wanglab/gogpt-training-data huggingface dataset:
Protein: Quinone oxidoreductase-like protein (Zinc-binding dehydrogenase family protein) (Q9LFK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADPH-dependent alkenal/one oxidoreductase, chloroplastic
Sequence:
MATTINKQVVLLDYVTGFAKESDLVITSTTIDLRVLKGSMTALVKNLYLSCDPYMRNRMRKPDPLSPATAQSFTPGKPISGFGVSKVIDSGHSDYEEGDLIWGAVGWEEYSVITPIPNLHFKIHHTNFPLSYYTGLLGMPGMTAYVGFYEICTPKKGDTVFVSAASGAVGQLVGQFAKLMGCYVVGSAGSKEKVDLLKNKFGFDDAFNYKEEHNLIGALKRCFPEGIDIYFENVGGKMLDAVILNMRPHGRIAACGMISQYNLKNPEGIYGLSLITYKRIRIEGFNCFDYFHKYSEFLEFVVPYIKEGKIKYVEDVADGLESAPAALVGLFHGKNVGKQLVVVSPS
Protein: BLOC-1-related complex subunit 5 (G3V1P3)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome membrane {ECO:0000256|ARBA:ARBA00004122}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004122}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004122}.
Interaction partners:
Sequence:
MTPSPAKHRAKMDDIVVVAQGSQASRNVSNDPDVIKLQEIPTFQPLLKGLLSGQTSPTNAKLEKLDSQQVLQLCLRYQDHLHQCAEAVAFDQNALVKRIKEMDLSVETLFSFMQERQKRYAKYAEQIQKVNEMSAILRRIQMGIDQTVPLLDRLNSMLPEGERLEPFSMKPDRELRL
Protein: Epoxide hydrolase B (EHB) (EC 3.3.2.10) (P95276)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Function: Could be involved in detoxification of extraneous host-cell epoxides. Catalyzes the hydrolysis of small aromatic epoxide-containing substrates such as trans-1,3-diphenylpropene oxide, trans and cis-stilbene oxide, and terpenoid epoxide.
Interaction partners:
Sequence:
MSQVHRILNCRGTRIHAVADSPPDQQGPLVVLLHGFPESWYSWRHQIPALAGAGYRVVAIDQRGYGRSSKYRVQKAYRIKELVGDVVGVLDSYGAEQAFVVGHDWGAPVAWTFAWLHPDRCAGVVGISVPFAGRGVIGLPGSPFGERRPSDYHLELAGPGRVWYQDYFAVQDGIITEIEEDLRGWLLGLTYTVSGEGMMAATKAAVDAGVDLESMDPIDVIRAGPLCMAEGARLKDAFVYPETMPAWFTEADLDFYTGEFERSGFGGPLSFYHNIDNDWHDLADQQGKPLTPPALFIGGQYDVGTIWGAQAIERAHEVMPNYRGTHMIADVGHWIQQEAPEETNRLLLDFLGGLRP
Protein: Biotin carboxyl carrier protein of acetyl-CoA carboxylase 2, chloroplastic (AtBCCP2) (BCCP-2) (Q9LLC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:11299381}.
