wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein 4 (MAP-4) (P27816)
Organism: Homo sapiens (Human)
Function: Non-neuronal microtubule-associated protein. Promotes microtubule assembly.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:34782749}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:29180244}. Note=Recruitment to microtubule is inhibited by microtubules polyglutamylation. {ECO:0000269|PubMed:34782749}.
Interaction partners:
- MAP/microtubule affinity-regulating kinase 3
- Acidic leucine-rich nuclear phosphoprotein 32 family member A
- Stathmin
Sequence:
MADLSLADALTEPSPDIEGEIKRDFIATLEAEAFDDVVGETVGKTDYIPLLDVDEKTGNSESKKKPCSETSQIEDTPSSKPTLLANGGHGVEGSDTTGSPTEFLEEKMAYQEYPNSQNWPEDTNFCFQPEQVVDPIQTDPFKMYHDDDLADLVFPSSATADTSIFAGQNDPLKDSYGMSPCNTAVVPQGWSVEALNSPHSESFVSPEAVAEPPQPTAVPLELAKEIEMASEERPPAQALEIMMGLKTTDMAPSKETEMALAKDMALATKTEVALAKDMESPTKLDVTLAKDMQPSMESDMALVKDMELPTEKEVALVKDVRWPTETDVSSAKNVVLPTETEVAPAKDVTLLKETERASPIKMDLAPSKDMGPPKENKKETERASPIKMDLAPSKDMGPPKENKIVPAKDLVLLSEIEVAQANDIISSTEISSAEKVALSSETEVALARDMTLPPETNVILTKDKALPLEAEVAPVKDMAQLPETEIAPAKDVAPSTVKEVGLLKDMSPLSETEMALGKDVTPPPETEVVLIKNVCLPPEMEVALTEDQVPALKTEAPLAKDGVLTLANNVTPAKDVPPLSETEATPVPIKDMEIAQTQKGISEDSHLESLQDVGQSAAPTFMISPETVTGTGKKCSLPAEEDSVLEKLGERKPCNSQPSELSSETSGIARPEEGRPVVSGTGNDITTPPNKELPPSPEKKTKPLATTQPAKTSTSKAKTQPTSLPKQPAPTTIGGLNKKPMSLASGLVPAAPPKRPAVASARPSILPSKDVKPKPIADAKAPEKRASPSKPASAPASRSGSKSTQTVAKTTTAAAVASTGPSSRSPSTLLPKKPTAIKTEGKPAEVKKMTAKSVPADLSRPKSTSTSSMKKTTTLSGTAPAAGVVPSRVKATPMPSRPSTTPFIDKKPTSAKPSSTTPRLSRLATNTSAPDLKNVRSKVGSTENIKHQPGGGRAKVEKKTEAAATTRKPESNAVTKTAGPIASAQKQPAGKVQIVSKKVSYSHIQSKCGSKDNIKHVPGGGNVQIQNKKVDISKVSSKCGSKANIKHKPGGGDVKIESQKLNFKEKAQAKVGSLDNVGHLPAGGAVKTEGGGSEAPLCPGPPAGEEPAISEAAPEAGAPTSASGLNGHPTLSGGGDQREAQTLDSQIQETSI
Protein: CREB-regulated transcription coactivator, isoform A (CREB-regulated transcription coactivator, isoform C) (Q9VVJ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MANPRKFSEKIALQKQKQAEGTAEFERIMKEVYATKRDEPPANQKILDGLVGGQEVSQSSPGAGNGTGGGGSGSGSGASGGGASPDGLGGGGGSPTAYRESRGRSVGVGPMRRPSERKQDRSPYGSSSTQQTLDNGQLNPHLLGPPTAESLWRRSSSDSALHQSALVAGFNSDVNSMGANYQQQQHQQQQQPGQPRSHSPHHGINRTMSPQAQRRKSPLLQPHQLQLQQLQQQQQQMQHQHQLHQQLQMQQLQQHQQQHQQQQQQQNTPYNNAKFTNPVFRPLQDQVNFANTGSLPDLTALQNYGPQQQQQQSQQQPSQQQQQLQQTLSPVMSPHNHRRERDQSPSPFSPAGGGGGAGPGSPYQQQQHSPTGNTQQQQQQHQQPSNSPHLSFTNLATTQAAVTTFNPLPTLGPHNATDYRQPPNPPSPRSSPGLLSSVSATDLHSSAPASPIRQQQQAHQQQQQQQQAQQQQQQFDNSYNSLNTSFHNQFEIFSLGDSNSSPEQQGFANNFVALDFDDLSGGGGGGPSGGGGSNGGGLTNGYNKPEMLDFSELSGSPEASGNNNHMRRGVSNLNNNGLSNGVVGSTHNGSTNLNGAGNNNSSSGGGTAQDPLGITTSPVPSPLGCPSSPLPIPIPMSAQSSPQQQHHHHQQQQQQHHQQQHHQQQQLSLSLHHSPHHSPMHSPHHGNSPLSSSSPVSHNACSNSNVVMNHQQQQQQHHHQQHHHQGSSQSHTPTTANIPSIIFSDYSSNADYTREIFDSLDLDLGQMDVAGLQMLSDQNPIMIADPNIEDSFRRDLN
Protein: Kappa-casein (P06796)
Organism: Mus musculus (Mouse)
Function: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk.
