wanglab/gogpt-training-data huggingface dataset:
Protein: Nephrocystin-3 (Q7TNH6)
Organism: Mus musculus (Mouse)
Function: Required for normal ciliary development and function. Inhibits disheveled-1-induced canonical Wnt-signaling activity and may also play a role in the control of non-canonical Wnt signaling that regulates planar cell polarity. Probably acts as a molecular switch between different Wnt signaling pathways. Required for proper convergent extension cell movements.
Subcellular location: Cell projection, cilium {ECO:0000250}. Note=Localization to cilium is mediated via interaction with UNC119 and UNC119B, which bind to the myristoyl moiety of the N-terminus. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase Nek8
- Ankyrin repeat and SAM domain-containing protein 6
- Inversin
- Nephrocystin-1
- Protein unc-119 homolog B
- Nephrocystin-4
- Protein fantom
- Centrosomal protein of 290 kDa
- IQ calmodulin-binding motif-containing protein 1
- ADP-ribosylation factor-like protein 3
Sequence:
MGTASSLVSPTGGEVIEDTYGAGGGEACEIPVEVKPKARLLRSSFRRGAGAGPGSLPRAAGGGGLLGASFKSTGSSVPELEYAAAEFERLKKEYEIFRVSKNQELLSMGRREAKLDTENKRLRAELQALQKTYQKILREKEGALEAKYQAMERAVTFEHDRDRVKRQFKIFRETKENEIQDLLRAKRELESKLQRLQAQGIQVFDPGESDSDDNCTDVTAAGTQCEYWASRALGSEHSIGSMIQLPQPFRGPEFAHSSIDVEGPFANINRDDWDAAVAGLLQATPLFSHSLWSHPVRCYLIYTDETQPEMELFLKDHSPKLKRMCETMGYFFLAVYFPLDVENQYLTVRKWEIEKSSLVILFLHSTLPSFLLEDCEEAFLQNPEGKPGLIYHRLEDGKVTCDSVQQFLDQVSNLGKTTKAKIIEHSGDPAEGVCKIYVGVEKIIKQDILGLENTDVEEKDGGREDSTPEEDDFGDVLWDIHDEQEQMEAFQQTSSSAHELGFEKYYQRLDDLVVAPAPIPPLLVSGGPGSGKSLLLSKWIQLQQKHFPNTLILSHFVGRPMSTSSESSLIIKRLTLKLMQHFWAVSALTLDPAKLLEEFPHWLEKLSARHQGSIIIIIDSIDQVQQVEKHMKWLIDPLPVNVRVIVSVNVETCPTAWRLWPTLHLDPLSPKDAISIITAECYSMDVRLSREQEKMLEQHCRPATTRHALYVTLFSKMMACAGRGGNVAETLHQCLQCQDTVSLYKLVLHHVRESMPSDRDKEWMTQILCLINVSHNGVSESELMELYPEMSWLSLTSIVHSLHKMHLLTYSCGLLRFQHLQAWETVRLQYLEDPALVSSYREKLISYFASQLSQDRVTWRSADELPWLFQQQGSKQKLHSCLLNLLVAQNLYKRGHFAELLSYWQFVGKDKGAMATEYFESLKQYENSEGEENMLCLADLYETLGRFLKDLGLLSQAVVPLQRSLEIRETALDPDHPRVAQSLHQLAGVYVQWKKFGDAEQLYKQALEISENAYGADHPHAARELEALATLYHKQNKYEQAEHFRKKSVIIRQQATRRKGSLYGFALLRRRALQLEELTLGKDKPENARTLNELGVLYFLQNNLETAEQFLKRSLEMRERVLGPDHPDCAQSLNNLAALCNEKKQYEKAEELYERALDIRRRALAPDHPSLAYTVKHLAILYKKTGKVDKAVPLYELAVEIRQKSFGPKHPSVATALVNLAVLHSQMKKHSEALPLYERALKIYEDSLGRMHPRVGETLKNLAVLSYEEGNFEKAAELYKRAMEIKEAETSLLGGKAPSRQSSSGDTFLFKTTHSPNVFLPQGQS
Protein: Protein pp71 (pp71) (71 kDa upper matrix phosphoprotein) (Phosphoprotein UL82) (ppUL82) (Tegument protein UL82) (P06726)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Stimulates viral immediate-early (IE) transcription. Plays a role in the inhibition of the host innate repsonse by targeting STING1 and thus the cGAS-STING pathway. Counteracts also host DAXX-mediated repression of viral transcription. Displaces a DAXX-binding protein, ATRX, from nuclear domain 10 sites (ND10) shortly after infection. Increases the basal level of SUMOylated DAXX in infected cells. Stimulates quiescent cells to re-enter the cell cycle, proceed through G1 and enter the S phase. Interacts with hypophosphorylated forms of RB1 and induces their degradation by the proteasome without involving ubiquitin conjugation.
