wanglab/gogpt-training-data huggingface dataset:
Protein: TATA-binding protein interacting (TIP20) domain-containing protein (Q387F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cullin 1, putative
- Cullin family profile domain-containing protein
- Cullin 4B, putative
- Cullin, putative
- Cullin, putative
- Cullin, putative
- RING-type domain-containing protein
- RING-type domain-containing protein
- DNA damage-binding protein 1
- Ubiquitin, putative
Sequence:
MEVFDLAAFRTRMNDVERDVRVMALFDLQQALKSTVFKPDSVTLSKIVEYVTTCFAQSEPCREVRCNAIRLVPQLLLLSGEKDQERLVSLLCTSSTSQRARFGEKGYSELHDSAARALKLACECMSSKARADVESWQRLVPVARKIADALSSALEKGVEGVVREGIYDCIGVLIYPFGRVFICDVGCVLTKNALADVHHTGQLRRRAISFLSLASPFLSEDLFDAVFEVGVRGLREGNHRGAVVMPYLQLYEGLVKGCPSRAKTGALETMKFLTDGLSARLSHESADADAFDDDDYEVCDATVRLMHLMVCQYSKELATIHCALFVQALEIARFDPNYCDNMGGLDGCDSSDASGLYFTEDDTDMSWRLRMWAARLLALLIELSPFSTELTHQLGCEVLSLIGDRVEEVQLAAIHFVDTVIQSSRGASVCTSLLLFLQGAIDPLLGALNTREPKVVVAAAKALQNLFYFHWSVFTTEVCRAHDIVDKLLKAHLTGKEYAVVELTALAVRMLEGTSHGQPNIKLVTKLLDTVYAAVDAYVCGGIGQIVVCSVKAMAHTSGLAGAAYCERCMELYISLALNANFGGELISSAVEATRHCMSTFAASLSVDYFRRCGGRLVVLSEGRQVAIRLLKDLTASVPAAQLQPQELERLSNSIGRQDRAVQQHIVSIVCNALDNSGQLTAETLEDMFEFARSNSLKSGDRLLVQATLEMLEKICRRFSNLGGRIVDQLLPTVWEILSSAPKCAGHHPLLLVRGTAVLIRSLHQMLEPAQRSDLVEQTLRYVSRSKFRETSSEILRGVASVDEGILERVGSLMSGDDSLLCICVGTIGMSVPLPDMWEARLFRFLSSTGAENLGSVVPLAVGRAVSNAQNRSLMERVVESATRNTGGAALFWRAIHEAALTTVAGAELSPFSDPFFCKGVVEKLMENLLEDDTETAATVLGSFAPFVRDYLIDITATHLSDELDSKKAVCITVQRYLLSSVKNTDECPRLVSAIERALRCLSRKADLRVRFAALQLFATLLSVKPHLLIGSYVRDVVYPCVLEELLEDPTLVLAINLGSCTHREDRGKEMRKLAFECVSMLLRDAEDRGKESILEYCGRYEELGRCLVHACGPRGGGETDGDINTKAMDLIVRFLRLCPSSPCDGSQVMVLYEKLKMALGVDIERTAQDASKKQLLKRQALNCIMCLSEWPPFSCHPQWQSLVLLAQQNPLLPEAIKVT
Protein: Preprolactin (Q91170)
Organism: Oncorhynchus keta (Chum salmon) (Salmo keta)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MARRSQGTKLHLAVLCLVVSCHAIGLSDLMERASQRSDKLHSLSTSLTKDLDSHFPPMGRVMMPRPSMCHTSSLQTPKDKEQALKVSENELISLARSLLLAWNDPLLLLSSEAPTLPHPSNGDISSKIRELQDYSKSLGDGLDIMVNKMGPSSQYISSIPFKGGDLGNDKTSRLINFHFLMSCFRRDSHKIDSFLKVLRCRATKIRPETC
Protein: Splicing factor 3B subunit 5 (SF3b5) (Pre-mRNA-splicing factor SF3b 10 kDa subunit) (Q9BWJ5)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex, a constituent of the spliceosome. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:28781166}.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 3
- Splicing factor 3B subunit 6
- Small nuclear ribonucleoprotein Sm D2
- Splicing factor 3B subunit 4
- Small nuclear ribonucleoprotein G
- Splicing factor 3A subunit 1
- U2 small nuclear ribonucleoprotein A'
- Splicing factor 3A subunit 2
- Small nuclear ribonucleoprotein E
Sequence:
