQSGEVRKEAPRDETKADTDTAPASFPAPGCCENCGISFSGDGTQRQRLKTLCKDCRAQRIAFNREQRMFKRVGCGECAACQVTEDCGACSTCLLQLPHDVASGLFCKCERRRCLRIVERSRGCGVCRGCQTQEDCGHCPICLRPPRPGLRRQWKCVQRRCLRGKHARRKGGCDSKMAARRRPGAQPLPPPPPSQSPEPTEPHPRALAPSPPAEFIYYCVDEDELQPYTNRRQNRKCGACAACLRRMDCGRCDFCCDKPKFGGSNQKRQKCRWRQCLQFAMKRLLPSVWSESEDGAGSPPPYRRRKRPSSARRHHLGPTLKPTLATRTAQPDHTQAPTKQEAGGGFVLPPPGTDLVFLREGASSPVQVPGPVAASTEALLQEAQCSGLSWVVALPQVKQEKADTQDEWTPGTAVLTSPVLVPGCPSKAVDPGLPSVKQEPPDPEEDKEENKDDSASKLAPEEEAGGAGTPVITEIFSLGGTRFRDTAVWLPRSKDLKKPGARKQ
Protein: Putative membrane protein insertion efficiency factor (P0A8C8)
Organism: Escherichia coli (strain K12)
Function: Could be involved in insertion of integral membrane proteins into the membrane.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00386, ECO:0000269|PubMed:21803992}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00386, ECO:0000269|PubMed:21803992}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00386, ECO:0000269|PubMed:21803992}. Note=Associated with the inner membrane via a putative N-terminal amphipathic helix.
Interaction partners:
- Ribonuclease P protein component
- Membrane protein insertase YidC
- Large ribosomal subunit protein bL34
- Protein translocase subunit SecE
- Serine--tRNA ligase
- tRNA modification GTPase MnmE
- Ribosomal RNA small subunit methyltransferase J
Sequence:
MAPPLSPGSRVLIALIRVYQRLISPLLGPHCRFTPTCSSYGIEALRRFGVIKGSWLTVKRVLKCHPLHPGGDDPVPPGPFDTREH
Protein: Serine/threonine protein phosphatase 2A regulatory subunit (A9UJN4)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable serine/threonine-protein phosphatase PP2A regulatory subunit
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Serine/threonine-protein phosphatase 2A regulatory subunit sur-6
- Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1
- Serine/threonine-protein phosphatase 2A regulatory subunit pptr-1
- EF-hand domain-containing protein
- EF-hand domain-containing protein
- J domain-containing protein
- Uncharacterized protein
- Probable protein phosphatase methylesterase 1
Sequence:
MLRSKKKDKENGKSEKKDKEKDKKSMKDDGAGSSKASTIPTIRTEDVGGDMIPADAPPPTNIGRTNTYGGGPVIPRRERRQSSSMFNISQNRELQRLPAIKDADPSERETLFIQKLRQCCVVFDFANDALSDLKFKEVKRAALNELVDHVSGAPKGSLSDAVYPEAIGMFSTNLFRPLSPPTNPIGAEFDPDEDEPTLEAAWPHLQLVYEFFLRFLECPDFQSQVAKRYIDQNFILRLLMIMDSEDPRERDFLKTTLHRIYGKFLGHRAYIRKQINNIFYSFIYETERHNGIAELLEILGSIINGFALPLKEEHKTFLLRVLLPLHKVKSLSVYHPQLAYCVVQFIEKDSSLTEPVISGMLRFWPKQHSPKEVMFLNELEEVLDVIEPNEFQKIMTPLFSQIARCVSSPHFQVAERALYYWNNEYVMSLVADNARVIIPIMFPVLFKNSKSHWNKTIHGLIYNALKMFMEMNQKLFDECSQAYQKDRVQEKTLNEEKERIWNNIEKQAMGNPQYVEVKALFARFNPDEIISSRQQNGVDENMKTSTVLSKDEILKNAVGVSSMKNDMDFGPNHKQSDFPPDEQTTRALGEYKRHDPFLKKVTSTDEQ
Protein: Fimbrin-4 (AtFIM4) (Fimbrin4) (Q9SJ84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cross-links actin filaments (F-actin). Stabilizes and prevents F-actin depolymerization mediated by profilin. May regulate actin cytoarchitecture, cell cycle, cell division, cell elongation and cytoplasmic tractus.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7G188}.
