wanglab/gogpt-training-data huggingface dataset:
Protein: Opsin-3 (Encephalopsin) (Panopsin) (Q9H1Y3)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor which selectively activates G proteins via ultraviolet A (UVA) light-mediated activation in the skin. Binds both 11-cis retinal and all-trans retinal. Regulates melanogenesis in melanocytes via inhibition of alpha-MSH-induced MC1R-mediated cAMP signaling, modulation of calcium flux, regulation of CAMK2 phosphorylation, and subsequently phosphorylation of CREB, p38, ERK and MITF in response to blue light. Plays a role in melanocyte survival through regulation of intracellular calcium levels and subsequent BCL2/RAF1 signaling. Additionally regulates apoptosis via cytochrome c release and subsequent activation of the caspase cascade. Required for TYR and DCT blue light-induced complex formation in melanocytes. Involved in keratinocyte differentiation in response to blue-light. Required for the UVA-mediated induction of calcium and mitogen-activated protein kinase signaling resulting in the expression of MMP1, MMP2, MMP3, MMP9 and TIMP1 in dermal fibroblasts. Plays a role in light-mediated glucose uptake, mitochondrial respiration and fatty acid metabolism in brown adipocyte tissues (By similarity). May be involved in photorelaxation of airway smooth muscle cells, via blue-light dependent GPCR signaling pathways (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:30168605, ECO:0000269|PubMed:31097585, ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:30168605}.
Interaction partners:
- Rab proteins geranylgeranyltransferase component A 2
- Kynurenine 3-monooxygenase
- Translation initiation factor eIF2B subunit beta
- Microtubule-associated protein 1 light chain 3 gamma
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit epsilon
Sequence:
MYSGNRSGGHGYWDGGGAAGAEGPAPAGTLSPAPLFSPGTYERLALLLGSIGLLGVGNNLLVLVLYYKFQRLRTPTHLLLVNISLSDLLVSLFGVTFTFVSCLRNGWVWDTVGCVWDGFSGSLFGIVSIATLTVLAYERYIRVVHARVINFSWAWRAITYIWLYSLAWAGAPLLGWNRYILDVHGLGCTVDWKSKDANDSSFVLFLFLGCLVVPLGVIAHCYGHILYSIRMLRCVEDLQTIQVIKILKYEKKLAKMCFLMIFTFLVCWMPYIVICFLVVNGHGHLVTPTISIVSYLFAKSNTVYNPVIYVFMIRKFRRSLLQLLCLRLLRCQRPAKDLPAAGSEMQIRPIVMSQKDGDRPKKKVTFNSSSIIFIITSDESLSVDDSDKTNGSKVDVIQVRPL
Protein: GPI mannosyltransferase 2 (EC 2.4.1.-) (GPI mannosyltransferase II) (GPI-MT-II) (Glycosylphosphatidylinositol-anchor biosynthesis protein 18) (P38211)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Responsible for the transfer of the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17615295}; Multi-pass membrane protein {ECO:0000269|PubMed:17615295}.