Interaction partners:
- Biotin carboxylase, chloroplastic
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- Cytochrome c1 1, heme protein, mitochondrial
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- EMBRYO DEFECTIVE 3147
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
Sequence:
MASLSVPCVKICALNRRVGSLPGISTQRWQPQPNGISFPSDVSQNHSAFWRLRATTNEVVSNSTPMTNGGYMNGKAKTNVPEPAELSEFMAKVSGLLKLVDSKDIVELELKQLDCEIVIRKKEALQQAVPPAPVYHSMPPVMADFSMPPAQPVALPPSPTPTSTPATAKPTSAPSSSHPPLKSPMAGTFYRSPGPGEPPFVKVGDKVQKGQIVCIIEAMKLMNEIEAEKSGTIMELLAEDGKPVSVDTPLFVIAP
Protein: Phytoene desaturase (Phytoene desaturase (3,4-didehydrolycopene-forming)) (Q67GI0)
Organism: Blakeslea trispora (Choanephora trispora)
Interaction partners:
Sequence:
MSDQKKHIVVIGAGIGGTATAARLAREGFRVTVVEKNDFSGGRCSFIHHDGHRFDQGPSLYLMPKLFEDAFADLDERIGDHLDLLRCDNNYKVHFDDGDAVQLSSDLTKMKGELDRIEGPLGFGRFLDFMKETHVHYEQGTFIAIKRNFETIWDLIRLQYVPEIFRLHLFGKIYDRASKYFQTKKMRMAFTFQTMYMGMSPYDAPAVYSLLQYTEFAEGIWYPRGGFNMVVQKLESIASKKYGAEFRYQSPVAKINTVDKDKRVTGVTLESGEVIEADAVVCNADLVYAYHHLLPPCNWTKKTLASKKLTSSSISFYWSMSTKVPQLDVHNIFLAEAYKESFDEIFNDFGLPSEASFYVNVPSRIDESAAPPNKDSIIVLVPIGHMKSKTGNSAEENYPELVNRARKMVLEVIERRLGVNNFANLIEHEEVNDPSVWQSKFNLWRGSILGLSHDVFQVLWFRPSTKDSTNRYDNLFFVGASTHPGTGVPIVLAGSKLTSDQVCKSFGQNPLPRKLQDSQKKYAPEQTSKTESHWIYYCLACYFVTFLFFYFFPRDDTTTPASFINQLLPNVFQVQNSNDIRI
Protein: Transposon Ty1-BR Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)] (Q12193)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLSNYPHISHGSACASVTSKEVHTNQDPLDVSASKIQEYDKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRPITDDELTFLYNAFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNPSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQKLTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSLKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKDSRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSNDLNIESDHDFQSDIELYPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISDIESTDSGGMHRLDVPLLAPMSQSNTHESSYASKSKDFRHSDSYSDNETNHTNVPISSTGGTNNKTVPQTSEQETEKRIIHRFTSDRILPSSESNSLHHVVPIKTSDTCFKENTEESIIADLPLPDLPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDKYYDRKEIDPKRVINSMFIFNRKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNSNKRIIAKLKMQYDTKIINLGESDDEIQHDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPNGRKLGAPGQPGLYINQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: Rho guanine nucleotide exchange factor 11 (RhoGEF glutamate transport modulator GTRAP48) (Q9ES67)
Organism: Rattus norvegicus (Rat)
Function: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Note=Translocated to the membrane upon stimulation. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-13
- Transforming protein RhoA
- Guanine nucleotide-binding protein subunit alpha-12
- Plexin B2
- RSA-14-44 protein.
- Rho guanine nucleotide exchange factor 12
- Plexin-B1
- Rho guanine nucleotide exchange factor 1
- A-kinase anchor protein 13
- Rho-related GTP-binding protein RhoB
Sequence:
