wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional activator GpuR (Q9I6K1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Guanidinopropionase
- 3-guanidinopropionate transport protein
- Guanidinobutyrase
- Probable sodium:solute symport protein
Sequence:
MGAGMLGNINDIDLRMLRTFCAIVEAGGFTAAQARLNTSLSRLSVLVRDLEVRLGYSLCRRGNGGFQLTEEGQELYDAALGLFSDIARFREQVRGLGGRDREALHLGCVDGVIGQHCLPLPLAIRLFRQRAPEVLLKLHTRRPDELEHAVLEERLQLAVGAFHHRLSGLYYQPLFREEQNLYCGSAHPFFARADDEPTLGEICAADYVGRGYMAENHRPHDLRFNQGTDAYTMEAIATLVFSGTYIGYLPTHYAATWVAEGRMRAIRPRQLAYDSEFHCITRQGHEERPTLTLFLRSLFEAQKQLGVQVPANTNGIARQL
Protein: BTB/POZ domain-containing protein 9 (Q8C726)
Organism: Mus musculus (Mouse)
Interaction partners:
- FAS-associated factor 1
- UBX domain-containing protein 7
- UBX domain-containing protein 1
- SKI family transcriptional corepressor 1
- Dual specificity mitogen-activated protein kinase kinase 5
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL23m
Sequence:
MSNSHPLRPFTAVGEIDHVHILSEHIGALLIGEEYGDVTFVVEKKHFPAHRVILAARCQYFRALLYGGMRESQPEAEIPLQDTTAEAFTMLLRYIYTGRATLTDEKEEVLLDFLSLAHKYGFPELEDSTSEYLCTILNIQNVCMTFDVASLYSLPKLTCMCCMFMDRNAQEVLASDGFLSLSKTALLNIVLRDSFAAPEKDIFLALLNWCKHNAKENHAEIMQAVRLPLMSLTELLNVVRPSGLLSPDAILDAIKVRSESRDMDLNYRGMLIPEENIATMKYGAQVVKGELKSALLDGDTQNYDLDHGFSRHPIDDDCRSGIEIKLGQPSIINHIRLLLWDRDSRSYSYFIEVSMDELDWIRVIDHSHYLCRSWQKLYFPARVCRYIRIVGTHNTVNKIFHIVAFECMFTNKAFTLEKGLIVPLENVATIADCASVIEGVSRSRNALLNGDTKNYDWDSGYTCHQLGSGAIVVQLAQPYIIGSIRLLLWDCDDRSYSYYVEVSTNQQQWTMVADRTKVSCKSWQSVTFERQPASFIRIVGTHNTANEVFHCVHFECPEQQSNQKEDSSEEPGTGDPSTPNQQLDPHAPRAPSASSLPPSPGPNSRSPNQQNQ
Protein: Kinesin-like protein KIFC3 (Q9BVG8)
Organism: Homo sapiens (Human)
Function: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:19041755}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19041755}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Apical cell membrane. On membrane organelles immediately beneath the apical plasma membrane of renal tubular epithelial cells. Localized in the distal tubules and loops of Henle in the kidney, but not in the proximal tubules or the glomeruli, with stronger staining in the apical area of these epithelial cells (By similarity). Localizes along zonula adherens only at mature cell-cell contacts. {ECO:0000250}.
Interaction partners:
- Calmodulin-regulated spectrin-associated protein 3
- Pleckstrin homology domain-containing family A member 7
- Kinesin-like protein KIF11
- Centrosomal protein of 170 kDa
- Kinesin light chain 2
- Kinesin-associated protein 3
- Kinesin-like protein KIF23
- Kinesin-like protein KIF15
- Kinesin-like protein KIF18A
- Kinesin-like protein KIF3B
Sequence:
