wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor MYB77 (Myb-related protein 77) (AtMYB77) (Myb-related protein R2) (AtMYBR2) (Q9SN12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in auxin response. Functions in auxin signal transduction and modulates lateral root growth. Interacts with ARF response factors to promote auxin-responsive gene expression. In response to auxin, binds sequence-specific motifs in the promoter of the auxin-responsive gene IAA19, and activates IAA19 transcription. The IAA19 transcription activation by MYB77 is enhanced by direct interaction between MYB77 and PYL8.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17675404}.
Interaction partners:
- Auxin response factor 7
- Abscisic acid receptor PYL8
- Abscisic acid receptor PYL9
- Auxin-responsive protein IAA19
Sequence:
MADRVKGPWSQEEDEQLRRMVEKYGPRNWSAISKSIPGRSGKSCRLRWCNQLSPEVEHRPFSPEEDETIVTARAQFGNKWATIARLLNGRTDNAVKNHWNSTLKRKCSGGVAVTTVTETEEDQDRPKKRRSVSFDSAFAPVDTGLYMSPESPNGIDVSDSSTIPSPSSPVAQLFKPMPISGGFTVVPQPLPVEMSSSSEDPPTSLSLSLPGAENTSSSHNNNNNALMFPRFESQMKINVEERGEGRRGEFMTVVQEMIKAEVRSYMAEMQKTSGGFVVGGLYESGGNGGFRDCGVITPKVE
Protein: Inner membrane protein YaiY (P0AAP7)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MADFTLSKSLFSGKYRNASSTPGNIAYALFVLFCFWAGAQLLNLLVHAPGVYERLMQVQETGRPRVEIGLGVGTIFGLIPFLVGCLIFAVVALWLHWRHRRQ
Protein: Cysteine-rich protein 2-binding protein (CSRP2-binding protein) (ADA2A-containing complex subunit 2) (ATAC2) (CRP2-binding partner) (CRP2BP) (Lysine acetyltransferase 14) (Q8CID0)
Organism: Mus musculus (Mouse)
Function: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Mainly nuclear. {ECO:0000250}.
Interaction partners:
- SAGA-associated factor 29
- YEATS domain-containing protein 2
- ZZ-type zinc finger-containing protein 3
- Histone acetyltransferase KAT2A
- Transcriptional adapter 3
- Protein Dr1
- Transcriptional adapter 2-alpha
- MAP3K12-binding inhibitory protein 1
- Histone acetyltransferase KAT2B
- WD repeat-containing protein 5
Sequence:
MDSSIHLSGLLSRHDDDATRTSTSEGLEEGEVEGETLLIVESEDQASVDLSHDQSGDSLNSDEGDVSWMEEQLSYFCDKCQKWIPASQLREQLSYLKGDNFFRFTCCDCSADGKEQYERLKLTWQQVVMLAMYNLSLEGSGRQGYFRWKEDICAFIEKHWTFLLGNRKKTSTWWSTVAGCLSVGSPVYFRSGAQEFGEPGWWKLVHNRPPTMRPEGEKLAASTLKVKASKPTLDPIITVEGLRKRASRNPVESAMELKEKRSRTQEAKDIRRAQKEAAGLLDRSTSSTPVKFISRGRRPDLILEKGEVIDFSSLSSSDRTPLTSPSPSPSLDFSAPGTPASHSATPSLLSEADLIPDVMPPQALFHDDDELEGDGVIDPGMEYIPPPAGSASGLLGSRKKVRAPEQIKQEVDSEEEKPDRMDGDSEDTDSNISLHTRAREKRKPPLEKDMKPKGPRYTPVSIYEEKLLLKRLEACPGAVAMTPEARRLKRKLIVRQAKRDRGLPLFDLDEVVNAALLLVDGIYGAKDGGASRLAAGQATYRTTCQDFRILDRYQTALPARKGFRHQTTRFLYRLVGSEDLAVDQSIISPYTSRILKPYIRRDYETKPPKLQLLSQIRSHLHRSDPHWTPGPDAPLDYCYVRPNHIPTINSMCQEFFWPGIDLSECLQYPDFSVVVLYKKVIVAFGFMVPDVKYNEAYISFLLVHPEWRRAGIATFMIYHLIQTCMGKDVTLHVSASNPAMLLYQKFGFKTEEYVLDFYDKYYPLESTECKHAFFLRLRR
Protein: Cholesterol side-chain cleavage enzyme, mitochondrial (EC 1.14.15.6) (CYPXIA1) (Cholesterol desmolase) (Cytochrome P450 11A1) (Cytochrome P450(scc)) (P05108)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones. Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
- Adrenodoxin, mitochondrial
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Steroidogenic acute regulatory protein, mitochondrial
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Steroid 21-hydroxylase
- Cytochrome P450 7B1
- Steryl-sulfatase
- Sulfotransferase 2B1
Sequence:
MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ
Protein: Glycolipid transfer protein 1 (O22797)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in glycolipids transfer.