MSIRLPHSIDRSASKKQSHLSSPIASWLSSLSSLGDSTPERTSPSHHRQPSDTSETTAGLVQRCVIIQKDQHGFGFTVSGDRIVLVQSVRPGGAAMKAGVKEGDRIIKVNGTMVTNSSHLEVVKLIKSGAYAALTLLGSSPPSVGVSGLQQNPSVAGVLRVNPIIPPPPPPPPLPPPQHITGPKPLQDPEVQKHATQILWNMLRQEEEELQDILPPCGETSQRTCEGRLSVDSQEADSGLDSGTERFPSISESLMNRNSVLSDPGLDSPQTSPVILARVAQHHRRQGSDAALLPLNHQGIDQSPKPLIIGPEEDYDPGYFNNESDIIFQDLEKLKSHPAYLVVFLRYILSQADPGPLLFYLCSEVYQQTNPKDSRSLGKDIWNIFLEKNAPLRVKIPEMLQAEIDLRLRNNEDPRNVLCEAQEAVMLEIQEQINDYRSKRTLGLGSLYGENDLLGLDGDPLRERQMAEKQLAALGDILSKYEEDRSAPMDFAVNTFMSHAGIRLRESRSSCTAEKTQSAPDKDKWLPFFPKTKKQSSNSKKEKDALEDKKRNPILRYIGKPKSSSQSIKPGNVRNIIQHFENSHQYDVPEPGTQRLSTGSFPEDLLESDSSRSEIRLGRSGSLKGREEMKRSRKAENVPRPRSDVDMDAAAEAARLHQSASSSASSLSTRSLENPTPPFTPKMGRRSIESPNLGFCTDVILPHLLEDDLGQLSDLEPEPEVQNWQHTVGKDVVANLTQREIDRQEVINELFVTEASHLRTLRVLDLIFYQRMRKENLMPREELARLFPNLPELIEIHNSWCEAMKKLREEGPIIRDISDPMLARFDGPAREELQQVAAQFCSYQSVALELIRTKQRKESRFQLFMQEAESHPQCRRLQLRDLIVSEMQRLTKYPLLLENIIKHTEGGTSEHEKLCRARDQCREILKFVNEAVKQTENRHRLEGYQKRLDATALERASNPLAAEFKSLDLTTRKMIHEGPLTWRISKDKTLDLQVLLLEDLVVLLQRQEERLLLKCHSKTAVGSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSELGPPQIYELVALTSSDKNIWMELLEEAVQNATKHPGAAPIPIHPSPPGSQEPAYQGSTSSRVEINDSEVYHTEKEPKKLPEGPGPEQRVQDKQLIAQGEPVQEEDEEELRTLPRAPPSLDGENRGIRTRDPVLLALTGPLLMEGLADAALEDVENLRHLILWSLLPGHTVKTQAAGEPEDDLTPTPSVVSITSHPWDPGSPGQAPTISDSTRLARPEGSQPEGEDVAVSSLAHLPPRTRSSGVWDSPELDRNPAAEAASTEPAASYKVVRKVSLLPGGGVGAAKVAGSNAIPDSGQSESELSEVEGGAQATGNCFYVSMPAGPLDSSTEPTGTPPSPSQCHSLPAWPTEPQPYRGVRGGQCSSLVRRDVDVIFHTIEQLTIKLHRLKDMELAHRELLKSLGGESSGGTTPVGSFHTEAARWTDYSLSPPAKEALASDSQNGQEQGSCPEEGSDIALEDSATDTAVSPGP
Protein: Heat shock 70 kDa protein 8 (Heat shock protein 70-8) (AtHsp70-8) (Heat-shock protein 70T-2) (Q9SKY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions.
Interaction partners:
- Heat shock protein 90-1
- Chaperone protein ClpB1
- Chaperone protein ClpB4, mitochondrial
- 15.7 kDa heat shock protein, peroxisomal
- DNAJ heat shock N-terminal domain-containing protein
- 26.5 kDa heat shock protein, mitochondrial
- 23.5 kDa heat shock protein, mitochondrial
- 17.6 kDa class I heat shock protein 3
- Heat shock protein 90-5, chloroplastic
- 23.6 kDa heat shock protein, mitochondrial
Sequence:
MAEAAYTVASDSENTGEEKSSSSPSLPEIALGIDIGTSQCSIAVWNGSQVHILRNTRNQKLIKSFVTFKDEVPAGGVSNQLAHEQEMLTGAAIFNMKRLVGRVDTDPVVHASKNLPFLVQTLDIGVRPFIAALVNNAWRSTTPEEVLAIFLVELRLMAEAQLKRPVRNVVLTVPVSFSRFQLTRFERACAMAGLHVLRLMPEPTAIALLYAQQQQMTTHDNMGSGSERLAVIFNMGAGYCDVAVTATAGGVSQIKALAGSPIGGEDILQNTIRHIAPPNEEASGLLRVAAQDAIHRLTDQENVQIEVDLGNGNKISKVLDRLEFEEVNQKVFEECERLVVQCLRDARVNGGDIDDLIMVGGCSYIPKVRTIIKNVCKKDEIYKGVNPLEAAVRGAALEGAVTSGIHDPFGSLDLLTIQATPLAVGVRANGNKFIPVIPRNTMVPARKDLFFTTVQDNQKEALIIIYEGEGETVEENHLLGYFKLVGIPPAPKGVPEINVCMDIDASNALRVFAAVLMPGSSSPVVPVIEVRMPTVDDGHGWCAQALNVKYGATLDLITLQRKM
Protein: Alpha-mannosidase (EC 3.2.1.-) (Q6P762)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Alpha-mannosidase 2C1
- Alpha-mannosidase
Sequence:
MGTGSLAPGVRAGGGNTGWLWMSSCNLGLPVLSISFLIWLLLAAPGAQAAGYKTCPTTKPGMLNVHLLPHTHDDVGWLKTVDQYYYGIMSDVQHASVQYILDSVIYSLLNDPTRRFIYVEMAFFSRWWKQQTNVTQDAVRNLVRQGRLEFVNGGWVMNDEAATHYGAIVDQMTLGLRFLQDTFGSDGLPRVAWHIDPFGHSREQASLFAQMGFDGFFLGRIDYQDKFNRKRKLKMEELWRASASLKPPAADLFTGVLPNNYNPPKDLCWDVLCTDPPVVDDPTSPEFNANKLVDYFLNLASSQKKYYRTNHTVMTMGSDFQYENANMWFKNMDKLIRLVNEQQANGSKVHVLYSTPSCYLWELNKANLTWTVKEDDFFPYADGPHMFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGPEAKVGPYGSGDSAPLNEAMAVLQHHDAVTGTARQNVVNDYAKQLAAGWGPCEVLVSNALARLSLYKQNFSFCREINISICPASQTSEHFRVIIYNPVGRKVDLMVRLPVSEGIFLVKDPNDRRISSNVVMVPSAYSKTYQWELLFPASVPALGFSIYSVNKMSGHNHQAHNLTARPKKSKSRVLVIENKYIRATFDSDTGLLRKIENLEQNISLPVRQGFFWYNASAGDEESPQASGAYIFRPSHRKPLPVSHWAQVTLVKTNLVQEVHQNFSAWCSQVIRLYEGQRHLELEWTVGPIPVKDDWGKEVISRFNTPMRTRGQFFTDSNGREILKRRDDFRPTWTLNQTEPVAGNYYPVNTRIYITDGHMQLTVLTDRSQGGSSLLDGSLELMVHRRLLVDDERGVAEPLLETDTGDKVRGRHLVILSSVSDAAARHRLLAEQEVLAPQVVLAHGGSSPYHSQAPKMQFSALRRELPPQVHLLTLARWGPKMLLLRLEHQFAVKEDSNRNLSSPVTLNLQNLFKTFTINYLQETTLAANQPLSRVSRLKWMTDTGPISYPAPSRLDPTSITLQPMQIRTFLASVQWQRLI
Protein: Protein CASC2, isoform 3 (Cancer susceptibility candidate gene 2 protein, isoform 3) (Q6XLA1)
Organism: Homo sapiens (Human)
Function: May act as a potential tumor suppressor.
Interaction partners:
Sequence:
MTQEKMYPHLFSERCANQHQHRTAEEKKYVSEKQLIHWRCEEPSAHHNSIDIKRMKHFGSALRLRQTFHLDTADHPCVITMNPALPWKLEGSNSTSTLPLPA
Protein: Uncharacterized RNA-binding protein C57A7.13 (P87143)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Splicing factor U2AF 59 kDa subunit
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43
- Uncharacterized mitochondrial carrier C12B10.09
- Uncharacterized protein C25H2.10c
- UPF0612 protein C337.02c
- Uncharacterized nucleolar protein C2C4.08
- Probable transcriptional repressor C1348.12
- Uncharacterized transcriptional regulatory protein C11D3.11c
- Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16
- Putative alpha-ketoglutarate-dependent sulfonate dioxygenase
Sequence:
MKDYYSENGFEEIFEEKGSTSSNISDNCASRDYDVNISSDNPRLLDSYRPKGNYGRDRNSPLSRHIGVPNQEIILQGLTPEILEEHIELALYATGAKVSTVTLIREKETQKSRCFAFAKFVSLQDSKDWMEANFPTLVIDGIDVSVRFSRAAREQIEGWCCQNCDILNYSYRESCFKCRVPRNQASIAIGNHKISKRNGDMDVSDVPSVYLILRNLDRSLSEETLWKGLSKLEIDVQRVFMIRYKFNDAFCGYAILEFKDVDESAKALMKARTYPGKGFTLASRKVSVDYIHDGVLIPAYTESARWQFPTKTGYLVYWDPELYCSIYVPEGIDTDQFKPIEVNKKPKKEKRARSSNYIDVPASKKVATSLQRWNDAQKELKDNIPDLSEEEEKLLLHFVWKSALICVLCERKFQSWGHVVKHITQSIMHNNNLKNHELVSSAELLMHRVRQTESVDYRDRATERRIVPAASSDTIVEAKKSSQGSSFHSTSNVSMKMLNSMGWNKGSGLGTNENGIKEAIQPTMYLPGVGLGNKGSKIQINMTPVDRVKDRARSLYFQNDKNNNL
Protein: Protein BANP (Btg3-associated nuclear protein) (Scaffold/matrix-associated region-1-binding protein) (Q8VBU8)
Organism: Mus musculus (Mouse)
Function: Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest and inhibits tumor growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:10940556, ECO:0000269|PubMed:12494467, ECO:0000269|PubMed:15371550, ECO:0000269|PubMed:16166625}. Nucleus speckle {ECO:0000250|UniProtKB:Q8N9N5}. Cytoplasm {ECO:0000250|UniProtKB:Q8N9N5}. Note=Primarily nuclear but translocates to the cytoplasm following MAPK1/MAPK3-mediated phosphorylation. {ECO:0000250|UniProtKB:Q8N9N5}.
Interaction partners:
- Cellular tumor antigen p53
- Histone deacetylase 1
Sequence:
MMSEQDLADVVQIAVEDLSPDHPVVLENHVVTDDDEPALKRQRLEINCQDPSIKSFLYSINQTICLRLDSIEAKLQALEATCKSLEEKLDLVTNKQHSPIQVPMVAGSPLGATQTCNKVRCVVPQTTVILNNDRQNAIVAKMEDPLSNRAPDSLENIISNAVPGRRQNTIVVKVPGQDDSHNEDGESGSEASDSVSNCGQPGSQNIGSNVTLITLNSEEDYPNGTWLGDENNPEMRVRCAIIPSDMLHISTNCRTAEKMALTLLDYLFHREVQAVSNLSGQGKHGKKQLDPLTIYGIRCHLFYKFGITESDWYRIKQSIDSKCRTAWRRKQRGQSLAVKSFSRRTPSSSSYSASETMMGTPPPTSELQQSQPQALHYALANAQQVQIHQIGEDGQVQVIPQGHLHIAQVPQGEQVQITQDSEGNLQIHHVGQDGQSWGLCQNPIPVSGDSVAQANPSQLWPLGGDTLDLPAGNEMIQVLQGAQLIAVASSDPAATGVDGSPLQGSDIQVQYVQLAPVSDHTAAAQTAEALQPTLQPDMQLEHGAIQIQ
Protein: Alpha-glucosidase (EC 3.2.1.20) (Maltase) (Q9C0Y4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.
Subcellular location: Secreted.
Interaction partners:
- Alpha-glucosidase
- Invertase
- Putative beta-glucosidase
- Alpha-galactosidase mel1
- Probable glucoamylase
- Hexokinase-1
- Hexokinase-2
- Glucan 1,3-beta-glucosidase
- Putative invertase
- Uncharacterized family 31 glucosidase C30D11.01c
Sequence:
MMISTAYQSLFLTALFSAISIAVGNVYQTLNVIGDRNVTIPTNGIPQRLSVYDPYRGVNCQGYQAVNISESQNGVTAYLALLGEPCYAYGTDYPLLFLNVTYEEADRVHISIKDANNTQFQFTSRKDLWDAPLYSPSYNNTNLLYNFSYNANPFEFWVTRKSDGEVLFDTRGQKLVFEDQYIELTTNMVENYNLYGLAETIHGLRLGNNLTRTFWANDEPSPVDQNMYGSHPYYLEQRYKADGINSTLNETTYTSSSHGVLMLTANGMDVLLRQDYLQYRMIGGVIDLFVYSGSTESPKETVKQFVQSIGKPAMHQYWTLGYHSCRWGYTNITEIMDVRQNYIDADIPVETFWSDIDYMEKYRDFTVDPVSYSKSDMQTFFSDLVSNHQHYVPIIDAAIYAANPYNHTDDSYYPYYAGVEKDIFLKNPNGSIYIGAVWPGFTAFPDFTNPDVVDYWKDCLINLTYAFGSNGTVPFSGIWTDMNEPSSFCVGSCGSAMIDLNPAEPLTGISKQYSIPEGFNVSNVTEYSSAYSASLSNYYATATSSVFQIVSPTATPLGLKPDYNIDWPPYAINNEQGNHDIANHIVSPNATTHDGTQRYDIFNMYGYGETKVSYAALTQISPNERPFILSRSTFLGSGVYGAHWLGDNHSLWSNMFFSISGMIVFNMMGIPMVGADVCGFLGDSDEELCSRWMAMGAFSPFYRNHNNIYQISQEPYTWSSVAEASRRAMYIRYSLLPYWYTIMAKASQDGTPALRALFVEFPNDPTLADVDRQFMVGDSLLVTPVLEPNVEYVQGVFPGDNSTVWYDWYNHTEIVRQYNENVTLYAPLEHINVAIRGGSVLPMQQPSLTTYESRQNPFNLLVALDRDGSATGELYLDDGVSIELNATLSVSFTFSDGVLSAVPTGSYEVSQPLANVTILGLTESPSSITLNGQNVSSFQYSNDTEELLITGLQNITSSGAFANSWNLTL
Protein: chitinase (EC 3.2.1.14) (G8BHR4)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- chitinase