MTDRYTIHSQLEHLQSKYIGTGHADTTKWEWLVNQHRDSYCSYMGHFDLLNYFAIAENESKARVRFNLMEKMLQPCGPPADKPEEN
Protein: Erythronate-4-phosphate dehydrogenase (EC 1.1.1.290) (P05459)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
Interaction partners:
- Phosphoserine aminotransferase
- D-erythrose-4-phosphate dehydrogenase
- 4-hydroxythreonine-4-phosphate dehydrogenase
- Pyridoxine 5'-phosphate synthase
- tRNA pseudouridine synthase A
- Pyridoxine/pyridoxal/pyridoxamine kinase
Sequence:
MKILVDENMPYARDLFSRLGEVTAVPGRPIPVAQLADADALMVRSVTKVNESLLAGKPIKFVGTATAGTDHVDEAWLKQAGIGFSAAPGCNAIAVVEYVFSSLLMLAERDGFSLYDRTVGIVGVGNVGRRLQARLEALGIKTLLCDPPRADRGDEGDFRSLDELVQRADILTFHTPLFKDGPYKTLHLADEKLIRSLKPGAILINACRGAVVDNTALLTCLNEGQKLSVVLDVWEGEPELNVELLKKVDIGTSHIAGYTLEGKARGTTQVFEAYSKFIGHEQHVALDTLLPAPEFGRITLHGPLDQPTLKRLVHLVYDVRRDDAPLRKVAGIPGEFDKLRKNYLERREWSSLYVICDDASAASLLCKLGFNAVHHPAR
Protein: UDP-2,3-diacetamido-2,3-dideoxy-D-glucuronate 2-epimerase (UDP-alpha-D-GlcNAc3NAcA 2-epimerase) (EC 5.1.3.23) (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid 2-epimerase) (G3XD61)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the epimerization of UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucuronic acid (UDP-alpha-D-GlcNAc3NAcA) to UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid (UDP-alpha-D-ManNAc3NAcA). Exhibits high specificity towards the substrate as UDP-alpha-D-GlcNAc, UDP-alpha-D-GlcNAcA (UDP-2-acetamido-2-deoxy-alpha-D-glucuronic acid) and UDP-alpha-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-glucose) cannot act as substrates.
Interaction partners:
- UDP-N-acetyl-D-glucosamine 6-dehydrogenase
- UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronate N-acetyltransferase
- LPS biosynthesis protein WbpG
- UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase
- Probable glycosyltransferase WbpH
- Probable glycosyl transferase WbpJ
- UDP-N-acetyl-2-amino-2-deoxy-D-glucuronate oxidase
- O-antigen translocase
- Putative imidazole glycerol phosphate synthase subunit hisF2
- Glycosyltransferase WbpL
Sequence:
MKILTIIGARPQFIKASVVSKAIIEQQTLSEIIVHTGQHFDANMSEIFFEQLGIPKPDYQLDIHGGTHGQMTGRMLMEIEDVILKEKPHRVLVYGDTNSTLAGALAASKLHVPIAHIEAGLRSFNMRMPEEINRILTDQVSDILFCPTRVAIDNLKNEGFERKAAKIVNVGDVMQDSALFFAQRATSPIGLASQDGFILATLHRAENTDDPVRLTSIVEALNEIQINVAPVVLPLHPRTRGVIERLGLKLEVQVIDPVGYLEMIWLLQRSGLVLTDSGGVQKEAFFFGKPCVTMRDQTEWVELVTCGANVLVGAARDMIVESARTSLGKTIQDDGQLYGGGQASSRIAEYLAKL
Protein: Rab15 effector protein (Q6BDI9)
Organism: Homo sapiens (Human)
Function: Regulates transferrin receptor recycling from the endocytic recycling compartment.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:16195351}. Note=Colocalizes with RAB11 and RAB15 to the endocytic recycling compartment.
