wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoglucomutase-like protein 5 (Q8BZF8)
Organism: Mus musculus (Mouse)
Function: Component of adherens-type cell-cell and cell-matrix junctions. Has no phosphoglucomutase activity in vitro.
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q15124}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15124}. Cell membrane, sarcolemma {ECO:0000269|PubMed:7890770}. Note=Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments. {ECO:0000250|UniProtKB:Q15124}.
Interaction partners:
- Dystrophin
- UTP--glucose-1-phosphate uridylyltransferase
- Utrophin
- Dystrobrevin alpha
- Delta-sarcoglycan
- Alpha-sarcoglycan
- Gamma-sarcoglycan
- Zeta-sarcoglycan
- Dystroglycan 1
- Beta-sarcoglycan
Sequence:
MEGSPIPVLTVPTAPYEDQRPTGGGGLRRPTGLFEGQRNYLPNFIQSVLSSIDLRDRQGCTMVVGSDGRYFSRTATEIVVQMAAANGIGRLIIGQNGILSTPAVSCIIRKIKAAGGIILTASHCPGGPGGEFGVKFNVANGGPAPDVVSDKIYQISKTIEEYAICPDLRIDLSRLGRQEFDLENKFKPFRVEIVDPVDIYLNLLRNIFDFNAIKSLLTGPSQLKIRVDAMHGVMGPYVRKVLCDELGAPANSAINCVPLEDFGGQHPDPNLTYATTLLEAMKGGEYGFGAAFDADGDRYMILGQNGFFVSPSDSLAIIAANLSCIPYFRQMGVRGFGRSMPTSTALDRVAKSMKVPVYETPAGWRFFSNLMDSGRCSLCGEESFGTGSDHLREKDGLWAVLVWLSIIAARKQSVEEIVRDHWAKYGRHYYCRFDYEGLEPKATYYIMRDLEALVTDKSFIGQQFAVGSHIYSIAKTDSFEYVDPVDGTVTKKQGLRIIFSDASRLIFRLSSSSGVRATIRLYAESYERDPSGHDQEPQAVLSPLIAIALKISQIHERTGRRGPTVIT
Protein: Mitochondrial GTPase 1 (Q03151)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial GTPase involved in assembly of the large ribosomal subunit. Plays a role in expression of the mitochondrial translational machinery.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}; Peripheral membrane protein {ECO:0000269|PubMed:12808030, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Large ribosomal subunit protein uL29m
- MIOREX complex component 8
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL17m
- rRNA methyltransferase 1, mitochondrial
- Acyl carrier protein, mitochondrial
- Large ribosomal subunit protein uL15m
Sequence:
MHINVRGTRKIISNVSSFTPRYEFPKYSMPLTDFKGHQVKALKTFEKLLPQMNMIIELRDIRAPLSTRNVVFDRIARKEHDVMKLVVYTRKDLMPGNKPYIGKLKNWHEELGEKFILLDCRNKTDVRNLLKILEWQNYELETNGGYLPMGYRALITGMPNVGKSTLINSLRTIFHNQVNMGRKFKKVAKTGAEAGVTRATSEVIRVTSRNTESRNEIYLIDTPGIGVPGRVSDHNRMLGLALCGSVKNNLVDPIFQADYLLYLMNLQNLNDGRTELYPGSTNSPTNDIYDVLRRLQVNKSQNEKSTAIEWTNKWRLHGKGIIFDPEVLLNNDEFSYKNYVNDQLEKLGDLSYEGLSNKLKGNPNQVF
Protein: Arrestin-C (Cone arrestin) (Q6DH07)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- ZPR1 zinc finger.