Sequence:
MLSNTLLALLATSASALAASNSVAVYWGQNGAGGQDRLSTYCADSNVDVVILSFLNDFPDPTNVNFANQCGATYPSGLLHCSAIGEDIKTCQASGKKVLLSLGGAAGNYGFKTTDDAVAYADTLWNKFGNGKDDEERPFDDAVVDGFDFDIELGTSTGYPELATALKSKFDSSKKYYLSASPQCVYPDAHVGPLLEKVPLDFAFIQFYNNPCSVDGQFNYDTWSKFASSSPNPDLKLYVGVPSTGNVAGYVDAATLAKSIDEIKCDKHFAGVSLWDASGAWLNTDASGANFADQVKKVLDDNTCPAPSSSSTTASPSTTTNNNKDIVDPTSAVVSPSGGYQNTTITKDPVVSTATNIHTTIITVTSCDDHKCSEVPVTTGVLTVSEVDTVYTTYCPLPTTSAKPTTSVKAPASTVTNIETAIVTITSCEDNKCTEVPVTTGVVTITDVDTVYTTYCPLPTTTAAASKPAPVAPVESSTAPAPVAPVESSTAPAPVAPVESSTAPAPVAPVESSTAPAPTVAAPSVEAETLTTTYDLTSTVAPEQQAPASSSAAAPEIISTYEGAAASNNAMWFSVPLVFIAALL
Protein: Zinc-finger homeodomain protein 9 (AtZHD9) (Homeobox protein 34) (AtHB-34) (Q9LHF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000250}. Note=Interactions with MIF proteins prevent nuclear subcellular location and leads to a scattered repartition throughout the cytoplasm.
Interaction partners:
- Homeobox-DDT domain protein RLT2
- Protein ANTHESIS POMOTING FACTOR 1
- RING/FYVE/PHD zinc finger superfamily protein
- Transcription factor bHLH154
Sequence:
MLEVRSMDMTPKSPEPESETPTRIQPAKPISFSNGIIKRHHHHHHNNNKVTYKECLKNHAAAIGGHALDGCGEFMPSPSSTPSDPTSLKCAACGCHRNFHRRETDDSSAVPPPSLLPSSTTTAAIEYQPHHRHHPPPPLAPPLPRSPNSSSPPPISSSYMLLALSGNNKTAPFSDLNFAAAANHLSATPGSRKRFRTKFSSNQKEKMHEFADRIGWKIQKRDEDEVRDFCREIGVDKGVLKVWMHNNKNSFKFSGGGATTVQRNDNGIGGENSNDDGVRGLANDGDGGGGRFESDSGGADGGGNVNASSSSS
Protein: GATA transcription factor 7 (O65515)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Probable serine/threonine protein kinase IREH1
- Protein EFFECTOR OF TRANSCRIPTION 2
- Myb family transcription factor EFM
- Protein ARABIDILLO 1
- Dof zinc finger protein DOF4.6
Sequence:
MECVEAFLGDFSVDDLLDLSNADTSLESSSSQRKEDEQEREKFKSFSDQSTRLSPPEDLLSFPGDAPVGDLEDLEWLSNFVEDSFSESYISSDFPVNPVASVEVRRQCVPVKPRSKRRRTNGRIWSMESPSPLLSTAVARRKKRGRQKVDASYGGVVQQQQLRRCCSHCGVQKTPQWRMGPLGAKTLCNACGVRFKSGRLLPEYRPACSPTFTNEIHSNSHRKVLELRLMKVADPARV
Protein: LIM domain kinase 2 (LIMK-2) (EC 2.7.11.1) (P53670)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP. Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity).
Subcellular location: [Isoform LIMK2A]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.; SUBCELLULAR LOCATION: [Isoform LIMK2B]: Cytoplasm {ECO:0000250|UniProtKB:P53671}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P53671}. Nucleus {ECO:0000250|UniProtKB:P53671}.; SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53671}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P53671}.
Interaction partners:
- Cofilin-1
- Cofilin 2
- Rho-associated protein kinase 1
- Rho-associated protein kinase 2
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase PAK 1
- Serine/threonine-protein kinase PAK 5
- Serine/threonine-protein kinase PAK 3
- Serine/threonine-protein kinase PAK 2
- non-specific serine/threonine protein kinase
Sequence:
MAALAGEEAWRCRGCGNYVPLSQRLYRTANEAWHSSCFRCSECQESLTNWYYEKDGKLYCHKDYWAKFGEFCHGCSLLMTGPAMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQDQLPYSVTLISMPATTECRRGFSVSVESASSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAINQTSQTLQLLIEHDPVPQRLDQLRLDTRLSPHMQSSGHTLMLSTLDAKENQEGTLRRRSLRRSNSISKSPGPSSPKEPLLLSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRNVDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRPPVEKAATKKRTLRKSDRKKRYTVVGNPYWMAPEMLNGKSYDETVDVFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCKLEPESRPAFSKLEDSFEALSLFLGELAIPLPAELEELDHTVSMEYGLTRDSPP
Protein: Small ribosomal subunit protein uS13A (40S ribosomal protein S18-A) (P0CX55)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS27A
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein eS26A
- Small ribosomal subunit protein uS3
Sequence:
MSLVVQEQGSFQHILRLLNTNVDGNIKIVYALTTIKGVGRRYSNLVCKKADVDLHKRAGELTQEELERIVQIMQNPTHYKIPAWFLNRQNDITDGKDYHTLANNVESKLRDDLERLKKIRAHRGIRHFWGLRVRGQHTKTTGRRRA
Protein: Lymphocyte-specific protein 1 (47 kDa actin-binding protein) (52 kDa phosphoprotein) (pp52) (Lymphocyte-specific antigen WP34) (P33241)
Organism: Homo sapiens (Human)
Function: May play a role in mediating neutrophil activation and chemotaxis.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Kinase suppressor of Ras 1
- CD209 antigen
- MAP kinase-activated protein kinase 2
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- Ubiquitin carboxyl-terminal hydrolase CYLD
- Rho guanine nucleotide exchange factor 12
- C-type lectin domain family 7 member A
- HLA class I histocompatibility antigen, A alpha chain
- C-type lectin domain family 4 member M
- RAF proto-oncogene serine/threonine-protein kinase
Sequence:
MAEASSDPGAEEREELLGPTAQWSVEDEEEAVHEQCQHERDRQLQAQDEEGGGHVPERPKQEMLLSLKPSEAPELDEDEGFGDWSQRPEQRQQHEGAQGALDSGEPPQCRSPEGEQEDRPGLHAYEKEDSDEVHLEELSLSKEGPGPEDTVQDNLGAAGAEEEQEEHQKCQQPRTPSPLVLEGTIEQSSPPLSPTTKLIDRTESLNRSIEKSNSVKKSQPDLPISKIDQWLEQYTQAIETAGRTPKLARQASIELPSMAVASTKSRWETGEVQAQSAAKTPSCKDIVAGDMSKKSLWEQKGGSKTSSTIKSTPSGKRYKFVATGHGKYEKVLVEGGPAP