wanglab/gogpt-training-data huggingface dataset:
Protein: Cystatin-D (Cystatin-5) (P28325)
Organism: Homo sapiens (Human)
Function: Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B.
Subcellular location: Secreted {ECO:0000269|PubMed:20189825}.
Interaction partners:
Sequence:
MMWPMHTPLLLLTALMVAVAGSASAQSRTLAGGIHATDLNDKSVQCALDFAISEYNKVINKDEYYSRPLQVMAAYQQIVGGVNYYFNVKFGRTTCTKSQPNLDNCPFNDQPKLKEEEFCSFQINEVPWEDKISILNYKCRKV
Protein: Wilms tumor 1 +KTS isoform (A9CSE6)
Organism: Glandirana rugosa (Japanese wrinkled frog) (Rana rugosa)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MGSDVRDMNTLLPPVSSLAGNSSCNVPVNSSAQWAPVLDFPPGAPYTSLAPHSFIKQEPAWNPDLHEDQCLSAFTVHFSGQFTGTAGACRYGAFGAPPPSQAFKGQPRMFPNSPYLPKCLENQQGIRNQGYSAMVFDGTPSYGHTPSHHTAQFPNHSFKHEDPITQQSSLGDQQYSVPPPVYGCHTPTDSCTGSQALLLRSPYNSDNLYQMTSQLECMTWNQMNLSSSLKGHGTTYENDSHSTPMLYSCGGQYRIHTHGVFRGLQDVRRVPGVTPAIVRSSTETNEKRPFMCAYPGCNKRYLKLSHLQMHSRKHTGEKPYQCDLKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWASCQKKFARSDELVRHHNMHQRNMTKLQLAL
Protein: Core gene UL16 family protein (ORF 33) (ORF33) (O40929)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MASRRRKLRNFLNKECIWTVNPMSGDHIKVFNACTSISPVYDPELVTSYALSVPAYNVSVAILLHKVMGPCVAVGINGEMIMYVVSQCVSVRPVPGRDGMALIYFGQFLEEASGLRFPYIAPPPSREHVPDLTRQELVHTSQVVRRGDLTNCTMGLEFRNVNPFVWLGGGSVWLLFLGVDYMAFCPGVDGMPSLARVAALLTRCDHPDCVHCHGLRGHVNVFRGYCSAQSPGLSNICPCIKSCGTGNGVTRVTGNRNFLGLLFDPIVQSRVTALKITSHPTPTHVENVLTGVLDDGTLVPSSKAPWVLLRMSDYFSRLLIYECKKLKALGLRSY
Protein: RNA helicase (EC 3.6.4.13) (F4ZS18)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSRWSSNKDKDAYSSFGSRNDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRGGFGKYERGGHSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNANITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
Protein: Probable acrEF/envCD operon repressor (P0ACT2)
Organism: Escherichia coli (strain K12)
Function: Potential regulator protein for the acrEF/envCD genes.
Interaction partners:
- Multidrug export protein AcrF
Sequence:
MAKRTKAEALKTRQELIETAIAQFAQHGVSKTTLNDIADAANVTRGAIYWHFENKTQLFNEMWLQQPSLRELIQEHLTAGLEHDPFQQLREKLIVGLQYIAKIPRQQALLKILYHKCEFNDEMLAEGVIREKMGFNPQTLREVLQACQQQGCVANNLDLDVVMIIIDGAFSGIVQNWLMNMAGYDLYKQAPALVDNVLRMFMPDENITKLIHQTNELSVM
Protein: Mannosyltransferase (EC 2.4.1.-) (B4DYW0)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}.