Interaction partners:
- Formin-like protein 16
- F-actin-capping protein subunit beta
- Glutathione S-transferase F5
- Actin-depolymerizing factor 5
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH8
- Formin-like protein 5
- Formin-like protein 1
Sequence:
MSSYVGVLVSDPWLQSQFTQVELRTLKSKFYSTKTRFGRVTVKHLPPVFAKLKYFNGKFDENEIKTILDESYPNRAKEVEFETFLRAFLSVQSRGSKGASSFLKTSTTTFHHSINESEKASYVSHINSYLKDEPNLKSYLPINPTTNALFDLVKDGVLLCKLINIAVPGTIDERAINTKKELNPWERTENLSLCLNSAKAIGCTVVNIGTQDIAEGTPHLVLGLIFQIIKIQLLADLNLKKTPQLVELVEENQDVEELMGLAPEKLLLKWMNFHLKKAGYEKQVTNFSSDVKDGEAYAYLLNALAPEHSTNVTLEIKDPSERATKVLEQAEKLDCKRFLSPKDIVEGSANLNLAFVAQLFHHRNGLSDESPKVPISVAEMVTEDEETSREERCFRHWMNSLGAVTYVDNVFEDVRNGWVLLEVLDKVSPGSVNWKHANKPPIKMPFKKVENCNQVIKIGKELNFSLVNVAGHDIMQGNKKLLLAFLWQLMRYTMLQILNNLRSHCQGKDITEADILNWANRKVKKSGRTSQAVSFKDKNLANGIFFLELLSAVEPRVVNWSLVSKGETQEEKNLNATYIISVARKLGCSIFLLPEDILEVNQRMMLILAASIMNWSLQQQSDTESTVSDDTDVSSVTEEISNLSTDDGSSDV
Protein: Galactinol synthase 3 (AtGolS3) (GolS-3) (EC 2.4.1.123) (O80518)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable galactinol--sucrose galactosyltransferase 5
- Probable galactinol--sucrose galactosyltransferase 1
- Probable galactinol--sucrose galactosyltransferase 6
- Probable galactinol--sucrose galactosyltransferase 2
- UDP-sugar pyrophosphorylase
- ADP-glucose phosphorylase
- UDP-glucose 4-epimerase 2
- Protein COLD-REGULATED 15A, chloroplastic
- UDP-glucose 4-epimerase 5
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3
Sequence:
MAPEMNNKLSYGEKKRAYVTFLAGTGDYVKGVVGLAKGLRKTKSKYPLVVAVLPDVPADHRRQLLDQGCVIKEIQPVYPPDNQTQFAMAYYVLNYSKLRIWKFVEYSKLIYLDGDIQVFENIDHLFDLPDGNFYAVKDCFCEKTWSHTPQYKIGYCQQCPDKVTWPESELGPKPPLYFNAGMFVYEPSLPTYYNLLETLKVVPPTPFAEQDFLNMYFKDIYKPIPPVYNLVLAMLWRHPENIELNEAKVVHYCAAGAKPWRFTGQEGNMEREDIKMLVEKWWDIYNDESLDYKNFNVHCGQKEDVHRKPKTLPQFFTDLSEADVLQCAKAPSAA
Protein: Protein Hikeshi (E9PPG8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU369060}. Cytoplasm, cytosol {ECO:0000256|RuleBase:RU369060}. Nucleus {ECO:0000256|RuleBase:RU369060}.