- Opsin-1, short-wave-sensitive 1
- Opsin-1, short-wave-sensitive 2
- Rhodopsin kinase grk7a
- Recoverin
- Green-sensitive opsin-2
- Green-sensitive opsin-1
- Cone transducin alpha subunit, alpha transducing activity polypeptide 2) subunit alpha-2)
- Retinoid isomerohydrolase
- Phosphatidylinositol transfer protein beta isoform
Sequence:
MADKVYKKTSGNGQLTLYLGKRDYVDHVDVVDAVEGAVKIDPADLGDKKVWVQLACAFRYGREDLDVIGLSFRKDIWIQHIQLYPEAGHKPTLTEMHNTLLKKAGEQGHPFTFNIPTNLPCSVTLQPGPDDKGKACGVDFEVKAYVAKSADDPDEKVDKKDTCRLVIRKIQFAPDNTGSGQKAELCKSFMMSDKPVLLEASLEKEIYYHGDPIPVNIKIKNETNKVVKRIRVTVDQTTDVVLYSADKYTKNVLTEEFGETVEANSSFEKSLDITPLLANNKEKRGLALDGRLKDEDTNLASTTIIRTGMDKEMLGILVSYKIKVNLMVSGGGLLGGLTASDVTVELPLTLMHPKPKD
Protein: D-aminoacyl-tRNA deacylase 2 (EC 3.1.1.96) (Animalia-specific tRNA deacylase) (ATD) (D-tyrosyl-tRNA(Tyr) deacylase 2) (L-alanyl-tRNA deacylase) (E1C762)
Organism: Gallus gallus (Chicken)
Function: Deacylates mischarged D-aminoacyl-tRNAs (By similarity). Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity). Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids (By similarity). Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr) (By similarity). By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS. Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site. Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo EEF1A1/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- AA_TRNA_LIGASE_II domain-containing protein.
- AA_TRNA_LIGASE_II domain-containing protein.
- AA_TRNA_LIGASE_II domain-containing protein.
Sequence:
MAAARPVLARALLQQCLFARLQVKPPEHGAEAEWEEIQRGLVIYICFFKGADEDLVPKIVNVLLNVKLSEDENGEYVSVLDLPGNVLIIPQATLGGKLKGRKMQYHTNIEKEKGMELYSQFVSLCEKELAANPKCMEAGVLVKHGTYGNRQVLKLDTNGPYTHLVEF
Protein: Ribonuclease 3 (EC 3.1.26.3) (Protein Drosha) (Ribonuclease III) (RNase III) (Q5HZJ0)
Organism: Mus musculus (Mouse)
Function: Ribonuclease III double-stranded (ds) RNA-specific endoribonuclease that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DROSHA cleaves the 3' and 5' strands of a stem-loop in pri-miRNAs (processing center 11 bp from the dsRNA-ssRNA junction) to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. Involved also in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in the formation of GW bodies.
Subcellular location: Nucleus {ECO:0000269|PubMed:29784949}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9NRR4}. Cytoplasm {ECO:0000269|PubMed:29784949}. Note=A fraction is translocated to the nucleolus during the S phase of the cell cycle. Localized in GW bodies (GWBs), also known as P-bodies. {ECO:0000250|UniProtKB:Q9NRR4}.
Interaction partners:
- Probable ATP-dependent RNA helicase DDX5
- Microprocessor complex subunit DGCR8
- Probable ATP-dependent RNA helicase DDX17
- Cellular tumor antigen p53
- Protein argonaute-2
- RNA-binding protein FUS
- TAR DNA-binding protein 43
- Protein argonaute-1
- Endoribonuclease Dicer
- RISC-loading complex subunit TARBP2
Sequence:
MQGNTCHRMSYHPGRGCPRGRGGHGARPSAPAFRPQNLRLLHPQQPPAQYQYEPPSAPSSSYSNSQAPSFMPPRPDFVPYPPPAAPSAQGPLPPCPVRPPYPNHQMRHPFPVPPCFPPMPPPMPCPNNPPASGAPPGQGTFPFMVPPPSMPHPPPPPVMPQQVNYQYPPGYSHSFPPPGFNSYQNNSSSFPPSANSSSTPHFRHLPPYSLPKAQNERRSPERLKHYDDHRHRDHSHGRGERHRSLERRERGRSPERRRPESRYRSDYDRGRTPPPRHRSYERSRERDRERHRHREARRSPSLERSYKKEYKRSGRSYALPVAPEPAGCTPELPGEMIKTTESWAPPPENVNHRSPSREKKRARWEEEKDRWSDSQGSGKEKNYTSIKEKEAEEVPPEKTEEEEEELLKPVWIRCTHSESYYSSDPMDQVGDSTVVGTSRLRDLYDKFEEELGNRQEKAKAARPPWEPPKTKLDEDLESSSESECETDDDSTCSSSSDSEVFDVIAEIKRKKAHPDRLHDELWYNDPGQMNDGPLCKCSAKARRTGIRHSIYPGEEAIKPCRPMTNNAGRLFHYRITVSPPTNFLTDRPTVIEYDDHEYIFEGFSMFAHAPLTNIPLCKVIRFNIDYTIHFIEEMMPENFCVKGLELFSLFLFRDILELYDWNLKGPLFEDSPPCCPRFHFMPRFVRFLPDGGKEVLSMHQILLYLLRCSKALVPEEEIANMLQWEELEWQKYAEECKGMIVTNPGTKPSSVRIDQLDREQFNPEVITFPIIVHFGIRPAQLSYAGDPQYQKLWKSYVKLRHLLANSPKVKQTDKQKLAQREEALQKIRQKNTMRREVTVELSSQGFWKTGIRSDVCQHAMMLPVLTHHIRYHQCLMHLDKLIGYTFQDRCLLQLAMTHPSHHLNFGMNPDHARNSLSNCGIRQPKYGDRKVHHMHMRKKGINTLINIMSRLGQDDPTPSRINHNERLEFLGDAVVEFLTSVHLYYLFPSLEEGGLATYRTAIVQNQHLAMLAKKLELDRFMLYAHGPDLCRESDLRHAMANCFEALIGAVYLEGSLEEAKQLFGRLLFNDPDLREVWLNYPLHPLQLQEPNTDRQLIETSPVLQKLTEFEEAIGVIFTHVRLLARAFTLRTVGFNHLTLGHNQRMEFLGDSIMQLVATEYLFIHFPDHHEGHLTLLRSSLVNNRTQAKVAEELGMQEYAITNDKTKRPVALRTKTLADLLESFIAALYIDKDLEYVHTFMNVCFFPRLKEFILNQDWNDPKSQLQQCCLTLRTEGKEPDIPLYKTLQTVGPSHARTYTVAVYFKGERIGCGKGPSIQQAEMGAAMDALEKYNFPQMAHQKRFIERKYRQELKEMRWEREHQEREPEEAEDIKK
Protein: Probable mannosyltransferase KTR3 (EC 2.4.1.-) (P38130)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possible glycosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Protein SVP26
- Glycolipid 2-alpha-mannosyltransferase
- Alpha-1,2 mannosyltransferase KTR1
- Alpha-1,2-mannosyltransferase MNN5
- Mannan polymerase complexes subunit MNN9
- Alpha-1,2-mannosyltransferase MNN2
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
Sequence:
MSVHHKKKLMPKSALLIRKYQKGIRSSFIGLIIVLSFLFFMSGSRSPEVPIAQGTSVSRVASKDYLMPFTDKSQGVIHPVDDGKKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAKYGTIPKDHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDIFKFLKVNNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDAYREYFDYLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLGFHHPDFTSCPIEQKIRLQNKCICEPSKDVTWTPDYFCTRKYFSAGNYKLPPGI
Protein: GEO05313p1 (LD11057p) (RE05245p) (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C) (Uncharacterized protein, isoform D) (Q9VI56)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tyrosine--tRNA ligase
- LD46233p
Sequence:
MTSTELKIGLTTSARPSSRVLKPPGGGHTNIFSEPDVAVPAPRAKYNQQNSSNLNACMGSTDPNKVVEKIREEVSIQKEEAKSAPPSQPKEPANKPAATNGEARGRVPPGGFSSGGFW
Protein: Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (EC 3.1.3.36) (Inositol polyphosphate 5-phosphatase J) (Phosphatidylinositol 1,3,4,5-tetrakisphosphate 5-phosphatase) (EC 3.1.3.56) (Phosphatidylinositol 1,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.56) (Proline-rich inositol polyphosphate 5-phosphatase) (Q9JMC1)
Organism: Rattus norvegicus (Rat)
Function: Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10593988}. Note=Predominantly localized to membrane ruffles.
Interaction partners:
- Inositol polyphosphate-1-phosphatase.