Interaction partners:
- Ras-related protein Rab-3C
- Ras-related protein Rab-3B
- Ras-related protein Rab-15
Sequence:
MGQKASQQLALKDSKEVPVVCEVVSEAIVHAAQKLKEYLGFEYPPSKLCPAANTLNEIFLIHFITFCQEKGVDEWLTTTKMTKHQAFLFGADWIWTFWGSNKQIKLQLAVQTLQMSSPPPVESKPCDLSNPESRVEESSWKKSRFDKLEEFCNLIGEDCLGLFIIFGMPGKPKDIRGVVLDSVKSQMVRSHLPGGKAVAQFVLETEDCVFIKELLRNCLSKKDGLREVGKVYISIL
Protein: Chaperone protein Skp (DNA-binding 17 kDa protein) (Histone-like protein HLP-1) (Seventeen kilodalton protein) (P0AEU7)
Organism: Escherichia coli (strain K12)
Function: Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.
Subcellular location: Periplasm {ECO:0000269|PubMed:1838129, ECO:0000269|PubMed:8730870}.
Interaction partners:
- Outer membrane protein A
- Outer membrane protein assembly factor BamA
- UDP-3-O-
- Chaperone SurA
- Outer membrane protein assembly factor BamB
- Periplasmic serine endoprotease DegP
- FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
- Outer membrane protein assembly factor BamD
- Outer membrane protein assembly factor BamC
- Outer membrane protein X
Sequence:
MKKWLLAAGLGLALATSAQAADKIAIVNMGSLFQQVAQKTGVSNTLENEFKGRASELQRMETDLQAKMKKLQSMKAGSDRTKLEKDVMAQRQTFAQKAQAFEQDRARRSNEERGKLVTRIQTAVKSVANSQDIDLVVDANAVAYNSSDVKDITADVLKQVK
Protein: Histone H3.2 (P84233)
Organism: Xenopus laevis (African clawed frog)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Protein BOBBER 1 (Q9LV09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Small heat shock protein required for the establishment of auxin gradients and for patterning of the apical domain of the embryo. Involved in the specification of the cotyledon primordia. Also required for normal inflorescence and floral meristem function, normal developmental patterning and thermotolerance. Acts as a molecular chaperone.
Subcellular location: Cytoplasm. Cytoplasmic granule. Note=cytoplasmic at basal temperatures, but forms heat shock granules containing canonical small heat shock proteins at high temperatures.