Interaction partners:
- GPI mannosyltransferase 1
- GPI mannosyltransferase 3
- GPI mannosyltransferase 2 subunit PGA1
- GPI ethanolamine phosphate transferase 1
- Protein PBN1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- GPI ethanolamine phosphate transferase 3
- GPI mannosyltransferase 4
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Sequence:
MIVGLTLYFVLFRSIQYLLVFLTPIRQFDTSTSLLLNELCSSPSEINSYWNKYFWNKLLSWDSVFFIKNITSKNGKPQFEHEYAFSQLWTFFVRLFIKSNNDSIYHALRVGVAIENVLFYLSGIVLYFLTKKIFSQNIRQSQFARTIAKKTSLLFFLTSAAGFLTSIYSEPLSFFFAFVGIWSRECSISVPVLGQFDISWRYWFPYSFISMACFTLASLNRSNCVLLGIYFIFDLIELTKNRKFVKAICFPLLSGSLMFSALLYQQYYLPYKTFCPQRGEWCKSQLFSSIFITKTSLYSYIQSHYWGVGLLKYWTPNNIPNFLFAVPNIIILIYSSIYFSKIYPSYNLKALVWITRALVVIVCFFAHVQILNRIASFLPLHLWYLADRLVKTSDPKKMENPKGDDKIVKFYIYWLAFWIPLQTILFAAFLPPA
Protein: V-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 2) (P31408)
Organism: Bos taurus (Bovine)
Function: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P21281}. Melanosome {ECO:0000250|UniProtKB:P21281}. Cytoplasm {ECO:0000250|UniProtKB:P62814}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit G 2
- V-type proton ATPase subunit H
Sequence:
MALRAMRGIVNGAAPELPVPTSGPLAGSREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVYETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH
Protein: Neuropeptide W (Preproprotein L8) (PPL8) [Cleaved into: Neuropeptide W-23 (NPW23) (L8); Neuropeptide W-30 (NPW30) (L8C)] (Q8K1M5)
Organism: Rattus norvegicus (Rat)
Function: Plays a regulatory role in the organization of neuroendocrine signals accessing the anterior pituitary gland. Stimulates water drinking and food intake. May play a role in the hypothalamic response to stress. When injected into the lateral cerebroventricle, it elevates prolactin (PRL) and corticosterone and lowers growth hormone (GH) release.
Subcellular location: Secreted.
Interaction partners:
- Neuropeptides B/W receptor type 1
- Neuropeptide B
Sequence:
MDLSALASSREVRGPGPGAPVNRPLLPLLLLLLLLPLPASAWYKHVASPRYHTVGRASGLLMGLRRSPYLWRRALGGAAGPLVGLPGQMARSALLLPSPGQELWEVRSRSSPAGLPVHATRSLRDLEGAGQPEQSLSFQSWTSAEPAARAFGETLRAQPWFLQQIIFADPVRLDDRLKNRWRPRA
Protein: INO80 complex subunit E (A0A140LG70)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNGQAEVEVDYKRKYKNLKRKLKFLVYEQECFQEELRRAQRKLLKVSRDKSFLLDRLLQYERVDEESSDSDATVSSDSDGEGARERDREAGKKRRSPGVPPVPSSSSPHLSLLSRSGALQSSASAQYLNAVVGPLSSSYPAGSGPAGGASGPFSWVPQQMLSEDAGEDEGDSEGESDRGEEERGEGDEAELVIDIPNE
Protein: Poly (ADP-ribose) polymerase 2 (G3V749)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Poly
- DNA repair protein XRCC1
- DNA polymerase beta
- Histone PARylation factor 1
- Poly [ADP-ribose] polymerase 1
- Caspase-3
- Caspase-9
- Caspase 7, isoform CRA_c
- Poly [ADP-ribose] polymerase
- Granzyme B
Sequence:
MAPRRRRSGCGRRVLNEAKRVDNGNRATDDSPPGKKVRTCQKKGPAAGGEDTDRTKGKQDSVKTLLVKGRAPVDPECTSKVGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQQNFSVWMRWGRVGKTGQHSLVACSGDLNKAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTEDENKTKQEETSKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTEKELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLRCALRPLDHESHEFKVISQYLQSTHAPTHKDYTMTLLEVFEVEKEGEKEAFRKDLPNRMLLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGMGKMAPSPAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPSQVHMRYLLKIQFNFLQLW
Protein: Uncharacterized protein (Q5AH63)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MLLPESIDTQSLIKRIVYYNNYDRSGWWRWRWLLWLLILIPIFAMIFLLSRRRRQNKVVAYNNPGPQPNGAYYNNNNQYQGGYQGGYQGNNDLPPQATPGYIPPAYPETSQQQGSYGGGYSSQQQNGYNPQQQNGYNPQQQQQQSGTYNSEEFSRPEGPPPAHTKGY
Protein: Regulator of G-protein signaling 1 (Q09777)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Negatively regulates pheromone signaling during mating. Acts in a negative feedback loop that is essential for the mating process. This loop acts to down-regulate cellular sensitivity to pheromone. Activated by ste11.