Interaction partners:
- Accelerated cell death 11
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MEGTVFTPCLEGMKHVKSDQGEMLTKPFLELCKTILPVIDKFGAAMTLVKSDIGGNITRLEKNYLSDPDKFKYLYTFVQVEIESKIAKGSSSCTNGLLWLTRAMDFLVELFRNLVAHQDWSMPQACADSYQKTLKKWHGWLASSTFSMALKLAPDRKKFMDVISGSGNIQADMERFCAEFGPFLHDNHKFLASVGMDDMKAS
Protein: Squalene epoxidase 1 (AtSQE1) (EC 1.14.14.17) (Protein DROUGHT HYPERSENSITIVE 2) (Squalene monooxygenase) (XF1 protein) (Q9SM02)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis. Can produce not only oxidosqualene, but also 2,3:22,23-dioxidosqualene. Main squalene epoxidase in the root. Sqe1 mutants may show defects in membrane lipid rafts, impairing the correct localization of RHD2 NADPH oxidase and the proper polarized production of ROS.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Inactive squalene synthase 2
- Squalene synthase 1
- Beta-amyrin synthase
- Amyrin synthase LUP2
- Cycloartenol synthase
- Camelliol C synthase
- Lupeol synthase 1
- Lanosterol synthase
- Marneral synthase
- Thalianol synthase 1
Sequence:
MESQLWNWILPLLISSLLISFVAFYGFFVKPKRNGLRHDRKTVSTVTSDVGSVNITGDTVADVIVVGAGVAGSALAYTLGKDKRRVHVIERDLSEPDRIVGELLQPGGYLKLLELGIEDCVEEIDAQRVYGYALFKNGKRIRLAYPLEKFHEDVSGRSFHNGRFIQRMREKAASLPNVQLEQGTVLSLLEENGTIKGVRYKNKAGEEQTAFAALTIVCDGCFSNLRRSLCNPQVEVPSCFVGLVLENCNLPYANHGHVVLADPSPILMYPISSTEVRCLVDVPGQKVPSIANGEMKNYLKTVVAPQMPHEVYDSFIAAVDKGNIKSMPNRSMPASPYPTPGALLMGDAFNMRHPLTGGGMTVALADIVVLRNLLRPLRDLSDGASLCKYLESFYTLRKPVAATINTLANALYQVFCSSENEARNEMREACFDYLGLGGMCTSGPVSLLSGLNPRPLTLVCHFFAVAVYGVIRLLIPFPSPKRIWLGAKLISGASGIIFPIIKAEGVRQMFFPATVPAYYYKAPTVGETKCS
Protein: SD09786p (Q960B3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHEAESVGGLGTESTPESPMSPQTPDPALLDVRQKVHRFEAFRTNICFIKQERHSLKLLENRRHPSFEDQSDDHHTPPATPPRRIRLPGLGSRGSSRSSSIPSFQAGIHEVRSEDEVDQISDFETDSHTAAEEYLVVDTTSEVVPSEEVADSKVDQQQVQRSISADQSKEALTLPLKMRNDFPRNYRSTPRRKTEIIGTTNEHLVGKFHSVYQPKDEEEEVVIELRDKSDKCVHPILEELIKTEEAYVNNLFTGIENYGNIFQRKDLPLGLRGKKYDLFGNIEQIAEFHRDEFLPMLQRNRRDLKRLFDEFLQFLDQHCFYGYVIFTMNKQKSLKLCDLYKNYFTSIRLERDDKLGINSFLVQPIQRMARYPLLLTQFINTFFKNRDIVMKPLIESCCRLEKRLRALLTTTNESEIINDIVDCHEFNVYYQGKFRKVNEFQVLDHKLKRSYRSKVFIFDKCIIYTEIKGKNLLFHGRYPCEHIGISAKTKSFTLYYERRKQQECEFTADPVQIAIWLDLIRDMINNYANEERQKLQERYSRENDHLHRKAPSFSLYRDSNRFSSDSGIGNIWIMPKADEDTISNRTTWYAAT
Protein: Homeotic protein Sex combs reduced (P09077)
Organism: Drosophila melanogaster (Fruit fly)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Controls the segmental transformation of the first to the second thoracic segment (prothorax to mesothorax) and of the labial palps into maxillary palps. In embryo, required for fusion of labial lobes and development of the T1 denticle belt. In adult, expression in the head is necessary for proper development of the labium. In the first thoracic segment of the adult, required for proper development of the sex comb and to suppress improper prothoracic wing development.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein extradenticle
