wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein phosphatase non-receptor type (EC 3.1.3.48) (A0A8I5ZUL2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
Interaction partners:
Sequence:
MVEQEGLPPRGPPEDNRYSAAVMTSRLRALGGRINNIRTSELPKEKTRSEVTCSIRFLDGLVQTFKVNKQDLGQSLLDMAYGHLGVTEKEYFGLQHGDDPVDSPRWLEASKPLRKQLKGGLPCILHFRVRYFIPDPNTLQQEQTRHLYFLQLKMDVCEGRLTCPLNSAVVLASYAVQSHIGDFNSSIHHPGYLADSQFIPDQNDDFLSKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELHGGRDLHNLDLMIGIASAGIAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKNLWKSCVEHHSFFQAKKLLPQEKNVLSQYWTLGSRNPKKSVNNQYCKKVIGGMVWNPVMRRSLSVERLETKSLPSRSPPITPNWRSPRLRHEIRKPRHSSADNLANEMTYITETEDVFYTYKGSLSPKDSDSEVSQNHSPHRGSLSENNPAQSCLTQKSSSSVSPCSNAPGSFSPDGVDQQFLEDYHKVTKGGSIEEASQYYCDKNDDGDGYLVLIRITPDKEGRFGFNLKGGVDQKMPLVVSRINPESPADTCMPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRESHSRELALVIRRKAVRSLAEIRSEDELSQLFPEAMFPACPEGGDSLEGSMELLKKGLESGTVLIQFEQLYRKKPGLAVTFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLVVMLTTLTERGRTKCHQYWPDPPDIMDHGIFHIQCQAEDCTIAYVSREMLVTNTETGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVKYVRSLRVGGEPALVHCSAGIGRTGVLVTMETAMCLIERNLPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEEGLVQTLDPS
Protein: RAB5A, member RAS oncogene family like (RAB5A, member RAS oncogene family, b (EC 3.6.5.2)) (Q7ZUG4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Early endosome antigen 1
- RAB guanine nucleotide exchange factor
- RAB guanine nucleotide exchange factor
- Ankyrin repeat and FYVE domain-containing 1
- ER membrane protein complex subunit 6
- Rab GDP dissociation inhibitor
- Rabenosyn, RAB effector.
- HESX homeobox 1.
- Rabaptin, RAB GTPase-binding effector protein 1.
Sequence:
MAGRGGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTLCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQRQASPNIVIALAGNKADLANKRALDFQDAQSYADDNSLLFMETSAKTSMNVSEIFMAIAKKLPKNEPQPAGANTARNRGVDLTETAQPAKGPCCST
Protein: isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (Q8MSW0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Probable arginine--tRNA ligase, cytoplasmic
- leucine--tRNA ligase
- Lysine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase
- leucine--tRNA ligase
- Probable proline--tRNA ligase, mitochondrial
Sequence:
MGKKLERNDVCRVPENINFPAEEENVLQKWRHENIFEKCSQLSKGKPKYTFYDGPPFATGLPHYGHILAGTIKDIVTRYAYQQGYHVDRRFGWDCHGLPVEFEIDKLLNIKGPEDVAKMGIAAYNAECRKIVMRYADEWENVVTRVGRWIDFKNDYKTLYPWYMESIWWIFKQLFDKGLVYQGVKVMPYSTACTTSLSNFEANQNYKEVVDPCVVVALEAVSLPNTFFLVWTTTPWTLPSNFACCVHPTMTYVKVRDVKSDRLFVLAESRLSYVYKSETEYEVKEKFVGKTLKDLHYKPLFPYFAKRGAEVKAYRVLVDEYVTEDSGTGIVHNAPYFGEDDYRVCLAAGLITKSSEVLCPVDEAGRFTNEASDFEGQYVKDSDKQIMAALKARGNLVSSGQVKHSYPFCWRSDTPLIYKAVPSWFVRVEHMSKNLLDCSSQTYWVPDFVKEKRFGNWLKEARDWAISRNRYWGTPIPIWRSPSGDETVVIGSIKQLAELSGVQVEDLHRESIDHIEIPSAVPGNPPLRRIAPVFDCWFESGSMPFAQQHFPFENEKDFMNNFPADFIAEGIDQTRGWFYTLLVISTALFNKAPFKNLIASGLVLAADGQKMSKRKKNYPDPMEVVHKYGADALRLYLINSPVVRAESLRFKEEGVRDIIKDVFLPWYNAYRFLLQNIVRYEKEDLAGNGQYTYDRERHLKNMDKASVIDVWILSFKESLLEFFATEMKMYRLYTVVPRLTKFIDQLTNWYVRLNRRRIKGELGADQCIQSLDTLYDVLYTMVKMMAPFTPYLTEYIFQRLVLFQPAGTLEHADSVHYQMMPVSQKKFIRNDIERSVALMQSVVELGRVMRDRRTLPVKYPVSEIIAIHKDSQILEAIKTLQDFILSELNVRKLTLSSDKEKYGVTLRAEPDHKALGQRLKGNFKAVMAAIKALRDDEIQKQVSQGYFDILDQRIELDEVRIIYCTSEQVGGNFEAHSDNEVLVLLDMTPNEELLEEGLAREVINRVQKLKKKAQLIPTDPVLIFHELAADNKAKQEVLEAQAQLAKVLSNYASIIKTAIKSEFAPYSSEQASKKRLIASELVDLKGVPLKLTICSTEELQLPNLPWLNISLAEDLVPRFGNSSKASLFLQHNVSKEIISLPTLRSELEHLFGLYGVNFNIYVVDHQKRTTALKSIDENLSGKLLVLTRSQDAPKLSAGYELSPAPYSKFINQHSGKSIFTENPLGRALC
Protein: GMP reductase (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase) (Guanosine monophosphate reductase) (P60560)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Bifunctional purine biosynthesis protein PurH
- Adenine phosphoribosyltransferase
- Xanthine-guanine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase
- Guanylate kinase
- Hypoxanthine phosphoribosyltransferase
- 5'/3'-nucleotidase SurE
- Guanosine-inosine kinase
Sequence:
MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFSMASALASFDILTAVHKHYSVEEWQAFINNSSADVLKHVMVSTGTSDADFEKTKQILDLNPALNFVCIDVANGYSEHFVQFVAKAREAWPTKTICAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGMIVSDGGCTTPGDVAKAFGGGADFVMLGGMLAGHEESGGRIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRIFNNL
Protein: Peptidyl-prolyl cis-trans isomerase FKBP3 (PPIase FKBP3) (EC 5.2.1.8) (25 kDa FK506-binding protein) (25 kDa FKBP) (FKBP-25) (FK506-binding protein 3) (FKBP-3) (Immunophilin FKBP25) (Rapamycin-selective 25 kDa immunophilin) (Rotamase) (Q00688)
Organism: Homo sapiens (Human)
Function: FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.
Subcellular location: Nucleus.
Interaction partners:
- Serine/threonine-protein kinase mTOR
- Histone deacetylase 1
- Histone deacetylase 2
- Calcineurin subunit B type 1
- E3 ubiquitin-protein ligase Mdm2
- Calmodulin-1
- Transcriptional repressor protein YY1
- Calmodulin-like protein 5
- Calmodulin-like protein 3
Sequence:
MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLVTAYNHLFETKRFKGTESISKVSEQVKNVKLNEDKPKETKSEETLDEGPPKYTKSVLKKGDKTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKIPPNAKLTFEVELVDID
Protein: cDNA: FLJ22686 fis, clone HSI10987 (Q9H614)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQEFARRYFRRSQALLGQTDGGAAGKDTDSLVQYTKAPIQESLLSLSDDVSKLAVASFLALMRFMGDQSKPRGKDEMDLLYELLKLCQQEKLRDEIYCQVIKQVTGHPRPEHCTRGWSFLSLLTGFFPPSTRLMPYLTKFLQDSGPSQELARSSQEHLQRTVKYGGRRRMPPPGEMKAFLKGQAIRLLLIHLPGGVDYRTNIQTFTVAAEVQEELCRQMGITEPQEVQEFALFLIKEKSQLVRPLQPAECLNSVVVDQDVSLHSRRLHWETPLHFDNSTYISTHYSQVLWDYLQGKLPVSAKADAQLARLAALQHLSKANRNTPSGQDLLAYVPKQLQRQVNTASIKNLMGQELRRLEGHSPQEAQISFIEAMSQLPLFGYTVYGVLRVSMQALSGPTLLGLNRQHLILMDPSSQSLYCRIALKSLQRLHLLSPLEEKGPPGLEVNYGSADNPQTIWFELPQAQELLYTTVFLIDSSASCTEWPSIN
Protein: Methyl-CpG binding domain protein 1 (A0A8I6A3W5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEAWQDCPALGPGWKRREAFRKSGASCGRSDIYYRSPTGEKIRSKIELTRYLGPACDLTLFDFRQGILCHPVPKTHPLAVPSKKKKKTSKPAKAKKQQVGPQRSEVRKETPREGNKVAPATALLPVTASAPAPVPVPVSAPAPAPAPLCCENCGIHLSWDGIKRERRRTLCKDCRAQRIAFNREQRMFKRVGCGECTACLVKEDCGVCSICCLQLPNDVASGLFCKCEQRRCLRIVEKNRGCGVCRGCQTQEDCGHCRICLRFPRPGLKRQWRCLQRRCFWGKYDHSKRGPRVASRRHSRAPPLPPHAASQHPEPTELHISDQTPTAPAEFVYDCVEEDELQPYTNQRQNRKCGACAACLRRMDCGHCDFCCDKPKFGGSNQKRQKCRWRQCLQFAMKRLLPSIGPGSEEEARLLPHHTHQKRSASTRQLQLSSPLKAPLAVVTTPPGPVQDSGKRQAGSGFVLPQPDTDLVYLQEGTSSLMQVPGPAAASTENPAQETQGSAPGWVVALPQVKQEKADAPEEWTAVTTFLTSSTVQPGFLSKASGLDPPPVKREPPGPEEDGEENKEDDVSESAPAEEIGGIGTPVITEIFSLGGTRLRDAEAWLPRSKDLKKPGAKMQ
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (A6M5L8)
Organism: Influenza A virus (A/swine/Iowa/4/1976(H1N1))
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}.
Interaction partners:
Sequence:
MASQGTKRSYEQMETGGERQDATEIRASVGRMIGGIGRFYIQMCTELKLSDYEGRLIQNSITIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRIDGKWMRELTLYDKEEIRRVWRQANNGEDATAGLTHIMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTIAMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGLAVASGHDFEREGYSLVGIDPFKLLQNSQVFSLIRPNENPAHKSQLVWMACHSAAFEDLRVSGFIRGKKVVPRGKLSTRGVQIASNENVEAMDSSTLELRSRYWAIRTRSGGNTNQQKASAGQISVQPTFSVQRNLPFERATVMAAFIGNNEGRTSDMRTEIIRMMESAKPEDLSFQGRGVFELSDEKATNPIVPSFDMNNEGSYFFGDNAEEYDN
Protein: Mitochondrial-processing peptidase subunit alpha-2 (Alpha-MPP 2) (Ddalpha-MPP 2) (Inactive zinc metalloprotease alpha-2) (Q54F93)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q86A84}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Mitochondrial-processing peptidase subunit beta
- Probable cytochrome b-c1 complex subunit 6
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- Cytochrome c oxidase subunit 5
- NADH dehydrogenase flavoprotein 2, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 4
Sequence:
MIGRFIARNYTTSIFQESKRIVESTTLSNGLKVVSLVGGYTGPAVSLGLYIKTGSRNETQETAGLNQVLKGLAFESNTNKLGIEVQRDIEVSGSTAFAQASRDNLLIALQTLPNRSLQMLNNLANITKPTLPYHEVRDVTEIIVKESEAYNHDSYSSIFESVHQTAFRGKTLGRPLVAPICNLGNITKDAVTNWVNSTYKPSNMILVGVGLSHNELIEEAEKVTFGNDESSTSISNETAQYIGGESLKYSSGNSKVVLAFEGTAQSNIKDVAAFSVLQSILGNGCPKTAPGHGRTSRLFSLTKNNSNIVNSEAFNLTYGDSGLFGVVAEVEGATVGKTVSLITSEIVAASKTAGQELERAKAVTKSSVLEQAESRTSALEFIGKQAIYTDKVLTPAEFAEEISKVTSEDIKRVAKKMTSKKPTLVVVGDVSDAPTIESVQSQLKL
Protein: Alba DNA/RNA-binding protein (At1g29250/F28N24_8) (F28N24.7 protein) (Q9LP53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alba DNA/RNA-binding protein
- AT3g07170/T1B9_17
- Alba DNA/RNA-binding protein
- Alba DNA/RNA-binding protein
- DEAD-box ATP-dependent RNA helicase 46
- Pre-mRNA cleavage factor Im 25 kDa subunit 2
- At5g12410
- La protein 1
- Putative RRM-containing protein family protein)
- THO complex subunit 4C
Sequence:
MEEITEGVNNMNLAVDTQKKNRIQVSNTKKPLFFYVNLAKRYMQQYTDVELSALGMAIATVVTVAEILKNNGFAVEKKIMTSTVDIKDDSRGRPVQKAKIEITLAKSEKFDELMAAANEEKEAAEAQEQN
Protein: Long-chain-fatty-acid--CoA ligase FadD13 (EC 6.2.1.3) (Fatty acyl-CoA ligase) (FACL) (FACL13) (Fatty acyl-CoA synthetase) (ACS) (FACS) (Very-long-chain fatty-acyl-CoA synthetase) (ACSVL) (P9WQ37)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. It has preference for the fatty acid with long chain length in the following order: hexacosanoic acid (C26), tetracosanoic acid (C24) and palmitic acid (C16).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22560731}; Peripheral membrane protein {ECO:0000269|PubMed:22560731}. Note=Membrane-associated through distinctive regions rich in arginine and aromatic residues. {ECO:0000269|PubMed:22560731}.
Interaction partners:
- Probable diacyglycerol O-acyltransferase Tgs4
- Putative FAD-containing monooxygenase MymA
- Putative diacyglycerol O-acyltransferase Rv3087
- Putative acetyl-hydrolase LipR
- Putative alcohol dehydrogenase D
- Putative oxidoreductase SadH
- Polyketide synthase Pks13
- Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks15
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phthioceranic/hydroxyphthioceranic acid synthase
Sequence:
MKNIGWMLRQRATVSPRLQAYVEPSTDVRMTYAQMNALANRCADVLTALGIAKGDRVALLMPNSVEFCCLFYGAAKLGAVAVPINTRLAAPEVSFILSDSGSKVVIYGAPSAPVIDAIRAQADPPGTVTDWIGADSLAERLRSAAADEPAVECGGDDNLFIMYTSGTTGHPKGVVHTHESVHSAASSWASTIDVRYRDRLLLPLPMFHVAALTTVIFSAMRGVTLISMPQFDATKVWSLIVEERVCIGGAVPAILNFMRQVPEFAELDAPDFRYFITGGAPMPEALIKIYAAKNIEVVQGYALTESCGGGTLLLSEDALRKAGSAGRATMFTDVAVRGDDGVIREHGEGEVVIKSDILLKEYWNRPEATRDAFDNGWFRTGDIGEIDDEGYLYIKDRLKDMIISGGENVYPAEIESVIIGVPGVSEVAVIGLPDEKWGEIAAAIVVADQNEVSEQQIVEYCGTRLARYKLPKKVIFAEAIPRNPTGKILKTVLREQYSATVPK
Protein: Na[+]/H[+] hydrogen antiporter 1, isoform A (Q9VM74)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MFSSHKKMTATGEPEAREDPSVGGAPATITTPTTIIAPTPIPVPSDVPMPNSNGSGNGAGNHRSTIVIESQPKRRVSIISDPPMIGGNGGLGTGYDNPAYEQNPRRKISQTSTHSHTDIGPARRKSILKDTAPHDNESDRVSTHSYENYRQNALDVLNAKYNGHQMGHNGGGSSNGGANYVEESWMYNFCLKCRGEEPSASWEPPFWQKIFPYPLCPTFRTVSRLISIILIGVLIWVTAFVIIGDSAAPGGQLFGLVVLTVAANFGGYLISLTTLPRLIGMLLVGILFQNVGWADIDGDFSKVTAHLRKFALTIILTRAGLEMEPEAFKKVYKTILKLGIIPWCVEAVVMAVMSHFLLDLPWIWAFLLGSIIAAVSPAVVVPCLFRLRTKGYGVAKGIPTLVVAVAGVDDALSVAIFGIISTVMFSDKGLAYQIAQAPVCILGGLGFGVVWGSLARIFPEKGDAYVVPLRTLLLFTGGLMAIYGSEELGFEGAGPLAVVFSAFVSNLFWCKDGWDVEDNPVSTAFEIFWMIFEPILFGLTGATIKIRELDSHTVSIGAACIFTGAILRILTTAGIAFGDRLNTKEKFFVGLSWMAKATVQAALGPVALKHLGDDATEEERNWANIVQTICVFSIVLTAPLGAIMISVTGTKLLTKTKQPQDLSGWRRSHRPSIRDISIIDEEEEREDPEIPEDKETHDNTLNNAHIPSISYTYNT
Protein: RTA1-domain-containing protein (Q86HF8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein
Sequence:
MNSSSVNLADLPKYPNLYGYEPSQGLSIAAIVCFSTVSLVLIILSIKFKKFYFLVAPGAGIVTVIGYAIRIKSAQDTHVLGTYIATTLLILLPPTALAAVFLFAQLGKIMKRTGIQHPIFKPNVVKYLFLIVDIFSIIIQGAGGALLAQSADNPDLDKPAKGVMLTGLCIALCSFTLFFFLIIYLYIKVLKVQEEDKKWRIIFIALFASGILIILRSIYRVAEYAGGYHSAVMINEPLFYGLDTLPMFLLMCIWIPFHPGFVSLSKKKENKEEDKKNYDTETRNGVELE
Protein: Checkpoint protein kinase, putative (AFU_orthologue AFUA_3G08100) (Q5B953)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Spindle assembly checkpoint component MAD1
Sequence:
MASPNSLSTAHATALHQQQYRQMSRASSVSRSGSRRSSPEVHNSVALRSNAASISKQYSAGDSSDDEVPEPKFSASVKALLDEDDGNASPRLRTRGLNEYRPNLRVGSAASSNERRSRTTSPLDQSNGSPAPRVVRIGSVLGSGSKLRREGSHLTSGENAEVEAEAKHYSSDFITPGPRTRSVRISTSRTHTRSPTSASPSGRRSASRSPLHEEGSADRPEEEGKSRYDDYAPIIGTSSVLRSRNPEDIGIQSSLRVKRVGRLTGTFLNGPARRGVLRRQSEEDQSPSYLSDSKEAEGGDNNDYNYKSARASSPKVSWADPEQPQKTTDYRRISSGDGPFSRSSSPKSYVSHSKSTPGSSSDASSKPSSSKEPIFKVPPPPTLPSTRDQENEPPPTFKRTKPQGFDFLDKPEKLSVVYGDDKKDQELPAGTSPRKILSNRSNNTPHRPAPPPPKMSVLETATATGGAATASQSRKKRSQVSINHKPFTRLDCIGRGGSSRVYRVMAENYKIFALKRVNLEDVDPTTLAGYKGEIDLLKKLENVDRVVRLFDWELNSDKRTLSVLMEIGESDLEKVLTYKLNAEDATFDINFTRFYWKEMLECVQAVHEYNVVHSDLKPANFLLVQGRLKLIDFGIANAIQDNTVNVHREQQVGTPNYMSPEALVDSNASLGLPASVGKMMKLGKPSDVWSLGCILYKMVYGQPPFAKIAKYYERIMAIPNPKVKIDFPAFGVGGIQVPPGLIRTLKGCLQRDQTLRPTISDLLGQRDPFLYPDAQLEGAVPITQDVLGRILVNVVNHCRVRGVPNDEELAAWPAGFFAKIKAALEENP
Protein: Coexpressed With Polycystins (B6VQ87)
Organism: Caenorhabditis elegans
Interaction partners:
- Paired amphipathic helix protein sin-3
- Coexpressed With Polycystins
- Secreted protein
- Coexpressed With Polycystins
- Histone deacetylase
- Histone deacetylase 1
- Putative histone deacetylase 2
- Secreted protein
- Mortality factor related protein 1
- Probable histone-binding protein lin-53
Sequence:
MRISMLSLFLLTFKAAGATCPCSGITVNGTDQEHCWQIQSRSEATWGSADDACVAVGGHLGHPLDINYEEILNYVQKQSSLPVLTGIVAGNTEIPIYGAICQSNNFYEVVANTTGFSNTPTSTTTCAYIKTSSSGLVFDSCSIDANVLCDRPLQKQDYCSIIANCSSTTTFLSTTTPVSSTTSNISLTSSSTQSYSSSTAGATSSLFTIKVTQSTTAAGNGQGGSGSGSATTTCKCSAGDVSATTAASACSEKSGCLKNQWKIFGMCVDWRAMLALLLIGLLLFLCCCICHCCMHACMFCTPGKREKEIRDPILPNRSVVAPIPIVAPGKMDYDVEKSEAVILPPPAIQPEPVYITVPEKHESVYGFHTKEIIHVMPEKPTTREIGTMTDPMDTELSTIMPVPVAAPVMKRKKVVKKPKKMFIPATEDPIEEDLAADIPIEMPESPGARSVAPLGDVVEPAPMIPLNFSRNPKPMMPEPQSHDDIPLPVNKSRNTVPPPVMQQKPNNASNNEEFDPSGLRSPPIPAGKPNNGTPKRMTFSPIADESEEENGARIPSPPRERRASGGRPGNNDGPNLSPNAALDPHPTLKNQRLNEMPSPTPANAPVPSKSPVSGASNNPFANLGGPSPAPAADGAGRAPQDDVGMRAARGRLGGAVRGGGGGGEAPNGWKPWAKGGARR
Protein: Dihydrofolate reductase (EC 1.5.1.3) (P0ABQ4)
Organism: Escherichia coli (strain K12)
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
Interaction partners:
- Thymidylate synthase
- Dihydromonapterin reductase
- Dihydrofolate synthase/folylpolyglutamate synthase
- Serine hydroxymethyltransferase
- Formyltetrahydrofolate deformylase
- Phosphoribosylglycinamide formyltransferase
- Bifunctional purine biosynthesis protein PurH
- Aminomethyltransferase
- Methionyl-tRNA formyltransferase
- Methionine synthase
Sequence:
MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR
Protein: Phospholipase (EC 3.1.4.4) (B0V1J1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidate cytidylyltransferase
- Phosphatidate cytidylyltransferase
- Cholinephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
- Phospholipid phosphatase 5.
- Choline/ethanolaminephosphotransferase 1
- Selenoprotein I
- Lecithin-cholesterol acyltransferase.
- Lysophosphatidylcholine acyltransferase 4
Sequence:
MSDSVENLDTRELGFSDAEDEPEEVDFDFNPSGASRIGFSAIYRTVGFKDTEAHVYLTSLPITAKILDVERFTRTQDRFKFSKHRSVSKAMPAVFKIELKHGNFTWIVKRKEKHFMELHRELLKYKTLMRIPLPTRSHTERRKSIKRSEVRQMPALPRGGGDGELAREEQVSSRRKQLEDYLNKLLKMAMYRKYYATMEFIDVSQLSFIQDLGPKGLEGIVYKRSGGHRIPGMNCCGHNEVCYRWSKRWLIVKDSFLLYMKPDTGAISFVLLVDNEFSIKMDSKQTETKHGVRIENLSRKLVLKFTSYRHARWWGQAIESFVRKHGKAFLRTHRFGSFAREEENIPSKWYVNGKTYMEDVANALEEAKEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFVMLYKEVELALGINSEYSKKTLMHLHPNIKVMRHPDHVSSSVYLWAHHEKIVVIDQSVAFVGGIDLAYGRWDDREHRLTDVGSVTRSVAQAIEQGLDSSTPKKKVSTSGNSSRSMVGDSVDLPKLKGIGRTRKTRFSLYHHIQRGLHHADSISSIDSTNKSGSVHSLQTGVGELMGNTRFWHGKDYCNFVFKDWVQLDKPFDDFIDRYTTPRMPWHDISSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSHSTGNDLKYQVPDTVHTKVQVLRSAADWSAGIKYHEESIHNAYIQVIAKSKHFIYIENQFFISCADNKHVYNKIGDAIIERIIRAHKENKKFRVYVVTPLLPGFEGDITTGGGNALQAVMHFNYRTMNRGEYSIISQLKKEMDDQWMNYISICGLRTHAELEGRLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKKDSEVAVIFEDSETTPSVMDGQEYQAGKFALQLRLECFKTILGAFTDPSIDVSDPISNSFYKDVWMSVSGRNVTIYEKVFRCLPSSLVRNKQELLSFQSKTGLDKEDPLKAQELLKKIRGFLVQFPLDFLCEENLMPSVGTKEHMVPTEIWT
Protein: Autophagy-related protein 9B (APG9-like 2) (Nitric oxide synthase 3-overlapping antisense gene protein) (Protein sONE) (Q674R7)
Organism: Homo sapiens (Human)
Function: Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). In addition to autophagy, also plays a role in necrotic cell death (By similarity).
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:18936157}; Multi-pass membrane protein {ECO:0000269|PubMed:18936157}. Note=Under amino acid starvation or rapamycin treatment, redistributes from a juxtanuclear clustered pool to a dispersed peripheral cytosolic pool (PubMed:18936157). The starvation-induced redistribution depends on ULK1 and ATG13 (PubMed:18936157). {ECO:0000269|PubMed:18936157}.
Interaction partners:
- Autophagy-related protein 9A
- Serine/threonine-protein kinase ULK2
- Serine/threonine-protein kinase ULK1
- WD repeat domain phosphoinositide-interacting protein 1
- Transmembrane protein 208
- Autophagy-related protein 2 homolog B
- Beclin-1
- Microtubule-associated protein 1 light chain 3 alpha
- Ubiquitin-like protein ATG12
- Autophagy-related protein 2 homolog A
Sequence:
MVSRMGWGGRRRRLGRWGDLGPGSVPLLPMPLPPPPPPSCRGPGGGRISIFSLSPAPHTRSSPSSFSPPTAGPPCSVLQGTGASQSCHSALPIPATPPTQAQPAMTPASASPSWGSHSTPPLAPATPTPSQQCPQDSPGLRVGPLIPEQDYERLEDCDPEGSQDSPIHGEEQQPLLHVPEGLRGSWHHIQNLDSFFTKIYSYHQRNGFACILLEDVFQLGQFIFIVTFTTFLLRCVDYNVLFANQPSNHTRPGPFHSKVTLSDAILPSAQCAERIRSSPLLVLLLVLAAGFWLVQLLRSVCNLFSYWDIQVFYREALHIPPEELSSVPWAEVQSRLLALQRSGGLCVQPRPLTELDIHHRILRYTNYQVALANKGLLPARCPLPWGGSAAFLSRGLALNVDLLLFRGPFSLFRGGWELPHAYKRSDQRGALAARWGRTVLLLAALNLALSPLVLAWQVLHVFYSHVELLRREPGALGARGWSRLARLQLRHFNELPHELRARLARAYRPAAAFLRTAAPPAPLRTLLARQLVFFAGALFAALLVLTVYDEDVLAVEHVLTAMTALGVTATVARSFIPEEQCQGRAPQLLLQTALAHMHYLPEEPGPGGRDRAYRQMAQLLQYRAVSLLEELLSPLLTPLFLLFWFRPRALEIIDFFHHFTVDVAGVGDICSFALMDVKRHGHPQWLSAGQTEASLSQRAEDGKTELSLMRFSLAHPLWRPPGHSSKFLGHLWGRVQQDAAAWGATSARGPSTPGVLSNCTSPLPEAFLANLFVHPLLPPRDLSPTAPCPAAATASLLASISRIAQDPSSVSPGGTGGQKLAQLPELASAEMSLHVIYLHQLHQQQQQQEPWGEAAASILSRPCSSPSQPPSPDEEKPSWSSDGSSPASSPRQQWGTQKARNLFPGGFQVTTDTQKEPDRASCTD
Protein: G1/S-specific cyclin-D3 (P30282)
Organism: Mus musculus (Mouse)
Function: Regulatory component of the cyclin D3-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Component of the ternary complex, cyclin D3/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex. Shows transcriptional coactivator activity with ATF5 independently of CDK4.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P30281}. Cytoplasm {ECO:0000250|UniProtKB:P30281}.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase 4 inhibitor C
- Cyclin-dependent kinase inhibitor 1C
- Retinoblastoma-like protein 2
- Retinoblastoma-associated protein
- Cyclin-dependent kinase 4 inhibitor D
Sequence:
MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQKEIKPHMRKMLAYWMLEVCEEQRCEEDVFPLAMNYLDRYLSCVPTRKAQLQLLGTVCLLLASKLRETTPLTIEKLCIYTDQAVAPWQLREWEVLVLGKLKWDLAAVIAHDFLALILHRLSLPSDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVLGLGACSMSADELTELLAGITGTEVDCLRACQEQIEAALRESLREAAQTAPSPVPKAPRGSSSQGPSQTSTPTDVTAIHL