wanglab/gogpt-training-data huggingface dataset:
Protein: Arylamine N-acetyltransferase 3 (EC 2.3.1.5) (Arylamide acetylase 3) (N-acetyltransferase type 3) (NAT-3) (P50296)
Organism: Mus musculus (Mouse)
Function: Participates in the detoxification of a plethora of hydrazine and arylamine drugs.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- Xanthine dehydrogenase/oxidase
- Arylamine N-acetyltransferase 1
- Carboxylesterase 1C
- Carboxylesterase 1E
- Carboxylesterase 1D
- Carboxylesterase 1F
- Arylamine N-acetyltransferase 2
- Myeloperoxidase
Sequence:
MDIEAYFERIGYQKSSNKLDLQTLTEILQHQIRAIPFENLNIHCGKTMELSLEDTFHQIVRKKRGGWCLQVNHLLYWALAMIGFETTMLGGCVYVPSACKYSNTMIHLLLQVTISGKTYIVDSAFPFSCQLWEPLELTSGKDQPQVPAIFHLREENGTWYLEQTKRQEYVSNQEFIDSNFLEKNTHRKIYSFTLEPRTIEDFWSISTYYQVSRTSVMTNTSLCSLHTKDGVHGLMGTILAYKKFNYKDNIDLVEFKTLKEEEIEEVLKSVFGIHLETKLVPKCGNVFFTI
Protein: Serine/threonine-protein kinase WNK1 (AtWNK1) (EC 2.7.11.1) (Protein kinase with no lysine 1) (Q9CAV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates flowering time by modulating the photoperiod pathway. Phosphorylates APRR3.
Interaction partners:
- Two-component response regulator-like APRR3
- Regulator of G-protein signaling 1
- Protein trichome birefringence-like 26
- peptidylprolyl isomerase
Sequence:
MNNLSYLEPDYSEFVEVDPTGRYGRYNEVLGKGASKTVYRAFDEYEGIEVAWNQVKLYDFLQSPEDLERLYCEIHLLKTLKHKNIMKFYTSWVDTANRNINFVTELFTSGTLRQYRLRHKRVNIRAMKHWCRQILRGLHYLHSHDPPVIHRDLKCDNIFVNGNQGEVKIGDLGLAAILRKSHAAHCVGTPEFMAPEVYEEAYNELVDIYSFGMCILEMVTFDYPYSECTHPAQIYKKVMSGKKPDALYKVKDPEVKCFIEKCLATVSLRVSARELLDDPFLRIDDGEFDLRSVDMEDSVGPLYRQPHHLPDYYNYPSNSSSLNRQYSNGNYPSNSSSLNRQYSNGYNSHHEYQNGWAYNPAETEETHGIELFESRNNDDQEEEKKSGNVDITIKGKRRDDGGLFLRLRIADKEGRVRNIYFPFDIETDTALSVATEMVAELDMDDHGVTKIANMIDGEISSLVPSWRPGPEFEECLAAAAAANAASICNNCVSNRTSMGSVMDFLRTNPGANVIQCCRNGCGETHGRFEEITIRETEVRLRELWKLQQQQESRELSSIDSGHNHSEEEEEEEVLYEDPENMFSCEAGNEINHISGSGSFSFMPSKYCDEPSEKTENQVQQELRWLKAKCQIELRDIQDEQLKTRWPESGEEVEISPKDGFLGSVSGLGREEDTVKEMFGERLVPKCLKRTTSLPVDAIDS
Protein: Outer membrane protein OprG (Q9HWW1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Oxygen-independent coproporphyrinogen III oxidase
- Cytochrome c oxidase, cbb3-type, CcoO subunit
- Outer membrane porin F
- cytochrome-c oxidase
- PhoP/Q and low Mg2+ inducible outer membrane protein H1
- UspA domain-containing protein
- Anaerobically-induced outer membrane porin OprE
- GDP-polyphosphate phosphotransferase
- alcohol dehydrogenase
- Cbb3-type cytochrome c oxidase subunit
Sequence:
MRKSWLTASLLALTVASPFAAADIQGHKAGDFIIRGGFATVDPDDSSSDIKLDGAKQRGTKATVDSDTQLGLTFTYMFADKWGVELVAATPFNHQVDVKGLGPGLDGKLADIKQLPPTLLLQYYPMGGTNSAFQPYGGLGVNYTTFFDEDLASNRKAQGFSSMKLQDSWGLAGELGFDYMLNEHALFNMAVWYMDIDTKASINGPSALGVNKTKVDVDVDPWVYMIGFGYKF
Protein: Homoserine kinase (HK) (HSK) (EC 2.7.1.39) (O43056)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Threonine synthase
- Homoserine dehydrogenase
- Aspartokinase
- Cystathionine beta-lyase
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Probable cystathionine gamma-synthase
- Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Bifunctional purine biosynthetic protein ADE1
- Anthranilate phosphoribosyltransferase
- Probable acetolactate synthase small subunit
Sequence:
MQKFQIKVPASSANIGPGFDVLGMSLEEYMTLDVEVSTESGPCVLTYEGDGKEHVSLDVQKNMITQTSLYVLRCNNISTFPYATKIHVINPIPLGRGMGSSGSAAIAGVMLANEIAKLGLSKLQMMDYVLMIERHPDNVMASMMGGFVGSFLRELSEEEKNAFSPSADDLLKNEALTLPPKSLGTFARLPWASELKAIVVIPEFHLATSKARSVLPTSYGRTDVVYNLQRLALLTTALGQTPINPHLVYEVMKDKVHQPYRASLIPGLQNILATLNPDTQPGLCGICLSGAGPTVLALATGNFDEIAHAMLSIFEKHGVKCRYLVLSPAFDGATVKYF
Protein: Pumilio homolog 1 (H0YEH2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}. Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
XQSPVGRHVVGVKGVGGMSVACVLKRKAVLWQDSFSPHLKHHPQEPANPNMPVVLTSGTGSQAQPQPAANQALAAGTHSSPVPGSIGVAGRSQDDAMVDYFFQRQHGEQLGGGGSGGGGYNNSKHRWPTGDNIHAEHQVRSMDELNHDFQALALEGRAMGEQLLPGKKFWETDESSKDGPKGIFLGDQWRDSAWGTSDHSVSQPIMVQRRPGQSFHVNSEVNSVLSPRSESGGLGVSMVEYVLSSSPGDSCLRKGGFGPRDADSDENDKGEKKNKGTFDGDKLGDLKEEGDVMDKTNGLPVQNGIDADVKDFSRTPGNCQNSANEVDLLGPNQNGSEGLAQLTSTNGAKPVEDFSNMESQSVPLDPMEHVGMEPLQFDYSGTQVPVDSAAATVGLFDYNSQQQLFQRPNALAVQQLTAAQQQQYALAAAHQPHIAGLAPAAFVPNPYIISAAPPGTDPYTAGLAAAATLGPAVVPHQYYGVTPWGVYPASLFQQQAAAAAAATNSANQQTTPQAQQGQQQVLRGGASQRPLTPNQNQQGQQTDPLVAAAAVNSALAFGQGLAAGMPGYPVLAPAAYYDQTGALVVNAGARNGLGAPVRLVAPAPVIISSSAAQAAVAAAAASANGAAGGLAGTTNGPFRPLGTQQPQPQPQQQPNNNLASSSFYGNNSLNSNSQSSSLFSQGSAQPANTSLGFGSSSSLGATLGSALGGFGTAGGLTNGSGRYISAAPGAEAKYRSASSASSLFSPSSTLFSSSRLRYGMSDVMPSGRSRLLEDFRNNRYPNLQLREIAGHIMEFSQDQHGSRFIQLKLERATPAERQLVFNEILQAAYQLMVDVFGNYVIQKFFEFGSLEQKLALAERIRGHVLSLALQMYGCRVIQKALEFIPSDQQNEMVRELDGHVLKCVKDQNGNHVVQKCIECVQPQSLQFIIDAFKGQVFALSTHPYGCRVIQRILEHCLPDQTLPILEELHQHTEQLVQDQYGNYVIQHVLEHGRPEDKSKIVAEIRGNVLVLSQHKFASNVVEKCVTHASRTERAVLIDEVCTMNDGPHSALYTMMKDQYANYVVQKMIDVAEPGQRKIVMHKIRPHIATLRKYTYGKHILAKLEKYYMKNGVDLGPICGPPNGII
Protein: HTH-type transcriptional regulator MlrA (MerR-like regulator A) (P33358)
Organism: Escherichia coli (strain K12)
Function: Activates transcription of csgD, the master regulator of biofilm formation, by binding to its promoter region. Also controls the transcription of cadC and ibaG. Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two c-di-GMP control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeR
- Diguanylate cyclase DgcM
- UPF0759 protein YecE
- NAD
- CsgBAC operon transcriptional regulatory protein
- Probable diguanylate cyclase DgcE
- Probable diguanylate cyclase DgcC
- Exodeoxyribonuclease I
- Cyclic di-GMP phosphodiesterase PdeH
- RNA polymerase sigma factor RpoS
Sequence:
MALYTIGEVALLCDINPVTLRAWQRRYGLLKPQRTDGGHRLFNDADIDRIREIKRWIDNGVQVSKVKMLLSNENVDVQNGWRDQQETLLTYLQSGNLHSLRTWIKERGQDYPAQTLTTHLFIPLRRRLQCQQPTLQALLAILDGVLINYIAICLASARKKQGKDALVVGWNIQDTTRLWLEGWIASQQGWRIDVLAHSLNQLRPELFEGRTLLVWCGENRTSAQQQQLTSWQEQGHDIFPLGI
Protein: Tyrosine-protein phosphatase non-receptor type 14 (EC 3.1.3.48) (Protein-tyrosine phosphatase PTP36) (Q62130)
Organism: Mus musculus (Mouse)
Function: Protein tyrosine phosphatase which may play a role in the regulation of lymphangiogenesis, cell-cell adhesion, cell-matrix adhesion, cell migration, cell growth and also regulates TGF-beta gene expression, thereby modulating epithelial-mesenchymal transition. Mediates beta-catenin dephosphorylation at adhesion junctions. Acts as a negative regulator of the oncogenic property of YAP, a downstream target of the hippo pathway, in a cell density-dependent manner. May function as a tumor suppressor.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocation into the nucleus is associated with induction of cell proliferation. Partially colocalized with actin filaments at the plasma membrane. {ECO:0000250}.
Interaction partners:
- Protein KIBRA
- Transcriptional coactivator YAP1
- Angiomotin
- Catenin beta-1
- WW domain-containing transcription regulator protein 1
- Receptor-type tyrosine-protein phosphatase gamma
Sequence:
MPFGLKLRRTRRYNVLSKNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKHLDKFANEPLLFFGVMFYVPNVSRLQQEATRYQYYLQVKKDVLEGRLRCSLEQVIRLAGLAVQADFGDYNQFDSQEFLREYVLFPMDLAMEEAALEELTQKVAQEHKAHSGILPAEAELMYINEVERLDGFGQEIFPVKDSHGNSVHLGIFFMGIFVRNRVGRQAVIYRWNDIGSVTHSKAAILLELIDKEETALFHTDDIENAKYISRLFTTRHKFYKQNKICTEQSNSPPPIRRQPTWSRSSLPRQQPYILPPMHVQCSEHYSETHTSQDSIFPGNEEALYCRSHNSLDLNYLNGTVTNGSVCSVHSVNSLSCSQSFIQASPVSSNLSIPGSDIMRADYIPSHRHSTIIVPSYRPTPDYETVMRQMKRGLMHADSQSRSLRNLNIINTHAYNQPEELVYSQPEMRERHPYTVPYAHQGCYGHKLVSPSDQMNPQNCAMPIKPGASSISHTVSTPELANMQLQGAQHYSTAHMLKNYLFRPPPPYPRPRPATSTPDLASHRHKYVSGSSPDLVTRKVQLSVKTFQEDSSPVVHQSLQEVSEPLTATKHHGGGGGTVNKRHSLEVMNSMVRGMEAMTLKSLNIPMARRNTLREQGPSEETGGHEVHGLPQYHHKKTFSDATMLIHSSESEEEEETLEAAPQVPVLREKVEYSAQLQAALARIPNRPPPEYPGPRKSVSNGALRQDQGTPLPAMARCRVLRHGPSKALSVSRAEQLAVNGASLGPSISEPDLTSVKERVKKEPVKERPVSEMFSLEDSIIEREMMIRNLEKQKMTGPQAQKRPLMLAALNGLSVARVSGREDGHHDATRVPIDERLRALKKKLEDGMVFTEYEQIPNKKANGVFSTATLPENAERSRIREVVPYEENRVELIPTKENNTGYINASHIKVVVGGSEWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRTKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPHHGCPEDVQGFLSYLEEIQSVRRHTNSVLEGIRTRHPPIVVHCSAGVGRTGVVILSELMIYCLEHNEKVEVPTMLRFLREQRMFMIQTIAQYKFVYQVLVQFLQNSRLI
Protein: 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (EC 4.1.1.45) (Picolinate carboxylase) (Q8R5M5)
Organism: Rattus norvegicus (Rat)
Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.
Interaction partners:
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynureninase
- Sentrin-specific protease 8
- Kynurenine 3-monooxygenase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Tryptophan 2,3-dioxygenase
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Coiled-coil domain containing 62
- Kynurenine formamidase
- Kynurenine--oxoglutarate transaminase 1
Sequence:
MKIDIHTHILPKEWPDLEKRFGYGGWVQLQQQGKGEAKMMKDGKVFRVIQQNCWDPEVRIREMNQKGVTVQALSTVPVMFSYWAKPKDTLELCQFLNNDLAATVARYPRRFVGLGTLPMQAPGLAVEEMERCVKELGFPGIQIGSHINMWDLNDPELFPIYTAAERLNCSLFVHPWDMQMDGRMAKYWLPWLVGMPSETTTAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTIGRIAHGFNMRPDLCARDNSSDPRKYLGSFYTDSLVHDPLSLKLLTDVIGKDRVILGTDYPFPLGEQEPGKLIESMADFDEETKDKLTAGNALTFLGLERKLFE
Protein: AH domain-containing protein (E1B6R4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGKIDKTVDPEFEAQCEVLKDIHRRYGLVVAAAKNFSHVLTQMAEAEKKLSESFYQLSMKEEQIKAQCTMTSETMRGVGEQAASLDACLRYFISSMETVYNQTITDTLHTIYNTESARIEYDVDRNDISAATNPPQGQLTKNLPVGATEKCEEKKAKYEKLKNDAKIKMRLLEENRISVVAAQLEKLQSALAAYYSGNAKLLEASVRELSFLQSPQPSFIPTM
Protein: Ectopic P granules protein 5 homolog (Q9VE34)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in autophagy. Plays a role in late steps of autophagy.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HCE0}. Lysosome {ECO:0000250|UniProtKB:Q9HCE0}.
Interaction partners:
- LD03592p
- Autophagy protein 5
- Autophagy-related protein 2
- Ubiquitin-like modifier-activating enzyme ATG7
- Syntaxin 17, isoform B
- Autophagy-related 14
- Pleckstrin homology and RUN domain containing M1
- Ubiquitin-like-conjugating enzyme ATG3
Sequence:
MATLEKPKKEKSKKSRNRVPIEKEEEEPAELSTSEEQRPAENVSLLEEFERVATLASSSSGEAIISHECCISSDVGVTSQEPEGTQEPTETEAQPSAPSAPPSTTVHVVQYPNLQPMQLSNAQVEEHSAKIVYRQAESPTGFALARSHIKLLSTEELRQIYDCPELELAKQFELEFLMNSLLETSEADPLYAAVMEYYELQGKITSNLHDVEKLRKGCAESQKQIWVRQPVTRTFSGTCGDGNVVQECVTYDVIQVDPIKLEVAKTSLTGLYDLVCHAYTNNSITAKITKVKVDQIINDLLTYPNLDGHSVVSLHHTQSGEALQCVSQLRRAISILFSFVRRPSPNANFDKDLKEWLRKLIALQLLLATREDHWFLLFNILRCPNGVGSWAAQFLQLPGTRAVRRGSQQNELPLDLNSPELNHCMAVLQILLMPVKKRNEYLKSQAQAHRELSDTPGATDRWIVVDSDGEDSHTPAGECVGLKESDLVALLNQMPFEKIFTSALRIEKFLDDYIIEPDMITAQQMLAVVVFFSQLVKTIGEGLLTYNNERYKQLAKRLGRLVRHTLQYVFDYNELFINNNLYKSSEMYERIQVELQALLVRACGYIYRTRNLGTWQYFSTLPFGTLDAEVIWHLFYYLNVGFPTDLANDLVSNAEAAFQAEDFWRKFDLANADVAPEDMYYLLQTFFEMANERNRSKDGSLVKAICLHIFHIGYIHKSTREICYKTARDMLANLMDEDLFGCVLVQLKMRYGEVDQAAYLFKALPLENWHPSMDTFEVLSNWLLHFDYQSSESQLARLIISHLNWGLDCEGRLFLPHNIHVRMAHLVNEALNKYAPEVIGASGISESVRQVSSLIDSTQSSREQFTNWCWRMVSVLRLHLMDQGVESVRRTLQHPTEPLLFIPELERMEMIFQGVNENRPLALYVGMLVSLHGHSIPLICQHGFILLQQLLLDHRHAATIRCLELIVPLFLETPETLANCESFQRLITTLLNADRTYLKLAKDMVYANSIGPILELLDNMLHHQIISYTSYGLCSPLNLLNIWLNCFTTLPGWSQNSNLLYLLDRMLRISYQFPDCRAQAVEFFYNYYKDCTEWKSAPKGSALKAFFGGQSVSRIPLISPQNCWLNLVILEIEFRLVDTRIFPELLRQISAQPVEAALKKTISLSKTSAFPASQLVIFKYAQLLASMESTHALFPIVCQKFFELYLWRVPTENESLNFSHNFGVSDKFYEYNVPLMKSIKSQLKSAESYYSALATKNANDDAMAHFYRNCCKLMQNCALWLEDTQINRFTSDAEHLPAQYNSEKLRELLSGHVNHWTEFLCLASLRKEQRHQADQWGRKVMRLSNQKAPRTPVQPKQRQPPAQHIKSLLKSYEKIVENPLHIRVEPIKTPPIDGVIVAQIQKKMTTLNSTANNYHYKTSELNSLDLNYLERVPTLYSMIPYEETRRKECTSLLFKRNCTAPAQIKLTPEHIRINDVISRKQAQNRERHDKIIEDILLAMSVESFAQAIEELGVCIGALLVAPLESSVTQIGVRVFYDIVDNLNEVTMKFQPTHDLYFQVLEKLGVFLEADQAAQGLAILRLALKRPDLLELLAGVFVPSRTDVDHFLSMYEFLIDSHLKHCDTQTLFVLFSKFDLLGWMEAYQPKLSEINRLLLLVLQGLEAWSQPDSSLLQDLFRRHLVHIFGYDFPQHYGEVMQLVLDRTSDQKLMPVVLLDLLNALFVRSNCAELSLQQSEVRVHELALDFARRQKLFTLKAATDTLLLLSRHFQKERLHHGLHGLYPKHKDYCQALVLWFTSFGHTLLASAICSYQELLADQISDIVFGSIVETYSPWLIPYTEETVSGVAHWIRQLTPGQSKVLLPWSEQHVSSCKLMIRSFVATIIQVLQYLPSSNKILEHVFAWYVHHFAQSSTTGHVLAPIHEGLAQLPWERFLPPAQHVELLYDSLQKFLPESHAMLGHIFIRIEWNNWFAQMPQPVSILSRLFTIFVKIAFEPNIHIHPNTSKILEDAIRYPWHLVECSELEQLLKWFVASVEPAIALKIPAESNYADRAVLELLRLACAMLPERSAQDAVVLGTAKRMLYTRSMVRMQRACGAKHQKLLATKEGERAFSNAFLELLDSIDGAISSCSEHRTMEEQRREALNLMLELVAPTQTQSQEVSNIHIKALVWWQQRCSPGNLVMCSTLPAIGHLNTYIASIYSLLEASIENYFRTSPEIASWHAPSWQGLMEALSMSLPKLDLMPIMQGSYFFSLHVFVLYKMEEIATDGDKVTFLQDLSQLLENLKTSPQTEPRMALVWGVIIARGCQIAQVNQQVKKPLHMLARHLQIASTKAEGWGDGLLGVIGLKSEVITNRRKVLTRCLACVIFSLFPANRDLRIPSEEYESALRELSMLLANKKFTDIKPLIVRAVSLLKESTFPDIRAVPHMVCRLISIFYEESYLTTIPEVWDFEFKLMAT
Protein: Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic (AtGSA1) (GSA 1) (EC 5.4.3.8) (Glutamate-1-semialdehyde aminotransferase 1) (GSA-AT 1) (P42799)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transaminase converting glutamate 1-semialdehyde (GSA) to 5-aminolevulinate (ALA). Involved in the biosynthesis of tetrapyrroles.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q42522}.
Interaction partners:
- Delta-aminolevulinic acid dehydratase 1, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
- Glutamyl-tRNA reductase 2, chloroplastic
- Probable glutamyl-tRNA reductase 3, chloroplastic
- Probable delta-aminolevulinic acid dehydratase 2, chloroplastic
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Porphobilinogen deaminase, chloroplastic
- Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic
- Argininosuccinate lyase, chloroplastic
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
Sequence:
MSATLTGSGTALGFSCSSKISKRVSSSPASNRCCIKMSVSVDEKKKSFSLQKSEEAFNAAKNLMPGGVNSPVRAFKSVGGQPVLIDSVKGSKMWDIDGNEYIDYVGSWGPAIIGHADDEVLAALAETMKKGTSFGAPCLLENVLAEMVISAVPSIEMVRFVNSGTEACMGVLRLARAFTNKEKFIKFEGCYHGHANAFLVKAGSGVATLGLPDSPGVPKAATSDTLTAPYNDLEAVEKLFAAHKGEISAVILEPVVGNSGFIPPTPEFINGLRQLTKDNGVLLIFDEVMTGFRLAYGGAQEYFGITPDLTTLGKIIGGGLPVGAYGGRRDIMEMVAPAGPMYQAGTLSGNPLAMTAGIHTLKRLKQAGTYEYLDKITKELTNGILEAGKKTGHPMCGGYISGMFGFFFAEGPVYNFADSKKSDTEKFGRFFRGMLEEGVYFAPSQFEAGFTSLAHTPEDIQLTIAAAERVLSRI
Protein: Cytoplasmic envelopment protein 2 (F5HEF2)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating.
Subcellular location: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04039, ECO:0000269|PubMed:15613308}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04039}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04039}. Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. {ECO:0000255|HAMAP-Rule:MF_04039}.
Interaction partners:
Sequence:
MASRRRKLRNFLNKECIWTVNPMSGDHIKVFNACTSISPVYDPELVTSYALSVPAYNVSVAILLHKVMGPCVAVGINGEMIMYVVSQCVSVRPVPGRDGMALIYFGQFLEEASGLRFPYIAPPPSREHVPDLTRQELVHTSQVVRRGDLTNCTMGLEFRNVNPFVWLGGGSVWLLFLGVDYMAFCPGVDGMPSLARVAALLTRCDHPDCVHCHGLRGHVNVFRGYCSAQSPGLSNICPCIKSCGTGNGVTRVTGNRNFLGLLFDPIVQSRVTALKITSHPTPTHVENVLTGVLDDGTLVPSSKAPWVLLRMSDYFSRLLIYECKKLKALGLRSY
Protein: CIN85 and CD2AP related, isoform A (Q9VA35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTTTNSSNSSTTSVTTQQQKEQIGGSSSTTSKVYIKKTGSSSNSTTSSTTTASSSAGRKESFGSRDSLNDILSETGLPTGNVAAQRKSLENKNLDLTKPPGVGASVSIGQQRSSTSSATTSSATTVATGLTSSSVSKSMENMLDEKVKSPPPPVLSKKPSVPLKKTPTGGVPMTGNLLGGKKKNTEGKLTTAVSHDLADGLAASKMLSGANQLPESGAAGNVVIRRAATIAVEDTDFDRVERASILTDMRQGRVKAPKRRPPSAAINVLGESNNNSVYVNGSGMSGSGGAGSASELSEDGGAGGKTSDDNSTGEEPQLAKPKPREWEKKKAPWMEELKASQVTRKKTSPSVEPRGASVAERTSKLFAAEQAVSSNSSSITTKVQSSAVTSSMFVENSTTSSSVITSSSHTTTNDAIMSRSLSAAKVQTASSDEETRATRPNSLAIRNQRSVSPLVKSSNASSSQSQEEKPTSQLNNHQDASSSRVAQLEQRVDKLEGLVLNQQRTIEELVNALKSEAERVKILRSELDKYAHKQTRRGKFDNWMF
Protein: Splicing factor U2AF 35 kDa subunit (U2 auxiliary factor 35 kDa subunit) (U2 snRNP auxiliary factor small subunit) (Q9D883)
Organism: Mus musculus (Mouse)
Function: Plays a critical role in both constitutive and enhancer-dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18758164}. Nucleus speckle {ECO:0000269|PubMed:18758164}.
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Serine/arginine-rich splicing factor 2
- Splicing factor 1
- Splicing factor U2AF 26 kDa subunit
- Serine/arginine-rich splicing factor 1
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 1
- Polycomb group protein ASXL1
- Serine/arginine-rich splicing factor 3
Sequence:
MAEYLASIFGTEKDKVNCSFYFKIGACRHGDRCSRLHNKPTFSQTIALLNIYRNPQNSSQSADGLRCAVSDVEMQEHYDEFFEEVFTEMEEKYGEVEEMNVCDNLGDHLVGNVYVKFRREEDAEKAVIDLNNRWFNGQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPISRELRRELYGRRRKKHRSRSRSRERRSRSRDRGRGGGGGGGGGGGRERDRRRSRDRERSGRF
Protein: RNA polymerase-associated protein LEO1 (Replicative senescence down-regulated leo1-like protein) (Q8WVC0)
Organism: Homo sapiens (Human)
Function: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Involved in polyadenylation of mRNA precursors. Connects PAF1C to Wnt signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:15791002}.
Interaction partners:
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein CTR9 homolog
- Transcription elongation factor SPT5
- Parafibromin
- Superkiller complex protein 8
- RNA polymerase II-associated factor 1 homolog
- FACT complex subunit SPT16
- Transcription elongation factor SPT4
- FACT complex subunit SSRP1
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MADMEDLFGSDADSEAERKDSDSGSDSDSDQENAASGSNASGSESDQDERGDSGQPSNKELFGDDSEDEGASHHSGSDNHSERSDNRSEASERSDHEDNDPSDVDQHSGSEAPNDDEDEGHRSDGGSHHSEAEGSEKAHSDDEKWGREDKSDQSDDEKIQNSDDEERAQGSDEDKLQNSDDDEKMQNTDDEERPQLSDDERQQLSEEEKANSDDERPVASDNDDEKQNSDDEEQPQLSDEEKMQNSDDERPQASDEEHRHSDDEEEQDHKSESARGSDSEDEVLRMKRKNAIASDSEADSDTEVPKDNSGTMDLFGGADDISSGSDGEDKPPTPGQPVDENGLPQDQQEEEPIPETRIEVEIPKVNTDLGNDLYFVKLPNFLSVEPRPFDPQYYEDEFEDEEMLDEEGRTRLKLKVENTIRWRIRRDEEGNEIKESNARIVKWSDGSMSLHLGNEVFDVYKAPLQGDHNHLFIRQGTGLQGQAVFKTKLTFRPHSTDSATHRKMTLSLADRCSKTQKIRILPMAGRDPECQRTEMIKKEEERLRASIRRESQQRRMREKQHQRGLSASYLEPDRYDEEEEGEESISLAAIKNRYKGGIREERARIYSSDSDEGSEEDKAQRLLKAKKLTSDEEGEPSGKRKAEDDDKANKKHKKYVISDEEEEDDD
Protein: UDP-glucuronosyltransferase 2B15 (UDPGT 2B15) (UGT2B15) (EC 2.4.1.17) (UDP-glucuronosyltransferase 2B36) (UDPGT 2B36) (P36511)
Organism: Rattus norvegicus (Rat)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (testosterone, androsterone) and estrogens (estradiol, epiestradiol, estriol, catechol estrogens). Displays glucuronidation activity toward several classes of xenoblotic substrates, including phenolic compounds (eugenol, 4-nitrophenol, 4-hydroxybiphenyl) and phenylpropanoids (naringenin, coumarins). Catalyzes the glucuronidation of monoterpenoid alcohols such as borneol, menthol and isomenthol, a class of natural compounds used in essential oils.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P54855}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 2E1
- Catechol O-methyltransferase
- Transmembrane O-methyltransferase homolog
- Aldo-keto reductase family 1, member C1
- Beta-glucuronidase
- Cytochrome P450 4A2
- UDP-glucose 6-dehydrogenase
- Cytochrome P450 4A10
Sequence:
MSGKWISALLLLQISFCFKSGNCGKVLVWPMEYSHWMNIKIILEELVQKGHEVTVLRPSAFVFLDPKETSDLKFVTFPTSFSSHDLENFFTRFVNVWTYELPRDTCLSYFLYLQDTIDEYSDYCLTVCKEAVSNKQFMTKLQESKFDVVFSDAIGPCGELIAELLQIPFLYSLRFSPGYTIEQYIGGVLFPPSYVPMIFSGLAGQMTFIERVHNMICMLYFDFWFQTFREKKWDPFYSKTLGRPTTLAEIMGKAEMWLIRSYWDLEFPHPISPNVDYIGGLHCKPAKPLPKDIEDFVQSSGEHGVVVFSLGSMVRNMTEEKANIIAWALAQIPQKVLWRFDGKKPPTLGPNTRLYKWLPQNDLLGHPKTKAFVTHGGANGIYEAIHHGIPMIGIPLFAEQHDNIAHMVAKGAAVEVNFRTMSKSDLLNALEEVIDNPFYKKNAMWLSTIHHDQPTKPLDRAVFWIEFVMRHKGAKHLRSLGHNLPWYQYHSLDVIGFLLSCVAVTVVLALKCFLFVYRFFVKKEKKTKNE
Protein: Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-) (GIY-YIG domain-containing protein 1) (Q9BQ83)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5'-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03100, ECO:0000269|PubMed:19596236}.
Interaction partners:
- Structure-specific endonuclease subunit MUS81
- Structure-specific endonuclease subunit SLX4
- DNA repair endonuclease XPF
- Structure-specific endonuclease subunit EME1
- DNA excision repair protein ERCC-1
- Fanconi anemia group D2 protein
- Protein SLX4IP
- DNA topoisomerase 3-alpha
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- RecQ-mediated genome instability protein 1
Sequence:
MGPAGVAARPGRFFGVYLLYCLNPRYRGRVYVGFTVNTARRVQQHNGGRKKGGAWRTSGRGPWEMVLVVHGFPSSVAALRFEWAWQHPHASRRLAHVGPRLRGETAFAFHLRVLAHMLRAPPWARLPLTLRWVRPDLRQDLCLPPPPHVPLAFGPPPPQAPAPRRRAGPFDDAEPEPDQGDPGACCSLCAQTIQDEEGPLCCPHPGCLLRAHVICLAEEFLQEEPGQLLPLEGQCPCCEKSLLWGDLIWLCQMDTEKEVEDSELEEAHWTDLLET