Subcellular location: Secreted.
Interaction partners:
- Alpha-S1-casein
- Beta-casein
- Alpha-lactalbumin
- Alpha-S2-casein-like B
- Chymosin
- Alpha-S2-casein-like A
Sequence:
MMRNFIVVVNILALTLPFLAAEIQNPDSNCRGEKNDIVYDEQRVLYTPVRSVLNFNQYEPNYYHYRPSLPATASPYMYYPLVVRLLLLRSPAPISKWQSMPNFPQSAGVPYAIPNPSFLAMPTNENQDNTAIPTIDPITPIVSTPVPTMESIVNTVANPEASTVSINTPETTTVPVSSTAA
Protein: GH22615p (Toutatis, isoform B) (Q95T46)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPGVYPVYTPVAAGNFSAGLINQAPVQPAMPFANVVAMSPRAVTPTRTRTPTPTPAPTPPPPPPTPLLMQASPTATALHVNACQSPPQQQHAQLMTMPSPPAIGVGTATNQMSPPPINIHAIQEAKEKLKQEKKEKHATKKLMKELAVCKTLLGEMELHEDSWPFLLPVNTKQFPTYRKIIKTPMDLSTIKKKLQDLSYKTREDFCVDVRQIFDNCEMFNEDDSPVGKAGHGMRKFFESRWGELTDKHS
Protein: DNA repair protein REV1 (EC 2.7.7.-) (Reversionless protein 1) (P12689)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis.
Subcellular location: Nucleus. Mitochondrion.
Interaction partners:
- DNA polymerase zeta catalytic subunit
- Proliferating cell nuclear antigen
- DNA polymerase eta
- DNA polymerase zeta processivity subunit
- DNA repair protein RAD5
- Postreplication repair E3 ubiquitin-protein ligase RAD18
- Ubiquitin-conjugating enzyme E2 13
- Ubiquitin-conjugating enzyme variant MMS2
- DNA repair protein RAD51
- Ubiquitin-conjugating enzyme E2 2
Sequence:
MGEHGGLVDLLDSDLEYSINRETPDKNNCLSQQSVNDSHLTAKTGGLNARSFLSTLSDDSLIEYVNQLSQTNKNNSNPTAGTLRFTTKNISCDELHADLGGGEDSPIARSVIEIQESDSNGDDVKKNTVYTREAYFHEKAHGQTLQDQILKDQYKDQISSQSSKIFKNCVIYINGYTKPGRLQLHEMIVLHGGKFLHYLSSKKTVTHIVASNLPLKKRIEFANYKVVSPDWIVDSVKEARLLPWQNYSLTSKLDEQQKKLDNCKTVNSIPLPSETSLHKGSKCVGSALLPVEQQSPVNLNNLEAKRIVACDDPDFLTSYFAHSRLHHLSAWKANLKDKFLNENIHKYTKITDKDTYIIFHIDFDCFFATVAYLCRSSSFSACDFKRDPIVVCHGTKNSDIASCNYVARSYGIKNGMWVSQAEKMLPNGIKLISLPYTFEQFQLKSEAFYSTLKRLNIFNLILPISIDEAVCVRIIPDNIHNTNTLNARLCEEIRQEIFQGTNGCTVSIGCSDSLVLARLALKMAKPNGYNITFKSNLSEEFWSSFKLDDLPGVGHSTLSRLESTFDSPHSLNDLRKRYTLDALKASVGSKLGMKIHLALQGQDDEESLKILYDPKEVLQRKSLSIDINWGIRFKNITQVDLFIERGCQYLLEKLNEINKTTSQITLKLMRRCKDAPIEPPKYMGMGRCDSFSRSSRLGIPTNEFGIIATEMKSLYRTLGCPPMELRGLALQFNKLVDVGPDNNQLKLRLPFKTIVTNRAFEALPEDVKNDINNEFEKRNYKRKESGLTSNSLSSKKKGFAISRLEVNDLPSTMEEQFMNELPTQIRAEVRHDLRIQKKIQQTKLGNLQEKIKRREESLQNEKNHFMGQNSIFQPIKFQNLTRFKKICQLVKQWVAETLGDGGPHEKDVKLFVKYLIKLCDSNRVHLVLHLSNLISRELNLCAFLNQDHSGFQTWERILLNDIIPLLNRNKHTYQTVRKLDMDFEV
Protein: Dynein regulatory complex subunit 7 (Coiled-coil domain-containing protein 135) (Coiled-coil domain-containing protein lobo homolog) (Q8IY82)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Involved in the regulation of flagellar motility (By similarity). Essential for male fertility, sperm head morphogenesis and sperm flagellum formation (By similarity).