Subcellular location: Nucleus {ECO:0000269|PubMed:11554925}. Cytoplasm {ECO:0000269|PubMed:11554925}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-1 subunit
- Guanine nucleotide-binding protein alpha-2 subunit
- Pheromone P-factor receptor
- Guanine nucleotide-binding protein subunit beta
- Protein kinase gsk3
- Protein kinase gsk31
- Mitogen-activated protein kinase spk1
Sequence:
MPALHNPSSPPPSYEAVTSYRNGNSIDSGDKRQQCSRLMKITSNGRPYSKDFLELFSTMVISTNFSRNRYRFSYVENSCTLLQLLSTLENLQLSQVNRIKSRCGSKVLKSTTKFTIPKTAAKCLCNTFLNARLLQIVNNPSARKFSNEKCLLQLTRKGYSVVSEFLQHNGHNSQAELYASKWNHSAPVIVSISRFSSTDQILKDSSFCEMLLVRMLGSVHEIGKSKNPLLVPVYSVSSPSPKDSLSKVTKYQMFGIDIAEWLMCNTMLLDWSEMETVASDLLIHSYIAYENNSETPLKFSYAKGVSYFLTGKGIATLGWTKNVSNNKLINKINEVEKGSTNKEILETILRKPNLQTYFFEFLKKNFCDENQRFYSEVCEFNDYFSHANETNDHEAIRESFAHACGIYNCFLSSNAPNAVNLPSDLYEKITNHMALAMEVEPLNEWLQLIHILLLEAQTAVLDLMAGDSLLKFLELNGGLGI
Protein: Tripartite motif-containing protein 59 (EC 2.3.2.27) (RING finger protein 104) (Tumor suppressor TSBF-1) (Q8IWR1)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase involved in different processes such as development and immune response. Serves as a negative regulator for innate immune signaling pathways by suppressing RLR-induced activation of IRF3/7 and NF-kappa-B via interaction with adapter ECSIT. Regulates autophagy through modulating both the transcription and the ubiquitination of BECN1. On the one hand, regulates the transcription of BECN1 through negatively modulating the NF-kappa-B pathway. On the other hand, regulates TRAF6-mediated 'Lys-63'-linked ubiquitination of BECN1, thus affecting the formation of the BECN1-PIK3C3 complex. In addition, mediates 'Lys-48'-linked ubiquitination of TRAF6 and thereby promotes TRAF6 proteasomal degradation. Acts also as a critical regulator for early embryo development from blastocyst stage to gastrula through modulating F-actin assembly and WASH1 'Lys-63'-linked ubiquitination (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22588174}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Intraflagellar transport protein 80 homolog
Sequence:
MHNFEEELTCPICYSIFEDPRVLPCSHTFCRNCLENILQASGNFYIWRPLRIPLKCPNCRSITEIAPTGIESLPVNFALRAIIEKYQQEDHPDIVTCPEHYRQPLNVYCLLDKKLVCGHCLTIGQHHGHPIDDLQSAYLKEKDTPQKLLEQLTDTHWTDLTHLIEKLKEQKSHSEKMIQGDKEAVLQYFKELNDTLEQKKKSFLTALCDVGNLINQEYTPQIERMKEIREQQLELMALTISLQEESPLKFLEKVDDVRQHVQILKQRPLPEVQPVEIYPRVSKILKEEWSRTEIGQIKNVLIPKMKISPKRMSCSWPGKDEKEVEFLKILNIVVVTLISVILMSILFFNQHIITFLSEITLIWFSEASLSVYQSLSNSLHKVKNILCHIFYLLKEFVWKIVSH
Protein: Sulfatase N-terminal domain-containing protein (C6SLX5)
Organism: Neisseria meningitidis alpha275
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVAYVFLFLFVTAALVLIIRSHYRWTYFFASALFVFLAGGMLMLTAQWQRALNFASVWFVVLILFHRLKIHYYKQPLLISDFLLIADWRNWETLFHYKEAVIGMAGLLALAAYAVFGWSGADSLDVPWRWAGAVLFAAAFVSMRHFSKHPGAVKTWLDSLPDDGRDVFLNLPMSCRAVFFQVPVFEGDGEAFARQMPSETRPCGMSDEKPDIVVTLMESTLDPHCFDFAAAKIPDLKMFGRQEDTVFSSPLRVHTFGGATWKSEFAFLAGVPSTDFGALASGVFYSVVPHLQTGLVRNLREHGYFCVVLSPFTKGNYNAKAAYDHFGFNLMFQPQDLGYPAPMGKNLWHISSEEMMQYARMILEKRHPDLENVRQPMFVYVLTMKEHGPYRTDTDNVFDLDAPDLNAKTISALNDYIGRIADLDKAVESFDRYLHERGKPFVFGYFGDHQVPFEGVSVRKKWDYAQPDYVTQFAVRSNIAGGFVQRQDFLDLAFAGGVLMEAAGLEAKDGFMRANMAMRGLCGGGLEDCPNRELVGNYRNYLYDVLKIVR
Protein: Cell division protein DrpB (Division ring protein B) (P76334)
Organism: Escherichia coli (strain K12)
Function: A non-essential division protein that localizes to the septal ring in low ionic strength medium.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000305|PubMed:15919996}. Note=Localizes to the septal ring before constriction, only when cells are grown at low ionic strength. {ECO:0000255|HAMAP-Rule:MF_00857, ECO:0000269|PubMed:32900831}.