- Inositol polyphosphate-5-phosphatase A
- Inositol-trisphosphate 3-kinase A
- Inositol-trisphosphate 3-kinase B
- Inositol-trisphosphate 3-kinase C
- Multiple inositol polyphosphate phosphatase 1
- Inositol polyphosphate multikinase
- Inositol polyphosphate 5-phosphatase K
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Transmembrane protein 132C
Sequence:
MEGQSRSGSAKSGTRTGLGPLPGTHGALQTGTPSKKVNSSFQLPAKNTGPTPSEPRLALAPVGPRAAVSPPSERPRLALSSPRPILAPLSTAGEQKRPPPHRSSKPAPTSVGQLVVSAAAGPKPPPVASVSILAPKSLGQLVISASAMPRPTPAPLGPILSPTSRDQKQLSPTSVGPKPALATSGLSLALASQEQPPQSPSSPSPVPSPVLSPSQESHLAPATVTSTPASERQLPARQKDTAVRRPIPPADGCLHTPVQAAGLATSPPRAQTSSDPRLSPSFRARPEAPRHSPEDPVLPPPPQTLPLDVSSGLPESGTRSPGLLSPTFRPGIPSNQTVPPPLPKPPRSPSRSPSRSPNRSPCVPPAPEVALPRPVTQGAGPGKCPSPNLQTQESPVATATSPTSSWSAQPTCKSDPGFRITVVTWNVGTAMPPDDVTSLLHLGGGHDSDGADMIAIGLQEVNSMINKRLKDALFTDQWSELFMDALGPFNFVLVSTVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAHGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSNQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPSGGPSPSGRESHRLQVTQHSYRSHMEYTVSDHKPVAARFLLQFAFRDDVPLVRLEVADEWARPEQAVVRYRVETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEEVDGNIYQVTFSEESLPKGHGDFILGYYSHHHSILIGVTEPFQISLPTSESASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPSLALRPSSRERRGGSRSPSPQSRQLPRVAPDRGHSSGSRGSSEEGPSGPPGPWAFPPAVPRSLGLLPALRLETVDPGGGGSWGPDQEAPDPNSLSPSPQGRLGLEDGGLGP
Protein: Xyloglucan endotransglucosylase/hydrolase (EC 2.4.1.207) (E3UZI8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted, cell wall {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space, apoplast {ECO:0000256|RuleBase:RU361120}.
Interaction partners:
Sequence:
MTMATLSSAFLFIFSCFLACSISVSGRPTTFLEDFRITWSDSHIKQIDGGRAIQLILDQNSGCGFASKRQYLFGRVSMKIKLIPGDSAGTVTAFYMNSDTDTVRDELDFEFLGNRTGQPYTVQTNIYAHGKGDREQRVNLWFDPAADFHTYTIMWNHHHIVFYVDEVPIRVYKNNEAKNIPYPKFQPMGVYSTLWEADDWATRGGLEKIDWSKAPFLAYYKDFDIEGCPVPGPANCASNPRNWWEGTAYQALNAMEARRYRWVRMNHMIYDYCTDKSRYPVTPPECMAGI
Protein: DJ-1 protein homolog F (AtDJ-1F) (Q9M1G8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in oxidative stress response.