- Homeobox protein abdominal-A
- Homeotic protein antennapedia
- Homeotic protein deformed
- Segmentation protein fushi tarazu
- Homeotic protein proboscipedia
Sequence:
MDPDCFAMSSYQFVNSLASCYPQQMNPQQNHPGAGNSSAGGSGGGAGGSGGVVPSGGTNGGQGSAGAATPGANDYFPAAAAYTPNLYPNTPQAHYANQAAYGGQGNPDMVDYTQLQPQRLLLQQQQQQQQQQHAHAAAAVAAQQQQQLAQQQHPQQQQQQQQANISCKYANDPVTPGGSGGGGVSGSNNNNNSANSNNNNSQSLASPQDLSTRDISPKLSPSSVVESVARSLNKGVLGGSLAAAAAAAGLNNNHSGSGVSGGPGNVNVPMHSPGGGDSDSESDSGNEAGSSQNSGNGKKNPPQIYPWMKRVHLGTSTVNANGETKRQRTSYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKMASMNIVPYHMGPYGHPYHQFDIHPSQFAHLSA
Protein: Uncharacterized aarF domain-containing protein kinase 5 (EC 2.7.11.-) (Q3MIX3)
Organism: Homo sapiens (Human)
Function: The function of this protein is not yet clear. It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
Sequence:
MWRPVQLCHFHSALLHSRQKPWPSPAVFFRRNVRGLPPRFSSPTPLWRKVLSTAVVGAPLLLGARYVMAEAREKRRMRLVVDGMGRFGRSLKVGLQISLDYWWCTNVVLRGVEENSPGYLEVMSACHQRAADALVAGAISNGGLYVKLGQGLCSFNHLLPPEYTRTLRVLEDRALKRGFQEVDELFLEDFQALPHELFQEFDYQPIAAASLAQVHRAKLHDGTSVAVKVQYIDLRDRFDGDIHTLELLLRLVEVMHPSFGFSWVLQDLKGTLAQELDFENEGRNAERCARELAHFPYVVVPRVHWDKSSKRVLTADFCAGCKVNDVEAIRSQGLAVHDIAEKLIKAFAEQIFYTGFIHSDPHPGNVLVRKGPDGKAELVLLDHGLYQFLEEKDRAALCQLWRAIILRDDAAMRAHAAALGVQDYLLFAEMLMQRPVRLGQLWGSHLLSREEAAYMVDMARERFEAVMAVLRELPRPMLLVLRNINTVRAINVALGAPVDRYFLMAKRAVRGWSRLAGATYRGVYGTSLLRHAKVVWEMLKFEVALRLETLAMRLTALLARALVHLSLVPPAEELYQYLET
Protein: Cystathionine beta-synthase (EC 4.2.1.22) (Q5EI65)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPAVPSSSESVGTGPVCPHAAKMLSNAANGESGINGDADDVFNGKAGHKLNETNGRHLKSLNGQHMEKGSEVSMERKWIRPDLPSRCTWKLGDLNMESPHNHYQRTKTSGILPNILSKIGETPMVRMNKIPKAFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTSARFDSPESHVGVAWRLKNEIPNAHILDQYRNPSNPLAHYDTTAEEILEQCGGKIDMLVAGAGTGGTITGIARKLKEKCPDIKIIGVDPEGSILAEPDELNKTDKTQYEVEGIGYDFIPTVLDRSVVDNWYKSNDEESFAMSRMLIREEGLLCGGSSGTAMSAAVNVAKELKEGQRCVVILPDSIRNYMSKFLSDKWMFEKGFMSEEDLVVNKPWWWNLTLQELRLSAPLTVLPLVSIKKTIQILKEKAFDQAPVVDEAGHILGMVTLGNMLASVLAGKVRPSDPISKVLYKQFKQVRLTDNLGKLSRILETDHFALVVHEQIQYMSDGSPKMRQMVFGVVTAIDLLNYVTMRERRERTLSECSLSEDQ
Protein: Nucleolar protein 12 (Nucleolar protein of 25 kDa) (Q8BG17)
Organism: Mus musculus (Mouse)
Function: May bind to 28S rRNA. In vitro binds single-stranded nucleic acids.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16430885}. Nucleus {ECO:0000250|UniProtKB:Q9UGY1}. Cytoplasm {ECO:0000250|UniProtKB:Q9UGY1}.