Subcellular location: Virion tegument {ECO:0000305}. Host nucleus {ECO:0000269|PubMed:19369322, ECO:0000269|PubMed:9000101}. Host endoplasmic reticulum {ECO:0000269|PubMed:28132838}. Note=Present in the nucleus shortly after infection as well as during the late phase of viral morphogenesis. Detected at nuclear domain 10 (ND10).
Interaction partners:
Sequence:
MSQASSSPGEGPSSEAAAISEAEAASGSFGRLHCQVLRLITNVEGGSLEAGRLRLLDLRTNIEVSRPSVLCCFQENKSPHDTVDLTDLNIKGRCVVGEQDRLLVDLNNFGPRRLTPGSENNTVSVLAFALPLDRVPVSGLHLFQSQRRGGEENRPRMEARAIIRRTAHHWAVRLTVTPNWRRRTDSSLEAGQIFVSQFAFRAGAIPLTLVDALEQLACSDPNTYIHKTETDERGQWIMLFLHHDSPHPPTSVFLHFSVYTHRAEVVARHNPYPHLRRLPDNGFQLLIPKSFTLTRIHPEYIVQIQNAFETNQTHDTIFFPENIPGVSIEAGPLPDRVRITLRVTLTGDQAVHLEHRQPLGRIHFFRRGFWTLTPGKPDKIKRPQVQLRAGLFPRSNVMRGAVSEFLPQSPGLPPTEEEEEEEEEDDEDDLSSTPTPTPLSEAMFAGFEEASGDEDSDTQAGLSPALILTGQRRRSGNNGALTLVIPSWHVFASLDDLVPLTVSVQHAALRPTSYLRSDMDGDVRTAADISSTLRSVPAPRPSPISTASTSSTPRSRPRI
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (P47515)
Organism: Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) (Mycoplasmoides genitalium)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyl dehydrogenase
- Pyruvate dehydrogenase E1 component subunit alpha
- Ribose-phosphate pyrophosphokinase
- L-lactate dehydrogenase
- Probable lipoate-protein ligase A
- Pyruvate kinase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Transketolase
Sequence:
MSKIQVNNIEALNNAMDLALERDQNVVLYGQDAGFEGGVFRATKGLQQKYGSERVWDCPIAENSMAGIGVGAAIGGLKPIVEIQFSGFSFPAMFQIFVHAARIRNRSRGVYTAPLVVRMPMGGGIKALEHHSETLEAIYAQIAGLKTVMPSNPYDTKGLFLAAIESPDPVIFFEPKKLYRAFRQEIPSDYYTVPIGEANLISEGSELTIVSYGPTMFDLINLVYSGELKDKGIELIDLRTISPWDKQTVFNSVKKTGRLLVVTEAVKSFTTSAEIITSVTEELFTYLKKAPQRVTGFDIVVPLARGEKYQFEINARVIDAVNQLLK
Protein: Cell division cycle and apoptosis regulator protein 1 (Cell cycle and apoptosis regulatory protein 1) (CARP-1) (Q8CH18)
Organism: Mus musculus (Mouse)
Function: Associates with components of the Mediator and p160 coactivator complexes that play a role as intermediaries transducing regulatory signals from upstream transcriptional activator proteins to basal transcription machinery at the core promoter. Recruited to endogenous nuclear receptor target genes in response to the appropriate hormone. Also functions as a p53 coactivator. May thus play an important role in transcriptional regulation. May be involved in apoptosis signaling in the presence of the retinoid CD437. Apoptosis induction involves sequestration of 14-3-3 protein(s) and mediated altered expression of multiple cell cycle regulatory genes including MYC, CCNB1 and CDKN1A. Plays a role in cell cycle progression and/or cell proliferation (By similarity). In association with CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. Can act as a both a coactivator and corepressor of AR-mediated transcription. Contributes to chromatin looping and AR transcription complex assembly by stabilizing AR-GATA2 association on chromatin and facilitating MED1 and RNA polymerase II recruitment to AR-binding sites. May play an important role in the growth and tumorigenesis of prostate cancer cells.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}.
