wanglab/gogpt-training-data huggingface dataset:
Protein: Protein NLRC5 (C3VPR6)
Organism: Mus musculus (Mouse)
Function: Probable regulator of the NF-kappa-B and type I interferon signaling pathways. May also regulate the type II interferon signaling pathway. Plays a role in homeostatic control of innate immunity and in antiviral defense mechanisms.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Interferon-induced helicase C domain-containing protein 1
- Antiviral innate immune response receptor RIG-I
- NLR family CARD domain-containing protein 4
- NACHT, LRR and PYD domains-containing protein 6
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 1a
- Interferon regulatory factor 1
- Caspase-1
Sequence:
MDAESIRLNNENLWAWLVRLLSKNPEWLSAKLRSFLPTMDLDCSYEPSNPEVIHRQLNRLFAQGMATWKSFINDLCFELDVPLDMEIPLVSIWGPRDEFSKQLGAGEESCPGPQLYHGAKRPFQSYGSSPRRKNSKKQQLELAKKYLKLLKTSAQQWHGGVCPGAWLTPHSPQTYIPPVLQWSRATAPLDAQEGATLGDPEAADNIDVSIQDLFSFKAHKGPRVTVLLGKAGMGKTTLAYRLRWRWAQGQLDRFQALFLFEFRQLNMITQLPTLPQLLFDLYLMPESEPDAVFQYLKENAQEVLLIFDGLDEALHADSVGTDNAGSALTLFSELCHGNLLPGCWVMTTSRPGKLPSCVPTEAATVHMWGFDGLRVEKYVTCFFSDLLSQELALKEMRTNARLRGMCAIPALCTVTCFCLRRLLPGSSPGQSAALLPTITQLYLQMVETFSPSETLLDTSILGFGKVALRGLDTGKVVFSVEDISPQLMSFGAVHSLLTSFCIHTRPGHEEIGYAFVHLSLQEFFAALYLMASHTVDKDTLVEYVTLNSHWVLRTKGRLGLSDHLPAFLAGLASHTCHMFLCQLAQQDRAWVGSRQAAVIQVLRKLASRKLTGPKMIELYHCVAETQDLELARFTAQSLPSRLSFHNFPLTHADLAALANILEHRDDPIHLDFDGCPLEPHCPEALVGCGQVENLSFKSRKCGDAFAEALCRSLPTMGSLKTLGLTGSRITAQGISHLIQTLPLCSQLEEVSLHDNQLKDPEVLSLVELLPSLPKLQKLDLSRNSFSRSILLSLVKVAITCPTVRKLQVRELDLIFYLSPVTETATQQSGASDVQGKDSLKEGQSRSLQLRLQKCQLRIRDAEALVELFQKSPQLEEVNLSGNHLEDDGCRLVAEAASQLHIAQKLDLSDNGLSQTGVTYVLKAMSTCGTLEDLHISLLNNTVVLTFAQEPREQEGSCKGRAPLISFVSPVTSELSQRSRRIRLTHCGFLAKHTETLCEALRASCQTHNLDHLDLSDNSLGGKGVILLTELLPGLGPLKSLNLSRNGLSMDAVFSLVQCLSSLQWVFHLDVSLESDCIFLRGAGTSRDALEPKFQTGVQVLELSQRYTSRSFCLQECQLEPTSLTFLCATLEKSPGPLEVQLSCKSLSDDSLKILLQCLPQLPQLSLLQLRHTVLSSRSPFLLADIFNLCPRVRKVTLRSLCHAVLHFDSNEEQEGVCCGFPGCSLSQEHMETLCCALSKCNALSQLDLTDNLLGDIGLRCLLECLPQLPISGWLDLSHNNISQEGILYLLETLPSYPNIQEVSVSLSSEQIFRMCFSKKEGAGTSLRLCECSFSPEQVSKLASSLSQAQQLTELWLTKCHLDLPQLTMLLNLVNRPTGLLGLRLEEPWVDSVSLPALMEVCAQASGCLTELSISEIQRKLWLQLEFPHQEGNSDSMALRLAHCDLETEHSHLMIQLVETYARLQQLSLSQVSFNDNDGTSSKLLQNILLSSCELKSFRLTFSQVSTKSLTHLAFGLGHCHHLEELDFSNNSLREEDTELLMGALQGTCRLKKLHLSFLPLGASSLALLIQGLSRMTLLQDLCLSHNQIGDVGTQCLAAILPKLPELRKFDLSHNQIGDVGTQCLAAILPKLPELRKFNLSHNQIGHVGTQCLAAILPKLPELRKFDLSRNQIGDVGTQCLAAILPKLPELRKFDLSGNRIGPAGGVQLVKSLTHFEHLEEIKLGNNALGEPTALELAQRLPPQLRVLCLPSSHLGPEGALGLAQALEQCPHIEEVSLAENNLAGGVPRFSKRLPLLRQIDLEFCKIEDQAARHLAANLTLFPALEKLLLSGNLLGDEVAAELAQVLPQMGQLKKVNLEWNRITARGAQLLAQGLVQGSCVPVIRLWNNPILNDVAQSLQSQEPRLDFSITDQQTL
