wanglab/gogpt-training-data huggingface dataset:
Protein: Histone-binding protein (A0A1D8PFV9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Snt1p
- SIR4-interacting protein SIF2
- Histone deacetylase
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
Sequence:
MTNKDQEQLLQDASTLLMFASSVAKHESSNQHSPTSNMSSPPTVQQLPQQPQQPLPQQYINSGSSTRKSSEHKETSVVSSPPSVKFVDIINNPQSASVTHEKNKPTTQSKRTSISMLVNDTPSDIAVKVTPQPRKSSISILMNPPEPVVTPSPPAVSGNYEMKQKSVSPTSGLPKKGSFKPNHERSRSTPEATIAKLELHHQQQLQQLQNQQNQSATPSPTPAFQRGIDLRSKERNTENAVIAAAALTAAVDNPLPLKTVEQKPVLVKERAQVVPVSVVPAVSKSEEDQLTEPEEEDEEEEMVEARVVPVPVPMPVFVQMPIDMNHSQIKQEVASDSTSKPAIPSKEKYVPPPLETYQVNPDSGLIGCICGIEDDDGFTIQCDVCFRWQHCVCMGYENAEEVPEDMYKCYYCDESKWGKFDPEASRLRTMQRLEIDRREDSNQASVKTLPQQQNQQQGTKRKQSNSEKADNKKRKTEDKISTNTNSSNSASGSPAPKFQSPRPDEMDDLPNKDNELLEDGITAESYQSVYYNLKENDYKRQAIKEFIDNIGSDFAGQFFKLPKSEQQGKHFRNVTIMSPNQFKSIKWSKINLPNYTKYLQEHNKLKKKNNFNKTTIQVKPYTDNQKQKFNGISKLALFISSNGGGSGGGSLTIPENTPIIEYLGEIDLFKNYCRDSINQYRMWGSPKPKVLKTTIPTQYSDETLDIVLDSRFVGNESRFIRKACPSSANCRIETVYVPEQNKFRFLVFTSKPITLKSENQDEELRLPWEWDVDHPILKLYANNNSEKFENLTNEEKSALITYIDNILHFVECGCSTSNNSSSCAIFKIKKATSYLMRSTRKASSLSNVNITKSKEELILPRPEKQYVSWEERLNQRNQRIQAELFSEKKKLGSDNNDGQQKVEEKEESALEEAKDGGADLGSGTMGMGANADDSKGEKKPPMLFKLPFKQQLLANLRSNVEMTTTVQQPTPVSSEDDSDPVAVEIPVPVVPELVAIIDKSIEEKLKPIIKQVEASTVTGEDVNLKVVEKVSLVSDNGDNRKHDVKLVPETAAPAKVVKKLSFADYKKMK
Protein: UDP-glucose 6-dehydrogenase 3 (UDP-Glc dehydrogenase 3) (UDP-GlcDH 3) (UDPGDH 3) (EC 1.1.1.22) (At-UGD3) (Q9LF33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers. Required for the formation of cell wall ingrowths on the outer cell walls of nematode-induced syncytia.
Interaction partners:
- UDP-D-apiose/UDP-D-xylose synthase 1
- UDP-D-apiose/UDP-D-xylose synthase 2
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- UDP-sugar pyrophosphorylase
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3
- UTP--glucose-1-phosphate uridylyltransferase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UDP-glucuronic acid decarboxylase 6
- UDP-glucuronic acid decarboxylase 5
Sequence:
MVKICCIGAGYVGGPTMAVIALKCPSVEVAVVDISVPRINAWNSDQLPIYEPGLDDVVKQCRGKNLFFSTDVEKHVREADIVFVSVNTPTKTRGLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILTHNSKGIKFQILSNPEFLAEGTAIEDLFMPDRVLIGGRETTEGFAAVKALKDIYAQWVPEERILTTNLWSAELSKLAANAFLAQRISSVNAMSALCEATGANVSEVSYAVGKDSRIGPKFLNSSVGFGGSCFQKDILNLVYICECNGLPEVAEYWKQVIKINDYQKTRFVNRIVSSMFNTVSNKKIAVLGFAFKKDTGDTRETPAIDVCKGLLGDKARLSIYDPQVTEEQIQRDLTMNKFDWDHPLHLQPMSPTTVKQVSVAWDAYTATKDAHGICILTEWDEFKKLDFQRIFENMQKPAFVFDGRNVVDADKLREIGFIVYSIGKPLDQWLKDMPALA
Protein: MGC114645 protein (Receptor like tyrosine kinase S homeolog precursor) (Q4V865)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLPGAPDPQESRRRRRGKLPGPGLWCWWPLLLSVLLQQPEKAHSGPGPSTDPGLNLYLSEEEVRRLIGLDAELYYIRNDIINHYALSFNLLVPSETNSLHFTWHSKSKVEYKLGFQVDNPIAMTMPLTNISMQGEVPSFLTVFRVDLYCSGKMDSEVLFLMQLNITINSAKNITVLNFKRRKMCYRKLEDLKVPMLQDKNSTRIHYDPVNIAPTTSTRVFYISVGVCCAVIFLVAIILAVLHLHSMKRVELDDSMSDSSSSQGLSQPSTQTTQYLRADTPNNATPVTSYPTLRIEKNDLKSVTLQEAKAKVKDISISRERVTLKDVLHEGTFGRIFHGILVDEKDPSKEKEVFVKTIKDQASEVQITMMLTESCKLRGLHHRNLLPIGHVCTEDGEKPMVLLPYMNWGNLKLFLRQCKLVEANNPQAISQQDLVHMAIQIACGMSYLARREVIHKDLAARNCVIDESLQVKITDNALSRDLFPMDYHCLGDNENRPVRWMALESLVNKEFSSAGDVWAFGVTLWELMTLGQTPYVDIDPFEMAAYLKDGYRITQPINCPDELFAVMACCWALDPEERPKFQQLVQCLTEFHSALGAYV
Protein: OTU domain-containing protein 4 (EC 3.4.19.12) (HIV-1-induced protein HIN-1) (Q01804)
Organism: Homo sapiens (Human)
Function: Deubiquitinase which hydrolyzes the isopeptide bond between the ubiquitin C-terminus and the lysine epsilon-amino group of the target protein. May negatively regulate inflammatory and pathogen recognition signaling in innate immune response. Upon phosphorylation at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like receptor signaling pathway, specifically deubiquitinates 'Lys-63'-polyubiquitinated MYD88 adapter protein triggering down-regulation of NF-kappa-B-dependent transcription of inflammatory mediators. Independently of the catalytic activity, acts as a scaffold for alternative deubiquitinases to assemble specific deubiquitinase-substrate complexes. Associates with USP7 and USP9X deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby promoting the repair of alkylated DNA lesions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25944111}. Nucleus {ECO:0000269|PubMed:25944111}. Note=Primarily cytoplasmic. {ECO:0000269|PubMed:25944111}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 7
- Ubiquitin carboxyl-terminal hydrolase 9X
- OTU domain-containing protein 3
- Polyubiquitin-C
Sequence:
MEAAVGVPDGGDQGGAGPREDATPMDAYLRKLGLYRKLVAKDGSCLFRAVAEQVLHSQSRHVEVRMACIHYLRENREKFEAFIEGSFEEYLKRLENPQEWVGQVEISALSLMYRKDFIIYREPNVSPSQVTENNFPEKVLLCFSNGNHYDIVYPIKYKESSAMCQSLLYELLYEKVFKTDVSKIVMELDTLEVADEDNSEISDSEDDSCKSKTAAAAADVNGFKPLSGNEQLKNNGNSTSLPLSRKVLKSLNPAVYRNVEYEIWLKSKQAQQKRDYSIAAGLQYEVGDKCQVRLDHNGKFLNADVQGIHSENGPVLVEELGKKHTSKNLKAPPPESWNTVSGKKMKKPSTSGQNFHSDVDYRGPKNPSKPIKAPSALPPRLQHPSGVRQHAFSSHSSGSQSQKFSSEHKNLSRTPSQIIRKPDRERVEDFDHTSRESNYFGLSPEERREKQAIEESRLLYEIQNRDEQAFPALSSSSVNQSASQSSNPCVQRKSSHVGDRKGSRRRMDTEERKDKDSIHGHSQLDKRPEPSTLENITDDKYATVSSPSKSKKLECPSPAEQKPAEHVSLSNPAPLLVSPEVHLTPAVPSLPATVPAWPSEPTTFGPTGVPAPIPVLSVTQTLTTGPDSAVSQAHLTPSPVPVSIQAVNQPLMPLPQTLSLYQDPLYPGFPCNEKGDRAIVPPYSLCQTGEDLPKDKNILRFFFNLGVKAYSCPMWAPHSYLYPLHQAYLAACRMYPKVPVPVYPHNPWFQEAPAAQNESDCTCTDAHFPMQTEASVNGQMPQPEIGPPTFSSPLVIPPSQVSESHGQLSYQADLESETPGQLLHADYEESLSGKNMFPQPSFGPNPFLGPVPIAPPFFPHVWYGYPFQGFIENPVMRQNIVLPSDEKGELDLSLENLDLSKDCGSVSTVDEFPEARGEHVHSLPEASVSSKPDEGRTEQSSQTRKADTALASIPPVAEGKAHPPTQILNRERETVPVELEPKRTIQSLKEKTEKVKDPKTAADVVSPGANSVDSRVQRPKEESSEDENEVSNILRSGRSKQFYNQTYGSRKYKSDWGYSGRGGYQHVRSEESWKGQPSRSRDEGYQYHRNVRGRPFRGDRRRSGMGDGHRGQHT
Protein: CMP-sialic acid transporter (CMP-SA-Tr) (CMP-Sia-Tr) (Solute carrier family 35 member A1) (O08520)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Transports CMP-sialic acid from the cytosol into the Golgi apparatus, functioning as an antiporter that exchanges CMP-sialic acid for CMP. Binds both CMP-sialic acid and free CMP, but has higher affinity for free CMP (By similarity). Also able to exchange CMP-sialic acid for AMP and UMP (By similarity). Also mediates the transport of CDP-ribitol (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:9310377}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAQARENVSLFFKLYCLAVMTLVAAAYTVALRYTRTTAKELYFSTTAVCVTEVIKLLISVGLLAKETGSLGRFKASLSENVLGSPKELMKLSVPSLVYAVQNNMAFLALSNLDAAVYQVTYQLKIPCTALCTVLMLNRTLSKLQWVSVFMLCGGVILVQWKPAQATKVVVEQSPLLGFGAIAIAVLCSGFAGVYFEKVLKSSDTSLWVRNIQMYLSGIVVTLVGTYLSDGAEIKEKGFFYGYTYYVWFVIFLASVGGLYTSVVVKYTDNIMKGFSAAAAIVLSTIASVMLFGLQITLSFAMGALLVCISIYLYGLPRQDTTCIQQEATSKERVIGV
Protein: Uncharacterized J domain-containing protein DjlC (P77359)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YbeU
- Chaperone protein HscC
Sequence:
MKTCWQILEIESTTQIDIIRQAYLARLPLCHPETDPQGFKALRQAYEEALRLAVNPVEEADDEEKDAAAEHEILRAFRTLLDSESDRFQPSAWQKFIQQLNTWNMEDVDQLRWPLCAIAIEARYLSLNCASLLAERLNWHSFNDSEGMDEEEREAFLEAIQAGDCFDFLSLLEYPIALQNQTVEYYFALERCCRYHPDYVTAFLAMEGPWLIPDDAKLHRKLLRWYSSVQTGMAELIPVAQQWQTEEPESEDARYYLCAQRLYCGEGESLLADLCAYWESYPSTQADNLLLQWSKRHCPDYFALLVMVIEARSMVDAQGQPLKYVPGESARTRLLWAEILHSGKLSPLGQSFIESLFFKRKAWAWWKSRVGSETEQDSPFLDLYRVAEQVVLEAFPKQEMLARLNTRLEGGDAHPLEAIVTRMLLTKVKLEPEDEDVDEPTPENHEEKNDEGEKPQSITSIIKISLTVLVIGYALGKIAMLFS
Protein: NF-kappa-B-activating protein (Q8N5F7)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Plays a role as a transcriptional corepressor of the Notch-mediated signaling required for T-cell development. Also involved in the TNF and IL-1 induced NF-kappa-B activation. Associates with chromatin at the Notch-regulated SKP2 promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:14550261}.
Interaction partners:
- Pre-mRNA-splicing factor SLU7
- Pre-mRNA-processing factor 17
- Peptidyl-prolyl cis-trans isomerase-like 1
- Pre-mRNA-splicing factor SYF2
- ATP-dependent RNA helicase DHX8
- Pre-mRNA-splicing factor CWC22 homolog
- PRKR-interacting protein 1
- Splicing regulator SDE2
- Serine/arginine repetitive matrix protein 2
- Protein FAM32A
Sequence:
MAPVSGSRSPDREASGSGGRRRSSSKSPKPSKSARSPRGRRSRSHSCSRSGDRNGLTHQLGGLSQGSRNQSYRSRSRSRSRERPSAPRGIPFASASSSVYYGSYSRPYGSDKPWPSLLDKEREESLRQKRLSERERIGELGAPEVWGLSPKNPEPDSDEHTPVEDEEPKKSTTSASTSEEEKKKKSSRSKERSKKRRKKKSSKRKHKKYSEDSDSDSDSETDSSDEDNKRRAKKAKKKEKKKKHRSKKYKKKRSKKSRKESSDSSSKESQEEFLENPWKDRTKAEEPSDLIGPEAPKTLTSQDDKPLNYGHALLPGEGAAMAEYVKAGKRIPRRGEIGLTSEEIASFECSGYVMSGSRHRRMEAVRLRKENQIYSADEKRALASFNQEERRKRENKILASFREMVYRKTKGKDDK
Protein: Glutathione reductase, mitochondrial (GR) (GRase) (EC 1.8.1.7) (P47791)
Organism: Mus musculus (Mouse)
Function: Maintains high levels of reduced glutathione in the cytosol.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:P00390}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000250|UniProtKB:P00390}.
Interaction partners:
- Glutathione synthetase
- Glutathione peroxidase 1
- Probable glutathione peroxidase 8
- Glutathione peroxidase 2
- Glutathione peroxidase 7
- Glutathione peroxidase 3
- Glutathione peroxidase 6
- Epididymal secretory glutathione peroxidase
- Glutathione hydrolase 1 proenzyme
- Thioredoxin
Sequence:
MALLPRALGVGAAPSLRRAARALTCAMASPGEPQPPAPDTSSFDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHVDYGFQSCEGKFSWHVIKQKRDAYVSRLNTIYQNNLTKSHIEIIHGYATFADGPRPTVEVNGKKFTAPHILIATGGVPTVPHESQIPGASLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRNFDSLISSNCTEELENAGVEVLKFTQVKEVKKTSSGLELQVVTSVPGRKPTTTMIPDVDCLLWAIGRDPNSKGLNLNKVGIQTDEKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAHRLFECKQDSKLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR
Protein: V-type proton ATPase subunit a (Q64F87)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGSMFRSEEVALVQLFLPTAAAYTCVSRLGELGLVEFRDLNASVSAFQRRFVVDVSRCEELEKTFTFLQEEVRRAGLVLPPPKGRLPAPPPRDLLRIQEETERLAQELRDVRGNQQALRAQLHQLQLHAAVLRQGHEPQLAAAHTDGASERTPLLQAPGGPHQDLRVNFVAGAVEPHKAPALERLLWRACRGFLIASFRELEQPLEHPVXGEPATWMT
Protein: Thioredoxin reductase (EC 1.8.1.9) (Caffeine resistance protein 4) (Q92375)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29509}.
Interaction partners:
- Peroxiredoxin tpx1
- Thioredoxin-1
- Vacuolar protein sorting-associated protein 54
- Vacuolar protein sorting-associated protein 52
- Thioredoxin-like protein 1
- Glutathione peroxidase-like peroxiredoxin gpx1
- Catalase
- Caffeine resistance protein 5
- Thioredoxin-2, mitochondrial
- Brefeldin A resistance protein
Sequence:
MTHNKVVIIGSGPAGHTAAIYLARGELKPVMYEGMLANGIAAGGQLTTTTDVENFPGFPDGINGTTLTENFRAQSLRFGTEIITETVSKLDLSSRPFKYWLEGAEEEEPHTADSVILATGASARRLHITGEDTYWQAGISACAVCDGAVPIYRNKPLAVVGGGDSAAEEAQFLTKYGSKVYVLVRRDKLRASPIMAKRLLANPKVEVLWNTVAEEAQGDGKLLNNLRIKNTNTNEVSDLQVNGLFYAIGHIPATKLVAEQIELDEAGYIKTINGTPRTSIPGFFAAGDVQDKVFRQAITSAGSGCQAALLAMHYLEELEDTD
Protein: Ultraviolet-B receptor UVR8 (Protein UV-B RESISTANCE 8) (RCC1 domain-containing protein UVR8) (Q9FN03)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: UV-B specific signaling component that acts as UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV-B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore.
Subcellular location: Nucleus {ECO:0000269|PubMed:17720867}. Cytoplasm, cytosol {ECO:0000269|PubMed:17720867}. Note=UV-B promotes rapid accumulation of UVR8 in the nucleus. {ECO:0000269|PubMed:17720867}.
Interaction partners:
- WD repeat-containing protein RUP2
- E3 ubiquitin-protein ligase COP1
- WD repeat-containing protein RUP1
- Casparian strip membrane protein 2
- Protein ROOT HAIR DEFECTIVE 3 homolog 2
- Early light-induced protein 2
- Transcription factor HY5
- Omega-amidase, chloroplastic
Sequence:
MAEDMAADEVTAPPRKVLIISAGASHSVALLSGDIVCSWGRGEDGQLGHGDAEDRPSPTQLSALDGHQIVSVTCGADHTVAYSQSGMEVYSWGWGDFGRLGHGNSSDLFTPLPIKALHGIRIKQIACGDSHCLAVTMEGEVQSWGRNQNGQLGLGDTEDSLVPQKIQAFEGIRIKMVAAGAEHTAAVTEDGDLYGWGWGRYGNLGLGDRTDRLVPERVTSTGGEKMSMVACGWRHTISVSYSGALYTYGWSKYGQLGHGDLEDHLIPHKLEALSNSFISQISGGWRHTMALTSDGKLYGWGWNKFGQVGVGNNLDQCSPVQVRFPDDQKVVQVSCGWRHTLAVTERNNVFAWGRGTNGQLGIGESVDRNFPKIIEALSVDGASGQHIESSNIDPSSGKSWVSPAERYAVVPDETGLTDGSSKGNGGDISVPQTDVKRVRI
Protein: Class E basic helix-loop-helix protein 23 (bHLHe23) (Class B basic helix-loop-helix protein 4) (bHLHb4) (Q8NDY6)
Organism: Homo sapiens (Human)
Function: May function as transcriptional repressor. May modulate the expression of genes required for the differentiation and/or maintenance of pancreatic and neuronal cell types. May be important for rod bipolar cell maturation (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- AP-3 complex subunit sigma-2
Sequence:
MAELKSLSGDAYLALSHGYAAAAAGLAYGAAREPEAARGYGTPGPGGDLPAAPAPRAPAQAAESSGEQSGDEDDAFEQRRRRRGPGSAADGRRRPREQRSLRLSINARERRRMHDLNDALDGLRAVIPYAHSPSVRKLSKIATLLLAKNYILMQAQALDEMRRLVAFLNQGQGLAAPVNAAPLTPFGQATVCPFSAGAALGPCPDKCAAFSGTPSALCKHCHEKP
Protein: Anoctamin-5 (Gnathodiaphyseal dysplasia 1 protein) (Transmembrane protein 16E) (Q75V66)
Organism: Homo sapiens (Human)
Function: Does not exhibit calcium-activated chloride channel (CaCC) activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15124103}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalized with CALR/calreticulin (PubMed:15124103). Shows an intracellular localization according to PubMed:22075693. {ECO:0000269|PubMed:15124103, ECO:0000269|PubMed:22075693}.
Interaction partners:
- Dysferlin
- Protein kinase C-binding protein NELL1
- Ribitol 5-phosphate transferase FKRP
- Monocyte to macrophage differentiation factor 2
- Protein kinase C-binding protein NELL2
- Alpha-sarcoglycan
- Beta-sarcoglycan
- Gamma-sarcoglycan
- Protein O-mannosyl-transferase 1
- Delta-sarcoglycan
Sequence:
MGDPDLLEVLAEEGEKVNKHIDYSFQMSEQSLSSRETSFLINEETMPAKRFNLFLRRRLMFQKNQQSKDSIFFRDGIRQIDFVLSYVDDVKKDAELKAERRKEFETNLRKTGLELEIEDKRDSEDGRTYFVKIHAPWEVLVTYAEVLGIKMPIKESDIPRPKHTPISYVLGPVRLPLSVKYPHPEYFTAQFSRHRQELFLIEDQATFFPSSSRNRIVYYILSRCPFGIEDGKKRFGIERLLNSNTYSSAYPLHDGQYWKPSEPPNPTNERYTLHQNWARFSYFYKEQPLDLIKNYYGEKIGIYFVFLGFYTEMLFFAAVVGLACFIYGLLSMEHNTSSTEICDPEIGGQMIMCPLCDQVCDYWRLNSTCLASKFSHLFDNESTVFFAIFMGIWVTLFLEFWKQRQARLEYEWDLVDFEEEQQQLQLRPEFEAMCKHRKLNAVTKEMEPYMPLYTRIPWYFLSGATVTLWMSLVVTSMVAVIVYRLSVFATFASFMESDASLKQVKSFLTPQITTSLTGSCLNFIVILILNFFYEKISAWITKMEIPRTYQEYESSLTLKMFLFQFVNFYSSCFYVAFFKGKFVGYPGKYTYLFNEWRSEECDPGGCLIELTTQLTIIMTGKQIFGNIKEAIYPLALNWWRRRKARTNSEKLYSRWEQDHDLESFGPLGLFYEYLETVTQFGFVTLFVASFPLAPLLALINNIVEIRVDAWKLTTQYRRTVASKAHSIGVWQDILYGMAVLSVATNAFIVAFTSDIIPRLVYYYAYSTNATQPMTGYVNNSLSVFLIADFPNHTAPSEKRDFITCRYRDYRYPPDDENKYFHNMQFWHVLAAKMTFIIVMEHVVFLVKFLLAWMIPDVPKDVVERIKREKLMTIKILHDFELNKLKENLGINSNEFAKHVMIEENKAQLAKSTL
Protein: Carboxysome assembly protein CcmM (CcmM58) (M58) (Carbon dioxide concentrating mechanism protein CcmM) (Carbonic anhydrase) (EC 4.2.1.1) (Q8YYI3)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Functions as a scaffold protein for the assembly of beta-carboxysomes, initiates carboxysome assembly by coalescing RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) (By similarity). Produced as a full-length (M58) and a short form (M35), possibly by alternative translation initiation; probably both forms are required for correct carboxysome assembly and growth. In this strain both forms are equally abundant.
Subcellular location: Carboxysome {ECO:0000269|PubMed:24907906}. Cytoplasm {ECO:0000305|PubMed:24907906}. Note=This cyanobacterium makes beta-type carboxysomes. Both isoforms are found equally distributed in the interior of the carboxysome. An unexpectedly large amount is found outside the carboxysome by immungold labelling, this might represent coalescing RuBisCO-CcmM. {ECO:0000269|PubMed:24907906}.
Interaction partners:
- Ribulose bisphosphate carboxylase large chain
- Carboxysome shell vertex protein CcmL
- Ribulose bisphosphate carboxylase small subunit
- Carbon dioxide concentrating mechanism protein
- Carboxysome shell protein CcmK
- Carboxysome shell protein CcmK
- carbonic anhydrase
- Carbon dioxide concentrating mechanism protein
- Carboxysome shell protein CcmK
- Carboxysome shell protein CcmK
Sequence:
MAVRSTAAPPTPWSRSLAEAQIHESAFVHPFSNIIGDVHIGANVIIAPGTSIRADEGTPFHIGENTNIQDGVVIHGLEQGRVVGDDNKEYSVWVGSSASLTHMALIHGPAYVGDNSFIGFRSTVFNAKVGAGCIVMMHALIKDVEVPPGKYVPSGAIITNQKQADRLPDVQPQDRDFAHHVIGINQALRAGYLCAADSKCIAPLRNDQVKSYTSTTVIGLERSSEVASNSLGAETIEQVRYLLEQGYKIGSEHVDQRRFRTGSWTSCQPIEARSVGDALAALEACLADHSGEYVRLFGIDPKGKRRVLETIIQRPDGVVAGSTSFKAPASNTNGNGSYHSNGNGNGYSNGATSGKVSAETVDQIRQLLAGGYKIGTEHVDERRFRTGSWNSCKPIEATSAGEVVAALEECIDSHQGEYIRLIGIDPKAKRRVLESIIQRPNGQVAPSSSPRTVVSASSASSGTATATATRLSTEVVDQVRQILGGGYKLSIEHVDQRRFRTGSWSSTGAISATSEREAIAVIEASLSEFAGEYVRLIGIDPKAKRRVLETIIQRP
Protein: IQ motif and SEC7 domain-containing protein 1 (Q8R0S2)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine nucleotide exchange factor activity is enhanced by lipid binding. Accelerates GTP binding by ARFs of all three classes. Guanine nucleotide exchange protein for ARF6, mediating internalization of beta-1 integrin (By similarity). Involved in neuronal development. In neurons, plays a role in the control of vesicle formation by endocytoc cargo. Upon long term depression, interacts with GRIA2 and mediates the activation of ARF6 to internalize synaptic AMPAR receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6DN90}. Nucleus {ECO:0000250|UniProtKB:Q6DN90}. Postsynaptic density {ECO:0000269|PubMed:20547133}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:20547133}. Note=At steady state, may be preferentially cytosolic. {ECO:0000250|UniProtKB:Q6DN90}.
Interaction partners:
- ADP-ribosylation factor 6
Sequence:
MWCLHCNSERTQSLLELELDSGVEGEAPSSETGTSLDSPSAYHQGPLVPGSSLSPDHYEHTSVGAYGLYAGPGPQQRTRRPRLQHSTSVLRKQAEEEAIKRSRSLSESYELSSDLQDKQVEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSVTNDGSQLGALVPSECGDLSDPALKSPAPSSDFADAITELEDAFSRQVKSLAESIDDALNCRSLHSEEVPASDTARARDTEPKPGLHGMDHRKLDEMTASYSDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRSGGAAQDYWALAHKEDKADTDTSCRSTPSLERPEPRLRVEHLPLLTIEPPSDSSVELSDRSDRSSLKRQSAYERSLGGQQGSPKHGPHGGPPKGLPREEPELRPRPPRPLESHLAINGSANRQSKSESDYSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKETRNSWDSPAFSNDVIRKRHYRIGLNLFNKKPEKGIQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSAMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCVCNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFVKNLRGVDDGEDIPRETLIGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHHGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSAVPGADIKVLINFNAPNPQDRKKFTDDLRESVAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNGTLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFQPPQPPVLCS
Protein: Uncharacterized protein YdfR (P76160)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Probable prophage lysozyme
- Prophage lysis protein S homolog EssQ
- Prophage antitermination protein Q homolog QuuQ
- Protein FlxA
- Uncharacterized protein YfdT
- Uncharacterized protein YfdR
Sequence:
MTQDYELVVKGVRNFENKVTVTVALQDKERFDGEIFDLDVAMDRVEGAALEFYEAAARRSVRQVFLEVAEKLSEKVESYLQHQYSFKIENPANKHERPHHKYL
Protein: Protein ref(2)P (Refractory to sigma P) (P14199)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for selective autophagy activation by ubiquitinated proteins. Implicated in sigma rhabdovirus multiplication and necessary for male fertility. Involved in activating transcription of Drs.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:22622177}.