Interaction partners:
- At5g50410
- Heat shock factor-binding protein
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- CLIP-associated protein
- Auxin response factor 3
- Elongator complex protein 3
- GrpE protein homolog 2
Sequence:
MAIISEVEEESSSSRPMIFPFRATLSSANPLGFLEKVFDFLGEQSDFLKKPSAEDEIVVAVRAAKEKLKKAEKKKAEKESVKPVEKKAEKEIVKLVEKKVEKESVKPTIAASSAEPIEVEKPKEEEEKKESGPIVPNKGNGTDLENYSWIQNLQEVTVNIPVPTGTKARTVVCEIKKNRLKVGLKGQDPIVDGELYRSVKPDDCYWNIEDQKVISILLTKSDQMEWWKCCVKGEPEIDTQKVEPETSKLGDLDPETRSTVEKMMFDQRQKQMGLPTSEELQKQEILKKFMSEHPEMDFSNAKFN
Protein: Solute carrier family 2, facilitated glucose transporter member 11 (Glucose transporter type 11) (GLUT-11) (Q9BYW1)
Organism: Homo sapiens (Human)
Function: Facilitative glucose transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12175779}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRALRRLIQGRILLLTICAAGIGGTFQFGYNLSIINAPTLHIQEFTNETWQARTGEPLPDHLVLLMWSLIVSLYPLGGLFGALLAGPLAITLGRKKSLLVNNIFVVSAAILFGFSRKAGSFEMIMLGRLLVGVNAGVSMNIQPMYLGESAPKELRGAVAMSSAIFTALGIVMGQVVGLRELLGGPQAWPLLLASCLVPGALQLASLPLLPESPRYLLIDCGDTEACLAALRRLRGSGDLAGELEELEEERAACQGCRARRPWELFQHRALRRQVTSLVVLGSAMELCGNDSVYAYASSVFRKAGVPEAKIQYAIIGTGSCELLTAVVSCVVIERVGRRVLLIGGYSLMTCWGSIFTVALCLQSSFPWTLYLAMACIFAFILSFGIGPAGVTGILATELFDQMARPAACMVCGALMWIMLILVGLGFPFIMEALSHFLYVPFLGVCVCGAIYTGLFLPETKGKTFQEISKELHRLNFPRRAQGPTWRSLEVIQSTEL
Protein: AE binding protein 2 (A0A669KBC9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSDGEPLSRMDSEDSISSTIMDVDSTISSGRSTPAMMNGQGSTTSSSKNIAYNCCWDQCQACFNSSPDLADHIRSIHVDGQRGGVFVCLWKGCKVYNTPSTSQSWLQRHMLTHSGDKPFKCVVGGCNASFASQGGLARHVPTHFSQQNSSKVSSQPKAKEESPSKAGMNKRRKLKNKRRRSLPRPHDFFDAQTLDAIRHRAICFNLSAHIESLGKGHSVVFHSTVIAKRKEDSGKIKLLLHWMPEDITMPQKRLKR
Protein: Serine/arginine-rich splicing factor 11 (Arginine-rich 54 kDa nuclear protein) (p54) (Splicing factor, arginine/serine-rich 11) (Q05519)
Organism: Homo sapiens (Human)
Function: May function in pre-mRNA splicing.
Subcellular location: Nucleus. Note=Colocalizes with spliceosome components.
Interaction partners:
- Serine/arginine repetitive matrix protein 1
- RNA-binding protein 39
- RNA-binding protein with serine-rich domain 1
- Serine/arginine-rich splicing factor 5
- RNA-binding protein 25
- Serine/arginine-rich splicing factor 7
- Serine/arginine-rich splicing factor 9
- Serine/arginine-rich splicing factor 3
- Serine/arginine-rich splicing factor 6
- Serine/arginine-rich splicing factor 4
Sequence:
MSNTTVVPSTAGPGPSGGPGGGGGGGGGGGGTEVIQVTNVSPSASSEQMRTLFGFLGKIDELRLFPPDDSPLPVSSRVCFVKFHDPDSAVVAQHLTNTVFVDRALIVVPYAEGVIPDEAKALSLLAPANAVAGLLPGGGLLPTPNPLTQIGAVPLAALGAPTLDPALAALGLPGANLNSQSLAADQLLKLMSTVDPKLNHVAAGLVSPSLKSDTSSKEIEEAMKRVREAQSLISAAIEPDKKEEKRRHSRSRSRSRRRRTPSSSRHRRSRSRSRRRSHSKSRSRRRSKSPRRRRSHSRERGRRSRSTSKTRDKKKEDKEKKRSKTPPKSYSTARRSRSASRERRRRRSRSGTRSPKKPRSPKRKLSRSPSPRRHKKEKKKDKDKERSRDERERSTSKKKKSKDKEKDRERKSESDKDVKQVTRDYDEEEQGYDSEKEKKEEKKPIETGSPKTKECSVEKGTGDSLRESKVNGDDHHEEDMDMSD
Protein: Putative cation exchanger C521.04c (Q9P7B3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Putative cation exchanger.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSQPADINQSESSAETITQGRRADRPEETPSSSVYEQNLRFGDFLMPTVGDADATDSLSQSTNDRDIYSPREIDQYTRKVSSRTDPSTSTISNARQHPRNSVSRLSRSSSNVRQQRDIPKQNFKVRPLSPLRGQSPASLRSEESFTLKERQNAINKTRAFGMRLWKPALYKKFRSINRDADIDIHDEPLKRPNTSISNVIWLICFGAPLFLVIFICYIFFTVLSFFNVPDAIVYSKLCRGLMFYLLYPFGQHVRHKVKRLSVRSPAHPIYQTQHSHYDETPTSHHPDPARLNFLSFSFCVNPMNQSLDCNTTPHRRNASSIIYTLMYYLIIAPTLLITSAICMFTIFFVPCARTLWAICRHLRTCPLSLSFRPNLALPLSMDSSDVVLLCVKKAASWKYYKYTIDGIYIIYFDMLALIIPTIFFGFFGSQGHWFTSSVFLFTASLVSIIPLAYFIGMAVASISAQSSMGMGAFINAFFGSVIEVFLYSVALRKGNAGLVEGSVIGSILAGLLLMPGLSMCAGAIRKKFQFFNIKSAGATSTMLLFAVLGAFAPTMLFRIYGPFRLDCEPCGANCQKCTKHYVLENDSLYKNRVLPFTYCCSIMLVLAYAIGLWFTLRTHASHIWQNFTADDISFLKAEEEVGEPVNQDTAGNMSDSSEGGEAVVNGNSQHHHNRDDASSGLSSNGSENESLEHEPTNELPQRPLVNQSQNSHGDDAPNWSRSKSAIILLSATFLYSLIAEILVEHVDTVLDKFAISEKFLGLTLFALVPNTTEFMNAISFALNENIALSMEIGSAYALQVCLLQIPCLMGYSLFQYYRSGDSISFKHLFTMVFPTWDMICVMICVFLLTYVHSEGKSNYFKGSILVLAYLVSMLGFTFFNY
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR2 (EC 3.1.3.95) (Myotubularin-related protein 2) (Phosphatidylinositol-3-phosphate phosphatase) (Q9Z2D1)
Organism: Mus musculus (Mouse)
Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards pho sphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. Binds phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Stabilizes SBF2/MTMR13 at the membranes. Specifically in peripheral nerves, stabilizes SBF2/MTMR13 protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14530412, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}. Early endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14530412}. Cell projection, axon {ECO:0000269|PubMed:23297362}. Endosome membrane {ECO:0000269|PubMed:23297362}; Peripheral membrane protein {ECO:0000305}. Note=Partly associated with membranes (PubMed:14530412, PubMed:23297362). Localizes to vacuoles in hypo-osmotic conditions (PubMed:16399794). {ECO:0000269|PubMed:14530412, ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
Interaction partners:
- Polyphosphoinositide phosphatase
- Myotubularin-related protein 5
- Myotubularin-related protein 12
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Myotubularin-related protein 13
- Phosphatidylinositol-3-phosphatase SAC1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol polyphosphate-4-phosphatase type I A
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
Sequence:
MEKSSSCESLGAQLPAARLPSEDSLSSASTSHSENSVHTKSASAISSDSISTSADNFSPDLRVLREANKLAEMEEPALLPGENIKDMAKDVTYICPFTGAVRGTLTVTSYRLYFKSMERDPPFVLDASLGVISRVEKIGGASSRGENSYGLETVCKDIRNLRFAHKPEGRTRRSIFENLMKYAFPVSNGLPLFAFEYKEVFPENGWKLYDPLLEYRRQGIPNESWRITKINERYELCDTYPALLVVPANIPDEELKRVASFRSRGRIPVLSWIHPESQATVTRCSQPMVGVSGKRSKEDEKYLQAIMDSNAQSHKIFIFDARPSVNAVANKAKGGGYESEDAYQNAELVFLDIHNIHVMRESLRKLKEIVYPTIEETHWLSNLESTHWLEHIKLILAGALRIADKVESGKTSVVVHCSDGWDRTAQLTSLAMLMLDGYYRTIRGFEVLVEKEWLSFGHRFQLRVGHGDKNHADADRSPVFLQFIDCVWQMTRQFPTAFEFNEYFLITILDHLYSCLFGTFLCNSEQQRGKENLPKKTVSLWSYINSQLEDFTNPLYGSYSNHVLYPVASMRHLELWVGYYIRWNPRMKPQEPIHSRYKELLAKRAELQRKVEELQREISNRSTSSSERASSPAQCVTPVQTVV
Protein: Androgen receptor (Dihydrotestosterone receptor) (Nuclear receptor subfamily 3 group C member 4) (P19091)
Organism: Mus musculus (Mouse)
Function: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P10275}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. {ECO:0000250|UniProtKB:P10275}.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- E3 ubiquitin-protein ligase Mdm2
- Nuclear receptor coactivator 4
- Hepatocyte nuclear factor 3-alpha
- Nuclear receptor coactivator 2
- Catenin beta-1
- Lysine-specific histone demethylase 1A
- Nuclear receptor corepressor 1
- Histone-lysine N-methyltransferase EZH2
Sequence:
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREAIQNPGPRHPEAANIAPPGACLQQRQETSPRRRRRQQHTEDGSPQAHIRGPTGYLALEEEQQPSQQQAASEGHPESSCLPEPGAATAPGKGLPQQPPAPPDQDDSAAPSTLSLLGPTFPGLSSCSADIKDILNEAGTMQLLQQQQQQQQHQQQHQQHQQQQEVISEGSSARAREATGAPSSSKDSYLGGNSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYASLLGGPPAVRPTPCAPLPECKGLPLDEGPGKSTEETAEYSSFKGGYAKGLEGESLGCSGSSEAGSSGTLEIPSSLSLYKSGALDEAAAYQNRDYYNFPLALSGPPHPPPPTHPHARIKLENPLDYGSAWAAAAAQCRYGDLGSLHGGSVAGPSTGSPPATTSSSWHTLFTAEEGQLYGPGGGGGSSSPSDAGPVAPYGYTRPPQGLTSQESDYSASEVWYPGGVVNRVPYPSPNCVKSEMGPWMENYSGPYGDMRLDSTRDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGENSNAGSPTEDPSQKMTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ
Protein: DNA polymerase beta (EC 2.7.7.7) (5'-deoxyribose-phosphate lyase) (5'-dRP lyase) (EC 4.2.99.-) (AP lyase) (EC 4.2.99.18) (Q8K409)
Organism: Mus musculus (Mouse)
Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. {ECO:0000250|UniProtKB:P06746}.
Interaction partners:
- DNA ligase 3
- DNA repair protein XRCC1
- DNA ligase 1
- Bifunctional polynucleotide phosphatase/kinase
- Flap endonuclease 1
- DNA repair nuclease/redox regulator APEX1
- Endonuclease 8-like 1 lyase Neil1)
- Poly [ADP-ribose] polymerase 1
- Poly [ADP-ribose] polymerase 2
- Ubiquitin carboxyl-terminal hydrolase 47
Sequence:
MSKRKAPQETLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVTGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEIKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPKLLHRVVEQLQKVHFITDTLSKGETKFMGVCQLPSEKDGKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYREPKDRSE
Protein: Gamma-glutamyl hydrolase 2 (AtGGH2) (EC 3.4.19.9) (Conjugase) (GH) (Gamma-Glu-X carboxypeptidase) (O65355)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cleaves the polyglutamate sidechains of folate polyglutamates in the vacuole. Is important for polyglutamyl tail length determination before vacuolar exit. Plays a role on folate stability and intracellular folate content. Has endopeptidase activity against 4-amino-10-methylpteroyl penta-, tetra-, tri- and di-gamma-L-glutamate substrates and is responsible for the production of folic acid, also called pteroylglutamic acid (PteGlu) from teroylpolyglutamates.