Interaction partners:
Sequence:
MFGCLVAGRLVQTAAQQVAEDKFVFDLPDYESINHVVVFMLGTIPFPEGMGGSVYFSYPDSNGMPVWQLLGFVTNGKPSAIFKISGLKSGEGSQHPFGAMNIVRTPSVAQIGISVELLDSMAQQTPVGNAAVSSVDSFTQFTQKMLDNFYNFASSFAVSQAQMTPSPSEMFIPANVVLKWYEAFSVSNIKAFYN
Protein: Defensin Lucifensin (Sericasin) (P86471)
Organism: Lucilia sericata (Green bottle fly) (Phaenicia sericata)
Function: Shows strong antibacterial activity against numerous Gram-positive bacteria. It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis. Shows antibacterial activity against the Gram-positive bacteria M.luteus, E.fecalis (MIC=32 mg/L), S.aureus (MIC=16 mg/L), S.carnosus (MIC=2 mg/L), S.pneumoniae (MIC=2 mg/L) and S.pyogenes (MIC=2 mg/L) and against a number of methicillin-resistant S.aureus and glycopeptide-intermediate S.aureus isolates. Does not show antibacterial activity against Gram-negative bacteria or antifungal activity against C.utilis. Shows slight antifungal activity against C.albicans.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710, ECO:0000269|PubMed:19921400, ECO:0000269|PubMed:21560219, ECO:0000269|PubMed:25182719}. Host cell membrane {ECO:0000305|PubMed:20508130}.
Interaction partners:
Sequence:
MKFFMVFAVTFCLALSFVSQSLALPADDEAHFVDGLEALKTIEPELHGRYKRATCDLLSGTGVKHSACAAHCLLRGNRGGYCNGRAICVCRN
Protein: Uncharacterized protein (Q57WN7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGQKPSITTLLRQCIYNQDTDGFRALIGEHENELIPGCLEDNIFVEVITKKCEPEIVDTVVKLANENQLASLVATAVLYD
Protein: ATP-dependent molecular chaperone HSP82 (82 kDa heat shock protein) (Heat shock protein Hsp90 heat-inducible isoform) (P02829)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CPR6
- Mitochondrial protein import protein MAS5
- Heat shock protein STI1
- Hsp90 co-chaperone Cdc37
- ATP-dependent molecular chaperone HSC82
- Hsp90 co-chaperone AHA1
- Protein SGT1
- Heat shock protein SSA1
- Co-chaperone protein SBA1
- Hsp90 co-chaperone HCH1
Sequence:
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD
Protein: Kelch-like protein 40b (Kelch repeat and BTB domain-containing protein 5b) (E9QJ30)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: ubstrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex (By similarity). Required for skeletal muscle development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q9D783}.
Interaction partners:
- Kelch-like protein 21
- Kelch-like protein 3
- Kelch-like protein 40a
- Kelch repeat and BTB domain-containing protein 8
- Speckle-type POZ protein
- Speckle-type POZ protein-like A
- Speckle-type POZ protein-like B
- Kelch-like protein 12
- Peflin
- Bardet-Biedl syndrome 1.
Sequence:
MALPIDPMEEPRMYQQTLLQDGLYDLLESDMMVDCVLKIKDKEFPCHRLVLAACSSYFRAFFKSGVEESKQREIVLEDVEPGVMGIILKYLYTSNINVTEQNVQDIFALSNMLQIPSIFTVCVSFLQKRLSLSNCLAIFRLGLMLDCPRLAISARNFACERFQFITRDEEFLQLTPSELAAVLASDSLNVETEQDVFEALIKWVGHDQENRIGDLPDLLDCIRLRLVPRDYFVKNVEKHEWLSSNPEITKKLQLVKDAHAGKLPELKKTKNKKSPSEEGQKKGDEEEVEEEEEQEERLPGILNDNLRFGMFLRELIFLINDSASVAYDPTGNDCYVASVSTQIPKNHCSLVTKENQIFVAGGLFFDEQSKDEQIYSYFLQFDPASSDWMGMPPIPSPRFLFGMGEAENFIFVIGGREMKEGENILNTVMVYDRQFLKWAESDPLPYLVYGHGVVSHNEMIYVIGGKGENKECLNRVCAYDIKTHQWKDLAPLNTARSLFGVTIHKNNIYVVAGVTDSGLTGSAEVYDIKTNKWSEFVEFPQDRSSLSLVSVSGVLYAVGGFAMFPKEDSDDLMPLEMNDIWRYDESERTWSGILRENRYASGATVLGVRLNTLRLTKM