Interaction partners:
- Hydroxyacylglutathione hydrolase 1, mitochondrial
- Hydroxyacylglutathione hydrolase 2, mitochondrial
- Probable hydroxyacylglutathione hydrolase 2, chloroplastic
- Hydroxyacylglutathione hydrolase cytoplasmic
- Lactoylglutathione lyase GLX1
- Probable lactoylglutathione lyase, chloroplastic
- Lactoylglutathione lyase
- Protein DJ-1 homolog C
- Protein DJ-1 homolog B
- Protein DJ-1 homolog D
Sequence:
MGSMAQKSVLMLCGEFMEAYETIVPLYVLQAFGVSVHCVSPGRKTGDKCVMAAHDLLGLEIYTELVVDHLTLNANFDGVIPDQYDAIIIPGGRFTELLSADEKCVSLVARFAELKKLIFTSCHSQLFLAAAGLLTGGMKCTAFESMKPFIELSGGAWWQQPGVQTLFEITDCVKDGSFMSTMGWPTLGHSLKVLLESLGSKISSSKENHQTSLLFLIGDCVEDYSINVPFKAFQALGCKVDAVTPTKKRGEKCATIVHDLEDGRQLPTEKFGHNFYVTVAWDDVSVDDYDCIVVPGGRSPELLVMNPKAVELVRKFVEKGKFVAAIGMGNWLLAATGALKKKRCASSYGTKVAVKVAGGEIVESERCVTDDKLVTAASTSDLPAFLYALSTALGLSVVF
Protein: Uncharacterized protein (Q38EY5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTFLYHRWYNDDFTIANTPSGSFRDVCMTWSYTDPRIKETTLIFLLSPSVALTEGAEGFVEHGLHALKIVHIRGATSQPSKGEVEEVVCCTVVEIVGSIPDGVVHGTGGVIFLSTRHFLFHIPTGEQSRTGGKEREDALDHFVFTEKNSWERRCGVVRPLYDVEPIRHVLYGAEGNKSPVLHIVTVVSQPSPSSVSMQSAVVDLLVVASSRDERDISQYSRTEQGLLGKTISRWRGSSKASGDSSVAVTHTFVVAVVRCEISTSADRPAAWKLLHLHVDRNVPFQRRLEELTGREDLCGVGCDRKGSNATAAHMDPSKCVWCYLPNEGGARAGYCGLVFALVPHKPSTKLTLVCGSYDPSGQSYRVGFVKGDDAHGVGPPLYEERDNTEEMLWSLAEGTHTVQMVMIGRPNEALHDNEGTCGGANFQGREGLRAQWRKSASSSTWMRKSGLATVLSFVVDFVDDGLHKSRNLRQGLHVAVCTAWERNRHGRFPLPRTVCWLGTIPLPIGQAATSAVLFHAEGNDEGMNVWRMMDRVNLSDCAAVCDDTVSWYHALPTSVVPTVAAPVSRTNLRCFVSVNTLLKKTQLTYVLDTRFVEEKTCEEQRPSLLSSLELSKLFYTRPAIAEEGHGAMYNRGATSDDCADLAAYVARSVASSSGPLMVAHIFNEAWRSVALVKHPETAVHAHDGVARDGLLPSTDGEMIALGDTVCHFLLLVLQELDWINSPQNTRLHILVLSILEAVYAEPQLPPSSRCFEEATNGGGKTQMLLVGVNEQRTVRLLLQGSGMWRRVAPMLFAWANYRFYGNGCENELEEDSDSLFEDTLRPFIEGWEKQENMAGFDSHACTASCNNDSESGESCLILKRCDVILRHLQHSQDCDKYRSAVAALFRGGVSLNRVTALASWAGDVQAVDPAVLLFQLLLEVCTQCEEHVQLAAAVDRETICQLTALVMQSRLPPVDTVKNDENSLPAAPDVLHSMSEVLSSWNFELLRDWPLGGTCGALPVVYLFYHMVGALMASPCDNMEDRRERCNIITHSVMLLQWLCGDDARQSTEVFGALISGKVPLVALCTVGGFAVQAGCAPSSGVPPCDAVARRSFNRVLYHLFVSPTTSVLPQLLLAEFGISYDYVSHEKIGFSVWKRVLEGDVAAAFSSRLLNQLHKSLGSFSNKKHPTRAVQVSLLLEYLRSVFMVSLPRLVMALGESEEIVEIALGSTIPSFIMSELSVDPVPPVEGCDNVTCVFFNVTREVKKLLHLYMEGSGEVRCLAMLFGVFCDSCKSLLGHVDDTENVRDSAQPGGVEREQSMFTFTLQEMYFISLQVLSSDMGRFVVVAELIRRSVRRQAVRDLEKSLHRFDASWLNNSSRLQEFISSAVANLDGVVSSLESVAPLYAHTLVMIFLDELVLLAGETTEAVGRVVASPSIPHEQGEGYYKGEVIVDLNDKLTKCVKQMAAEKWKGLRKEDRRLIARVLSSCLVPSSDEAFGDGGYEESDVHLQMRDVKVRMSKSLQRRTIDPTVMGIVVGEASANESDKFPVELRRNNDSDGVLKVGGDAERAEFALLVKEEAYVRRKLKGQLLDSYAELINGNGVHDSLAILYLALREEQRRRRFVEYVTECKDFVLDFAISLHMLMREYYNEGVYHLQEKALREMERRVGLLLLQEREARTAIEAVHSVGRDIYFCWEKEQRSLFEGESRCRLAMLEDEENTRDAIYEHFAKEEVAVVRRCEERLEEEAWRQEEEQWALEMKQREDEEVSAARTQNKKPSEGKRTGTSAFTRWQERRLQMVMVHEEVSEPMEQERCPTSSITEAEALPTTKPEILPRERTTAFVQDPVEALTSLVRTEPTEESVDGRGYSALFDSSESLFGAISRFQQQIISTVAPPPLSVAKQKEQEQGGEMPHQSPTELTANPHSSTQTQQPVGSEWEWGWDEVPDDAGGSWKVSRNDCKTGVATENYLTTRIPDEKKEEFSEKIIKLEALSKAVKPRPQRRRPFGGVVNLHAKPTEGKVSPINDSIPETGQEEQQIGEISLRSADEGHAKEVSTLLTSTEMWNAKGEELHPFSATVGEPLDVATSSLWVGEHQMNLAVSDVCEEVVCHTEYLPKDSLEMSSVILSLSSFHVMQEEEGGARLALLNEERIGRVFLNRRLVMGL
Protein: ATP-binding cassette alpha-factor transporter (A0A1D8PKI5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Alpha-factor pheromone receptor
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Kar4p
- Sap30p
- Mating-type-like protein A1
- Asg7p
- Fus1p
Sequence:
MFQEKSEKSSFPKRSSSLRSPSDSPAITSKNVFMFVNYSKDWPLILVGILLMGGSAIATPMNTYIYGEIMGKLSQFYLQDQSNHSFSQDIVKLCVGLIGIGCCKMILVWLGMFTWLKFGEIQQSRARMQIYNKIINESQSWYDSKQNLIGQLTQINRCIEELRSCNGEILASLMQTIVLILALLIMSFYQSWSTTLIIMASFPIMALCGWYFGKLTYKAQQDENEVTSKASKVFNWCYVNPEMVRFFNSKNIELTKFKQLIEKSAQFYYKLSHAVAANTAVLKTLTLMMFVQGFWFGNYLLSHKTITINQLFTCFSSCLMLGQAVSGITELLAILNTGHAAADKISGFLLQPPSKAKLLLLHSKYPPFEIGSIYFKNVWFESNSQNSVAILQDVSFGILQNQFNYVIGKSGSGKSTIAKLLMRLYSVSRGTIEIDTVSIDKLDPKYICQNITLLEQNPVIFDDKTIAENIAIAIVDDYDSLQAIPYYLIEQSAHFALLSDLDLNMKVNHLTLSGGQQQRISIARAYLKNSPVLIMDESFSALDTETKQGLIEKVKKWRIGKTTIFITHEYKNILDDENVIILDQGMIKNQGQFKKMKNEEIVQNYKSQGIETSSYETTSQSFSDNTKLPDGDYNYKTNPYILKDLESQIKEDTDNEKLMGVLAILRYCSSTINGKSLLGFGILLAIFQGVSSPVFSYCFSKLLSTSLDSSIGLNSTQKILQWSCISLSIAIFTGVTSYLSEFILNYCGENWIVSLRQLTFFKLNNQDLSFFTGFDTNWSSSEITALLMNDTRDLRNLISQFFPLLANLVSMTLIGIIWSIVSGWKLALVGISFVPLVLLVTVLYGKILESIENKYKCKVNNVELDLYRTITTIRTIKIFNIQQYFETVFKEDLKVLNSIGVYRALQTGIGFAISDLFSSIGQAIILFYGMKLISQFQYNYSQLLQVITLLSFTISNASILIHQLPEITRGQRAGTFIVKLLKDITSTMEVNDSCGVSSVRKRNSKSGSDSIGTIGPVKDNQLFKKVTTDNDTLAISFNNVSFSYPNKLHYILQLKSISLDVKKFTTIGIVGQSGSGKSTILKILFRLYDIKISPDSNTTKKYHDQTVKIFNQNLYLINSGLLCQTIAIVPQFPKFFSGTIYDNLTYGINNTNSAGSNSSSSVSDSEIIKILKLVNLHQFIVSLPQGLLTIMNDSDNDNDNGNENENENENGNTISTSSSTSFTFSGGQLQLLAIARALLRNPKILLLDECTSNLDPITTKIIINVIKSLHGKLTILFVTHDKELMRIADNLIVMKDGQIVEQGDFQQLISNDGEFTKITKTII
Protein: Galactinol synthase 4 (AtGolS4) (GolS-4) (EC 2.4.1.123) (O22693)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable galactinol--sucrose galactosyltransferase 1
- Probable galactinol--sucrose galactosyltransferase 6
- Probable galactinol--sucrose galactosyltransferase 5
- Probable galactinol--sucrose galactosyltransferase 2
- UDP-sugar pyrophosphorylase
- ADP-glucose phosphorylase
- UDP-glucose 4-epimerase 5
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 3
- UDP-glucose 4-epimerase 2
- UDP-glucose 4-epimerase 4
Sequence:
MAPEISVNPMYLSEKAHQAPPRRAYVTFLAGNGDYVKGVVGLAKGLRKVKSAYPLVVAMLPDVPEEHREILRSQGCVVREIEPVYPPDNQVEFAMAYYVLNYSKLRIWNFEEYSKMIYLDADIQVFDNIDHLFDLSDAYFYAVMDCFCEKTWSHSLQYSIGYCQQCPEKVTWPEDMESPPPPLYFNAGMFVFEPSPLTYESLLQTLEITPPSPFAEQDFLNMFFEKVYKPIPLVYNLVLAMLWRHPENVELEKVKVVHYCAAGSKPWRYTGEEANMDREDIKMLVDKWWDVYNDESLDFKSKIPADAEETVTKSSILASVLEPEMTYFPAPSAA
Protein: DLGAP1 protein (Discs, large (Drosophila) homolog-associated protein 1, isoform CRA_d) (Q6IS01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKGLSGSRSHHHGVTCDSACDSLSHHSDRKPYLLSPVEHHPADHPYYTQRNSFQAECVGPFSDPLASSTFPRRHYTSQQELKDECALVPRTLATKANRIPANLLDQFERQLPLSRDGYHTLQYKRTAVEHRSDSPGRIRHLVHSVQKLFTKSHSLEGPSKGSVNGGKASPDEAQAARYGKRSKSKERRAEPKARPSTSPGWWSSDDNLDGDMCIYHAPSGVMTMGRCPDRSASQYFLEAYNTISEQAVKASRSNNDVKCSTCANLPVSLDTPLLKKSAWSSTLTVSRAREVYQKASVNMDQAMVKSESCQQERSCQYLQVPQDEWTGYTPRGKDDEIPCRRMRSGSYIKAMGDEDSGDSDTSPKPSPKVAARRESYLKATQPSLTELTTLKISNEHSPKLQIRSHSYLRAVSEVSINRSLDSLDPAGLLTSPKFRSRNESYMRAMSTISQVSEMEVNGQFESVCESVFSELESQAVEALDLPMPGCFRMRSHSYVRAIEKGCSQDDECVSLRSSSPPRTTTTVRTIQSSTGSLDKKLESWALG
Protein: Ubiquitin carboxyl-terminal hydrolase 42 (EC 3.4.19.12) (Deubiquitinating enzyme 42) (Ubiquitin thioesterase 42) (Ubiquitin-specific-processing protease 42) (Q9H9J4)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme which may play an important role during spermatogenesis.