Interaction partners:
Sequence:
MAPRRLLLVGEGNFSFAAALSETLDQSTQLTATCLQRPAELARDPLAWENLQCLRERGIDVRFGVDCTQLADVFELHEREFDQIYFNFPHCGRKAGVAKNRELLAKFFQSCADVLAEEGEVHVALCRGQGGTPADKPQREWHNSWQVVAMAALGGLILSDVYPFSCKAVAGYKCTGYRSQDKSFHVEGALNHIFTRSLPFEGSQPRIFRIKLGNQWFSFPEPEALVGKLNRLAMASRGARQRLKGSGASSGDTAPAADKLRELLGSREAGGAEHRTELSGNKAGQVWAPEGSTAFKCLLSARLCAALLSNISDCDETFNYWEPTHYLIYGEGFQTWEYSPAYAIRSYAYLLLHAWPAAFHARILQTNKILVFYFLRCLLAFVSCICELYFYKAVCKKFGLHVSRMMLAFLVLSTGMFCSSSAFLPSSFCMYTTLIAMTGWYMDKTSIAVLGVAAGAILGWPFSATLGLPIAFDLLVMKHRWKSFFHWSLMALILFLVPVVVIDSYYYGKLVIAPLNIVLYNVFTPHGPDLYGTEPWYFYLINGFLNFNVAFALALLVLPLTSLMEYLLQRFHVQNLGHPYWLTLAPMYIWFIIFFIQPHKEERFLFPVYPLICLCGAVALSALQKCYHFVFQRYRLEHYTVTSNWLALGTVFLFGLLSFSRSVALFRGYHGPLDLYPEFYRIATDPTIHTVPEGRPVNVCVGKEWYRFPSSFLLPDNWQLQFIPSEFRGQLPKPFAEGPLATRIVPTDMNDQNLEEPSRYIDISKCHYLVDLDTMRETPREPKYSSNKEEWISLAYRPFLDASRSSKLLRAFYVPFLSDQYTVYVNYTILKPRKAKQIRKKSGG
Protein: tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ALKBH8 (EC 2.1.1.229) (Alkylated DNA repair protein alkB homolog 8) (Alpha-ketoglutarate-dependent dioxygenase ALKBH8) (S-adenosyl-L-methionine-dependent tRNA methyltransferase ALKBH8) (Q96BT7)
Organism: Homo sapiens (Human)
Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA. Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly). Required for normal survival after DNA damage. May inhibit apoptosis and promote cell survival and angiogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17979886, ECO:0000269|PubMed:20308323, ECO:0000269|PubMed:34948388}. Nucleus {ECO:0000269|PubMed:20308323}. Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:20308323}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Nucleic acid dioxygenase ALKBH1
- DNA oxidative demethylase ALKBH2
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
- tRNA
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4
- Elongator complex protein 3
- Alpha-ketoglutarate-dependent dioxygenase FTO-)-demethylase FTO)
- 18S rRNA
Sequence:
MDSNHQSNYKLSKTEKKFLRKQIKAKHTLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKELRPQALPPGLMVVEEIISSEEEKMLLESVDWTEDTDNQNSQKSLKHRRVKHFGYEFHYENNNVDKDKPLSGGLPDICESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSLGSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQASESLKSGIITSDVGDLTLSKRGLRTSFTFRKVRQTPCNCSYPLVCDSQRKETPPSFPESDKEASRLEQEYVHQVYEEIAGHFSSTRHTPWPHIVEFLKALPSGSIVADIGCGNGKYLGINKELYMIGCDRSQNLVDICRERQFQAFVCDALAVPVRSGSCDACISIAVIHHFATAERRVAALQEIVRLLRPGGKALIYVWAMEQEYNKQKSKYLRGNRNSQGKKEEMNSDTSVQRSLVEQMRDMGSRDSASSVPRINDSQEGGCNSRQVSNSKLPVHVNRTSFYSQDVLVPWHLKGNPDKGKPVEPFGPIGSQDPSPVFHRYYHVFREGELEGACRTVSDVRILQSYYDQGNWCVILQKA
Protein: Acetylcholine receptor subunit gamma (P18916)