Protein: Putative acetyl-CoA carboxylase biotin-containing subunit (Single hybrid motif superfamily protein) (Q8GRT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASCSLGVPKIKISAVDLSRVRSGSLLIPYNQRSLLRQRPVKYLSLKTTFGSVKAVQVSTVPTAETSATIEVKDSKEIKSSRLNAQLVPKPSEVEALVTEICDSSSIAEFELKLGGFRLYVARNIADNSSLQPPPTPAVTASNATTESPESNGSASSTSLAISKPASSAADQGLMILQSPKVGFFRRSKTIKGKRLPSSCKEKDQVKEGQILCYIEQLGGQFPIESDVTGEVVKILREDGEPVGYNDALISILPSFPGIKKLQ
Protein: GM02880p (PAR domain protein 1-alpha) (PAR-domain protein 1, isoform B) (PAR-domain protein 1, isoform K) (PAR-domain protein 1, isoform P) (Q7KKI2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDRERSSPTLIETGLKNLIGGRDGNYPLISGINGKSTSNSKEIICPDDKYKEEGDIWNVEAQTAFLGPNLWDKTLPYDADLKVTQYADLDEFLSENNIPDGLPGTHLGHSSGLGHRSDSLGHAAGLSLGLGHITTKRERSPSPSDCISPDTLNPPSPAESTFSFASSGRDFDPRTRAFSDEELKPQPMIKKSRKQFVPDELKDDKYWARRRKNNIAAKRSRDARRQKENQIAMRARYLEKENATLHQEVEQLKQENMDLRARLSKFQDV
Protein: Mediator of RNA polymerase II transcription subunit 26 (Cofactor required for Sp1 transcriptional activation subunit 7) (CRSP complex subunit 7) (Mediator complex subunit 26) (Q7TN02)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 30
Sequence:
MTAAPASPQQMRDRLLQAIDSQSNIRNMVAVLEVISSLERYPITKEALEETRLGKLINDVRKKTKNEELAKRAKRLLRSWQKLIEPVHQNEVALRALAGAAGSANGGAHNCRPEMGVAGAPKSIHDLKNRNDIQRLPGQRLDRLGSRKRRGDQRDLGHPGPPHKVSKGSPDPLVPNASPLPTNGISGSPESLPSPLDGSGHLGPDGSRLEPSDNEKHSTKIPVNAVRPRPSSPGLGKPPVPCLQTKAAQLQQLDRADESPGPPYPRGSSRCSFSPRNSRHEGSFSRHRSSYIPKGQVSSPSPWPQPPDNTQVPSPLPLAQPPTPPVRRQELLPNAESPVHWPEQSEGHPRLTGPACRAGFSPDSSKADSDATSSGGSDSKKKKRYRPRDYTVNLDGQVAEAGVKPVRLKERKLTFDPMTRQIRPLTQKEPVRADSPVPTEQLPRTELEQQEVKASLQSPFEQTNWKELSRNEIIQSYLSRQSSLLSSSGAQTPGAHHFMAEYLKQEESSRQGARQPHVLLPLPTPTDLPGLTREVTQDDLDRIQAQQWPGVNGCEDTQGNWYDWTQCISLDPHGDDGRLNILPYVCLD
Protein: Malate dehydrogenase (EC 1.1.1.37) (O15769)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MRTSATLQFKVAVLGAAGGIGQPLSLILKTNPLVSHLSCYDIHGVTGVAADLSHICSPAKVTGHLKDELHKAVDGADVVIIPAGTPRKPGMTREDLFSVNATIVRDLVSACAKQCPKALIGVVSNPVNSVVPIASEVLKKAGVFDPARLFGITTLDVVRARTFVAEAAGKSPYDVNVQVVGGHSGPTIIPLLSQAGVSLTEEQVKAITHRVQYGGDEVVKAKGGAGSATLSMAYAAGEWMSSVLKGLRGDKGIVECTYVQTDIIPGVNFFGCPVELGKGGVEKIHKPVFDAYEQSLLEKCVADLEKNIAAGFAFGSRQ
Protein: Partitioning defective 6 homolog alpha (PAR-6) (PAR-6 alpha) (PAR-6A) (Q6B4M5)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9NPB6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NPB6}. Note=Colocalizes with GTP-bound CDC42 or RAC1 at membrane ruffles and with PARD3 at epithelial tight junctions. Recruited to the centrosome by a microtubule and dynein-dynactin-dependent mechanism. {ECO:0000250|UniProtKB:Q9NPB6}.