Interaction partners:
- Cellular tumor antigen p53
Sequence:
MTIVDKASESSDPSAYQNQPGSSEAVSPGDMDAGSASWGAVSSLNDVSNHTLSLGPVPGAVVYSSSSVPDKSKPSPQKDQALGDGIAPPQKVLFPSEKICLKWQQTHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSHDVKNGGELTHPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNPPHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNASASVQNWSVNRSSVIPEHPKKQKITISIHNKLPVRQCQSQPNLHSNSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKVTKPIPRSESCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKENGIGTIVSSHSPGQDAEDEEATPHELQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKLMPAPLLSLPEDKILETFRLSNKLKGSTDEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSHHHSRHRSGVELDWVRHHYTEGERGWGREKFYPDRPRWDRCRYYHDRYALYAARDWKPFHGGREHERAGLHERPHKDHNRGRRGCEPARERERHRPSSPRAGAPHALAPHPDRFSHDRTALVAGDNCNLSDRFHEHENGKSRKRRHDSVENSDSHVEKKARRSEQKDPLEEPKAKKHKKSKKKKKSKDKHRDRDSRHQQDSDLSAACSDADLHRHKKKKKKKKRHSRKSEDFVKDSELHLPRVTSLETVAQFRRAQGGFPLSGGPPLEGVGPFREKTKHLRMESRDDRCRLFEYGQGKRRYLELGR
Protein: Hyaluronan and proteoglycan link protein 4 (Brain link protein 2) (Q80WM4)
Organism: Mus musculus (Mouse)
Function: Essential for the proper localization of brevican (BCAN), mainly as a perineuronal nets (PNNs)-type deposition in the brainstem and cerebellum thereby playing a key role in the formation and structural organization of PNNs. Contributes to the formation and transmission of inhibitory GABAergic synapses between Purkinje cells and deep cerebellar nuclei neurons.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9ESM3}.
Interaction partners:
- IQ domain-containing protein F5
Sequence:
MACAPGALGHRALWAVAWGLLLLVPVLAGAQRGRKKVVHVLEGESGSVVVQTAPGQVVSHRGGTIVLPCRYHYEAAAHGHDGVRLKWTKVVDPLAFADVFVALGPQHRAFGPYRGRAELQNDGPGDASLVLRNVTLQDYGRYECEVTNELEDDVGMVKLDLEGVVFPYHPRGGRYKMTFVEAQRACAEQDGILASAEQLHAAWRDGLDWCNAGWLRDGSVQYPVSHAREPCGGTGSTGAGGGTNGGVRNYGYRHNAEERYDAFCFTSNLPGRVFFLKPLRPVALAGAVRACAARGATVAKVGQLFAAWKLQLLDRCTAGWLADGSARYPIVNPRTRCGGPRPGVRSLGFPDASRRLFGVYCYRAPGAPDPAPGGWGWGWAGGGGWAGGSRDPAAWTPLRV
Protein: Bestrophin-1 (Vitelliform macular dystrophy protein 2 homolog) (O88870)
Organism: Mus musculus (Mouse)
Function: Forms calcium-sensitive chloride channels. Permeable to bicarbonate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:29121962}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76090}. Basolateral cell membrane {ECO:0000250|UniProtKB:O76090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76090}. Note=Localized at the surface membrane of microdomains adjacent to glutamatergic synapses. {ECO:0000269|PubMed:23021213}.
Interaction partners:
- Retinoid isomerohydrolase
- Volume-regulated anion channel subunit LRRC8A
- Retinaldehyde-binding protein 1
- Amine oxidase [flavin-containing] B
- H
Sequence:
MTITYTNKVANARLGSFSSLLLCWRGSIYKLLYGEFLVFIFLYYSIRGLYRMVLSSDQQLLFEKLALYCDSYIQLIPISFVLGFYVTLVVSRWWSQYENLPWPDRLMIQVSSFVEGKDEEGRLLRRTLIRYAILGQVLILRSISTSVYKRFPTLHHLVLAGFMTHGEHKQLQKLGLPHNTFWVPWVWFANLSMKAYLGGRIRDTVLLQSLMNEVCTLRTQCGQLYAYDWISIPLVYTQVVTVAVYSFFLACLIGRQFLNPNKDYPGHEMDLVVPVFTILQFLFYMGWLKVAEQLINPFGEDDDDFETNWIIDRNLQVSLLSVDGMHQNLPPMERDMYWNEAAPQPPYTAASARSRRHSFMGSTFNISLKKEDLELWSKEEADTDKKESGYSSTIGCFLGLQPKNYHLPLKDLKTKLLCSKNPLLEGQCKDANQKNQKDVWKFKGLDFLKCVPRFKRRGSHCGPQAPSSHPTEQSAPSSSDTGDGPSTDYQEICHMKKKTVEFNLNIPESPTEHLQQRRLDQMSTNIQALMKEHAESYPYRDEAGTKPVLYE