Organism: Rattus norvegicus (Rat)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MHGGQGPQLLLLLLATCLGAQSRNQEERLLADLMRNYDPHLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPKDYEGLWILRVPSTMVWQPDIVLGNNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSSCSISVTYFPFDWQNCSLVFQSQTYSTSEINLQLSQEDGQAIEWIFIDPEAFTENGEWAIRHRPAKMLLDPVTPAEEAGHQKVVFYLLIQRKPLFYVINIIVPCVLISSVAILIYFLPAKAGGQKCTVATNVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLMVVTILIVVNSVVVLNVSLRSPHTHSMARGVRKVFLRLLPQLLRMHVHPRAPAAVQDARLRLQNGSSSGWPIMTREEGDLCLPRSELLFRQRQRNGLVQAVLEKLENGPEMRQSQEFCGSLKQASPAIQACVDACNLMARARHQQSHFDSGNEEWLLVGRVLDRVCFLAMLSLFICGTAGIFLMAHYNQVPDLPFPGDPRPYLPLPD
Protein: Palmitoyltransferase (EC 2.3.1.225) (O97224)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNDNESLDSEVLEKQYEIIKYAKYQDFIRLQILIQPYLLNNDIEMLNSINILHWACYCGFTELVKKLISFNCDIEKEDLVNNDTPIYYAIKNSNYEIVLLLIKCFGISILFHKNRRRMSPFLTAICEFNEDKILEALHILELLYMNGVSLEEQNEHGQTALFLSVKKNNISTLQWLLTKEVNINHRDFYGNTVLHIAVRHCDIDILRLLCDYGCLNMVYYSSIENKNTNVFQLCIKNRYFLVYILLKKWVLQNKICSKLKICKTIYAFYFWFFAILNLIVYFNIAHSFSIINKYHFKSLIWITIWFFQQFLWCMLYFKSPGFYKENHMFNKNKKNIQSSKYKNSNPMYNGTFKTNAEYQLNNIEREIFQINKKLISTNFNTLTPINHDQALSNKYNDILINLEYQKLSLYSQVSQERINSLDEDYRNAILYNQNPRNICVTCNIIKPPRVHHCAECFHCIVHQDHHCVWVDNCIGIKNQRCFYMFIFCIFVLLLYNYYYVYLYFHLFQATINYAFGSLVILCNFINVTLFAFITYLFARNTRTILTNVTFYEHYKKPNHITDKYNTDLRCWDFQNLNLKGILKNIYYFWSLNYDEPYIRQCTKTSNDVCYTLISNT
Protein: Farnesyl pyrophosphate synthase (FPP synthase) (PgFPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase) (Q4JHN6)
Organism: Panax ginseng (Korean ginseng)
Function: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity). Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Promotes the accumulation of ginsenosides.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P14324}.
Interaction partners:
Sequence:
MSDLKTRFLEVYSVLKSELLNDPAFEFTDDSRQWVERMLDYNVPGGKLNRGLSVIDSYKLLKEGKELSDDEIFLSSALGWCIEWLQAYFLVLDDIMDSSHTRRGQPCWFRLPKVGMIAVNDGILLRNHIPRILKKHFRQKPYYVDLLDLFNEVEFQTASGQMIDLITTLVGEKDLSKYSLPIHRRIVQYKTAYYSFYLPVACALLMSGEDLEKHTNVKDILIEMGTYFQVQDDYLDCFGAPEVIGKIGTDIEDFKCSWLVVKALELSNEEQKKFLHENYGKDDPASVAKVKELYNTLKLQDVFAEYESKSYDKLIKFIEAHPSQAVQAVLKSFLGKIYKRQK
Protein: Short-chain dehydrogenase/reductase aba4 (EC 1.1.1.-) (Abscisic acid biosynthesis cluster protein 4) (Q14RS1)
Organism: Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Interaction partners:
Sequence:
MSSQPFTNKVIALTGSASGIGLETAKLLASRGARLSLADIQEDKLKELQAXXESEYHVDVITTKVDVRKFGEVEAWINKTIDNFGKLDGSANLAGVAPESIGLKGIVEQDLDEWEFVLGVNLTGTMNSLKAQLKVMANNGSIVNASSIRGLTGAAKNASYSSAKHGIIGLTRTAAKEVGGKGIRVNAICPGRISTPMLKTAENSIGLHLQPGSANYPPIALGRDGEAKEVAQLVAFLLSDESTYISGADISIDGGWRC
Protein: Linear element protein rec25 (Meiotic recombination protein rec25) (Meiotically up-regulated gene 19 protein) (Q9C115)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: During meiotic DNA recombination, binds to and may help activate DNA double-strand break (DSB) hotspot sites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23395004, ECO:0000269|PubMed:28469148, ECO:0000269|PubMed:33825974}. Chromosome {ECO:0000269|PubMed:23395004}. Note=Localizes to chromosomal double-strand break (DSB) hotspot sites during the meiotic cell cycle. {ECO:0000269|PubMed:23395004}.