Interaction partners:
- Partitioning defective 3 homolog
- Protein kinase C zeta type
- Cell division control protein 42 homolog
- Protein kinase C iota type
- Protein PALS1
- Ras-related C3 botulinum toxin substrate 1
- Dishevelled segment polarity protein 2
- small monomeric GTPase
- Glycogen synthase kinase-3 beta
- Par-6 family cell polarity regulator beta
Sequence:
MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRTSVRGFQEFSRLLCVVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEGDSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPSSVGPGPTDPDSDDDNSDPVIENRHPPCSNGLSQGPLCWDLQPGCLHPSAGSSLPSLDSREQANSGWGNGMRGDVSGFSL
Protein: Anti-sigma-D factor RsdA (Regulator of SigD) (Sigma-D anti-sigma factor RsdA) (P9WJ71)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigD. ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor. Neither S1P nor S2P proteases have been so far identified for this anti-sigma factor.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- ECF RNA polymerase sigma factor SigD
- Uncharacterized protein
- LuxR family transcriptional regulator
- Anti-sigma-E factor RseA
- Transmembrane protein
- Probable conserved transmembrane protein
- Uncharacterized protein
- Probable conserved transmembrane protein
Sequence:
MREFGNPLGDRPPLDELARTDLLLDALAEREEVDFADPRDDALAALLGQWRDDLRWPPASALVSQDEAVAALRAGVAQRRRARRSLAAVGSVAAALLVLSGFGAVVADARPGDLLYGLHAMMFNRSRVSDDQIVLSAKANLAKVEQMIAQGQWAEAQDELAEVSSTVQAVTDGSRRQDLINEVNLLNTKVETRDPNATLRPGSPSNPAAPGSVGNSWTPLAPVVEPPTPPTPASAAEPSMSAGVSESPMPNSTSTVAASPSTPSSKPEPGSIDPSLEPADEATNPAGQPAPETPVSPTH
Protein: Methylmalonyl-CoA mutase, mitochondrial (MCM) (EC 5.4.99.2) (Methylmalonyl-CoA isomerase) (P22033)
Organism: Homo sapiens (Human)
Function: Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:24458}. Mitochondrion {ECO:0000269|PubMed:28943303}. Cytoplasm {ECO:0000269|PubMed:28943303}.
Interaction partners:
- Methylmalonic aciduria type A protein, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Corrinoid adenosyltransferase MMAB
- Cobalamin trafficking protein CblD
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Methionine synthase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Lysosomal cobalamin transport escort protein LMBD1
Sequence:
MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV
Protein: Adenosine kinase (AK) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase) (Q9VU39)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368116}.
Interaction partners:
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- AMP deaminase
- Adenylate kinase 2
- 5'-nucleotidase
- 5'-nucleotidase
- purine-nucleoside phosphorylase
- GTP:AMP phosphotransferase, mitochondrial
- 3',5'-cyclic-AMP phosphodiesterase, isoform I
- Adenylate kinase 1
Sequence:
MTSTLQEGILVGCGNPLLDISAVVPLNFLQKYSMNEDDAILAEDRHMPIYGELVEGYQAEFLAGGSVQNSLRIAQWILRQPRVAVFFGCVGEDRYANILKEKAQAAGLDVHYQVKKDVPTGTCAVLITGTHRSLCANLAAANNFTIDHLEEPSNKALVDNAQYYYISGFFLTVNPPSIMQVAATAHAKQRPFLMNLSAPFISQFYMAPLLAALPYVDIIFGNEAEAQAFAEAQQWPSGDLREIGKRLVAMEKKNPTRPRIAILTQGCDPVLLIQQDSVQEFPVTKLAVHEIVDTNGAGDAFVGGFLSQFVQGKSLDVCIRCGNYAAGHIIKNPGCTYSGEPEFVE