Subcellular location: Vacuole {ECO:0000305|PubMed:21070406}. Secreted, extracellular space {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Note=Extracellular or cell-wall bound.
Interaction partners:
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Folylpolyglutamate synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Probable ubiquitin-conjugating enzyme E2 24
- Probable gamma-glutamyl hydrolase 3
- Gamma-glutamyl hydrolase 1
- GTP cyclohydrolase 1
Sequence:
MWSYVWLPLVALSLFKDSIIMAKAATILLPSQTGFDISRSPVCSAPDPNLNYRPVIGILSHPGDGASGRLSNATDASSIAASYVKLAESGGARVIPLIFNEPEEILFQKLELVNGVILTGGWAKEGLYFEIVKKIFNKVLERNDAGEHFPIYAICLGFELLTMIISQNRDIFEKMDARNSASSLQFVENVNIQGTIFQRFPPELLKKLGTDCLVMQNHRFGISPQSFEGNIALSNFFKIVTTCVDDNGKVYVSTVQSTKYPVTGFQWHPEKNAFEWGSSKIPHSEDAIQVTQHAANHLVSEARKSLNRPESKKVLSNLIYNYKPTYCGYAGIGYDEVYIFTQQRSLL
Protein: Prostaglandin E synthase (EC 5.3.99.3) (Glutathione peroxidase PTGES) (EC 1.11.1.-) (Glutathione transferase PTGES) (EC 2.5.1.18) (Microsomal glutathione S-transferase 1-like 1) (MGST1-L1) (Microsomal prostaglandin E synthase 1) (MPGES-1) (p53-induced gene 12 protein) (O14684)
Organism: Homo sapiens (Human)
Function: Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway. Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli. Plays a key role in inflammation response, fever and pain (By similarity). Catalyzes also the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively.
Subcellular location: Membrane {ECO:0000269|PubMed:10377395, ECO:0000269|PubMed:16439136, ECO:0000269|PubMed:18682561, ECO:0000269|PubMed:27684486}; Multi-pass membrane protein {ECO:0000303|PubMed:18682561}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10869354}. Note=Colocalizes with PTGS1/COX-1 and PTGS2/COX-2 in the perinuclear compartment. {ECO:0000269|PubMed:10869354}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 2
- Prostaglandin G/H synthase 1
- Prostacyclin synthase
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Carbonyl reductase 1])
- Carbonyl reductase 3
- Prostaglandin E2 receptor EP4 subtype
Sequence:
MPAHSLVMSSPALPAFLLCSTLLVIKMYVVAIITGQVRLRKKAFANPEDALRHGGPQYCRSDPDVERCLRAHRNDMETIYPFLFLGFVYSFLGPNPFVAWMHFLVFLVGRVAHTVAYLGKLRAPIRSVTYTLAQLPCASMALQILWEAARHL
Protein: Fmp45p (A0A1D8PR25)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- RRM domain-containing protein
- Hgt19p
Sequence:
MRALNIIPVFFLVGSVLLLILTIINGAGTSSVLGKFYWSETDTSGLTGVPYNKTRWTFYRMCGVDHNKNAHCGKSQAAFPYSPEDNFGRNSGIPQNFIDDRDTYYYLSRVGWAFILVGLFFGVAAMVAAPLNFCYFVAGIVGSTTAFVSLLFTITAACCITAAHTKGRREWNRAGFPTVLGAKAFGILWTAVACLLISFVSLVVLTCLSRTSTRRRNRGVGVTNGSEVTPRGEQETYAKESSGEIPRGEYESGNHPVTGPGEGERLSNASKFRFFRVKRAKSEDV