Interaction partners:
- Ribosome biogenesis protein BRX1 homolog
- Probable rRNA-processing protein EBP2
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- GTP-binding protein 4
- ATP-dependent RNA helicase DDX55
- mRNA turnover protein 4 homolog
- Ribosomal L1 domain-containing protein 1
- ATP-dependent RNA helicase DDX18
- Ribosome biogenesis protein WDR12
Sequence:
MGRNKKKKKRDGDDRRPRLVLNFDEEKRREYLTGFHKRKVERKKAAIEEIKQRLKQEQKKLREERHQEYLKMLAEREEALEEADELERLVTAKTESVQYDHPNHTVTVTTISDLDLSGARLLGLPLPEQGDQDGSQEEEMSSLEKPTKALPRKSKDPLLSQRISSLTATLHAHSRKKVKRKHPRRAQDSTKKPPSATRTSKTQRRRRMTGKARHNGE
Protein: T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (Chaperonin CCT7) (Q9SF16)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit alpha
- TCP-1/cpn60 chaperonin family protein
- T-complex protein 1 subunit zeta 1
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit zeta 2
- T-complex protein 1 subunit epsilon
- ATP binding protein
Sequence:
MASMMQPQIILLKEGTDTSQGKAQLVSNINACTAVGDVVRTTLGPRGMDKLIHDDKGSVTISNDGATIMKLLDIVHPAAKILVDIAKSQDSEVGDGTTTVVLLAAEFLKEAKPFIEDGVHAQNLIRSYRTASTLAIAKVKELAVSIEGKSVEEKKGLLAKCAATTLSSKLIGGEKEFFATMVVDAVMAIGNDDRLNLIGIKKVPGGNMRDSFLVDGVAFKKTFSYAGFEQQPKKFLNPKILLLNIELELKSEKENAEIRLSDPSQYQSIVDAEWNIIYDKLDKCVESGAKVVLSRLAIGDLATQYFADRDIFCAGRVAEEDLNRVAAAAGGTVQTSVNNIIDEVLGTCEIFEEKQVGGERFNIFSGCPSGRTATIVLRGGADQFIEEAERSLHDAIMIVRRAVKNSTVVPGGGAIDMEISKYLRQHSRTIAGKSQLFINSYAKALEVIPRQLCDNAGFDATDVLNKLRQKHAMQSGEGASYGVDINTGGIADSFANFVWEPAVVKINAINAATEAACLILSVDETVKNPKSESAQGDAAGAMGRGRGGGRGRGMRRR
Protein: Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1C (Phosphatidylinositol 3-phosphate 5-kinase) (EC 2.7.1.150) (Phosphatidylinositol 3-phosphate 5-kinase type III) (PIPkin-III) (Type III PIP kinase) (Protein FORMS APLOID AND BINUCLEATE CELLS 1C) (Q9SSJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate (By similarity).
