wanglab/gogpt-training-data huggingface dataset:
Protein: ADP-ribose glycohydrolase MACROD1 (MACRO domain-containing protein 1) (O-acetyl-ADP-ribose deacetylase MACROD1) (EC 3.1.1.106) (Protein LRP16) ([Protein ADP-ribosylaspartate] hydrolase MACROD1) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD1) (EC 3.2.2.-) (Q9BQ69)
Organism: Homo sapiens (Human)
Function: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Plays a role in estrogen signaling. Binds to androgen receptor (AR) and amplifies the transactivation function of AR in response to androgen. May play an important role in carcinogenesis and/or progression of hormone-dependent cancers by feed-forward mechanism that activates ESR1 transactivation. Could be an ESR1 coactivator, providing a positive feedback regulatory loop for ESR1 signal transduction. Could be involved in invasive growth by down-regulating CDH1 in endometrial cancer cells. Enhances ESR1-mediated transcription activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:23474712}. Note=Recruited to DNA lesions, probably via mono-APD-ribosylated proteins. {ECO:0000269|PubMed:23474712}.
Interaction partners:
- Poly [ADP-ribose] polymerase 1
- ADP-ribose glycohydrolase OARD1
- ADP-ribosylhydrolase ARH3
- Poly
- Estrogen receptor
- Core histone macro-H2A.2
- Protein UXT
Sequence:
MSLQSRLSGRLAQLRAAGQLLVPPRPRPGHLAGATRTRSSTCGPPAFLGVFGRRARTSAGVGAWGAAAVGRTAGVRTWAPLAMAAKVDLSTSTDWKEAKSFLKGLSDKQREEHYFCKDFVRLKKIPTWKEMAKGVAVKVEEPRYKKDKQLNEKISLLRSDITKLEVDAIVNAANSSLLGGGGVDGCIHRAAGPLLTDECRTLQSCKTGKAKITGGYRLPAKYVIHTVGPIAYGEPSASQAAELRSCYLSSLDLLLEHRLRSVAFPCISTGVFGYPCEAAAEIVLATLREWLEQHKDKVDRLIICVFLEKDEDIYRSRLPHYFPVA
Protein: DEAD-box ATP-dependent RNA helicase 3B, chloroplastic (ZmRH3B) (EC 3.6.4.13) (A0A1D6LAB7)
Organism: Zea mays (Maize)
Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:22576849}.
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- Ribosome biogenesis protein WDR12 homolog
- Auxin-responsive protein
- Pescadillo homolog
Sequence:
MASLTLPALALALSNPGAVRLRAAAFRCWALRRRGWAAAGALASPNSVLSEHAFKRLQLGSDDEDGEGPYGSDADEGFEAGEGDNEELAIARLGLPDELVATLEKRGITHLFPIQRAVLIPALEGRDLIARAKTGTGKTLAFGIPMIKQLIEQDDGRITRRGRTPRVLVLAPTRELAKQVEKEIKESAPKLGTVCVYGGVSYNVQQNALSRGVDVVVGTPGRIIDLINGGSLQLGEVQYLVLDEADQMLAVGFEEDVETILQQLPAGRQSMLFSATMPSWVKKLSRRYLNNPLTIDLVGDQDEKLAEGIKLYAIPLTTTSKRTVLSDLITVYAKGGKTIVFTRTKKDADEVSLALTNSIASEALHGDISQHQRERTLNGFRQGKFTVLVATDVAARGLDIPNVDLIIHYELPNDPETFVHRSGRTGRAGKAGTAILMFTSSQKRTVKSLERDVGCNFEFISPPSIEEVLESSAEHVIATLRGVHPESTKYFLGAAEKLTEELGPHALASALAHLSGFSQPPSSRSLISHEQGWVTLQLTREQGFGRGFFSPRSVTGFLSDVCSAAADEVGKIYLTADENVQGAVFDLPEEIAKDLLTMELPPGNTLTKISKLPALQDDGPATDSYGRFSNDRGSRNNRRSRGGGASRGRGGWDTDGEDRFRRGGRSLRSDNDSWSDDDWSGGGRKSNRSSSFGSRSSSYSSRGSPSFGGRSSSFGGRESNRSFSGACFNCGESGHRATDCPNK
Protein: Transcription factor Sp2 (Q9D2H6)
Organism: Mus musculus (Mouse)
Function: Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSDPQMSMAATAAVSPSDYLQPAAATTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPCKNSFSILSSKGNILQIQGSQLSTSYPGGQFVFAIQNPTLINKGSRSNASIQYQVPQIQGNSSQTIQVQPSLTNQIQVIPGTNQAITTPSTSGHKPVPIKPAPVQKSSTTTTPVQSGANVVKLTGGGSNMTLTLPLNNLVNTSDIGGPAQLLTESPPTPLSKTNKKARKKSLPVSQPSVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQQALRVVQAASATLPTVPQKPSQNFQIQTTEPTPTQVYIRTPSGEVQTVLVQDSPPATAATTSTVTCNSPALRAPHLSGTSKKHSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPTQIQLQMEQALAGEAQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHVCHIPDCGKTFRKTSLLRAHVRLHTGERPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFECAQCQKRFMRSDHLTKHYKTHLGTKGL
Protein: NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (Q1ZXW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000471}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
TYIAVPAEILGIILPLLLGVAFLVLAERKVMAFVQRRKGPDVVGSFGLLQPLADGSKLILKEPISPSSANFFLFRMAPVATFMLSLVARAVVPFDYGMVLSDPNIGLLYLFAISSLGVYGIIIAGRSSNSKYAFLGALRSAAQMVSYEVSIGLILITVLICVGPRNSSEIVMAQKQIWSGIPLFPVLVMFLISRLAETNRAPFDLPEAEAESVAGYNVEYSSMGSALFFLGEYANMILMSGPCTLFFPGGWPPILDLPIFKKIPGSIWFSIKVLLFLFLYIWVRAAFPRYRYDQLMGLGRKVFLPLSLARVVPVSGLLVTFQWLP
Protein: Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (AtB beta) (PP2A, subunit B, beta isoform) (Q39247)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment.
Interaction partners:
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Serine/threonine-protein phosphatase PP2A-4 catalytic subunit
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' 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 65 kDa regulatory subunit A gamma isoform
Sequence:
MNGGDDAATSGPPPSLEWRFSQVFGERTAGEEVQEVDIISAIEFDKSGDHLATGDRGGRVVLFERTDTKDHGGSRKDLEQTDYPVRHPEFRYKTEFQSHEPEFDYLKSLEIEEKINKIRWCQPANGALFLLSTNDKTIKYWKVQEKKIKKISEMNIDPSESSNIPPQLVTNGLPADKGHDYLSKDFSFPPGGIPSLRLPVVVTSQETNLVARCRRVYAHAHDYHINSISNSSDGETFISADDLRVNLWNLEISNQSFNIVDVKPTNMEDLTEVITSAEFHPIHCNMLAYSSSKGSIRLIDMRQSALCDSHTKLFEEPEAPGSRSFFTEIIASISDIKFSKDGRYILSRDYMTLKLWDINMDSGPVASYQVHEHLRPRLCDLYENDSIFDKFECCLSGDGLRVATGSYSNLFRVFGASQGSTEAATLEASKNPMRRQIQTPARPSRSIGSMTRVVRRGSESPGTEANGNAYDFTTKLLHMAWHPTENSIACAAANSLYMYYA
Protein: GTP-binding protein Di-Ras3 (Distinct subgroup of the Ras family member 3) (Rho-related GTP-binding protein RhoI) (O95661)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
Sequence:
MGNASFGSKEQKLLKRLRLLPALLILRAFKPHRKIRDYRVVVVGTAGVGKSTLLHKWASGNFRHEYLPTIENTYCQLLGCSHGVLSLHITDSKSGDGNRALQRHVIARGHAFVLVYSVTKKETLEELKAFYELICKIKGNNLHKFPIVLVGNKSDDTHREVALNDGATCAMEWNCAFMEISAKTDVNVQELFHMLLNYKKKPTTGLQEPEKKSQMPNTTEKLLDKCIIM
Protein: Neuropeptides B/W receptor type 1 (G-protein coupled receptor 7) (P49681)
Organism: Mus musculus (Mouse)
Function: Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Neuropeptide W
- Neuropeptide B
- Pro-neuropeptide Y
Sequence:
MHNLTLFESGGDNVSCGGSSLGCPNGSSLAPLPLPQPLAVAVPVVYGVICAVGLAGNSAVLYVLLRTPRMKTVTNVFILNLAIADELFTLVLPINIADFLLRRWPFGEVMCKLIVAVDQYNTFSSLYFLAVMSADRYLVVLATAESRRVSGRTYGAARAVSLAVWALVTLVVLPFAVFARLDEEQGRRQCVLVFPQPEAFWWRASRLYTLVLGFAIPVTTICALYTTLLCRLRAIQLDSHAKALDRAKKRVTLLVAAILAVCLLCWTPYHLSTIVALTTDLPQTPLVIGISYFITSLSYANSCLNPFLYAFLDDSFRRSLRQLVSCRSA
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 3 (BLOC-1 subunit 3) (Q6QNY0)
Organism: Homo sapiens (Human)
Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- SNARE-associated protein Snapin
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Dysbindin
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- BLOC-2 complex member HPS3
- BLOC-2 complex member HPS6
- BLOC-2 complex member HPS5
Sequence:
MASQGRRRRPLRRPETVVPGEATETDSERSASSSEEEELYLGPSGPTRGRPTGLRVAGEAAETDSEPEPEPEPTAAPRDLPPLVVQRESAEEAWGTEEAPAPAPARSLLQLRLAESQARLDHDVAAAVSGVYRRAGRDVAALASRLAAAQAAGLAAAHSVRLARGDLCALAERLDIVAGCRLLPDIRGVPGTEPEKDPGPRA
Protein: Branched-chain amino acid ABC transporter, permease protein (Q5LNC0)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein, putative
- Branched-chain amino acid ABC transporter, ATP-binding protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, ATP-binding protein
Sequence:
MFYREAGDFKTSYQADSQTFPIKFDRYRYYVVLAVAFGIIPFIINDYWANALLIPFLIYAIAAIGLNILVGYCGQVSLGTGGFMAVGAYACYKLMTAFPEVSMFIHVILAGGITAAVGVLFGLPSLRIKGFYLAVATLAAQFFLVWLFNRVPWFYNYSASGQINAPERDTFGIIITGPNAPAWATYLFCLVFLTACALIARNLTRGTMGRTWMAIRDMDIAAEIIGVNPLKAKMTAFAVSSFFIGISGALFFALYLGAVEVGEAFGIQKSFLVLFMVIIGGLGSIFGSFAGAAFLVLLPVVLKVVGADMLGWPTDIVAHLQLVIVGGLIVVFLIMEPHGLAQLWRVAKEKLRLWPFPH
Protein: Cholinergic receptor, nicotinic, alpha polypeptide 10 (B2RX82)
Organism: Mus musculus (Mouse)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-5
- Acetylcholine receptor subunit alpha
- Neuronal acetylcholine receptor subunit alpha-9
Sequence:
MGTRSHHLGPGFLLLLFLPAECLGAEGRLAHKLFRDLFANYTSALRPVADTDQTLNVTLEVTLSQIIDMDERNQVLTLYLWIRQEWTDAYLHWDPKAYGDLDAIRIPSSLVWRPDIVLYNKADTQPPASASTNVVVRHDGAVRWDAPAITRSSCRVDVSAFPFDAQRCGLTFGSWTHGGHQLDVRPRGTSASLADFVENVEWRVLGMPARRRVLTYGCCSEPYPDVTFTLLLRRRAAAYVCNLLLPCVFISLLAPLAFHLPADSGEKVSLGVTVLLALTVFQLILAESMPPAESVPLIGKYYMATMTMVTFSTALTILIMNLHYCGPNAHPVPAWARVLLLGHLAKGLCVRERGEPCGQSKPLESAPSLQPPAGPPAGPCHEPRCLCHQEALLHHVASIAGTFRSHRAAQRRHEDWKRLARVMDRFFLGIFFCMALVMSLLVLVQAL
Protein: Glycogen phosphorylase 1 (GP1) (EC 2.4.1.1) (Q00766)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May provide energy to overcome environmental stresses.
Interaction partners:
- Glycogen debranching enzyme
- Phosphoglucomutase-1
- 1,4-alpha-glucan-branching enzyme
- 4-alpha-glucanotransferase
- UTP--glucose-1-phosphate uridylyltransferase 1
- Probable phosphoglucomutase-2
- UTP--glucose-1-phosphate uridylyltransferase 2
- alpha-amylase
- Glycogen [starch] synthase
- Nudix hydrolase domain-containing protein
Sequence:
MSTTIPLKHTARTTTGVVPPTEKKKGSKLFALKTDFLKNDEDSIQKDILDHVEYTLARTKYNFDSFSAYQGSAYSVRDRLIERWNETQQYYTERDPKRVYYLSMEFLMGRSLQNAIYNMNLKDEYHNALLELGFEMEDLYEEEKDAALGNGGLGRLAACFMDSLATLKYPAWGYGLRYNYGMFEQGIYDGYQTEVPDYWLVAGNPWEIERLDVQYTVRFYGQVTEKKSSDGSKFEWDHGELVQAIAYDTPVPGYHTTNTNNIRLWSSKPHKEFDLDAFNGGNYLSAVEAKQRSENITSVLYPNDNTYSGKELRLKQQYFFVAATLCDVIRRFKKSHQNWQDFPNKVAIQLNDTHPTIGVVELFRKLIDEEGLQWEEAWDIVTKTFAYTNHTILPEALEMWPVSLIEDLLPRHMQLIYGINHRFLIQVTQKWPGDIGKMRGLSIIQEGEEKRVRMAHLAIVGSHCVNGVAAMHSELVKHKVFPDFFCLWPEKFQNKTNGVTPRRWIEQANPGLSAIFTKWLGTDKWTTNLELVKGIKEHMDNPELIAEWKYVKQGNKQRLAEFILKHCGIHVNPNALFDVHIKRIHEYKRQLLNILSVIYRYLSIKKMSPKDRAQVVPRVVIFAGKAAPGYVMAKRHIKLINSVAEVINRDKEVDQYLKVVFIANYNVSIAQVIVPASDINQQISTAGTEASGTSNMKFTMNGSLIIGTLDGANVEIAEEVGQENMFIFGLRTSEVEAAREKMTNKEVNIDPRLQEVFLNIELGTFGPPDVFRPILDSLIFSDFYLSIQDFPLYLDSQASVDELWKDQSAWVKKSIINSASTYFFSSDRAMNEYAEQIWDIKPCEVETTLNRRY
Protein: Calponin-homology (CH) domain-containing protein (Q38CH8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEFPQVTCDDVNALVQMCSIPHETAITSLKQCSSSLFVLLYQRLFNCTIVGIESSPYTVEQKKWNVKCVLNELCAKCGMNVEGIDAEKIVQLNEEHISRLIALFLEIANRMSIHTGAGRGALPVGAGLTAPTPFPAAALRPKLAEVPRDPAEDGTWYPPAAATHVLPTHLMRPVHAAEGHMRAAVQAYLHHNESSYRGHHDSAQLGDAVDSAHEKHKDNHDSMRSGRKFYADVVEAEMSVSDVANSGDDDKATLLDEEDDGGSGGSFVNTEEKEIPTSQLVEVWSAQVIPPKRHIGMGDSPDLTELRGQLTAMDKCLRRGEQRRVRLRHQQRQQSAAQNQRGHMDPVSDGVSAQMWRDRRAIASAFLPHGLNVDTIKGNKFYEKQPRRMIDYERRNEKIEMLRSVRFIDELEREVGRKMVQQHRDTTMKLREEVKAALERDRQEVLERRRLIREEDQKYRNAYTAILTAASNDLRMTKVLMLERMQHLAQQHALSLRESRRMCQLLKRESKERVRHDLLRYASAVTEWQSHFVI
Protein: Gamma-tubulin complex component 6 (GCP-6) (Q96RT7)
Organism: Homo sapiens (Human)
Function: Gamma-tubulin complex is necessary for microtubule nucleation at the centrosome.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11694571, ECO:0000269|PubMed:14654843}.
Interaction partners:
- Tubulin gamma-1 chain
- Gamma-tubulin complex component 2
- Gamma-tubulin complex component 3
- Gamma-tubulin complex component 4
- Mitotic-spindle organizing protein 1
- Gamma-tubulin complex component 5
- Mitotic spindle organizing protein 2B
- Protein NEDD1
- Tubulin gamma-2 chain
- Centrosomal P4.1-associated protein
Sequence:
MASITQLFDDLCEALLPAAKTHLGQRSVNRKRAKRSLKKVAYNALFTNLFQDETQQLQPDMSKLPARNKILMLSFDLRVGGLGPKADRLEELVEELEAAPCCPLLEVGSVLDLLVQLAGSGPPQVLPRKRDYFLNNKHVGRNVPYSGYDCDDLSVFEMDVQSLISREECLCHSMIQETLQVMEAAPGTGLPTVGLFSFGDPCGDRFERDTRVSLFGALVHSRTYDMDVRLGLPPVPDNADLSGLAIKVPPSVDQWEDEGFQSASNLTPDSQSEPSVTPDVDLWEAALTYEASKRRCWERVGCPPGHREEPYLTEAGRDAFDKFCRLHQGELQLLAGGVLQAPQPVLVKECELVKDVLNVLIGVVSATFSLCQPAQAFVVKRGVHVSGASPESISSLLSEVAEYGTCYTRLSHFSLQPVLDSLYSKGLVFQAFTSGLRRYLQYYRACVLSTPPTLSLLTIGFLFKKLGRQLRYLAELCGVGAVLPGTCGGGPRAAFPTGVKLLSYLYQEALHNCSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDAYGEFMIQVNHEYLSFRDKLYWTHGYVLISKEVEDCVPVFLKHIAHDIYVCGKTINLLKLCCPRHYLCWSDVPVPRISVIFSLEELKEIEKDCAVYVGRMERVARHSSVSKEEKELRMEIAKQELIAHAREAASRVLSALSDRQMSERMALDARKREQFQRLKEQFVKDQERRQAARQEELDDDFSYARELRDRERRLKSLEEELERKARQALVDHYSKLSAEAARREQKALWRIQRHRLESARLRFLLEDEKHIQEMLKAVSEAHQPQEPPDVLLSVHPQVTSPGPEHPEGGQGCDSGSAEQHSPAWDGWNRPGLLTPQPLKPLAVGAGGRGLQQAEGARPFSDSLSIGDFLPVGPGAEPSVQTGMVPLLEVALQTINLDLPPSAPGEAPAAASTQPSRPQEYDFSTVLRPAVATSPAPGPLQAAECSLGSSGLQLWEDSCGKMDACGSASRETLLPSHPPRRAALEEGSSQPTERLFGQVSGGGLPTGDYASEIAPTRPRWNTHGHVSDASIRVGENVSDVAPTQPRWNTHGHVSNASISLGESVSDVAPTRPRWNIHGHVSNASIRVGENVSDVAPTRPRWNTHGHVSNASIRVGENVSDVAPTRPRWNTHGHVSDASISLGESVSDMAPARPRWNTHGHVSDASISLGESVSDMAPTRPRWNTHGHVSDTSIRVGENVSDVAPIRSRCNTHGHVSDASISLGEPVSDVVSTRPRWNTHVPIPPPHMVLGALSPEAEPNTPRPQQSPPGHTSQSALSLGAQSTVLDCGPRLPVEVGPSLSSPSSGCGEGSISVGENVSDVAPTQPWWPNTPGDSVSEELGPGRSGDTEDLSPNWPLNSQEDTAAQSSPGRGEEAEASAAEAQGGEQAYLAGLAGQYHLERYPDSYESMSEPPIAHLLRPVLPRAFAFPVDPQVQSAADETAVQLSELLTLPVLMKRSITAPLAAHISLVNKAAVDYFFVELHLEAHYEALRHFLLMEDGEFAQSLSDLLFEKLGAGQTPGELLNPLVLNSVLSKALQCSLHGDTPHASNLSLALKYLPEVFAPNAPDVLSCLELRYKVDWPLNIVITEGCVSKYSGVFSFLLQLKLMMWALKDVCFHLKRTALLSHMAGSVQFRQLQLFKHEMQHFVKVIQGYIANQILHVTWCEFRARLATVGDLEEIQRAHAEYLHKAVFRGLLTEKAAPVMNVIHSIFSLVLKFRSQLISQAWGPPGGPRGAEHPNFALMQQSYNTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYYQDA
Protein: Interferon lambda-4 (IFN-lambda-4) (K9M1U5)
Organism: Homo sapiens (Human)
Function: Cytokine that may trigger an antiviral response activating the JAK-STAT pathway and up-regulating specifically some interferon-stimulated genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23291588}. Secreted {ECO:0000269|PubMed:23291588}.
Interaction partners:
Sequence:
MRPSVWAAVAAGLWVLCTVIAAAPRRCLLSHYRSLEPRTLAAAKALRDRYEEEALSWGQRNCSFRPRRDPPRPSSCARLRHVARGIADAQAVLSGLHRSELLPGAGPILELLAAAGRDVAACLELARPGSSRKVPGAQKRRHKPRRADSPRCRKASVVFNLLRLLTWELRLAAHSGPCL
Protein: Outer membrane porin G (Outer membrane protein G) (P76045)
Organism: Escherichia coli (strain K12)
Function: Forms channels functionally larger than those of classical porins.
Subcellular location: Cell outer membrane; Multi-pass membrane protein.
Interaction partners:
- Putative ABC transporter periplasmic-binding protein YcjN
- Outer membrane porin F
- Inner membrane ABC transporter permease protein YcjO
- Outer membrane protein A
- Inner membrane ABC transporter permease protein YcjP
- Kojibiose phosphorylase
- N-acetylneuraminic acid outer membrane channel protein NanC
- 3-dehydro-D-guloside 4-epimerase
- Ferrichrome outer membrane transporter/phage receptor
- Outer membrane porin C
Sequence:
MKKLLPCTALVMCAGMACAQAEERNDWHFNIGAMYEIENVEGYGEDMDGLAEPSVYFNAANGPWRIALAYYQEGPVDYSAGKRGTWFDRPELEVHYQFLENDDFSFGLTGGFRNYGYHYVDEPGKDTANMQRWKIAPDWDVKLTDDLRFNGWLSMYKFANDLNTTGYADTRVETETGLQYTFNETVALRVNYYLERGFNMDDSRNNGEFSTQEIRAYLPLTLGNHSVTPYTRIGLDRWSNWDWQDDIEREGHDFNRVGLFYGYDFQNGLSVSLEYAFEWQDHDEGDSDKFHYAGVGVNYSF
Protein: D-3-phosphoglycerate dehydrogenase (3-PGDH) (EC 1.1.1.95) (A10) (Q61753)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
Interaction partners:
- Phosphoserine aminotransferase
- Phosphoglycerate mutase 1
- Phosphoserine phosphatase
- Bisphosphoglycerate mutase
- Phosphoglycerate mutase 2
- Serine hydroxymethyltransferase, mitochondrial
- Asparagine synthetase
- Serine hydroxymethyltransferase, cytosolic
- Delta-1-pyrroline-5-carboxylate synthase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
Sequence:
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWDRKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTVGYDPIISPEVAASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEAMGTLMHAWAGSPKGTIQVVTQGTSLKNAGTCLSPAVIVGLLREASKQADVNLVNAKLLVKEAGLNVTTSHNPGVPGEQGSGECLLTVALAGAPYQAVGLVQGTTPMLQMLNGAVFRPEVPLRRGQPLLVFRAQPSDPGMLPTMIGLLAEAGVQLLSYQTSMVSDGEPWHVMGLSSLLPSLETWKQHVLEAFQFCF
Protein: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (Pyruvate dehydrogenase complex component E2) (PDC-E2) (PDCE2) (Q8BMF4)
Organism: Mus musculus (Mouse)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P08461}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- [Pyruvate dehydrogenase
- Pyruvate dehydrogenase protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Citrate synthase, mitochondrial
- ATP-citrate synthase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MWRVCARRARSAVPRDGFRARWAALKEGPGAPCGSPRIGPAAVRCGSGIPRYGVRSLCGWSSGSGTVPRNRLLRQLLGSPSRRSYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEAFKNYTLDLAAAAAPQAAPAAAPAPAAAPAAPSASAPGSSYPTHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGAPLCIIVEKQEDIAAFADYRPTEVTSLKPQAAPPAPPPVAAVPPTPQPVAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPSKAAPAAAAAMAPPGPRVAPAPAGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPITMLL
Protein: Anaphase-promoting complex subunit 14 (20S cyclosome/APC complex protein apc14) (Overlapping meiotic transcript protein 1) (O42659)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Appears to play a role in spore wall formation.
Subcellular location: Ascus epiplasm {ECO:0000269|PubMed:12786945}.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 13
- Anaphase-promoting complex subunit 15
- Cullin-1
Sequence:
MDPFAGTGQSKSYRTFGNVFQRLSMSGNPKPLAKKPLLLPEASKAIEFWNYRDVIGGEEAEQERNERASRIAISRIASSRSSIPEYRQAIMQHLTKHVQQLDQLAEW
Protein: Uncharacterized protein (Q38B14)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFYRTKKVIINSLFSDSSWYCTFRFRNPMTSQRRSCHEGIPSGRVTGNSVTLLSEMRENNAIGVEAVGKERKRPDAMTVLSNVFRTNPAALRLHRELTICIASGETERASDLASVLAGLVKRTTRLDDIEQKCAEEGGRSKVPNDPVPVVGEETVEFLTSNVVRGVSSQSRLESIEILHNDAPGAPYLGEKVAEAAEVKDSEPLPFWKNPDALRLTLLESAFEMALADDNENPLQPGSVEADCLEKERMEILDAYLKREGKRWELQKAAVARAIVATVKDLGVVPEDIHAALQAEGELRLNGSDKRFNVLKHCNIIVRGEVPEVMELQMKGTATRNVEASVSQELDVLINRMSSTGTPLSQRDKDLALFELVMSKSKMRYVVGLHRELQVALDTAPALRKLAVEHRAKSGSVLFVERALKMLNKVAPDGSETTAEDVECIDTISTPVLPFTFMLKMCLWFEAPVAM
Protein: DNA-binding protein inhibitor ID-2a (Inhibitor of DNA binding 2, dominant negative helix-loop-helix protein) (Inhibitor of DNA binding/differentiation 2) (Inhibitor of DNA-binding 2a) (Q7SZQ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Oligodendrocyte transcription factor 1
- Oligodendrocyte lineage transcription factor 2.
- Transcription factor 3a.
Sequence:
MKAISPVRSFRKSSASVTTTEHSLGISRSKTPVDDPLSLLYNMNDCYSKLKELVPSIPQNKNVSKMEILQHVIDYILDLQIALDSNSAITSLHHPRAGQGTSRTPLTTLNTDISILSLQTPEFPSDLITEDSRTLYR
Protein: EP2C protein (Q8SQD4)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRQRLLPFFTSLLLVALLFPGLSQARHVNHSATEALRELREGATGQGTNRSQLLRHPVKRAPIIRRIPYYPEVESDLRIVDCKRSEGFCQEYCNYLETQVGYCSKKKDACCLH