Interaction partners:
- Linear element protein rec27
- Linear element protein rec10
- Linear element protein Mug20
- Linear element-associated protein hop1
- Meiotic recombination protein rec24
- Meiotic recombination protein rec12
- Meiotic recombination protein rec11
- Meiotic recombination protein rec15
- Mei4-dependent protein 2
- Meiotic recombination protein rec8
Sequence:
MVKGSVTNTSSIVKQFEKSSIKHETETIAFAKQFINECIREFQEQKDNVVEEKNTDQNHQNQNQEGVIIEIYQELLQKVDLISSELRQNLSSLQLRFQEVERDTGHDLLNVLNSLSQEARLAQKVLEEDGSQQGSQLIQGLLTCFQSTGN
Protein: Dihydroneopterin aldolase 2 (DHNA2) (EC 4.1.2.25) (7,8-dihydroneopterin aldolase) (AtFolB2) (Q9FM54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of 7,8-dihydroneopterin into 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin tetrahydrofolate. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin.
Interaction partners:
- Folate synthesis bifunctional protein
- Folate synthesis bifunctional protein
- GTP cyclohydrolase 1
- Dihydrofolate synthetase
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Aminodeoxychorismate synthase, chloroplastic
- D-amino-acid transaminase, chloroplastic
- Folylpolyglutamate synthase
- Probable dihydroneopterin aldolase 3
Sequence:
MEKDMAMMGDKLILRGLKFYGFHGAIPEEKTLGQMFMLDIDAWMCLKKAGLSDNLADSVSYVDIYNVAKEVVEGSSRNLLERVAGLIASKTLEISPRITAVRVKLWKPNVALIQSTIDYLGVEIFRDRATE
Protein: Dihydropyrimidinase-related protein 4 (DRP-4) (Collapsin response mediator protein 3) (CRMP-3) (UNC33-like phosphoprotein 4) (ULIP-4) (O35098)
Organism: Mus musculus (Mouse)
Function: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Dihydropyrimidinase-related protein 5
- Uridine 5'-monophosphate synthase
Sequence:
MSFQGKKSIPRITSDRLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVMGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPINPDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVFSAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAGRFIPRKTFPDFVYKRIKARNRLAEIHGVPRGLYDGPVHEVMLPAKPGSGTQARASCSGKISVPPVRNLHQSGFSLSGSQADDHIARRTAQKIMAPPGGRSNITSLS
Protein: 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1) (P62193)
Organism: Rattus norvegicus (Rat)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC1 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P62191}; Lipid-anchor {ECO:0000250|UniProtKB:P62191}.
Interaction partners:
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 11
- Proteasome
Sequence:
MGQSQSGGHGPGGGKKDDKDKKKKYEPPVPTRVGKKKKKTKGPDAASKLPLVTPHTQCRLKLLKLERIKDYLLMEEEFIRNQEQMKPLEEKQEEERSKVDDLRGTPMSVGTLEEIIDDNHAIVSTSVGSEHYVSILSFVDKDLLEPGCSVLLNHKVHAVIGVLMDDTDPLVTVMKVEKAPQETYADIGGLDNQIQEIKESVELPLTHPEYYEEMGIKPPKGVILYGPPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVAEEHAPSIVFIDEIDAIGTKRYDSNSGGEREIQRTMLELLNQLDGFDSRGDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDEKTKKRIFQIHTSRMTLADDVTLDDLIMAKDDLSGADIKAICTEAGLMALRERRMKVTNEDFKKSKENVLYKKQEGTPEGLYL
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FPR9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MKFTHQFVLSLIALAKLVMADSQQFGIISIASGSDLQYASAFFDSNNLVVGHQPNNQFALVVTDDGKLKSTSGNQFIAVDANSGNLKEVSDSNSASVGFSIKNGHLLYLNSESFYAVPGASSGATWSLSTKNTNSAQGAAASPVVLRTQSTTGTDVVADFTPAAMSSVSSVVPSSISSVHPSSLVSSGSTLVLSKASGSAVPISQIGDGQIQATATSHVPPVQSHNGAIGQHGPYLGMHAGVAAAAIAYLL
Protein: Dinoflagellate viral nucleoprotein 5 (DNVP5) (K9NVA6)
Organism: Hematodinium sp
Function: DNA-binding protein, which similarly to histones, may compact DNA into chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:23159597, ECO:0000269|PubMed:29670105}. Chromosome {ECO:0000269|PubMed:23159597}. Note=Localizes to condensed chromosomes (PubMed:23159597). Localizes upstream and downstream of transcription start sites of chromatin (PubMed:29670105). {ECO:0000269|PubMed:23159597, ECO:0000269|PubMed:29670105}.