Interaction partners:
- U2 snRNP-associated SURP motif-containing protein
- Pre-mRNA-processing factor 40 homolog A
- THO complex subunit 2
- DNA topoisomerase 1
- Transcription elongation regulator 1
- Bcl-2-associated transcription factor 1
- Serine and arginine-rich splicing factor 11
Sequence:
MAQFGGQKNPPWATQFTATAVSQPAALGVQQPSLLGASPTIYTQQTALAAAGLTTQTPANYQLTQTAALQQQAAAVLQQQYSQPQQALYSVQQQLQQPQQTILTQPAVALPTSLSLSTPQPAAQITVSYPTPRSSQQQTQPQKQRVFTGVVTKLHDTFGFVDEDVFFQLGAVKGKTPQVGDRVLVEATYNPNMPFKWNAQRIQTLPNQNQSQTQPLLKTPTAVIQPIVPQTTFGVQAQPQPQSLLQAQISAASITPLLQTQPQPLLQQPQQKAGLLQPPVRIVSQPQPARRLDPPSRFSGRNDRGDQVPNRKDDRSRERDRERRRSRERSPQRKRSRERSPRRERERSPRRVRRVVPRYTVQFSKFSLDCPSCDMMELRRRYQNLYIPSDFFDAQFTWVDAFPLSRPFQLGNYCNFYVMHREVESLEKNMAVLDPPDADHLYSAKVMLMASPSMEDLYHKSCALAEDPQDLRDGFQHPARLVKFLVGMKGKDEAMAIGGHWSPSLDGPNPEKDPSVLIKTAIRCCKALTGIDLSVCTQWYRFAEIRYHRPEETHKGRTVPAHVETVVLFFPDVWHCLPTRSEWETLSRGYKQQLVEKLQGERKKADGEQDEEEKDDGEVKEIATPTHWSKLDPKAMKVNDLRKELESRALSSKGLKSQLIARLTKQLKIEEQKEEQKELEKSEKEEEDEDDKKSEDDKEEEERKRQEEVERQRQERRYILPDEPAIIVHPNWAAKSGKFDCSIMSLSVLLDYRLEDNKEHSFEVSLFAELFNEMLQRDFGVRIYKSLLSLPEKEDKKDKEKKSKKEERKDKKEEREDDIDEPKPKRRKSGDDKDKKEDRDERKKEEKRKDDSKDDDETEEDNNQDEYDPMEAEEAEDEDDDREEEEVKRDDKRDVSRYCKDRPAKDKEKEKPQMVTVNRDLLMAFVYFDQSHCGYLLEKDLEEILYTLGLHLSRAQVKKLLNKVVLRESCFYRKLTDTSKDDENHEESEALQEDMLGNRLLLPTPTIKQESKDGEENVGLIVYNGAMVDVGSLLQKLEKSEKVRAEVEQKLQLLEEKTDEDGKTILNLENSNKSLSGELREVKKDLGQLQENLEVSENMNLQFENQLNKTLRNLSTVMDDIHTVLKKDNVKSEDRDEKSKENGSGV
Protein: Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) (Q9PTS2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway. Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme (By similarity). In vitro also decarboxylates pentacarboxylate porphyrinogen I.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P70697}.
Interaction partners:
- Protoporphyrinogen oxidase
- Uroporphyrinogen III synthase.
- Coproporphyrinogen oxidase.
- Ferrochelatase
- Hydroxymethylbilane synthase a.
- Delta-aminolevulinic acid dehydratase
- Hydroxymethylbilane synthase, b.
- Uncharacterized protein.