Subcellular location: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A8JAM0}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A8JAM0}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8JAM0}. Note=Associated with the outer doublet microtubules (OD). {ECO:0000250|UniProtKB:A8JAM0}.
Interaction partners:
- Dynein regulatory complex protein 1
- Dynein regulatory complex subunit 4
- Dynein regulatory complex subunit 2
- Dynein regulatory complex subunit 5
- Coiled-coil domain-containing protein 40
- Dynein regulatory complex protein 9
- Dynein regulatory complex subunit 3
- Outer dynein arm-docking complex subunit 4
Sequence:
MEVLREKVEEEEEAEREEAAEWAEWARMEKMMRPVEVRKEEITLKQETLRDLEKKLSEIQITVSAELPAFTKDTIDISKLPISYKTNTPKEEHLLQVADNFSRQYSHLCPDRVPLFLHPLNECEVPKFVSTTLRPTLMPYPELYNWDSCAQFVSDFLTMVPLPDPLKPPSHLYSSTTVLKYQKGNCFDFSTLLCSMLIGSGYDAYCVNGYGSLDLCHMDLTREVCPLTVKPKETIKKEEKVLPKKYTIKPPRDLCSRFEQEQEVKKQQEIRAQEKKRLREEEERLMEAEKAKPDALHGLRVHSWVLVLSGKREVPENFFIDPFTGHSYSTQDEHFLGIESLWNHKNYWINMQDCWNCCKDLIFDLGDPVRWEYMLLGTDKSQLSLTEEDDSGINDEDDVENLGKEDEDKSFDMPHSWVEQIEISPEAFETRCPNGKKVIQYKRAKLEKWAPYLNSNGLVSRLTTYEDLQCTNILEIKEWYQNREDMLELKHINKTTDLKTDYFKPGHPQALRVHSYKSMQPEMDRVIEFYETARVDGLMKREETPRTMTEYYQGRPDFLSYRHASFGPRVKKLTLSSAESNPRPIVKITERFFRNPAKPAEEDVAERVFLVAEERIQLRYHCREDHITASKREFLRRTEVDSKGNKIIMTPDMCISFEVEPMEHTKKLLYQYEAMMHLKREEKLSRHQVWESELEVLEILKLREEEEAAHTLTISIYDTKRNEKSKEYREAMERMMHEEHLRQVETQLDYLAPFLAQLPPGEKLTCWQAVRLKDECLSDFKQRLINKANLIQARFEKETQELQKKQQWYQENQVTLTPEDEDLYLSYCSQAMFRIRILEQRLNRHKELAPLKYLALEEKLYKDPRLGELQKIFA
Protein: Serine/threonine-protein kinase ppk25 (EC 2.7.11.1) (O59697)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta
- 5'-AMP-activated protein kinase subunit gamma
- Autophagy-related protein 17
Sequence:
MKPNTTNLRNECWDTFSIPKRSQNIKINQSTKHQRSISDFVGTAGPGRQVGNWIIKKTIGAGSMGKVKLVVNILTGEKAALKMIPFTPNNTSQTVRVQREALLGRLLRHPNICRVIDCIRTPACTYILFEYVPGGQLLEYILARGKLDEDLARSFAMQLINALVYLHKNFIVHRDLKIENVLLTQDSRQVKLIDFGLSNFYSKDDLLRTYCGSLYFAAPELLDAKPYIGPEVDVWSLGVVIYVMVCGRVPFDDVSVPMLHSKIKSGKLEFPSYISEDCCSLIAAMLNVNPRKRCSLEQAAKFPWLKKNSFCLYLPIPLTSIPSTPSIRSHVFKPPFNLKVLQLLHEHGLASIPELKHELYMAYIERKTTSLVCLYLLGVESLAPALRIPTALPPVYSRHQRHHSEILGAMDLTEKITAMQCPP
Protein: Profilin-2 (Profilin II) (Q9JJV2)
Organism: Mus musculus (Mouse)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Toll-like receptor 12
- Toll-like receptor 11
- Vasodilator-stimulated phosphoprotein
- Actin, cytoplasmic 1
- Protein diaphanous homolog 1
- Protein diaphanous homolog 2
- Actin, cytoplasmic 2
- Cofilin-2
- Profilin-1
- Profilin-4
Sequence:
MAGWQSYVDNLMCDGCCQEAAIVGYCDAKYVWAATAGGVFQSITPVEIDMIVGKDREGFFTNGLTLGAKKCSVIRDSLYVDGDCTMDIRTKSQGGEPTYNVAVGRAGRVLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF
Protein: Endo-beta-1,4-glucanase A (Endoglucanase A) (EC 3.2.1.4) (Carboxymethylcellulase A) (Cellulase A) (Q5BDU5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- 1,4-beta-D-glucan cellobiohydrolase C
- 1,4-beta-D-glucan cellobiohydrolase B
- Endo-beta-1,4-glucanase celB
- Glucanase
- Extracellular endoglucanase, putative
- Endo-beta-1,4-glucanase B
- beta-glucosidase
- Probable beta-glucosidase A
- Endo-1,4-beta-xylanase B
Sequence:
MRSLVLLSSVLALVAPSKGAFTWLGTNEAGAEFGEGSYPGELGTEYIWPDLGTIGTLRNEGMNIFRVAFSMERLVPDSLAGPVADEYFQDLVETVNGITALGAYAVLDPHNYGRYYGNIITSTDDFAAFWTILATEFASNELVIFDTNNEYHTMDQSLVLNLNQAAIDAIRASGATSQYIFAEGNSWTGAWTWVDVNDNMKALTDPQDKLIYEMHQYLDSDGSGTNTACVSSTIGSERVTAATNWLRENGKLGVLGEFAGANNQVCKDAVADLLEYLEENSDVWLGALWWAAGPWWGDYMFNMEPTSGIAYQEYSEILQPYFVGSQ
Protein: Accessory gland protein Acp29AB (O46197)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for physiological and behavioral changes in mated female flies.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Accessory gland protein Acp62F
- Accessory gland protein Acp36DE
- Accessory gland-specific peptide 26Aa
- Uncharacterized protein, isoform A
- Accessory gland protein Acp76A
- Accessory gland-specific peptide 26Ab
- Accessory gland protein Acp53Ea
- ACP53C14B
- Accessory gland-specific peptide 70A
- Serpin 28F
Sequence:
MYASNLLYLLALWNLWDLSGGQQDIPNGKATLPSPQTPQNTIDQIGINQNYWFTYNALKQNETLAIIDTMEMRIASSLLEFKAQMEIQLQPLKIIMRHHASNIKASNNIKMRRFEKVGSRHFHIEKNLMQTWFEAYVTCRKMNGHLANIQDEMELDGILALAPNNSYWIDISKLVENGGTFVSTLTGREPFFVKWKSNQDTKKKNQCVYIYAKEMSYDECFEKKSFVCQADQWA
Protein: Beta-secretase 1 (EC 3.4.23.46) (Aspartyl protease 2) (ASP2) (Asp 2) (Beta-site amyloid precursor protein cleaving enzyme 1) (Beta-site APP cleaving enzyme 1) (Memapsin-2) (Membrane-associated aspartic protease 2) (P56819)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (By similarity). Cleaves CHL1 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P56817}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P56817}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P56817}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P56817}. Endosome {ECO:0000250|UniProtKB:P56817}. Cell surface {ECO:0000250|UniProtKB:P56817}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P56817}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P56817}. Membrane raft {ECO:0000250|UniProtKB:P56818}. Lysosome {ECO:0000250|UniProtKB:P56817}. Late endosome {ECO:0000250|UniProtKB:P56817}. Early endosome {ECO:0000250|UniProtKB:P56817}. Recycling endosome {ECO:0000250|UniProtKB:P56817}. Cell projection, axon {ECO:0000250|UniProtKB:P56818}. Cell projection, dendrite {ECO:0000250|UniProtKB:P56818}. Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine which blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity). {ECO:0000250|UniProtKB:P56817, ECO:0000250|UniProtKB:P56818}.
Interaction partners:
- Amyloid-beta precursor protein
- Reticulon-3
- Reticulon-4
- Presenilin-1
- Reticulon-2
- Beta-secretase 2
- Golgi associated, gamma adaptin ear containing, ARF binding protein 1
- Disintegrin and metalloproteinase domain-containing protein 10
- Nicastrin
- Cyclin-dependent kinase 5
Sequence:
MAPALRWLLLWVGSGMLPAQGTHLGIRLPLRSGLAGPPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKSVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHIPNIFSLQLCGAGFPLNQTEALASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAVSQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTADMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRHQHDDFADDISLLK
Protein: Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon) (Q16537)
Organism: Homo sapiens (Human)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Cytoplasm.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Shugoshin 1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Apoptosis regulator Bcl-2
- Meiotic recombination protein REC8 homolog
- Protein phosphatase 1 regulatory subunit 1A
Sequence:
MSSAPTTPPSVDKVDGFSRKSVRKARQKRSQSSSQFRSQGKPIELTPLPLLKDVPSSEQPELFLKKLQQCCVIFDFMDTLSDLKMKEYKRSTLNELVDYITISRGCLTEQTYPEVVRMVSCNIFRTLPPSDSNEFDPEEDEPTLEASWPHLQLVYEFFIRFLESQEFQPSIAKKYIDQKFVLQLLELFDSEDPRERDYLKTVLHRIYGKFLGLRAFIRKQINNIFLRFVYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLVKVLIPLHTVRSLSLFHAQLAYCIVQFLEKDPSLTEPVIRGLMKFWPKTCSQKEVMFLGELEEILDVIEPSQFVKIQEPLFKQIAKCVSSPHFQVAERALYYWNNEYIMSLIEENSNVILPIMFSSLYRISKEHWNPAIVALVYNVLKAFMEMNSTMFDELTATYKSDRQREKKKEKEREELWKKLEDLELKRGLRRDGIIPT
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FIK0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MQFSKIITALSIAGAVIAAPANVHHEHKNKRDVVTKTVHNQVTVTAGAPPAVNTGLLKEDAVLGSSNEASAPVASSQAPAQQAAAPQSEAASPAPASSSQAAASSSAPKSSGSSSSFSGSAKGITYSPYNADGSCRSASDVASDLAKLSSYSMIRLYGVDCNQVENVFKAKAAGQKLFLGIFFVDQIQAGVDTMKAAVESYGSWDDVYTVSIGNELVNGGQATPDQVGQYVATGRSALKAAGYSGPVVSVDTFIAVINNPALCQYSDYMAVNAHAYFDQNTVAEDAGTWLVQQIQRVWTACDGKKDVLITESGWPSQGETLGVAVASKQNQEAAIASIEKACGDDTILFTAFNDYWKADGPYNCEKYWGIY
Protein: Probable 3-hydroxyisobutyrate dehydrogenase-like 1, mitochondrial (HIBADH-like) (EC 1.1.1.31) (Q9SZE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Probable 3-hydroxyisobutyryl-CoA hydrolase 3
- 3-hydroxyisobutyryl-CoA hydrolase-like protein 1, mitochondrial
- 3-hydroxyisobutyryl-CoA hydrolase-like protein 4, mitochondrial
- 3-hydroxyisobutyryl-CoA hydrolase-like protein 3, mitochondrial
- 3-hydroxyisobutyryl-CoA hydrolase-like protein 5
Sequence:
MPLLLRRFPSPSVVSSFFLRRSMASSTISSDIITPSNTKIGWIGTGVMGRSMCGHLIKAGYTVTVFNRTISKAQTLIDMGANVADSPNSVAEQSDVVFTIVGYPSDVRHVLLDPKSGALSGLRQGGVLVDMTTSEPSLAEEIAKAASFKNCFSIDAPVSGGDLGAKNGKLSIFAGGDETTVKRLDPLFSLMGKVNFMGTSGKGQFAKLANQITIASTMLGLVEGLIYAHKAGLDVKKFLEAISTGAAGSKSIDLYGDRILKRDFDPGFYVNHFVKDLGICLNECQRMGLALPGLALAQQLYLSLKAHGEGDLGTQALLLALERLNNVSVQSSDS
Protein: Alternative protein CHTF8 (L0R4W3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKEPRIFPRERPTPWTRAPLPPRGRLDGSLGPQGGPVLNTGHPLGVNSDPFLMAAGSLGGNLTPFPRNPSPFPASSGSLASNPAPFPAGARDPSMASFPRGMNPTGTGAVSFPRPGGLLGPGPGPGPTLNPRTGALPGPGPLSNPRLGGLPGPGPMSNPRAGGLLGAGPDPRGGGPMGPGSGPNLRAGVLLTSGNGPPNPRPVGLGPGPNPNLRSGFLGTNPAPRSGVFPGPGLGPNPRPSGLGPGPNLDARAGGLLGTGSGLNLRMAGPQGLDLAPILRAAGLLGANSASFSQASGNMGTSPSSMARVPGPMGPNSGPSSRGIGLPGPNPSPMSRAPGPIGPNSAHFSRPVGPMGVNANPFPRGAGSSAFSQSSGTLASNPATFQRSAGLQGSNPTIFPRASGPLGPNPANFPRATGLQGPSPTTFPRSTGPLGPGQVTFPRPAAGHLGPSPAGPVGINPAPFTRPTGTLGLNPASFPRMNGPAGKSFVPFPRVGSLPGTNPAAFPRPGGPMAAMYPNGMLPP
Protein: Protein phosphatase 1 regulatory subunit 1B (DARPP-32) (Dopamine- and cAMP-regulated neuronal phosphoprotein) (Q9UD71)
Organism: Homo sapiens (Human)
Function: Inhibitor of protein-phosphatase 1.
Subcellular location: Cytoplasm.
Interaction partners:
- Cyclin-dependent kinase 5
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
Sequence:
MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRPNPCAYTPPSLKAVQRIAESHLQSISNLNENQASEEEDELGELRELGYPREEDEEEEEDDEEEEEEEDSQAEVLKVIRQSAGQKTTCGQGLEGPWERPPPLDESERDGGSEDQVEDPALSEPGEEPQRPSPSEPGT
Protein: Photosystem II CP43 reaction center protein (PSII 43 kDa protein) (Protein CP-43) (P0C367)
Organism: Oryza sativa subsp. japonica (Rice)
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01496}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01496}.
Interaction partners:
- Cytochrome b559 subunit alpha
- Cytochrome b559 subunit beta
- Photosystem II D2 protein
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Photosystem II reaction center protein H
- Photosystem II reaction center protein K
- Photosystem II reaction center protein J
- Photosystem II reaction center protein L
- Photosystem II reaction center protein Z
Sequence:
MKILYSLRRFYHVETLFNGTFVLAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVLDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGIGAFLLVLKALYFGGIYDTWAPGGGDVRKITNLTLSPGVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGFICVFGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLATSHFVLGFFFFVGHLWHAGRARAAAAGFEKGIDRDLEPVLYMTPLN
Protein: polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Polynucleotide phosphorylase 1) (B1H2A4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LESSIKSDQIITAINGVKDKNFMLHYEFPPYATNETGKVTGVNRRELGHGALAEKALCPVIPKDFPFTIRVTSEVLESNGSSSMASACGGSLALMDAGVPISSAVAGVAVGLVTKSNPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGVPVKIIMEAIQQATVAKREILQTMSKTISKPRASRKENGPVVETVKVPLSKRAKFIGPGGYHLKKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNSQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVLKTLNDRSSIVMGEPISQSSSNSSP
Protein: Putative transport protein Rv1101c (P9WFM3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized membrane protein Rv3835
Sequence:
MNTEFTLTQKRALAILTLIALLFGAYFLRNYFVLIVVAAVGAYLFTPLFKWFTKRFNTGLSAACTLLSALAAVVVPVGALVGLAIVQIARMVDSVADWVRTTDLSTLGDKILQFVNGLFDRVPFLHITVTADALRKAMISVAQNVGEWLLHFLRDAAGSLAGVITSAIIFVYVFVALLVNREKLRTLIGQLNPLGEDVTDLYLQKMGSMVRGTVNGQFVIAACQGVAGAASIYIAGFHHGFFIFAIVLTALSIIPLGGGIVTIPFGIGMIFYGNIAGGIFVLLWHLLVVTNIDNVLRPILVPRDARLNSALMLLSVFAGITMFGPWGIIIGPVLMILIVTTIDVYLAVYKGVELEQFEAPPVRRRWLPRRGPATSRNAPPPSTAE
Protein: Staufen (Q6JPI2)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MDVTMSQAPKSPAAPLPKIQILNKNQHSPLPQPLSIPSTASPLPSENAGRPLQNSALPSPSVTSSGPTAVSSNMANPKEKTPMCLVNELARFNKIQPVYKLLSEQGPAHSKVIPLGRWQDYSLLERVGEERPRQMFTVQLTLGDQYWEAEGTSIKKAQHAAAAKALEGTKYPKPTVRPVRDSITPTVELNALCMKLGRKPIYKPLDPYTGIRSAYNYNMRGGGYPPRYFYPFPVAPILYQVELSVGGQQFHGKGRTRQAAKHDAAARALKSLHHEPLPDKPALNGKAADEENLNKSEISQVFEIALKRNMSVNFEVTKETGPPHMKSFLTKVIVGEFLGEGEGKSKKISKKNAAIAVLEELRKLPPLPTVEKMRPKIKKKTKSIVKLPTSPEYGQGMNPISRLAQIQQAKKGKEPEYILITERGLPRRREFVMQVKVGNHAAEGSGTNKKVAKRNAAENMLEILGFKVPPPPPKPALKTEEKLPVKKPGDGRKVTFYEPGSGEDGANHNKDDEFRMPYHSHQQLPAGILPMVPEVAQAVGVNQGLHTKEFNRVAPNPAKATVTAMIARELLYAGISPTADTILKNNNAAGHVLRGPFTRPSEQLNYLSRVQGLEVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELDQQNPEMPRTGNGPMSVCVKPEMESDPLLKPANSNTLGQTLDSTA
Protein: THP3 homolog C2A9.11c (Q1MTP1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for transcription elongation. May also be involved in pre-mRNA splicing (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein CSN12 homolog
- Protein scd2/ral3
- 26S proteasome complex subunit rpn15
- Cytochrome c1, heme protein, mitochondrial
- PCI domain-containing protein C1105.07c
- UPF0400 protein C337.03
- Enhancer of rudimentary homolog 1
Sequence:
MKKEHHSPWPDSLKEFIGRCIQDAEENSQPELEDEVKLLISRQYEMGNIWNVDWSSMNLESLRKLTNAQNTIIEDKKRKVEKPVSGNQFSLLSEEDEVDKKEKRRRRFENGSRSQNNAKSEELKVNPENGAIIGRSTELEKRYLRLTSAPDPDTVRPLPVLKQTLELLKKKWKEEKNYAYICDQFKSLRQDLTVQRIQNEFSVLVYEIHARIALEKGDVGEYNQCQTQLFHLYSFGIPGNTKEFLAYRILYMLFTKNRSEMNSLLANLKEEDKTNAAVTHALEVRSAMATGDYYKFFHLYLVAPNMGGYLMDLFIERERVQAMIMMCKAYRPSLTMEFLANTLAFEEMEDCVNFFRSCNAVYDSKDPNRILMKESTDRFEKCMKKHAVVDIKGQI