Interaction partners:
Sequence:
MAAMKKAMKVKKSAKKSAKKSGKKGGMKKKAKRVSKVARGKRAKSSVFRGTKERTSGGLTKNSLVKNKQGRVVSKKQSEHGKKIFKKHGLQKWIDAVTKARKALGIKGFQAVGGSSAKGKILLAKSRSFYKK
Protein: 3-isopropylmalate dehydratase (EC 4.2.1.33) (Alpha-IPM isomerase) (IPMI) (Isopropylmalate isomerase) (O14289)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Interaction partners:
- 3-isopropylmalate dehydrogenase
- 2-isopropylmalate synthase
- Dihydroxy-acid dehydratase, mitochondrial
- Homocitrate synthase, mitochondrial
- Multifunctional tryptophan biosynthesis protein
- Histidinol-phosphate aminotransferase
- Dihydroorotate dehydrogenase
- Probable acetolactate synthase small subunit
- Probable ketol-acid reductoisomerase, mitochondrial
- Adenylosuccinate synthetase
Sequence:
MSPSVASPKTLYDKVWDSHVVDLQEDGTCLLYIDRHLIHEVTSPQAFEGLRTAGRKVRHPELALATVDHNIPTDPRKDMKDIASFIHQPDSRTQVLALENNIKEFGLTYYGMNDRRQGIVHVIGPEQGFTLPGTTLVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTILQRKSKNMRIRVNGKLPEGIASKDLILHIIGVIGTAGGTGSVIEFCGEAIEGLSMEARMSMCNMSIEAGARAGMIAPDATTFEYVKNRPLAPKGDDWEQAVAYWKTLRSDENAKYDIEVEINAADVLPTVTWGTSPQDVIPINGNIPDPAHVKDNVRAASIQRSLEYMGLKPNTSIVSYPIDKVFIGSCTNSRIEDLRLAAAVVKGRKVAANVKDAMIVPGSGLVKKMAEAEGLDQIFIEAGFDWREAGCSMCLGMNPDQLKPYERCASTSNRNFEGRQGAKGRTHLVSPAMAAAAAIKGHLCNVREFFGDVSNGSPSIITNKNYDPSHDVEGDIGLSVDDATDAVTDADGIATNVAGSVSSGSAGIPKFTVVEGIAAPLPMANVDTDKIIPKQFLKTIKRTGLGQFAFYEIRYDADGKEIPDFVLNREPYRHATVLVAHDNFGCGSSREHAPWALNDFGIRVIIAPSFADIFFNNCFKNGMLPIPTPIEQVNDMMKAAENQVKFSVDLVNQTITYGDKQVKFDVEPFRKHCLVNGLDDIGLTLQKETMIDAFEAAREENFPWMNIKRSRARLSPVKSNKQSSSRNDW
Protein: Scarecrow, isoform C (A8Y525)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSSHGLAYTTRIERKSYRELQINRDQYFVTAPNEEDLVMSLSPKDTLIHTAISQHHQVDTSTKLNTNETSTQNTVSTAAAAAVAHHHHNLSSIHHLQNLHSQHQSTLFNSNHSTPFSVTDILSPIEESYRKLELNGNPPSPFRSNSSSSSINSPGTLTTSTMANPYAMGTLYHSPGVQTYCGPTDNLSLAGHYTDMRNSASWYGSTANDPRFAISRLMSSSASGTMSHMGNMSGLAACSVSDSKPLQFPLAQRRKRRVLFTQAQVYELERRFKQQRYLSAPEREHLASLIHLTPTQPASSPRRVAVPVLVKDGKPCSGNNSSSQSQQHGTNSTSAGNNTGSANNGNANSGIVSVTANVSGGLNLITGDAPNSHSPDTSSSLLASYGTVGGSNVAMLQQPCNNTLMSNSLAMAYRNQNNFISNGHQQQCGGYLPLQGRAW
Protein: Innexin inx6 (Innexin-6) (Gap junction protein prp6) (Pas-related protein 6) (Q9VR82)
Organism: Drosophila melanogaster (Fruit fly)
Function: Structural components of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
Sequence:
MYAAVKPLSNYLRLKTVRIYDPIFTLHSKCTIVILLTCTFLLSAKQYFGEPILCLSSERQADYVQSYCWTMGTYILPAEVDRDGGSSWEYALYAPTSTAAETFNVSSLRALVAQNEQYARFISIAEGVGPETRGVTKRMYLRYYQWVFMILLFQSLLFYFPSFLWKVWEGQRMEQLCCEVGDALIVEATYRTRLQMLTRYFRAQFAPIHWCYSIKYAFCELLNVFISILNFWLMDVVFNGFWYKYIHALAAIPVYDWNLWNLMTSRVFPKVAKCEMFVYGPSGTPNIMDILCVLPLNILNEKIFAVLYVWFLFIALLAIMNILYRLLVICCPELRLQLLRTHLNGMPKSHVREVLASAGYGDWFVLMCVSINVNPTLFRELLEQLYAKLNQARCTEPVFAEQPCQQVPQLAQVPQLFSHAKLDRCPSRNCSLLIDPTADRHSICTESSHRVTAMPTAPTLNLMAPNDEIISMDRFFHESHA