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9VY98)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
- Distracted, isoform B
Sequence:
MGNFVSRQNAAVEEADPSTNNAYKYPPRMGNFFGTHFIMGGERFDTPQPESYLFGENADLNFLGNRPTAFPYPPPQANEPTKTLKSLVNIRKESVRFVKTMNDKKLGGVLEKPKMKEIDRDLDLDKEKSNVTIEDVDGNVLCSMGLGGGDADMTPPPPPCSYNIEFTFDSDAKCAITIYYFCSEDVSPSGVTLVPREGLTSETYHYEKGINQCFSQPSHVFNPQQMPEDELGYSPGREQYPVAIHCVVEEGSDECRQSHTTICVIDHHPENGSYVLRALKQKIFVDGLCYLLQEIYGIENKAVNKTSLDEEIDDHGSECVICMSETRDTLILPCRHLCLCNSCADSLRYQANNCPICRAPFRALLQIRAVQKGISTHVLHQNTPTSAAGEPAPVDVPPGYIPVSLIEALNGPPQYVARARNSEHDVTDSAATVAASTMTSADIKATSPIKSSSQRRPKIKKNASTCTSTSEVGTITNQSGGGNGSSTHSVEIESDPKKSSTATCTSPTLGASTSPEPKQDKLQIVNERKYPRSTAGSGGDGSAGTDDDVDSENEKLSPLLSPGSKSKNVSSKSLKQVVACLEADDDVDNKSSTGDGPTEESSLKKGSSIKRTKPRPELSGSGAPSPAEATAEDSDYYTPEDTQNSILSPLCPTERAKSGDPLGAGSLGNGGLSVGRSAGSVGGQAGVGPVVVGFSSAVKKNLHKKSTSVGNMVGSGSVTTVVDLKSNNVSSLPDMLDSPISGNSASTRSSSDSYSSSSSTKQLLSSNPTTTAANIIVDDKTALQNAVNV
Protein: Eukaryotic translation initiation factor 3 subunit H (eIF3h) (Eukaryotic translation initiation factor 3 subunit 3) (eIF-3-gamma) (eIF3 p40 subunit) (O15372)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit C-like protein
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MASRKEGTGSTATSSSSTAGAAGKGKGKGGSGDSAVKQVQIDGLVVLKIIKHYQEEGQGTEVVQGVLLGLVVEDRLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTYYGSFVTRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLSLKAYRLTPKLMEVCKEKDFSPEALKKANITFEYMFEEVPIVIKNSHLINVLMWELEKKSAVADKHELLSLASSNHLGKNLQLLMDRVDEMSQDIVKYNTYMRNTSKQQQQKHQYQQRRQQENMQRQSRGEPPLPEEDLSKLFKPPQPPARMDSLLIAGQINTYCQNIKEFTAQNLGKLFMAQALQEYNN
Protein: Esterase PHB depolymerase (A0A0H3LGG4)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MGPFMHTGLYVAQSWRDYLGQQPDKLPIARPTIALAAQAFRDEIVLLGLKARRPVSNHRVFERISQEVAAGLEFYGNRGWLEKPSGFFAQPPPLTEVAVRKVKDRRRSFYRIFFDSGFTPHPGEPGSQRWLSYTANNREYALLLRHPEPRPWLVCVHGTEMGRAPLDLAVFRAWKLHDELGLNIVMPVLPMHGPRGQGLPKGAVFPGEDVLDDVHGTAQAVWDIRRLLSWIRSQEEESLIGLNGLSLGGYIASLVASLEEGLACAILGVPVADLIELLGRHCGLRHKDPRRHTVKMAEPIGRMISPLSLTPLVPMPGRFIYAGIADRLVHPREQVTRLWEHWGKPEIVWYPGGHTGFFQSRPVRRFVQAALEQSGLLDAPRTQRDRSA
Protein: Corneodesmosin (S protein) (Q15517)
Organism: Homo sapiens (Human)
Function: Important for the epidermal barrier integrity.
Subcellular location: Secreted. Note=Found in corneodesmosomes, the intercellular structures that are involved in desquamation.
Interaction partners:
- Desmocollin-1
- Desmoglein-1
- Psoriasis susceptibility 1 candidate gene 1 protein
- Loricrin
- Coiled-coil alpha-helical rod protein 1
- Kallikrein-7
- Late cornified envelope protein 2B
- HLA class I histocompatibility antigen, C alpha chain
- Late cornified envelope protein 3D
- Small proline-rich protein 2G
Sequence:
MGSSRAPWMGRVGGHGMMALLLAGLLLPGTLAKSIGTFSDPCKDPTRITSPNDPCLTGKGDSSGFSSYSGSSSSGSSISSARSSGGGSSGSSSGSSIAQGGSAGSFKPGTGYSQVSYSSGSGSSLQGASGSSQLGSSSSHSGNSGSHSGSSSSHSSSSSSFQFSSSSFQVGNGSALPTNDNSYRGILNPSQPGQSSSSSQTFGVSSSGQSVSSNQRPCSSDIPDSPCSGGPIVSHSGPYIPSSHSVSGGQRPVVVVVDQHGSGAPGVVQGPPCSNGGLPGKPCPPITSVDKSYGGYEVVGGSSDSYLVPGMTYSKGKIYPVGYFTKENPVKGSPGVPSFAAGPPISEGKYFSSNPIIPSQSAASSAIAFQPVGTGGVQLCGGGSTGSKGPCSPSSSRVPSSSSISSSSGLPYHPCGSASQSPCSPPGTGSFSSSSSSQSSGKIILQPCGSKSSSSGHPCMSVSSLTLTGGPDGSPHPDPSAGAKPCGSSSAGKIPCRSIRDILAQVKPLGPQLADPEVFLPQGELLNSP
Protein: Protein ORM2 (Q06144)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SPOTS complex that acts as a negative regulator of sphingolipid synthesis. Acts by inhibiting serine palmitoyltransferases (LCB1 and LCB2) activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:20182505}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:20182505}.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 2
- Protein ORM1
- Serine palmitoyltransferase-regulating protein TSC3
- Phosphatidylinositol-3-phosphatase SAC1
- Serine/threonine-protein kinase YPK1
- Serine/threonine-protein kinase YPK2/YKR2
- Ceramide synthase LAG1
- Inositol phosphorylceramide synthase catalytic subunit AUR1
- Ceramide synthase LAC1
Sequence:
MIDRTKNESPAFEESPLTPNVSNLKPFPSQSNKISTPVTDHRRRRSSSVISHVEQETFEDENDQQMLPNMNATWVDQRGAWLIHIVVIVLLRLFYSLFGSTPKWTWTLTNMTYIIGFYIMFHLVKGTPFDFNGGAYDNLTMWEQINDETLYTPTRKFLLIVPIVLFLISNQYYRNDMTLFLSNLAVTVLIGVVPKLGITHRLRISIPGITGRAQIS
Protein: Antifungal protein (Psc-AFP) (P85102)
Organism: Cullen corylifolium (Malaysian scurfpea) (Psoralea corylifolia)
Function: Inhibits soybean trypsin. Has antifungal activity against R.cerealis, A.brassicae and A.niger, and weak antifungal activity against F.oxysporum.
Interaction partners:
Sequence:
EWEPVQNGGSSYYMVPRIWA
Protein: Exocyst complex component 4 (Exocyst complex component Sec8) (rSec8) (Q62824)
Organism: Rattus norvegicus (Rat)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96A65}. Cell projection {ECO:0000269|PubMed:21658605}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96A65}. Note=Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). Localizes at the leading edge of migrating cells (PubMed:21658605). {ECO:0000250|UniProtKB:Q96A65, ECO:0000269|PubMed:21658605}.
Interaction partners:
- Exocyst complex component 3
- Exocyst complex component 6
- Exocyst complex component 2
- Exocyst complex component 8
- Exocyst complex component 7
- Exocyst complex component 5
- Exocyst complex component 1
- Ras-related protein Ral-A
- Exocyst complex component
- Exocyst complex component 1-like
Sequence:
MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIEELHRHLYIKSTSRVVQRNKEKGKMSSHGKDASPGPLIDVSNISTPRKFLDATQYSAAGSSSVREMNLQDIKEDLDCDPEENSTLFMGILIQGLARLKKIPETVKAIKERLEQELKQIVKRSTTQVADSAYQRGESLTVDNQPRLLLELLELLFDKFNAVASAHSIVLGYLQDSVGTQPTQQEEIKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYASTGREFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNLIEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCLLREFLTIYIKNIFLNQVLTEINKEIEGVTKTSDPLKILANADTMKVLGVQRPLLQSTIIVEKTVQDLMNLMHDLSAYSDQFLNMVCVKLQEYKDTCSTAYRGIVQSEEKLVISASWAKDDDISRLLKSLPNWTNMAQPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEWLAGRTKSAFSSLSASQMLSPAQESHVNMDLPPVSEQIMQTLSELAKSFQDMADRCLLVLHLEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAMEEAMSASLQQHKFQYIFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYYEMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGDQTTQNTRLQRLKEIICEQAAIKQATKDKKITTV
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-4) (Phospholipase C-beta-4) (PLC-beta-4) (Q9QW07)
Organism: Rattus norvegicus (Rat)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q15147}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Guanine nucleotide-binding protein G
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Guanine nucleotide-binding protein subunit alpha-15
- Guanine nucleotide-binding protein subunit alpha
- Protein kinase C gamma type
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRLAAIPKDPKILAALESVGKSENDLEGRILCVCSGTDLVNIGFTYMVAENPEITKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFLTNTSGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYQMSKYCEDLFGDLLLKQALESHPLEPGRLLPSPNDLKRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASILEDDNEEEIESADQEEEAHPEYKFGNELSADDFSHKEAVANSVKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQLRAMGIETSDIADVPSDTSKNDKKGKANPAKANVTPQSSSELRPTTTAALGSGQEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEIKKETEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLRKLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
Protein: Retroviral-like aspartic protease 1 (EC 3.4.23.-) (Skin-specific retroviral-like aspartic protease) (SASPase) (Skin aspartic protease) (TPA-inducible aspartic proteinase-like protein) (Q09PK2)
Organism: Mus musculus (Mouse)
Function: Protease responsible for filaggrin processing, essential for the maintenance of a proper epidermis organization.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRNPGGPGWASKRPLQKKQNTACLCAQQPARHFVPAPFNSSRQGKNTAQPTEPSLSSVIAPTLFCAFLYLACVTAELPEVSRRMATSGVRSKEGRREHAFVPEPFTGTNLAPSLWLHRFEVIDDLNHWDHATKLRFLKESLKGDALDVYNGLSSQAQGDFSFVKQALLRAFGAPGEAFSEPEEILFANSMGKGYYLKGKVGHVPVRFLVDSGAQVSVVHPALWEEVTDGDLDTLRPFNNVVKVANGAEMKILGVWDTEISLGKTKLKAEFLVANASAEEAIIGTDVLQDHNAVLDFEHRTCTLKGKKFRLLPVGSSLEDEFDLELIEEEEGSSAPEGSH
Protein: Keratin-associated protein 9-1 (Keratin-associated protein 9-like 3) (A8MXZ3)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
Sequence:
MTHCCSPCCQPTCCRTTCCRTTCWKPTTVTTCSSTPCCQPSCCVPSCCQPCCHPTCCQNTCCRTTCCQPTCVASCCQPSCCSTPCCQPTCCGSSCCGQTSCGSSCCQPICGSSCCQPCCHPTCYQTICFRTTCCQPTCCQPTCCRNTSCQPTCCGSSCCQPCCHPTCCQTICRSTCCQPSCVTRCCSTPCCQPTCGGSSCCSQTCNESSYCLPCCRPTCCQTTCYRTTCCRPSCCCSPCCVSSCCQPSCC
Protein: DNA replication complex GINS protein sld5 (Q9P7C8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The GINS complex plays an essential role in the initiation of DNA replication. Has a role in chromosome segregation and is required for bir1 localization.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA replication licensing factor mcm7
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm4
- DNA replication complex GINS protein psf1
- DNA replication complex GINS protein psf3
- DNA replication complex GINS protein psf2
- DNA replication licensing factor mcm3
- DNA polymerase epsilon subunit B
Sequence:
MEWDADDLLIEPTTEVENDYEDLCTQWVNERMAPDLLPFAEEIVSRVLDRIEAQRETLQLAIGTSSATSYRSVLMQTELERVKFVLRSYMRTRINKIDKYAQYIQSHPNLLLYLSSPERQYLLRHQQIVHRHYMDSFLREVPAKMNKLDDKVGNLSMVASPDMDTAVFCVVNESVEENFRVSENEYITLDKGDVLILRYSVISDYLRLGVVSLI
Protein: Flagellum-specific ATP synthase (EC 7.1.2.2) (P26465)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Flagellar FliJ protein
- Flagellar biosynthetic protein FliQ
- Flagellar M-ring protein
- Flagellar assembly protein FliH
- Flagellar biosynthetic protein FliP
- Flagellar motor switch protein FliG
- Flagellar motor switch protein FliN
- Flagellar biosynthetic protein FlhB
- Flagellar biosynthesis protein FlhA
- Flagellar biosynthetic protein FliR
Sequence:
MTTRLTRWLTALDNFEAKMALLPAVRRYGRLTRATGLVLEATGLQLPLGATCIIERQDGPETKEVESEVVGFNGQRLFLMPLEEVEGILPGARVYARNGHGDGLQSGKQLPLGPALLGRVLDGGGKPLDGLPAPDTLETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTRADVIVVGLIGERGREVKDFIENILGPDGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIHGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALITEQHYARVRLFKQLLSSFQRNRDLVSVGAYAKGSDPMLDKAITLWPQLEAFLQQGIFERADWEDSLQALDLIFPTV
Protein: Geraniol 8-hydroxylase (EC 1.14.14.83) (Cytochrome P450 76B6) (Geraniol 10-hydroxylase) (CrG10H) (Q8VWZ7)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Hydroxylase involved in the biosynthesis of hydroxygeraniol, a precursor of the terpenoid indole alkaloids such as vinblastine and vincristine. Also able to hydroxylate in vitro nerol and to catalyze 3'-hydroxylation of the flavanone naringenin to form eriodictyol. No activity with apigenin, kaempferol, p-coumaric acid and ferulic acid as substrates.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19504099}; Single-pass membrane protein {ECO:0000269|PubMed:19504099}. Note=The N-terminal transmembrane helix is necessary and sufficient for endoplasmic reticulum targeting.
Interaction partners:
Sequence:
MDYLTIILTLLFALTLYEAFSYLSRRTKNLPPGPSPLPFIGSLHLLGDQPHKSLAKLSKKHGPIMSLKLGQITTIVISSSTMAKEVLQKQDLAFSSRSVPNALHAHNQFKFSVVWLPVASRWRSLRKVLNSNIFSGNRLDANQHLRTRKVQELIAYCRKNSQSGEAVDVGRAAFRTSLNLLSNLIFSKDLTDPYSDSAKEFKDLVWNIMVEAGKPNLVDFFPLLEKVDPQGIRHRMTIHFGEVLKLFGGLVNERLEQRRSKGEKNDVLDVLLTTSQESPEEIDRTHIERMCLDLFVAGTDTTSSTLEWAMSEMLKNPDKMKKTQDELAQVIGRGKTIEESDINRLPYLRCVMKETLRIHPPVPFLIPRKVEQSVEVCGYNVPKGSQVLVNAWAIGRDETVWDDALAFKPERFMESELDIRGRDFELIPFGAGRRICPGLPLALRTVPLMLGSLLNSFNWKLEGGMAPKDLDMEEKFGITLQKAHPLRAVPSTL
Protein: [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrial (EC 2.7.11.2) (PDK P45) (Pyruvate dehydrogenase kinase isoform 2) (PDH kinase 2) (Q64536)
Organism: Rattus norvegicus (Rat)
Function: Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:22910903}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- [Pyruvate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Ac1164
- [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial
- RPTOR independent companion of MTOR, complex 2
- Serine/threonine-protein kinase mTOR
Sequence:
MRWFRALLKNASLAGAPKYIEHFSKFSPSPLSMKQFLDFGSSNACEKTSFTFLRQELPVRLANIMKEINLLPDRVLSTPSVQLVQSWYVQSLLDIMEFLDKDPEDHRTLSQFTDALVTIRNRHNDVVPTMAQGVLEYKDTYGDDPVSNQNIQYFLDRFYLSRISIRMLINQHTLIFDGSTNPAHPKHIGSIDPNCSVSDVVKDAYDMAKLLCDKYYMASPDLEIQEVNATNATQPIHMVYVPSHLYHMLFELFKNAMRATVESHESSLTLPPIKIMVALGEEDLSIKMSDRGGGVPLRKIERLFSYMYSTAPTPQPGTGGTPLAGFGYGLPISRLYAKYFQGDLQLFSMEGFGTDAVIYLKALSTDSVERLPVYNKSAWRHYQTIQEAGDWCVPSTEPKNTSTYRVS
Protein: Cysteine--tRNA ligase (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) (Q9CEJ0)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
Interaction partners:
Sequence:
MKIYNTYSRQLEDFQPIEPGKVKMYVCGPTVYNYIHVGNARSVVAFDLVRKYLEFRGFEVQYISNFTDVDDKIINGAKAANMTTTDFSERYIAAFYEDTDALNVKRASQNPKATEFIEAMIEFIQELVDKEFAYVSQGDVYFRVSKSKDYAKLANKNLADLLAGASGRTDEETKLKESPADFALWKSAKADEVSWQAPWGAGRPGWHIECSVMSTSLLGETIDIHGGGADLEFPHHTNEIAQSEAKTGQKFVNYWMHNGFVNVDGEKMSKSLGNFTTVHELLQVVNPQILRFFLATTHYRRPVNFTDDALTEAENNIKKIENAYRHLDEQAESNLSALTTFRNDFVAAMDEDFNIANGMTVFYDFVSWVNKGNGGPEVKEFFDQVLEILGIKFKFEQSLDSEIEAMIEARQLAREVRDFAKSDEIRDALKAQGIVLEDTKDGVRWHRE
Protein: Peroxiredoxin-1 (EC 1.11.1.24) (Natural killer cell-enhancing factor A) (NKEF-A) (Proliferation-associated gene protein) (PAG) (Thioredoxin peroxidase 2) (Thioredoxin-dependent peroxide reductase 2) (Thioredoxin-dependent peroxiredoxin 1) (Q06830)
Organism: Homo sapiens (Human)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:9497357}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Interaction partners:
- Sulfiredoxin-1
- Thioredoxin
- Peroxiredoxin-5, mitochondrial
- Thioredoxin, mitochondrial
- Tyrosine-protein kinase ABL1
- Sestrin-2
- Nuclear factor erythroid 2-related factor 2
- Mitogen-activated protein kinase kinase kinase 5
- Superoxide dismutase
- Peroxiredoxin-2
Sequence:
MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK
Protein: Aldo-keto reductase family 1 member B10 (G3V786)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATFVELSTKAKMPIVGLGTWKSTPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLLQDPKIKEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQVFDFQLSDQEMATILSFNRNWRACLLPESFTVTSA
Protein: UNC93-like protein C922.05c (Q9URX1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSSDNLDISMEKKYSADVDVEKAPTPEYGEVETAPLSQSSWIYRRPRIGRFKSLAYGSALTQTIIVSWVCFLCPGMFNALSGLGGGGEVNADVANDANVALYSTFAGLGFFAGSICNLIGVKLTLAIGGTGYSVYTASLLCYKHVYNRGFVIFGGCYLGLTAGMLWAAQGAVIMSYPREENKARYIAIFWGIFNLGAVIGSIVPLAQTMHSSVNSVGDGTYAGFIVLMAVGSALALFMVSPEKTVKEDGKFVHIEKSMGWKKELLGLVQTLYKEYWVLLLFPMFFSSNWFTTYQFNDFNLAYFNIRTRSLNNLLYWFAQIMGSAVAALFLDWQRFNRVIRARVGWGLVFVLICVIWGGGLAFQLKYTRKSVAESDFVVTDFTHRGYTGYAFLYIFYGMLDAIFQSYAYWIIGSLSNDTNKLAVYMGFYKSLQSAGAAITYRMDTLNIPYMNYFASCWALLCGSLIVASPVIWKKIKLTTEGIEDEIPPLANGLAVDGPVVPLKE