Interaction partners:
- Uncharacterized protein YedJ
Sequence:
MEYGSTKMEERLSRSPGGKLALWAFYTWCGYFVWAMARYIWVMSRIPDAPVSGFESDLGSTAGKWLGALVGFLFMALVGALLGSIAWYTRPRPARSRRYE
Protein: Beta-defensin 103 (Beta-defensin 3) (BD-3) (DEFB-3) (HBD3) (hBD-3) (Defensin, beta 103) (Defensin-like protein) (P81534)
Organism: Homo sapiens (Human)
Function: Exhibits antimicrobial activity against Gram-positive bacteria S.aureus and S.pyogenes, Gram-negative bacteria P.aeruginosa and E.coli and the yeast C.albicans. Kills multiresistant S.aureus and vancomycin-resistant E.faecium. No significant hemolytic activity was observed.
Subcellular location: Secreted.
Interaction partners:
- Beta-defensin 1
- C-C chemokine receptor type 2
- C-C chemokine receptor type 6
- Beta-defensin 104
- C-C chemokine receptor-like 2
- Defensin beta 4A
- Beta-defensin 105
- Beta-defensin 106
- C-X-C chemokine receptor type 4
- Beta-defensin 107
Sequence:
MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTRGRKCCRRKK
Protein: DNA repair protein rhp51 (RAD51 homolog) (P36601)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required both for recombination and for the repair of DNA damage caused by X-rays. Binds to single and double-stranded DNA, in the presence of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical nucleoprotein filaments.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- ATP-dependent DNA helicase srs2
- DNA repair protein rhp54
- DNA repair and recombination protein rad22
- ATP-dependent DNA helicase hus2/rqh1
- Exodeoxyribonuclease 1
- Crossover junction endonuclease mus81
- Replication factor A protein 1
- Meiotic recombination protein rdh54
- F-box DNA helicase protein 1
- DNA topoisomerase 3
Sequence:
MADTEVEMQVSAADTNNNENGQAQSNYEYDVNVQDEEDEAAAGPMPLQMLEGNGITASDIKKIHEAGYYTVESIAYTPKRQLLLIKGISEAKADKLLGEASKLVPMGFTTATEYHIRRSELITITTGSKQLDTLLQGGVETGSITELFGEFRTGKSQICHTLAVTCQLPIDMGGGEGKCLYIDTEGTFRPVRLLAVADRYGLNGEEVLDNVAYARAYNADHQLELLQQAANMMSESRFSLLVVDSCTALYRTDFSGRGELSARQMHLARFMRTLQRLADEFGIAVVITNQVVAQVDGISFNPDPKKPIGGNILAHSSTTRLSLRKGRGEQRICKIYDSPCLPESEAIFAINSDGVGDPKEIIAPV
Protein: Microsomal glutathione S-transferase 2 (Microsomal GST-2) (Microsomal GST-II) (EC 1.11.1.-) (EC 2.5.1.18) (EC 4.4.1.20) (Glutathione peroxidase MGST2) (Leukotriene C4 synthase MGST2) (Microsomal glutathione S-transferase II) (A0A8I5ZLK2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369123}. Microsome membrane {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369123}.