Protein: Beta-lactamase (EC 3.5.2.6) (Cephalosporinase) (P05193)
Organism: Citrobacter freundii
Function: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- HTH-type transcriptional activator AmpR
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- Beta-hexosaminidase
- Anhydromuropeptide permease
Sequence:
MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQWRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGALAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPARVEAAWRILEKLQ
Protein: Pcbp2 protein (Poly(rC) binding protein 2) (Q4V8F6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLETLSQSPPKGVTIPYRPKPSSSPVIFAGGQAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
Protein: APC membrane recruitment protein 2 (Amer2) (Protein FAM123A) (Q8N7J2)
Organism: Homo sapiens (Human)
Function: Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22128170}; Peripheral membrane protein {ECO:0000269|PubMed:22128170}. Note=Translocates to the cell membrane following binding to PtdIns(4,5)P2.
Interaction partners:
Sequence:
METSRSRGGGGAVSERGGAGASVGVCRRKAEAGAGTGTLAADMDLHCDCAAETPAAEPPSGKINKAAFKLFKKRKSGGTMPSIFGVKNKGDGKSSGPTGLVRSRTHDGLAEVLVLESGRKEEPRGGGDSGGGGGGRPNPGPPRAAGPGGGSLASSSVAKSHSFFSLLKKNGRSENGKGEPVDASKAGGKQKRGLRGLFSGMRWHRKDKRAKAEAAEGRAPGGGLILPGSLTASLECVKEETPRAAREPEEPSQDAPRDPAGEPAGGEEVPAPADRAPARSCREAEGLAHPGDTGARGEDAAGHRRAEPGPGEVRTAEDASRTGAVPVKTVPLVDSEGGSGRAPAAPDPASVDPPSDPSADRICLMFSDVTSLKSFDSLTGCGDIIADQEEEAGPSCDKHVPGPGKPALSKKNPGVVAYQGGGEEMASPDEVDDTYLQEFWDMLSQTEEQGPEPQEGAAKVAAALETKVVPETPKDTRCVEAAKDASSVKRRRLNRIPIEPHPKEEPKHPEKEQQEGVPNSDEGYWDSTTPGPEEDSSSSGKKAGIPRDSYSGDALYDLYADPDGSPATLPGGKDNEETSSLSRLKPVSPGTITCPLRTPGSLLKDSKIPISIKHLTNLPSSHPVVHQQPSRSEMPRTKIPVSKVLVRRVSNRGLAGTTIRATACHDSAKKL
Protein: A-kinase anchor protein 7 isoforms alpha and beta (AKAP-7 isoforms alpha and beta) (A-kinase anchor protein 18 kDa) (AKAP 18) (Protein kinase A-anchoring protein 7 isoforms alpha/beta) (PRKA7 isoforms alpha/beta) (O43687)
Organism: Homo sapiens (Human)
Function: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium.
Subcellular location: [Isoform Alpha]: Lateral cell membrane; Lipid-anchor. Note=Targeted predominantly to the lateral membrane.; SUBCELLULAR LOCATION: [Isoform Beta]: Apical cell membrane; Lipid-anchor. Note=Targeted predominantly to the apical membrane.
Interaction partners:
Sequence:
MGQLCCFPFSRDEGKISELESSSSAVLQRYSKDIPSWSSGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK