wanglab/gogpt-training-data huggingface dataset:
Protein: Abscisic acid receptor PYL9 (PYR1-like protein 2) (OsPYL2) (PYR1-like protein 9) (OsPYL9) (Regulatory components of ABA receptor 9) (Q5Z8S0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in abscisic acid (ABA) signaling during seed germination and abiotic stress response. Acts as positive regulator of ABA-mediated inhibition of seed germination, and tolerance to drought and cold stresses. Inhibits the activity of the protein phosphatases PP2C06 and PP2C09 when activated by abscisic acid (ABA).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26362328}. Nucleus {ECO:0000269|PubMed:26362328}.
Interaction partners:
- Probable protein phosphatase 2C 6
- Protein phosphatase 2C 53
- Protein phosphatase 2C 50
- Probable protein phosphatase 2C 30
- Probable protein phosphatase 2C 68
- Probable protein phosphatase 2C 8
- protein-serine/threonine phosphatase
- Probable protein phosphatase 2C 49
- Protein phosphatase 2C 51
- protein-serine/threonine phosphatase
Sequence:
MEAHVERALREGLTEEERAALEPAVMAHHTFPPSTTTATTAAATCTSLVTQRVAAPVRAVWPIVRSFGNPQRYKHFVRTCALAAGDGASVGSVREVTVVSGLPASTSTERLEMLDDDRHIISFRVVGGQHRLRNYRSVTSVTEFQPPAAGPGPAPPYCVVVESYVVDVPDGNTAEDTRMFTDTVVKLNLQMLAAVAEDSSSASRRRD
Protein: Phospholipid phosphatase 4 (EC 3.1.3.4) (EC 3.6.1.75) (Phosphatidic acid phosphatase type 2 domain-containing protein 1A) (Q5VZY2)
Organism: Homo sapiens (Human)
Function: Magnesium-independent phospholipid phosphatase with broad substrate specificity. Preferentially catalyzes the conversion of diacylglycerol pyrophosphate into phosphatidate but can also act on phosphatidate and lysophosphatidate. Phospholipid phosphatases are involved in both the synthesis of lipids and the degradation or generation of lipid-signaling molecules like diacylglycerol.
Subcellular location: Membrane {ECO:0000305|PubMed:17590538}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Phosphatidate phosphatase LPIN1
- Phospholipid phosphatase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Patatin-like phospholipase domain-containing protein 2
- 1-acylglycerol-3-phosphate O-acyltransferase PNPLA3
- 2-acylglycerol O-acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Phospholipase D1
Sequence:
MRELAIEIGVRALLFGVFVFTEFLDPFQRVIQPEEIWLYKNPLVQSDNIPTRLMFAISFLTPLAVICVVKIIRRTDKTEIKEAFLAVSLALALNGVCTNTIKLIVGRPRPDFFYRCFPDGVMNSEMHCTGDPDLVSEGRKSFPSIHSSFAFSGLGFTTFYLAGKLHCFTESGRGKSWRLCAAILPLYCAMMIALSRMCDYKHHWQDSFVGGVIGLIFAYICYRQHYPPLANTACHKPYVSLRVPASLKKEERPTADSAPSLPLEGITEGPV
Protein: ICP27 (I3TCB5)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
Interaction partners:
Sequence:
MVLVCAGGGAGPPPGGRNEEGFGRAGPGTTGIRTSTTRPVVVCSRVPTTVTLLCLSPIRARSLATGAPPPEAISDTPAPTAADSPVMATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLASDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGPRTRGVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTAAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF
Protein: Nuclear factor kappaB subunit p65 (RELA proto-oncogene, NF-kB subunit) (V-rel reticuloendotheliosis viral oncogene homolog A (Avian)) (Q7TQN4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Transcription factor RelB
- NF-kappa-B inhibitor alpha
- NF-kappa-B inhibitor beta
- Nuclear factor NF-kappa-B p105 subunit
- Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2, p49/p100, isoform CRA_a.
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Histone lysine acetyltransferase CREBBP
- REL proto-oncogene, NF-kB subunit
- NF-kappa-B inhibitor epsilon
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPPRRIAVPSRGPTSVPKPAPQPYAFSTSLSTINFDEFSPMVLPPGQISNQALALAPSSAPVLAQTMVPSSAMVPSLAQPPAPVPVLAPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNNTDPGVFTDLASVDNSEFQQLLNQGVAMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPATLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS
Protein: Multiprotein-bridging factor 1 (Q6FJN0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Transcriptional coactivator that stimulates transcriptional activity by bridging regulatory proteins and TBP, thereby recruiting TBP to promoters occupied by DNA-binding regulators.
Interaction partners:
- Small ribosomal subunit protein uS3
- 40S ribosomal protein S30
- Small ribosomal subunit protein uS10
- Candida glabrata strain CBS138 chromosome D complete sequence
- Small ribosomal subunit protein uS5
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Small ribosomal subunit protein eS21
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MSDWESHTVIGQKARAGGSGPRANVARTQGQINAARRQGLVLSVDKKYGTANTKGDAEGQRLTKVDRETDIVKPKKLDANVGKTIARVRTEKKMSQKDLATKINEKPTVINDYEAGRAIPNQQVLGKMERALGVKLRGKAIGEPLGGPKKK
Protein: Enoyl-CoA delta isomerase 1, mitochondrial (MECI) (EC 5.3.3.8) (3,2-trans-enoyl-CoA isomerase) (Delta(3),Delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Dodecenoyl-CoA isomerase) (P23965)
Organism: Rattus norvegicus (Rat)
Function: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11781327}.
Interaction partners:
- Enoyl-CoA delta isomerase 2
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal bifunctional enzyme
- 3-ketoacyl-CoA thiolase, mitochondrial
- 3-ketoacyl-CoA thiolase A, peroxisomal
- 2,4-dienoyl-CoA reductase [
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Delta
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MALAAARRVLLQAGSRLGRRGAVDGARRFSNKRVLVEKEGEAGIAVMKFKNPPVNSLSLEFLTEFVISLEKLENDKSIRGVILTSERPGIFSAGLDLMEMYGRNPAHYAEYWKAVQELWLRLYLSNLTLISAINGASPAGGCLMALTCDYRIMADNSKYTIGLNESLLGIVAPFWLKDNYVNTIGHRAAERALQLGTLFPPAEALKVGLVDEVVPEDQVHSKARSVMAKWFTIPDHSRQLTKSMMRKATADNLIKQREADIQNFTSFISRDSIQKSLHVYLEKLKQKKG
Protein: Protein LIAT1 (Ligand of ATE1 protein) (Q810M6)
Organism: Mus musculus (Mouse)
Function: May be involved in ATE1-mediated N-terminal arginylation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:33443146}. Cytoplasm {ECO:0000269|PubMed:33443146}. Note=Shuttles between the cytoplasm and nucleoplasm, a significant portion localizes to the nucleolus. {ECO:0000269|PubMed:33443146}.
Interaction partners:
Sequence:
MAGRGGTGAAEYGEEGEEEEEEEAREGGAEGSPGSKLPPIVGTASELAKRKVKKKKKKKKTKGSGKGDADKHHSRGRKNQPLSSSFHDILNPHKDHGLRAEPRDKEENRQTLPYSYSINHPCFAEIEDTLSSQINESLRWDGILTDPEAEKERIRIYKLNRRKRYRLMALKCFHSDPCVEESVENLPYLSDKDCSPCSKQPSSKGDHAHSYFEASKLLHPELATTVAE
Protein: Interleukin-31 (IL-31) (Q6EBC2)
Organism: Homo sapiens (Human)
Function: Activates STAT3 and possibly STAT1 and STAT5 through the IL31 heterodimeric receptor composed of IL31RA and OSMR. May function in skin immunity. Enhances myeloid progenitor cell survival in vitro (By similarity). Induces RETNLA and serum amyloid A protein expression in macrophages (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Oncostatin-M-specific receptor subunit beta
- Interleukin-31 receptor subunit alpha
- Oncostatin-M
- Interleukin-13
- Tyrosine-protein kinase JAK1
- Interleukin-17A
- Thymic stromal lymphopoietin
- Interferon gamma
- Interleukin-4
- Interleukin-11
Sequence:
MASHSGPSTSVLFLFCCLGGWLASHTLPVRLLRPSDDVQKIVEELQSLSKMLLKDVEEEKGVLVSQNYTLPCLSPDAQPPNNIHSPAIRAYLKTIRQLDNKSVIDEIIEHLDKLIFQDAPETNISVPTDTHECKRFILTISQQFSECMDLALKSLTSGAQQATT
Protein: Zinc finger and BTB domain-containing protein 1 (Q9Y2K1)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Represses cAMP-responsive element (CRE)-mediated transcriptional activation. In addition, has a role in translesion DNA synthesis. Requires for UV-inducible RAD18 loading, PCNA monoubiquitination, POLH recruitment to replication factories and efficient translesion DNA synthesis. Plays a key role in the transcriptional regulation of T lymphocyte development (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21706167}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20797634}. Note=Localized in dot-like structures in the nucleus (PubMed:21706167). Colocalized with SMRT in nuclear bodies (PubMed:20797634). The sumoylated form is preferentially located in the nucleoplasm outside the nuclear bodies (PubMed:20797634). {ECO:0000269|PubMed:20797634, ECO:0000269|PubMed:21706167}.
Interaction partners:
Sequence:
MAKPSHSSYVLQQLNNQREWGFLCDCCIAIDDIYFQAHKAVLAACSSYFRMFFMNHQHSTAQLNLSNMKISAECFDLILQFMYLGKIMTAPSSFEQFKVAMNYLQLYNVPDCLEDIQDADCSSSKCSSSASSKQNSKMIFGVRMYEDTVARNGNEANRWCAEPSSTVNTPHNREADEESLQLGNFPEPLFDVCKKSSVSKLSTPKERVSRRFGRSFTCDSCGFGFSCEKLLDEHVLTCTNRHLYQNTRSYHRIVDIRDGKDSNIKAEFGEKDSSKTFSAQTDKYRGDTSQAADDSASTTGSRKSSTVESEIASEEKSRAAERKRIIIKMEPEDIPTDELKDFNIIKVTDKDCNESTDNDELEDEPEEPFYRYYVEEDVSIKKSGRKTLKPRMSVSADERGGLENMRPPNNSSPVQEDAENASCELCGLTITEEDLSSHYLAKHIENICACGKCGQILVKGRQLQEHAQRCGEPQDLTMNGLGNTEEKMDLEENPDEQSEIRDMFVEMLDDFRDNHYQINSIQKKQLFKHSACPFRCPNCGQRFETENLVVEHMSSCLDQDMFKSAIMEENERDHRRKHFCNLCGKGFYQRCHLREHYTVHTKEKQFVCQTCGKQFLRERQLRLHNDMHKGMARYVCSICDQGNFRKHDHVRHMISHLSAGETICQVCFQIFPNNEQLEQHMDVHLYTCGICGAKFNLRKDMRSHYNAKHLKRT
Protein: Transcription factor cbf12 (C-promoter element-binding factor-like protein 12) (O74412)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcription factor which function may be to trigger the increase of adhesion at stationary phase, possibly by counteracting or replacing cbf11 at the respective promoters. May also play a cbf11-antagonistic role in the regulation of a number of other important processes such as extracellular material production, colony morphogenesis, ploidy maintenance, or meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:19101542}.
Interaction partners:
- Transcription factor cbf11
- Zinc finger protein zfs1
- Uncharacterized transcriptional regulatory protein C2H10.01
- Triacylglycerol lipase ptl1
- Galactose-specific cell agglutination protein gsf2
- Sphingosine N-acyltransferase lag1
- Uncharacterized transcriptional regulatory protein C15D4.02
- Uncharacterized transcriptional regulatory protein C530.11c
- Putative cell agglutination protein pfl3
- GTPase-GDP dissociation stimulator arz1
Sequence:
MSPNVQKRPSSEDIKTQEFYDSTRNIRRVATAIGSINANLESPQLYSLAKSTSLQEPVRIYGDSVSPAISSSKAHSTSSVSPYYSEKNESQALNADGTAFANPSFHSFGLPQEDSQDNTQTYSTPYTTMNPSNEMHPYPPATFENNYSVLPDHSSQPNAYSFTGSNILPTQSPSLNQMQDYQNLQQNGSSNTTIPSFSSQHDLSQGLTHQPVPNHDEYAFSYPYELQRKPLIPAHPVPSFRPTSALKVNMNSNVPSSDSVRNSSPNQYYASTSKQSIPSQSQNLQPPQKASVLGTVNNYRQYQNSFISLNDYQAAQSNISSPSSRFPTPYSPSVPFGTYQEKEKSYSQDHAELSYYQQSPSMMPPYDRSSVYFQQPLSRTDVPNQSFQQYPTTVDGGSMIPNLYPTSAEQMGLYPQDSQNKDTYPKSLVNRPSSAVCEPARNDSIPMMVYSQPVTIEQRIQYVLSNCHCLSAFYLCMPSLCQKSYGTERRYLCPPIVLYLLGTTWLNNVTDNLKISAQTLEDKDNPKFAKNIFYYNADGALISPETDIAKSTYQLTNYNENTNFDSFPVWGNALLKTIYYTGQGKNDGFGRSTFLQLSVQSKTKYFKLENLRLGVISKPSQKRALMKVSDMSIRHGDCVCLFNRYRAQHNNALFLGTSNVQRAISKVSLNMKYNSNYFPTTDAPNDAENEGAGLAMANNLWEPFYIFSVDELNKGNNSNPSDSRSKVLCSNMVIILVSKITGVQSPPLILKKHDNWKVSLSSRAPSEAINCLSKLAFQCHETKRFLYIDEKQSSEISFTSGELEYSDPNDPTKATHSVLPWSAMWSIISTQSVRTMFYNEPIHQNAFHVVPSMPFVKFIRLDENSMFHIYGTGFANDVQIWMAYTRCEVKSINAFKPDTTLPPDIISDSRFSSRVYACTANLIELICEIPVCMFEPTVELSPILLFQYETLFHSGYKWPLESH
Protein: Probable serine/threonine-protein kinase drkA (EC 2.7.11.1) (Receptor-like kinase 1) (Receptor-like kinase A) (Vesicle-associated receptor tyrosine kinase-like protein 1) (Q54H46)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKKLPFLIIIIYIFLILISISSSIDYNYNNDIDNNNNNIINRNKNKNKNNLYNNKVIIKNDDNDDEINNKFKIRLDDNEDQDIYNEYHFLSKVHNRLAFNIFGSSSENSGSGSNSNSNSKNTDSSTGPTPSPISINGTLNSTATVYWSGGKSSCKSVNCTEEGFSTGDSYACSYEITPTYQRGQWEKGVKYFKDPLPKSILTSQVVGVSFVINGVVGCTPLKQELTTIEFLIQDVQVGQTISTNRSDDCSCGICYKDYEILPQSYDLLGYNKSGLNKVQLLLLDNSICATSLDIIFYYHPSTIPPTPTPTPSKPTISLLKKYLIIGFSIVGGLLIIGGCFLLIRNRYRSSGYYKPDKNDYTQIKDGKDIDIHQIKIGVRIGKGNYGEVYLGTWRGSQVAVKKLPAHNINENILKEFHREINLMKNLRHPNVIQFLGSCLIPPDICICTEYMPRGSLYSILHDQALQLQWSLLIKMMIDAAKGVIYLHNSTPVILHRDLKSHNLLVDENWKVKVADFGLSTIEQQGATMTACGTPCWTSPEVLRSQRYTEKADVYSFGIILWECATRQDPYFGIPPFQVIFAVGREGMRPPVPQNGPPKYIQLLIDCLNENPSHRPTMEQCLERLESIDSSGYSDLQYVRQQL
Protein: Zinc finger and SCAN domain-containing protein 30 (ZNF-WYM) (Zinc finger protein 397 opposite strand) (Zinc finger protein 397OS) (Q86W11)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 397
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger and SCAN domain-containing protein 20
- Zinc finger protein 444
- Zinc finger protein 232
Sequence:
MSGEATVLAYHAPEEQEGLLVVKVEEENYVLDQDFGLQENPWSQEVFRQKFRQFSYSDSTGPREALSRLRELCCQWLRPEVHSKEQILELLMLEQFLAILPEELQAWLREHRPENGEEAVTMLEELEKELEEPRQQDTTHGQEMFWQEMTSTGALKSLSLNSPVQPLENQCKTETQESQAFQERDGRMVAGKVLMAKQEIVECVASAAMISPGKLPGETHSQRIAEEALGGLDNSKKQKGNAAGNKISQLPSQDRHFSLATFNRRIPTEHSVLESHESEGSFSMNSNDITQQSVDTREKLYECFDCGKAFCQSSKLIRHQRIHTGERPYACKECGKAFSLSSDLVRHQRIHSGEKPYECCECGKAFRGSSELIRHRRIHTGEKPYECGECGKAFSRSSALIQHKKIHTGDKSYECIACGKAFGRSSILIEHQRIHTGEKPYECNECGKSFNQSSALTQHQRIHTGEKPYECSECRKTFRHRSGLMQHQRTHTRV
Protein: Probable methyltransferase TARBP1 (EC 2.1.1.-) (TAR RNA-binding protein 1) (TAR RNA-binding protein of 185 kDa) (TRP-185) (Q13395)
Organism: Homo sapiens (Human)
Function: Probable S-adenosyl-L-methionine-dependent methyltransferase which methylates RNA molecules such as tRNAs.
Interaction partners:
- T-complex protein 1 subunit delta
- RNA-binding protein 8A
- Exosome RNA helicase MTR4
- Small subunit processome component 20 homolog
- Elongation factor 1-alpha 1
- tRNA
- tRNA
- U3 small nucleolar RNA-associated protein 4 homolog
- Pseudouridylate synthase TRUB1
- Protein RRP5 homolog
Sequence:
MEWVLAEALLSQSRDPRALLGALCQGEASAERVETLRFLLQRLEDEEARGSGGAGALPEAAREVAAGYLVPLLRSLRGRPAGGPDPSLQPRHRRRVLRAAGAALRSCVRLAGRPQLAAALAEEALRDLLAGWRAPGAEAAVEVLAAVGPCLRPREDGPLLERVAGTAVALALGGGGDGDEAGPAEDAAALVAGRLLPVLVQCGGAALRAVWGGLAAPGASLGSGRVEEKLLVLSALAEKLLPEPGGDRARGAREAGPDARRCWRFWRTVQAGLGQADALTRKRARYLLQRAVEVSAELGADCTCGPQEGNGPSLFWWSERKKDELLKFWENYILIMETLEGNQIHVIKPVLPKLNNLFEYAVSEENGCWLFHPSWHMCIYKRMFESENKILSKEGVIHFLELYETKILPFSPEFSEFIIGPLMDALSESSLYSRSPGQPIGSCSPLGLKLQKFLVTYISLLPEEIKSSFLLKFIRKMTSRHWCAVPILFLSKALANVPRHKALGIDGLLALRDVIHCTMITHQILLRGAAQCYLLQTAMNLLDVEKVSLSDVSTFLMSLRQEESLGRGTSLWTELCDWLRVNESYFKPSPTCSSIGLHKTSLNAYVKSIVQEYVKSSAWETGENCFMPDWFEAKLVSLMVLLAVDVEGMKTQYSGKQRTENVLRIFLDPLLDVLMKFSTNAYMPLLKTDRCLQLLLKLLNTCRLKGSSAQDDEVSTVLQNFFMSTTESISEFILRRLTMNELNSVSDLDRCHLYLMVLTELINLHLKVGWKRGNPIWRVISLLKNASIQHLQEMDSGQEPTVGSQIQRVVSMAALAMVCEAIDQKPELQLDSLHAGPLESFLSSLQLNQTLQKPHAEEQSSYAHPLECSSVLEESSSSQGWGKIVAQYIHDQWVCLSFLLKKYHTLIPTTGSEILEPFLPAVQMPIRTLQSALEALTVLSSDQVLPVFHCLKVLVPKLLTSSESLCIESFDMAWKIISSLSNTQLIFWANLKAFVQFVFDNKVLTIAAKIKGQAYFKIKEIMYKIIEMSAIKTGVFNTLISYCCQSWIVSASNVSQGSLSSAKNYSELILEACIFGTVFRRDQRLVQDVQTFIENLGHDCAANIVMENTKREDHYVRICAVKFLCLLDGSNMSHKLFIEDLAIKLLDKDELVSKSKKRYYVNSLQHRVKNRVWQTLLVLFPRLDQNFLNGIIDRIFQAGFTNNQASIKYFIEWIIILILHKFPQFLPKFWDCFSYGEENLKTSICTFLAVLSHLDIITQNIPEKKLILKQALIVVLQWCFNHNFSVRLYALVALKKLWTVCKVLSVEEFDALTPVIESSLHQVESMHGAGNAKKNWQRIQEHFFFATFHPLKDYCLETIFYILPRLSGLIEDEWITIDKFTRFTDVPLAAGFQWYLSQTQLSKLKPGDWSQQDIGTNLVEADNQAEWTDVQKKIIPWNSRVSDLDLELLFQDRAARLGKSISRLIVVASLIDKPTNLGGLCRTCEVFGASVLVVGSLQCISDKQFQHLSVSAEQWLPLVEVKPPQLIDYLQQKKTEGYTIIGVEQTAKSLDLTQYCFPEKSLLLLGNEREGIPANLIQQLDVCVEIPQQGIIRSLNVHVSGALLIWEYTRQQLLSHGDTKP
Protein: Jhy protein (Juvenile hydrocephalus protein) (E9Q793)
Organism: Mus musculus (Mouse)
Function: Required for the normal development of cilia in brain ependymal cells lining the ventricular surfaces.
Interaction partners:
Sequence:
MNKYKPVPKLSSQSPVHHTNLRIPPSGRPFKKEDFLNLISKDSLESDSESLPQEAKSWSDIKDQIQDKDMEPDSLEEDSPSETEEAVNRKAAHNTNREDLSAHDAGVNHSQHQVEDKYSDLRYDPNWKNKREEGQPLAGEALPGSADSSSENLPLAPLYPSREPSMGLSAGKGKEKKSPQSEASLLGSEFLSPKYERSTRQNGFFSELSDSDQEEKSSGLSQYLKSSSSHNDVFLPGSRGPRRRKSKQYFVEKNKLTLGLPMPKTDSYLQLHNKKRGETRLEQISYPVRDTDKMTVQNDKEVENTFMDPEDKWHQRAKQLKNYQEHLSQYEDTKSGNVPRGQSSDAANGQQPSRRTAKARVRKQRKHQKGLKSLGTKELVVSQNNQNNPFQQPQNQRQTADASAKHELAAQTNASNPNLQDARTLTHNPKVTSDSFVSPKQALDRALYKNSISGLNANKRRGHRREEERILYQPQPIYVFSDTHLQDFNELPHRHESPSQRAPQSDHHMNTHRSTKTKKPAKQPQAETKYKNIEMLWKFHSSSDMEPASASPDSRLAQIMEQHQQALMQLAEVQPSEGSLASIILPPILSRVESESQLNSERSHRHQVKMARSNSEGYLLQLERGKRHRKRSSTKSSKLKGYQKRDVKLGGLGPDFASVRDKMQMLMQQKEYAQQVKDYNMKALSILSKPQTSKTESKSAISRKKALDYAKTIPKPKPPNLPDQTAKKTKNSRHSEKEGGLPEISLLEILQSRHEREKQAVAAFKVLHIV
Protein: Mitochondrial ribosomal protein S23 (Q8IP62)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS9m
- GEO10172p1
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS7m
- Large ribosomal subunit protein mL66
- Mitochondrial ribosomal protein S21, isoform A
- 28S ribosomal protein S14
- LD06441p
Sequence:
MAQSRLEKIGTIFTRVQGLLRGGAMKTEDKPIWYDVYAAFPPKLEPRFDRPAPEIPVRQIFYAEDVVRAKLHKENKPQETISLFDHRRSTQSQQFVQIYQDLKGQGALDEQRIYETALDLLAEQRQQARLETTPEECLPEQDSESKSQLLSDFKEAVVSQQITSSPAPPAPKGKKEANVGINIDSLFKD
Protein: Histone H3 variant (Q387X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Histone H4
- Histone H4
- Histone H2A
- Histone H2A
- SET domain-containing protein
- ATP synthase subunit beta
- Histone H2B
- SET domain-containing protein
- Uncharacterized protein
- Histone H2B
Sequence:
MAQMKKITPRPVRPKSVASRPIQSVARAPVKKVENTPPQKRHHRWRPGTVALREIRRLQSSTDFLIQRAPFRRFLREVVSNLKDSYRMSAACVDAIQEATETYITSVFMDANLCTLHANRVTLFPKDIQLALKLRGERN
Protein: Coiled-coil domain containing 183 (HCG2039834, isoform CRA_c) (G5E9W6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRHSETDVEEQTQELKTITQLQEQCRALQIQGVKENMDQNKATLALLRSNIRRGAQDWALAKKYDQWTISKACGKNLPLRLAHCRSTMEVVREKLRKYVFDRVNMHNLLIHLVRRRGQKLESMQLELDSLRSQPDASKEELRLLQIIRQLENNIEKTMIKIITSQNIHLLYLDLLDYLKTVLAGYPIELDKLQNLVVNYCSELSDMKIMSQDAMMITDEVKEHEAKGGVLHRGAPGKGEPAQPAEEADRQDPHEGDQREVPPGPDGLGLPLEPDEHGDPEIEEKRDLHSRNGIPVGRDCCGGEGQECCTVLSRLGHH
Protein: 40S ribosomal protein S8 (Q57YL6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribosomal protein S19, putative
- 60S ribosomal protein L4
- 60S ribosomal protein L27, putative
- 60S ribosomal protein L18a
- 60S ribosomal protein L7a
- Elongation factor 2
- 40S ribosomal protein S15a, putative
- 60S ribosomal protein L2, putative
- Large ribosomal subunit protein uL5
- Ribosomal protein
Sequence:
MGIVRSRLHKRKITGGKTKIHRKRMKAELGRLPANTKLGPRRVSPVRARGGNFKLRGLRLDTGNFAWGTEASAQRARILDVVYNATSNELVRTKTLVKNCIVVVDAAPFRLWYAKHYGIDLGASKSKKATQKSTEKKSKKSAHAAVEKYDVKKASSKLKRKWEYRRKHHKIEKALADQLREGRLLARITSRPGQTGRADGALLEGAELQFYLKKLDKKKR
Protein: Prostaglandin reductase 1 (PRG-1) (15-oxoprostaglandin 13-reductase) (EC 1.3.1.48) (Dithiolethione-inducible gene 1 protein) (D3T-inducible gene 1 protein) (DIG-1) (Leukotriene B4 12-hydroxydehydrogenase) (NAD(P)H-dependent alkenal/one oxidoreductase) (EC 1.3.1.74) (P97584)
Organism: Rattus norvegicus (Rat)
Function: NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX) (By similarity). Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha (By similarity). Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). Plays a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one. Inactivates 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q29073}.
Interaction partners:
Sequence:
MVQAKTWTLKKHFEGFPTDSNFELRTTELPPLNNGEVLLEALFLSVDPYMRVAAKKLKEGDSMMGEQVARVVESKNSAFPTGTIVVALLGWTSHSISDGNGLRKLPAEWPDKLPLSLALGTVGMPGLTAYFGLLDICGLKGGETVLVNAAAGAVGSVVGQIAKLKGCKVVGTAGSDEKVAYLKKLGFDVAFNYKTVKSLEEALRTASPDGYDCYFDNVGGEFSNTVILQMKTFGRIAICGAISQYNRTGPCPPGPSPEVIIYQQLRMEGFIVTRWQGEVRQKALTDLMNWVSEGKIRYHEYITEGFEKMPAAFMGMLKGDNLGKTIVKA
Protein: Uncharacterized protein YHR127W (P38833)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Mitotic spindle-associated protein SHE1
- Uncharacterized protein YHR202W
- RNA annealing protein YRA1
- Uncharacterized acyltransferase YDR018C
Sequence:
MARNRTTSKKNVQSKRLIDRVVPMDKIKKVGVAKKKTVEHTKEGFSVVNGKLVSSNDVGVLLREAQGAIDKRTNVSQRNRKKGIKNNRPHKDINSSPDWGNAHRGTDWQSEKANGMNRAKNSRNFTTNIKLQRQHFGEEIQGGSQLVISTNSDASDKLLMLFNLTLGVNQENLKNVLENISQVQIAQIRVRDLPSGSATAKVRLAYPTTQSLEKVRKLFHGALVDGRRIQVVIASDESSHLSY