- 5-aminolevulinate synthase.
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MMDKDSFILPKDFPELRNDTFLRAARGEEIEHIPVWCMRQAGRYLPEFRESRAGKDFFETCRSPEACCELTLQPLRRFPFDAAIIFSDILVVPQAMGMEVQMCPGKGPTFPEPLKEPEDLQRLKTQVDVYSELDYVFKAITLTRHKIEGKVPLIGFTGAPWTLMSYMIEGGGSATHSKAKRWLYRYPEASHKLLSQLTDVIVEYLLGQVKAGAQALQVFESHTGCLGPVEFKEFSLPYLRDIARRVKDKIKESGLDNVPMIVFAKDGHYGLEDLSESAYEVVGLDWTIDPRSARVRTGGKVSLQGNMDPCALYGTKESISEIVRRMLEGFGTKGYIANLGHGLYPDMDPENVGAFVEAVHNHSRQLLKR
Protein: Coiled-coil domain containing 106 (K7EMI9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNDRSSRRRTKPPEAASSALALMNSVKTQLHMALERNSWLQKRIEDLEEERDFLRCQLDKFISSARMEAEDHCRMKPGPRRMEGDSRGGAGGEASDPESAASSLSGASEEGSASERRRQKQKGGASRRRFGKPKARERQRVKDADGVLCRYKKILGTFQKLKSMSRAFEHHRVDRNTVALTTPIAELLIVAPEKLAEVGEFDPSKERLLEYSRRCFLALDDETLKKVQALKKSKLLLPITYRFKR
Protein: Uncharacterized protein Rv0477 (P9WKV9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Deoxyribose-phosphate aldolase
- Uncharacterized protein Rv0476
- Heparin-binding hemagglutinin
Sequence:
MKALVAVSAVAVVALLGVSSAQADPEADPGAGEANYGGPPSSPRLVDHTEWAQWGSLPSLRVYPSQVGRTASRRLGMAAADAAWAEVLALSPEADTAGMRAQFICHWQYAEIRQPGKPSWNLEPWRPVVDDSEMLASGCNPGSPEESF
Protein: DNA polymerase iota (EC 2.7.7.7) (Eta2) (RAD30 homolog B) (Q9UNA4)
Organism: Homo sapiens (Human)
Function: Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:12606586}. Note=Binding to ubiquitin mediates localization to replication forks after UV-induced DNA damage. {ECO:0000250|UniProtKB:Q6R3M4}.
Interaction partners:
- Proliferating cell nuclear antigen
- RNA polymerase I-specific transcription initiation factor RRN3
- Polyubiquitin-C
- DNA repair protein REV1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Nucleolar transcription factor 1
- Cellular tumor antigen p53
- NAD-dependent protein deacetylase sirtuin-7
- DNA polymerase zeta catalytic subunit
Sequence:
MEKLGVEPEEEGGGDDDEEDAEAWAMELADVGAAASSQGVHDQVLPTPNASSRVIVHVDLDCFYAQVEMISNPELKDKPLGVQQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIAAEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIPGIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHYGRESRQCPIPSHVIQKLGTGNYDVMTPMVDILMKLFRNMVNVKMPFHLTLLSVCFCNLKALNTAKKGLIDYYLMPSLSTTSRSGKHSFKMKDTHMEDFPKDKETNRDFLPSGRIESTRTRESPLDTTNFSKEKDINEFPLCSLPEGVDQEVFKQLPVDIQEEILSGKSREKFQGKGSVSCPLHASRGVLSFFSKKQMQDIPINPRDHLSSSKQVSSVSPCEPGTSGFNSSSSSYMSSQKDYSYYLDNRLKDERISQGPKEPQGFHFTNSNPAVSAFHSFPNLQSEQLFSRNHTTDSHKQTVATDSHEGLTENREPDSVDEKITFPSDIDPQVFYELPEAVQKELLAEWKRAGSDFHIGHK
Protein: RecQ-like DNA helicase BLM (EC 5.6.2.4) (Bloom syndrome protein homolog) (DNA 3'-5' helicase BLM) (RecQ helicase homolog) (Q9I920)
Organism: Gallus gallus (Chicken)
Function: ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair (By similarity). Involved in 5'-end resection of DNA during double-strand break (DSB) repair (By similarity). Negatively regulates sister chromatid exchange (SCE) (By similarity). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution (By similarity). Binds DNA. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Fanconi anemia group M protein
- DNA topoisomerase
- Replication protein A 70 kDa DNA-binding subunit
- RecQ-mediated genome instability protein 1
- Replication protein A 14 kDa subunit
- Uncharacterized protein.