Interaction partners:
- Phosphoinositide phosphatase SAC5
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphoinositide phosphatase SAC2
- Phosphoinositide phosphatase SAC3
- Phosphoinositide phosphatase SAC4
- Phosphatidylinositol 3-kinase VPS34
- Phosphoinositide phosphatase SAC7
- Phosphoinositide phosphatase SAC8
- Protein VAC14 homolog
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2A
Sequence:
MGIPDGSLLDLIDKVRSWITSDSSDSLFLLSSSKQDFGIMPIVSKMCHDCGTKVEQGYCCLSCGSCWCKSCSDTEESKMKLCRECDAEVRELRVKSYDKVHPRDSPDPPSSLATESESLASSLEIRDCRNMASIRCYPSRGEEEEARYCGKQLLSPSSDNYQDSSDIESGSVSARHELFSCKSSAGSSPHDSPLRNNFSPLGRFVQHAKDLRSPTVCSFDNHQEQLLADNLVKPGQGVLEQEDHEEEEDKLQQPLDFENNGRIWYPPPPEDENDDAESNYFHYDDEDDDIGDSATEFSLSSSFSSHIPTKEKLGENSNEPLRTVVHDHFRALVAELLRGEELSPSDDGSAGEWLDIVTALAWQAANFVKPDTRAGGSMDPGNYVKIKCVASGNQNESILIRGIVCSKNITHKRMISQYKNPRVMLLAGSLEYQRVAGQLASFNTLLQQENEHMKAIIAKIESLRPNVLLVEKSASSYAQQYLLEKEISLVLNVKRSLLDRIARCTGAVLCPSLDSISTARLGHCELFRTERVLEQHEAGNQSNRKPSRTLMYFEGCPRRLGCTVVLRGSCREELKKVKHVIQYAVFAAYHLSLETSFLADEGASLPKIRLKQPGMVRTASQRRIIDEGISLITQSPTETDSQALLETAAHEDEHTAPMPEHEVCESLCEDFDPTQIFPPSSEVETEQSDTLNGDFANNLVTRSYSSNQLNDLHEPTLCLSSEIPETPTQQPSGEEDNGRGEEENQLVNPQDLPQHESFYEDDVSSEYFSAADSHQSILVSFSSRCVLKESVCERSRLLRIKFYGSFDKPLGRYLKDDLFDKTSSCRSCKELVDAHVLCYSHQNGNLTINVRRLPSMKLPGEQDGKIWMWHRCLRCAHVDGVPPATRRVVMSDAAWGLSFGKFLELSFSNHATANRVASCGHSLQRDCLRFYGFGNMVAFFRYSPINILTVLLPPSMLEFNSHPQQEWIRTEAAELVGKMRTMYTEISDMLNRMEEKSSLLEPEQSEACDLHSRIIGLIDQLVKEKDEYDDALQPIFEENLQIQGSLDILELNRLRRALMIGAHAWDHQLYLLNSQLKKASVFKTGDDNAPRNPEMHDPPKIDRRMQEGSDERDEQSHTDSEANGDNKDPENIPSPGTSLSERIDSAWLGSFQNLEKAETIAETEGFSAVNSSLRRLARPIRVQSFDSAIRFQERIQKGLPPSSLYLSTLRSFHASGEYRNMVRDPVSNVMRTYSQMLPLEVQKLDLIVGSAPTYISSASQMADGARMLIPQRGLNDIVVPVYDDDPASVVSYAINSKEYKEWIVNKGLASSSSSSNLNNRESEPSAFSTWRSLSMDVDYIQHAVYGSSQDDRKSPHLTISFSDRASSSSTATEGKVKFSVTCYFATQFDTLRKTCCPSEVDFVRSLSRCQRWSAQGGKSNVYFAKSLDERFIIKQVVKTELDSFEDFAPEYFKYLKESLSSGSPTCLAKILGIYQVSIKHPKGGKETKMDLMVMENLFYNRRISRIYDLKGSARSRYNPNTSGADKVLLDMNLLETLRTEPIFLGSKAKRSLERAIWNDTNFLASVDVMDYSLLVGFDEERKELVLGIIDFMRQYTWDKHLETWVKASGILGGPKNASPTIVSPKQYKRRFRKAMTTYFLTVPEPWTS
Protein: Deuterosome assembly protein 1 (Coiled-coil domain-containing protein 67) (Q05D60)
Organism: Homo sapiens (Human)
Function: Key structural component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells and can generate more than 100 centrioles. Probably sufficient for the specification and formation of the deuterosome inner core. Interacts with CEP152 and recruits PLK4 to activate centriole biogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Note=Localizes to the deuterosome. {ECO:0000250}.
Interaction partners:
- Coiled-coil domain-containing protein 78
Sequence:
MENQAHNTMGTSPCEAELQELMEQIDIMVSNKKMDWERKMRALETRLDLRDQELANAQTCLDQKGQEVGLLRQKLDSLEKCNLAMTQNYEGQLQSLKAQFSKLTNNFEKLRLHQMKQNKVPRKELPHLKEEIPFELSNLNQKLEEFRAKSREWDKQEILYQTHLISLDAQQKLLSEKCNQFQKQAQSYQTQLNGKKQCLEDSSSEIPRLICDPDPNCEINERDEFIIEKLKSAVNEIALSRNKLQDENQKLLQELKMYQRQCQAMEAGLSEVKSELQSRDDLLRIIEMERLQLHRELLKIGECQNAQGNKTRLESSYLPSIKEPERKIKELFSVMQDQPNHEKELNKIRSQLQQVEEYHNSEQERMRNEISDLTEELHQKEITIATVTKKAALLEKQLKMELEIKEKMLAKQKVSDMKYKAVRTENTHLKGMMGDLDPGEYMSMDFTNREQSRHTSINKLQYENERLRNDLAKLHVNGKSTWTNQNTYEETGRYAYQSQIKVEQNEERLSHDCEPNRSTMPPLPPSTFQAKEMTSPLVSDDDVFPLSPPDMSFPASLAAQHFLLEEEKRAKELEKLLNTHIDELQRHTEFTLNKYSKLKQNRHI
Protein: 1,3-beta-glucanosyltransferase PGA4 (EC 2.4.1.-) (GPI-anchored protein 4) (Q5AJY5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis. Plays a key role in virulence.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:18712765, ECO:0000269|PubMed:20641015, ECO:0000269|PubMed:20864472}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Interaction partners:
- Glucan 1,3-beta-glucosidase BGL2
- Cell surface GPI-anchored protein ECM33
- Ecm33p
- Crh-like protein UTR2
- Cell surface mannoprotein MP65
Sequence:
MLFRSLVTYLSLVSSVLSIASIKVEGNAFWDSESGDRFYIRGVDYQPGGSSELEDPLADTNVCERDVKYFQELGINTIRVYSIDNTKNHTECMDTLAKAGIYVILDVNTPHSSITRSDAACSYNTDYLQEVFASIVEFAQFDNTLGFFAGNEVINDGPSLEAAPYVKAVVRDMKTFIKNRGFRTIPVGYSAASVDEYRLPSGLYFNCGDDDMARIDMYGINDYSWCGDASMTTSQYSQQMKDFANYTVPLFFSEFGCNAKRPRPFSEIEAIYSTEMSSVFSGGLVYEYSEEASNYGLVELKGDSVTTNDDFDNLKSQFEKTKNPSGDGGYLKSTGGNKCPPKSNIWNVTEEIPDTPKGALKYLKGLAEPTGHGFDAYVQGNCNAKGNNVDDTGNYTSSITASSRASPSQTSQVSSSSATSANSTSSKKNDAAVEGAGFLSVIALAAGIALL
Protein: Malonyl-CoA decarboxylase (EC 4.1.1.9) (Q6NCB2)
Organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Interaction partners:
- 3-methylmercaptopropionyl-CoA ligase
- Biotin carboxylase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- methylmalonate-semialdehyde dehydrogenase
- acetyl-CoA C-acyltransferase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
- Beta-ketothiolase
- Acetyl-CoA C-acetyltransferase
- Acetyl-CoA C-acetyltransferase
Sequence:
MKLMPIATTADRASEFLGGLFNSLTERGRSLFGLTSSQPMSGDELIALSETLLSRRGEASGVALAASLLAGYEAADEDDKLAFLDALAEQFGPDLAELNTAIEAFRADASAEATGELLRAAEPRRQELIRRLNHAPGGTAALVKMREAVLARIAAHPQLRHVDDDFVHLFTSWFNRGFLVLQRIDWTTPANILEKIIRYEQVHTIHDWDDLRARLAPPDRRCYGFFHPRLVDEPLIFVEVALTKDSPAAIAPLLDLEREPIAASDATTAVFYSISNTQQGLAGISFGNFLIKQVVEEIKRELPNVQTFVTLSPVPGFAKWLKRERDNPDSTLLDASARTALEALDTPNWFDDADTADRLKPIVLQLAAAYFLQAKGPNGRPLDPVARFHLGNGARLDRLNFLGDRSPNGMRQSHGLMVNYLYALGDIEANHEALFERGQIAAASAVRKLVPTKPVTSEPRKGNGKTASAPQAAPTA
Protein: G_PROTEIN_RECEP_F1_2 domain-containing protein (Q17889)
Organism: Caenorhabditis elegans
Interaction partners:
- SKN-1 Dependent Zygotic transcript
- SKN-1 Dependent Zygotic transcript
- Apyrase apy-1
- ACid Phosphatase family
Sequence:
MSEQYRYFLLICSSFSFSINLTAITFCYNMYQPHVYPSDFDCPAYPTFFQGILKISELKLTILLYLSIIVWLTIASMILVTLTFLKKFCTSTAANYNMIVMFLNFVFNVAIMRNFLKHGTGINDAIVYYLNKQSHVCLNVPEWLEHNMEITVFLVVAFGMNLPFLYGIVDNSVRLFYRYAINKRNHRLMHIEPIVDDIIRYRRRVQSEPNIPLVVNEEVELPPSYTEAIAMIEQAPVQESNEASIESRDPIHSRNNRSSNTNENNDGNTNDQTDYENKETDNERSGNETTSNLSANQMRIIVSEAVQNAMAHLIAVSDRAQTSSLYQSVVVNEIELQNTSSSQSETQEYDKEDKDVEESSDEENDHDN
Protein: AT19630p (Q5U0U3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYDYFYDFFGFSDYRQGGSFGNNVSYYDDMYRWIDGDYNYYDYPNGGGGGSGGGGGSVSGGTVLPLSAGGSQNSPMASGQRSARGSASGPSASPSLMGVGRGHGITVPRGRVVGQRGSISRLGAQTVPQAAGAAAAAGQAAAAVAQRGATGQGAPAATGGFRGVLPTRPSARGTQHVKPLQNLPAGAAFKTFMEGN
Protein: NADH-quinone oxidoreductase subunit M (EC 7.1.1.-) (NADH dehydrogenase I subunit M) (NDH-1 subunit M) (NUO13) (P0AFE8)
Organism: Escherichia coli (strain K12)
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit K
- NADH-quinone oxidoreductase subunit N
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit H
Sequence:
MLLPWLILIPFIGGFLCWQTERFGVKVPRWIALITMGLTLALSLQLWLQGGYSLTQSAGIPQWQSEFDMPWIPRFGISIHLAIDGLSLLMVVLTGLLGVLAVLCSWKEIEKYQGFFHLNLMWILGGVIGVFLAIDMFLFFFFWEMMLVPMYFLIALWGHKASDGKTRITAATKFFIYTQASGLVMLIAILALVFVHYNATGVWTFNYEELLNTPMSSGVEYLLMLGFFIAFAVKMPVVPLHGWLPDAHSQAPTAGSVDLAGILLKTAAYGLLRFSLPLFPNASAEFAPIAMWLGVIGIFYGAWMAFAQTDIKRLIAYTSVSHMGFVLIAIYTGSQLAYQGAVIQMIAHGLSAAGLFILCGQLYERIHTRDMRMMGGLWSKMKWLPALSLFFAVATLGMPGTGNFVGEFMILFGSFQVVPVITVISTFGLVFASVYSLAMLHRAYFGKAKSQIASQELPGMSLRELFMILLLVVLLVLLGFYPQPILDTSHSAIGNIQQWFVNSVTTTRP
Protein: Uncharacterized protein At1g32220, chloroplastic (Q9FVR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 6
- At1g72040
Sequence:
MTSFLSFSAISAHPPTFSGASFRPRSFSPRLFKSCVKCTYAEAGLSSASWSAPIDIVADVKSERVVVLGGNGFVGSAICKAAISNGIEVVSVSRSGRPNFEDSWLDQVTWVTGDVFYLNWDEVLLGATAVVSTIGGFGNEEQMKRINGEANVTAVNAAKDFGVPKFVLITVHDYNLPPFILSNGYFTGKRNAEAELLSKYPTSGVVLRPGFIYGKRKVNGIEVPLDLVGEPLDKIYDSAERFIRPLRSLPASDLILAPPVNVDDLALAVINAVKDDDFFGIFTIEQIKEAAAKMRA