Interaction partners:
- Autophagy-related 8a, isoform A
- GH01161p
- Atypical protein kinase C
- FI11917p
- Autophagy protein 5
- Autophagy-related 8b, isoform A
- E3 ubiquitin-protein ligase parkin
- Autophagy protein 12-like
- Autophagy-related 1, isoform B
- Transmembrane GTPase Marf
Sequence:
MPEKLLKITYQGAGPQKKINAYLRMPSQNYTILRREIELYLFQERQLPKCDVRTFWIDADKDEIEIVNQNDYEIFLAKCESNMHVQVAPLAPVEEPKATKQEGSSANAEAPSVDDPSNFTIHDAVECDGCGLAPLIGFRYKCVQCSNYDLCQKCELAHKHPEHLMLRMPTNNGPGMVDAWFTGPGLGRRSGRRSRGHCPFQETNQADPAGEPARDSRRERRQARRHAGVLTQFVEMMTNLPLNTTTATAPAEPQKPKAAEQTESPPQAEPTVTAEKAAESEAKPTEPKKVNTDQSVPRTEDPVTTPRSTQPTTPVINLDNISQIVPPEYMSAGIEILNNFSEMFSKIIDTTEGGDSGIFAPSTTPSAENKKPEEQGQSSGQSGASSANQSAVPSAAPSANQSNVPSANQSATPSISGSIPDAQLETEPLNPKPSETTTETEQERRRSDSLDPEWQLIDNAYSANNSNLINLDTTNPTAAPQEPVRDFGQLGELLRQHMNEEARVEQASANTQTAQVDTVSTSTSTTSVTTNSVGTSPAAPDDKRTVPVYHTDESINKSIHAMMAMGFSNEGAWLTQLLESVQGNISAALDVMNVSQNRN
Protein: TNF receptor-associated factor 1 (Epstein-Barr virus-induced protein 6) (Q13077)
Organism: Homo sapiens (Human)
Function: Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
Interaction partners:
- Baculoviral IAP repeat-containing protein 3
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- TNF receptor-associated factor 2
- Baculoviral IAP repeat-containing protein 2
- Tumor necrosis factor receptor superfamily member 1B
- Tumor necrosis factor receptor superfamily member 1A
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor receptor superfamily member 9
- TRAF family member-associated NF-kappa-B activator
- Tumor necrosis factor alpha-induced protein 3
Sequence:
MASSSGSSPRPAPDENEFPFGCPPTVCQDPKEPRALCCAGCLSENPRNGEDQICPKCRGEDLQSISPGSRLRTQEKAHPEVAEAGIGCPFAGVGCSFKGSPQSVQEHEVTSQTSHLNLLLGFMKQWKARLGCGLESGPMALEQNLSDLQLQAAVEVAGDLEVDCYRAPCSESQEELALQHFMKEKLLAELEGKLRVFENIVAVLNKEVEASHLALATSIHQSQLDRERILSLEQRVVELQQTLAQKDQALGKLEQSLRLMEEASFDGTFLWKITNVTRRCHESACGRTVSLFSPAFYTAKYGYKLCLRLYLNGDGTGKRTHLSLFIVIMRGEYDALLPWPFRNKVTFMLLDQNNREHAIDAFRPDLSSASFQRPQSETNVASGCPLFFPLSKLQSPKHAYVKDDTMFLKCIVETST
Protein: Immediate early response 3-interacting protein 1 (Q9VTE1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Protein kish
- Mitochondrial ribosomal protein S21, isoform A
Sequence:
MFTLWTLIESSLLCLNAVCILHEERFLAKFGWGRQAGQQDFGAPTAKDQVLNLIRSIRTVAKIPLIFLNIIAIIFKLLLG