- DNA repair protein RAD51 homolog 1
- DNA replication ATP-dependent helicase/nuclease DNA2
- Replication factor A protein 2
- RecQ-mediated genome instability protein 2
Sequence:
MEEARAATNGGSGESQKLSNGEKSSQLEPGDVGNELLADIELEEDDYLDVVPPSPEEELPSFSPSVRNVSNIFKESPTDGRSAVHGTESEPELMAPKQPAAEQDSSAEHADKGLHLEQQLYSVMEDICKLVDAIPLHELTSISCAKELLQQRELRRKLLADSGALNTNSVNGPRNWKACVQQDPSSRPGTPLCSGPGRGVSSVGSTPKSTNLPSVLSRTVNSSSFSTIRNQTLDKLDTSYSSKETDQEVICLEPAALPSPKVNGKGSTSLSRPSEASFNGSWCEKPTGRDSGNWRVPERPTASTALKAQHTAPAGNPASGCWDVNDTDFDLDHFDIDDFDEGWEEAVAPEAAPEAPPAPQWQPLREGSASLRCRLLAAAAGSAPGPHPTAPKSGCGISAKSSSEPLVHNPAHERFRGMKFSHSEEMLKIFHRKFGLHSFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSAGVTVVISPLRSLIIDQVQKLKTLDIASTYLTGDITDADASKTYMQLSKKDPIIKLLYVTPEKVCASNRLLSALENLYNRKLLARFVIDEAHCVSQWGHDFRKDYKRLNMLRKKFHSVPMMALTATANPRVQKDIQNQLEMLKPQVFTMSFNRHNLKYDVLPKKPKKVAMDCLEWIKKYHPHDSGIIYCLSRHECDTTAAILQKEGLAALAYHAGLTDSNRDLVQKKWVNQEGCQVICATIAFGMGIDKPDVRYVIHASLPKSIEGYYQESGRAGRDGEMSHCLLFYSYSDVTRLRRLILMEKDGNSHTRQTHFNNLYSMVHYCENVVDCRRIQLLAYFGETDFNPNFCKDHPEVICDNCSRKKDYKSRNVTDEVKSIIRFVQQHCGQVGGINGNRNTGSGRYTLNMMVDIFLGAKSAKIQSGIFGKGAAYSRHNVERLFRKLVLDKILDEDLYITANDQAVAYVVLGEKAQAVLNGLLQVEFHETENASAIRKQRASVTKMSQREEMVKKCLGELTDTCKTLGKIFDVHYFNIFSTSTLKKIAETLSSDAEVLLQIDGVTEDKLEKYGAEIIKVMDKYSEWTTPEDAACQSVDTAPGSAGTPGSEEEAADDVVTSSYFGGNANQRRKRKRLPNSGESKRKKTSSGGSQQFYSKGARYRRARRAPGSRAAAPAQSSALRGAGARLGIMAPPKPSSRHFLQPSYAVL
Protein: Formate channel FocB (Formate transporter FocB) (P77733)
Organism: Escherichia coli (strain K12)
Function: Involved in the bidirectional transport of formate during mixed-acid fermentation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- DNA-binding transcriptional activator HyfR
- Hydrogenase-4 component A
- Hydrogenase-4 component D
- Hydrogenase-4 component F
- Hydrogenase-4 component B
- Hydrogenase-4 component G
- Hydrogenase-4 component J
- Hydrogenase-4 component E
- Formate hydrogenlyase transcriptional activator FhlA
Sequence:
MRNKLSFDLQLSARKAAIAERIAAHKIARSKVSVFLMAMSAGVFMAIGFTFYLSVIADAPSSQALTHLVGGLCFTLGFILLAVCGTSLFTSSVMTVMAKSRGVISWRTWLINALLVACGNLAGIACFSLLIWFSGLVMSENAMWGVAVLHCAEGKMHHTFTESVSLGIMCNLMVCLALWMSYCGRSLCDKIVAMILPITLFVASGFEHCIANLFVIPFAIAIRHFAPPPFWQLAHSSADNFPALTVSHFITANLLPVMLGNIIGGAVLVSMCYRAIYLRQEP
Protein: Akirin-1 (protein mighty) (Q99LF1)
Organism: Mus musculus (Mouse)
Function: Molecular adapter that acts as a bridge between proteins, and which is involved skeletal muscle development. Functions as signal transducer for MSTN during skeletal muscle regeneration and myogenesis. May regulate chemotaxis of both macrophages and myoblasts by reorganising actin cytoskeleton, leading to more efficient lamellipodia formation via a PI3 kinase dependent pathway. In contrast to AKIRIN2, not involved in nuclear import of proteasomes (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H9L7}.