Interaction partners:
Sequence:
MAGDSSLLAAVSLLSACQQSYFALQVGRVRLKYKIAPPAVTGSLEFERIFRAQQNSLEFYSVFIISLWMAGWYFNQVFATCLGLLYIYARHKYFWGYAEAAEKRIIGFRLSLGILALLTVLAVLGVASRFLDEYLDFHVAKKLKRPF
Protein: Acetyltransferase At1g77540 (EC 2.3.1.-) (Minimal acetyltransferase) (Q9CAQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses in vitro histone acetyltransferase activity with histones H3 and H4.
Subcellular location: Peroxisome {ECO:0000269|PubMed:19329564}.
Interaction partners:
- Cytochrome P450, family 705, subfamily A, polypeptide 32
- Berberine bridge enzyme-like 27
- BTB/POZ domain-containing protein At4g08455
- At1g12570
- Monothiol glutaredoxin-S12, chloroplastic
- RNA ligase/cyclic nucleotide phosphodiesterase family protein
- Eukaryotic translation initiation factor 3 subunit K
- ABC transporter C family member 13
- ABC transporter C family member 11
- Agmatine deiminase
Sequence:
MTNTAATTEAKMATEPPKIVWNEGKRRFETEDHEAFIEYKMRNNGKVMDLVHTYVPSFKRGLGLASHLCVAAFEHASSHSISIIPSCSYVSDTFLPRNPSWKPLIHSEVFKSSI
Protein: Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (P84309)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30803}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30803}. Cell projection, cilium {ECO:0000269|PubMed:21670265}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Guanine nucleotide-binding protein G
- Rap guanine nucleotide exchange factor 3
- Guanine nucleotide-binding protein G
- Adenylate cyclase type 6
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rap guanine nucleotide exchange factor 4
- Guanine nucleotide-binding protein G
Sequence:
MSGSKSVSPPGYAAQTAASPAPRGGPEHRAAWGEADSRANGYPHAPGGSTRGSTKRSGGAVTPQQQQRLASRWRGGDDDEDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDGGRGSRRQRRGAAGGGSTRAPPAGGSGSSAAAAAAAGGTEVRPRSVELGLEERRGKGRAAEELEPGTGIVEDGDGSEDGGSSVASGSGTGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQIAYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAISLHTNSQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGDRNAYLKEHSIETFLILSCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSLFMLSFYLSCFLLLALVVFVSVIYACVKLFPTPLQTLSRKIVRSKKNSTLVGVFTITLVFLSAFVNMFMCNSKNLVGCLAEEHNITVNQVNACHVMESAFNYSLGDEQGFCGSPQPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIEFIYVLIVEVPGVTLFDNADLLVTANAIDFSNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKAGKTHIKAIADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
Protein: Proteasome regulatory non-ATPase subunit 6 (Q586L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome subunit beta
- Proteasome regulatory ATPase subunit 5
- Proteasome subunit beta
- Proteasome regulatory non-ATPase subunit 8
- Proteasome regulatory ATPase subunit 6
- Ubiquitin carboxyl-terminal hydrolase
- 26S proteasome regulatory subunit 4 homolog
- Proteasome regulatory non-ATP-ase subunit 5
- Proteasome regulatory non-ATP-ase subunit
- Proteasome subunit beta
Sequence:
MEKDLDSLWDTAEDFIADGRRTEARGVLEDIVSTDVTADDAIGLRAKERAIYRLAEILSVEKQTDMLVQLLSAIRSFFALLPKAKATRMVRKMFDLILNSGASLDRQMEVCRDMIAWARQEKRTFLRQRLQHRLAEVQFARNERQEALTTLQALLREVRRLDDRALLLDIHLLESHIYYSIRNISRARAALVAARTNANSIYCPPLAQAEIDLQSGVLHAEEHDAKTAFSYLYEAFEGFHQLGDQARQARKALHYMILAKIATNSPDELSALLSSKNVLEYKGADMVALHGVADAYNSQDTHLFNRIMQENKNAPFLEDEVLQRQLSEMYKSLLEGHLLKLLEPYSRVQISYLAELLKLDVETVESQVSQLILDKKLAGIVDQQHQCVVVFDEQDAKREKAKQKGDGTSDGSHGVSHSSAYHSGGTGTSGSGDVTSATTLYQDALDALEKYDKLVTALFDKANGKFDALVEENLAKRTAAKQVDAKGKKAKDEAGSGAEKGDGKKPKSEPKKE
Protein: RuvB-like helicase 2 (EC 3.6.4.12) (Dreptin) (Drep) (Reptin) (Q9V3K3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a transcriptional coactivator in Wg signaling caused by altered arm signaling. Pont and rept interfere antagonistically with nuclear arm signaling function, and are required to enhance or reduce arm activity, respectively. Also an essential cofactor for the normal function of Myc; required for cellular proliferation and growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:11080158}.
Interaction partners:
- Actin-related protein 5
- RuvB-like helicase 1
- Brahma associated protein 55kD
- DNA methyltransferase 1-associated protein 1
- Transcription-associated protein 1
- YEATS domain-containing protein 4
- Actin-related protein 8
- NuA4 complex subunit EAF3 homolog
- Inhibitor of growth protein
- Chromatin-remodeling ATPase INO80
Sequence:
MAETEKIEVRDVTRIERIGAHSHIRGLGLDDVLEARLVSQGMVGQKDARRAAGVVVQMVREGKIAGRCILLAGEPSTGKTAIAVGMAQALGTETPFTSMSGSEIYSLEMSKTEALSQALRKSIGVRIKEETEIIEGEVVEIQIERPASGTGQKVGKVTLKTTEMETNYDLGNKIIECFMKEKIQAGDVITIDKASGKVNKLGRSFTRARDYDATGAQTRFVQCPEGELQKRKEVVHTVTLHEIDVINSRTHGFLALFSGDTGEIKQEVRDQINNKVLEWREEGKAEINPGVLFIDEVHMLDIECFSFLNRALESDMAPVVVMATNRGITRIRGTNYRSPHGIPIDLLDRMIIIRTVPYSEKEVKEILKIRCEEEDCIMHPDALTILTRIATDTSLRYAIQLITTANLVCRRRKATEVNTEDVKKVYSLFLDENRSSKILKEYQDDYMFSEITEEVERDPAAGGGAKRRVEGGGGDAQPMEH
Protein: Protein DOP1B (Q9Y3R5)
Organism: Homo sapiens (Human)
Function: May play a role in regulating membrane trafficking of cargo proteins. Together with ATP9A and MON2, regulates SNX3 retromer-mediated endosomal sorting of WLS away from lysosomal degradation.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:30213940}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q03921}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q03921}.
Interaction partners:
- Protein MON2 homolog
Sequence:
MDPEEQELLNDYRYRSYSSVIEKALRNFESSSEWADLISSLGKLNKALQSNLRYSLLPRRLLISKRLAQCLHPALPSGVHLKALETYEIIFKIVGTKWLAKDLFLYSCGLFPLLAHAAVSVRPVLLTLYEKYFLPLQKLLLPSLQAFIVGLLPGLEEGSEISDRTDALLLRLSLVVGKEVFYTALWGSVLASPSIRLPASVFVVGHINRDAPGREQKYMLGTNHQLTVKSLRASLLDSNVLVQRNNLEIVLFFFPFYTCLDSNERAIPLLRSDIVRILSAATQTLLRRDMSLNRRLYAWLLGSDIKGNTVVPESEISNSYEDQSSYFFEKYSKDLLVEGLAEILHQKFIDADVEERHHAYLKPFRVLISLLDKPEIGPQVVGNLFLEVIRAFYSYCRDALGSDLKLSYTQSGNSLISAIKENRNASEIVKTVNLLITSLSTDFLWDYMTRCFEECFRPVKQRYSVRNSVSPPPTVSELCALLVFLLDVIPLELYSEVQTQYLPQVLGCLVQPLAEDMEALSLPELTHALKTCFKVLSKVQMPPSYLDTESTSGTSSPVKGENGKIILETKAVIPGDEDASFPPLKSEDSGIGLSASSPELSEHLRVPRVSLERDDVWKKGGSMQRTFLCIQELIANFASKNIFGVQLTASGEESKSEEPAGKRDRDGTQSLAANDSSRKNSWEPKPITVPQFKQMLSDLFTARGSPFKTKSSESPSSSPSSPARKNGGEWDVEKVVIDLGGSREERREAFAAACHLLLDCATFPVYLSEEETEQLCATLFQLPGAGDSSFPSWLKSLMTICCCVTDCYLQNVAISTLLEVINHSQSLALVIEDKMKRYKSSGHNPFFGKLQMVTVPPIAPGILKVIAEKTDFYQRVARVLWNQLNKETREHHVTCVELFYRLHCLAPTANICEDIICHALLDPDKGTRLEALFRFSVIWHLTREIQGSRVTSHNRSFDRSLFVVLDSLACTDGAIGAAAQGWLVRALSLGDVARILEPVLLLLLQPKTQRTSIHCLKQENSADDLHRWFNRKKTSFREACAVPEPQESGSEEHLPLSQFTTVDREAIWAEVEKEPEKYPLRGELSEEELPYYVELPDRTAHGAPDSSEHTESADTSSCHTDSENTSSFSSPSHDLQELSNEENCCAPIPMGGRAYPKRSALLAAFQSESFKAGAKLSLVRVDSDKTQASESFSSDEEADLELQALTTSRLLKQQRERQEAVEALFKHILLYLQPYDSRRVLYAFSVLEAVLKTNPKEFIEAVSRTSMDTSSTAHLNLISNLLARHQEALIGQSFYGKLQTQVPNVCPHSLLLELLTYLCLSFLRSYYPCYLKVSHRDILGNRDVQVKSVEVLIRIMMQLVSVAKSSEGKNVEFIHSLLQRCKVQEFVLLSLSASMYTSQKRYGLATAHHGRALPEDSLFEESLINLGQDQIWSEHPLQIELLKLLQVLIVLEHHLGRAHEEAENQPDLSREWQRALNFQQAISALQYVQPHPLTSQGLLVSAVVRGLQPAYGYGMHPAWVSLVTHSLPYFGKSLGWTVTPFVVQICKNLDDLVKQYESESVKLSVSTTSKRENISPDYPLTLLEGLTTISHFCLLEQANQNKKTMAAGDPANLRNARNAILEELPRTVNTMALLWNVLRKEETQKRPVDLLGATKGSSSVYFKTTKTIRQKILDFLNPLTAHLGVQLTAAVAAVWSRKKAQRHSKMKIIPTASASQLTLVDLVCALSTLQTDTLLHLVKEVVKRPPQVKGGDEKSPLVDIPVLQFCYAFLQRLPVPALQENFSSLLGVLKESVQLNLAPPGYFLLLSMLNDFVTRTPNLENKKDQKDLQEITQKILEAVGNIAGSSLEQTSWLSRNLEVKAQPQASLEESDAEEDLYDAAAASAMVSSSAPSVYSVQALSLLAEVLASLLDMVYRSDEKEKAVPLISRLLYYVFPYLRNHSAYNAPSFRAGAQLLSSLSGYAYTKRAWRKEVLELFLDPAFFQMDTSCVHWKSIIDHLLTHEKTMFKDLMNMQSSSLKLFSSFEQKAMLLKRQAFAVFSGELDQYHLYLPLIQERLTDNLRVGQTSIVAAQMFLFFRVLLLRISPQHLTSLWPIMVSELIQTFTQLEEDLKDEDESLRSTNKVNRTKVSVPDANGPSVGEIPQSELILYLSACKFLDTALSFPPDKMPLFQIYRWAFIPEVDTEGPAFLSDVEENHQECKPHTVRILELLKLKFGEISSSDEITMKSEFPLLRQHSVSSIRQLMPFFMTLNGAFKTQRQLPADSPGTPFLDFPVTDSPRILKQLEECIEYDFLEHPEC