Interaction partners:
Sequence:
MACGATLKRPMEFEAALLSPGSPKRRRCAPLPGPTPGLRPPDAEPPPLQMQTPPASLQQPAPPGSERRLPTPEQIFQNIKQEYNRYQRWRHLEVVLSQSEACTSETQPSSSALTAPGSPGAFWMKKDQPTFTLRQVGIICERLLKDYEDKVREEYEQILSTKLAEQYESFVKFTHDQIMRRYGTRPTSYVS
Protein: Dynein regulatory complex subunit 4 (Growth arrest-specific protein 8) (A0A087WZT7)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEEAEERHQVEIKVYKQKVKHLLYEHQNNLTEMKAEGTVVMKLAQKEHRIQESVLRKDMRALKVELKEQELASEVVVKNLRLKHTEEITRMRNDFERQVREIEAKYDKKMKMLRDELDLRRKTELHEVEERKNGQIHTLMQRHEEAFTDIKNYYNDITLNNLALINSLKEQMEDMRKKEDHLEREMAEVSGQNKRLADPLQKAREEMSEMQKQLANYERDKQILLCTKARLKVREKELKDLQWEHEVLEQRFTKVQQERDELYRKFTAAIQEVQQKTGFKNLVLERKLQALSAAVEKKEVQFNEVLAASNLDPAALTLVSRKLEDVLESKNSTIKDLQYELAQVCKAHNDLLRTYEAKLLAFGIPLDNVGFKPLETAVIGQTLGQGPAGLVGTPT
Protein: Maintenance of ploidy protein mob2 (O74558)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for coordinating polarized cell growth during interphase with the onset of mitosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12456722}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12456722}. Note=Localizes to the cell periphery and to the division site during septation and cytokinesis.
Interaction partners:
- Serine/threonine-protein kinase orb6
- Leucine-rich repeat-containing protein sog2
- Mo25-like protein
- Serine/threonine-protein kinase nak1
- Cell polarity protein mor2
- Metallothionein expression activator
- Dual specificity protein kinase lkh1
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MFLLNSLSRITRGNRSKRHQNLSDASSSSGSFSKKSSTSQLVRTGSPSVEPTALYLQQPFVRTHLVKGNFSTIVSLPRFVDLDEWVALNVYELFTYLNHFYDVFATFCTVKTCPVMSAAANFDYTWLDNNRKPVHLPAPQYIEYVLAWIENRLHDQNVFPTKAGLPFPSNFLVIVKAIYKQMFRIFAHMYYAHYAEILHLSLEAHWNSFFAHFIAFGKEFQLLDKRDTAPLKDLIVVLENQGNI
Protein: Thermosome, alpha subunit (Q3AF10)
Organism: Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Interaction partners:
- Chaperone protein DnaK
- Protein GrpE
- Co-chaperonin GroES
- Heat-inducible transcription repressor HrcA
- Chaperone protein DnaJ
- Flagellar motor switch protein
- Inosine-5'-monophosphate dehydrogenase
- Negative regulator of genetic competence clpC/mecB
- Bifunctional NAD
- ATP-dependent protease ATPase subunit HslU
Sequence:
MKKENQTQEIEERYQALFSNAAAVKALTQVVANSLGPKGLDAMLVDRFGEVVVTNDGVTILTLMDAQHPAARMVVNMARAQEREVGDGTTTAAVLAGALVSEGVNQILKGVPVSKVLAGMNRALNHALFLIRKNAIKVGSITDDRLLAAAKIAGRGDERVAAILRDAAAMLEDKLQDPGFKLADLVLAKVGADTTLIPGVVINKSPLWEEGSQKLQEVRLLVLDDGLYPEEVEEEALASEAGFEQYLKNQKIFQENLKKLKELGVKLILLTRGISDIAEEFCYENEIMVITRITQKELKRVLEFTGARAAKRTSLNKPVEELQKMLGYARTCFYDSRLDFTIIEGGAGKATATVLIGAATDEVVDEQERIAKDAAGSFAAAYRSGVLPGGGAFFLYLSREVESLKNRLPGMESYGVMAFSEALKVPFRVMAENAGFNGLEKLGDLMTLQVQKNNYALGLDFETGEFIDMIAGGVVDPAEVVYQAVKNASEVAISLLKINTIIKMKDYEVLKEGEQEDGGKR
Protein: Glycogen synthase (EC 2.4.1.21) (Starch [bacterial glycogen] synthase) (P0A6U8)
Organism: Escherichia coli (strain K12)
Function: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Interaction partners:
- Glycogen debranching enzyme
- Glucose-1-phosphate adenylyltransferase
- Glycogen phosphorylase
- 1,4-alpha-glucan branching enzyme GlgB
- 4-alpha-glucanotransferase
- Maltodextrin phosphorylase
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Trehalose-6-phosphate hydrolase
Sequence:
MQVLHVCSEMFPLLKTGGLADVIGALPAAQIADGVDARVLLPAFPDIRRGVTDAQVVSRRDTFAGHITLLFGHYNGVGIYLIDAPHLYDRPGSPYHDTNLFAYTDNVLRFALLGWVGAEMASGLDPFWRPDVVHAHDWHAGLAPAYLAARGRPAKSVFTVHNLAYQGMFYAHHMNDIQLPWSFFNIHGLEFNGQISFLKAGLYYADHITAVSPTYAREITEPQFAYGMEGLLQQRHREGRLSGVLNGVDEKIWSPETDLLLASRYTRDTLEDKAENKRQLQIAMGLKVDDKVPLFAVVSRLTSQKGLDLVLEALPGLLEQGGQLALLGAGDPVLQEGFLAAAAEYPGQVGVQIGYHEAFSHRIMGGADVILVPSRFEPCGLTQLYGLKYGTLPLVRRTGGLADTVSDCSLENLADGVASGFVFEDSNAWSLLRAIRRAFVLWSRPSLWRFVQRQAMAMDFSWQVAAKSYRELYYRLK
Protein: Multicopper oxidase abr1 (EC 1.-.-.-) (Conidial pigment biosynthesis oxidase abr1) (Q4WZB4)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Multicopper oxidase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall. The first step of the pathway is the production of the heptaketide naphtopyrone YWA1 by the polyketide synthase alb1 though condensation of acetyl-CoA with malonyl-CoA. The naphtopyrone YWA1 is then converted to the pentaketide 1,3,6,8-tetrahydroxynaphthalene (1,3,6,8-THN) by the heptaketide hydrolyase ayg1 though chain-length shortening. 1,3,6,8-THN is substrate of the hydroxynaphthalene reductase arp2 to yield scytalone. The scytalone dehydratase arp1 then reduces scytalone to 1,3,8-THN. 1,3,8-THN is also substrate of the hydroxynaphthalene reductase arp2 to yield vermelone. Vermelone is further converted by the multicopper oxidase abr1 to 1,8-DHN. Finally the laccase abr2 transforms 1,8-DHN to DHN-melanin. DHN-melanin biosynthesis appears to be initiated in endosomes where early enzymes (abl1, ayg1, arp1 and arp2) localize, with exocytosis leading to melanin deposition on the cell surface where late enzymes (abr1 and abr2) localize. DHN-melanin is an important structural component of the outer cell wall and is required for the presence of conidial surface hydrophobins. DHN-melanin also plays a crucial role in fungal virulence, including a protective role against the host's immune defenses. DHN-melanin protects also conidia against amoeba predation.
Subcellular location: Secreted {ECO:0000269|PubMed:26972005}. Cell surface {ECO:0000269|PubMed:24123270, ECO:0000269|PubMed:26972005}. Note=Localized at the surface of stalks and conidiophores, but not in young hyphae (PubMed:24123270). {ECO:0000269|PubMed:24123270}.
Interaction partners:
- Hydroxynaphthalene reductase arp2
- Heptaketide hydrolyase ayg1
- Conidial pigment polyketide synthase alb1
- Scytalone dehydratase arp1
Sequence:
MFHSRALLLSWLVGFTAAKDIHLDWNITWVWAAPDGFGRPMIGINNEWPCPIVNADLGDRLIVDVHNGLGNQSTGIHWHGFHQYMTGTMDGSNQVTQCALPPGSSMRYEFDVNQTGTYWYHSHEMGQYPDGLRGPFIVRDPSPPFAYDDEFTLTLTDHYHEQMSVLLQQYEADSVGAQAGVNEPLPAAALINEGFDTTTLRVEPNKTYLIHLVCVGNWPGHVIVFDDHEISVVEVDGTWVDAYPARDKKIRLATGQRMSILLKTKDNTDRNYAIWDSMDVNMMFFYQNRAIPEGFNPNTTAWLVYDEAKELPPAPDVHELDPNNDFVDDLVFVPASHEPLLEKVDRQIIFDTGVTQRDGRSVYTINGQTYVDPEEPTLYTALAASPENASNASLYGQVNPFVVQYGEVVEIIINNHHGNLHPWHMHGHQFQVLQRTIPEGGYFDGYFANISSTPVKRDTIMVQNHGHAVLRFRANNPGVWLIHCHIEWHVTKGLTGTLIEAPAQMHKISVPLDHQRICPSYGTPPGGTPSSPPHDAPRPDGASGSPQYPPKPWGEPDASAPEQDDSQPGGTPDSPEDFPQPWGEPEESPQEPPQPWSPSNNAQPPANTYAPEYPSGYVPVAPGPVIIDSELHYGGKSSHVECSGVNAGHTQDTTTGGDGCANAS
Protein: Flagellum transition zone component (Q9NH46)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MQSGVGNITTPTSPQQLVVEAPAELLETCGVQYPAAADVNEGEVVDSKALSAAPGERDVSGCGPTLLSLLYSTQKKDEVGHRAVTPMLWECNGAQKRCHSSKRDFTTCVKARKSPPPGSATGSGTGAIRDFLRPYRESHSKRFRAKVVDCRAALSVDDQIITLKNENAKYKAQLLTKDVQLKELEAALRAFRAPRVPVPSGVTEPAEVGGCYNGTDTEVARLTRENGEVWRRLQQSHAQLAVWKRDARVSKLQELKMELAVYQAEVARLVAEVPSSGGAGGAQNHPARSKLQREAETSRAKDLFIAELKERASENATALRKCMDDAMRTKSTLEQVREENELISKELCLFRKTALALTRVQEELRATQCELAEARERLQAFEQMMHTVGGPEEVKAVVKERDALLTLLKQHNAREAAYHREFFTRQREMKESMERCLQEAVQQERALAQDREMQLRRSCLMWKERCERLLPDKSFEQGRLIEGGGTVVGDEEQQTELHQLPKKIVTPFMDNSQRQRLLTKHIDDVLIVRQVSSTSAPASSSTTLSPVSGLSKLSITDTTQSQSSPHGMQVSHPGNEDASSPVKGNVMSSQKGSSGDAPVPPTERTDPDGGAVSYPASSAVISAERTSLVESSKGDIVTSISTEEGAVQLPRGLMTAGVDSSDDSGSELSDLAVGIEEGKTPSFRLHGNSDGQLIPEVVSRMPLTLRTVSSNGVAAVLTVASPPPRVSVPPAPVPRESAGSIASSENKLSDVNAAVPPPRVSVPPAPVPRESAGSIASSENKLSDVNVAVPPPRVSVPPAPVPRESAGSIASSENKLSDVNVAVPPPRVSVPPAPVP