MVPSRRTWNLGATPSLRGLWRVGRAPEPEPGMARPAPAPASPAARPFPHTGPGRLRTGRGKDTPVCGDEDSSARSAARPALAQCRALSVDWAGPGSPHGLYLTLQVEHLKEKLISQAQEVSRLRSELGGTDLEKHRDLLMVENERLRQEMRRCEAELQELRTKPAGPCPGCEHSQESAQLRDKLSQLQLEMAESKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQARNQHLQEQVAMQRQVLKEMEQQLQSSHQLTARLRAQIAMYESELERAHGQMLEEMQSLEEDKNRAIEEAFARAQVEMKAVHENLAGVRTNLLTLQPALRTLTNDYNGLKRQVRGFPLLLQEALRSVKAEIGQAIEEVNSNNQELLRKYRRELQLRKKCHNELVRLKGNIRVIARVRPVTKEDGEGPEATNAVTFDADDDSIIHLLHKGKPVSFELDKVFSPQASQQDVFQEVQALVTSCIDGFNVCIFAYGQTGAGKTYTMEGTAENPGINQRALQLLFSEVQEKASDWEYTITVSAAEIYNEVLRDLLGKEPQEKLEIRLCPDGSGQLYVPGLTEFQVQSVDDINKVFEFGHTNRTTEFTNLNEHSSRSHALLIVTVRGVDCSTGLRTTGKLNLVDLAGSERVGKSGAEGSRLREAQHINKSLSALGDVIAALRSRQGHVPFRNSKLTYLLQDSLSGDSKTLMVVQVSPVEKNTSETLYSLKFAERVRSVELGPGLRRAELGSWSSQEHLEWEPACQTPQPSARAHSAPSSGTSSRPGSIRRKLQPSGKSRPLPV
Protein: RNA uridylyltransferase (EC 2.7.7.52) (Q38CM2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MALVRRIGSSLLSHKEYSRFLDNRKWLEGALEGFSIENVLGISQLSSRPSVLMYGSCVSGTAFSNADADYAVLFLTQGNTEESSMANMLNYTHSKFIEVKREHHQRVLLAILEHIRVSFCSTVLKCEQIYSARVPFIRLFKSSANNTEGSHLDVSLSFDGPRNSLLLRLYMEGDPRLRCGVLCAKKWCRSQGILDARRGWISAYALTVMYIFYMQVTKRAVRIIDESEVNNILYCMSKQMLEGVNECFPFVGDVCSCSDVDIQNVLSDLHGFFHFFGGSMCFDFDTDVVDIRKNDKLVSKESWLEGINHFDEKTRWNLLGYETIMIRDPYEDHNLGRSVDFFRGERIREVFRLASETKIEDVLNELAKQGRLSSV
Protein: Allantoinase (Eurofung) (Q5B4C7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- allantoicase
- Uricase
- Purine permease
- Dihydroorotate dehydrogenase
- Ureidoglycolate hydrolase, putative
- NADH-cytochrome b5 reductase 1
- NADH-cytochrome b5 reductase 2
Sequence:
MNGEIPSIAVFTSSRAVIGGRLTSATIVVSRTTGKVTAVFDSVIPASDFPDGTPYTDFSPYVLLPGLVDAHVHLNEPGRTEWEGFYTGTQAAAFGGVTTVIDMPLNAIPPTTTVENFKLKLKAAEGKCWVDVGFYGGIIPGNAGELKALVREGVRGFKGFLIDSGVDEFPAVSSEDVRKAMAELADEPTTLMFHAEMVPPKTPSELPEVMPEGAPEAYSTFLASRPSEYELCAVEEILSLSHLAPKLPLHIVHLSAMEAIPLLRKARAEGVPITAETCYHYLSLAAEEIRDGDTRHKCCPPIRSKSNQDALWAELDRHAEDGVIKTIVSDHSPCTPDLKLLPSHIPGNCSHGSSKHANTTPVVNEGSFLSAWGGISSVGLGLPILWTELSRRKGLTSSPDDTTTKQALQDIVHLCCANTAAQVGLHKSKGDLVPGYDADFCVFDDTAEWEVEPSTMLFRNKCSPYQGRTMRGMVRETWLRGEKIFNRDDGFTVKAPSGSLLLEKRV
Protein: Rho-related protein racL (Q9GPQ8)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Mss4-like family protein
- Cofilin-1A
Sequence:
MQYIKMVICGDGAVGKTSLLIAFASGEFPRDYQPTVFDNFSTLYMFQNKAYNLGLFDTAGQEDFDRLRPLGYNDTDLFLICYSVINPPSYANVYDKWYSEIKLYTGSEIPLILVGTQNDLRHDKATRETLALKQQAPISYEEGMMMRKRIGAKAFTECSVVSGKNVKQVFEEAIKVYQDRQIEISKSKEKNNCIIL
Protein: Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18) (P53714)
Organism: Sus scrofa (Pig)
Function: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity. Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation. Integrin alpha-L/beta-2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}. Membrane raft {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}.
Interaction partners:
- Integrin subunit alpha M
- Integrin subunit alpha L
- Intercellular adhesion molecule 1
- Filamin A
- TYRO protein tyrosine kinase-binding protein
- Complement C3
- Integrin beta-1
- Intercellular adhesion molecule 3
- Junctional adhesion molecule C
- Thy-1 membrane glycoprotein
Sequence:
MLCRCSPLLLLVGLLTLRSALSQECAKYKVSTCRDCIESGPGCAWCQKLNFSGQGEPDSVRCDTREQLLAKGCVADDIVDPRSLAETQEDQAGGQKQLSPQKVTLYLRPGQAATFNVTFRRAKGYPIDLYYLMDLSYSMLDDLINVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPEKLRNPCPNKEKECQAPFAFRHVLKLTDNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKSSNEFDYPSVGQLAHKLAESNIQPIFAVTKKMVKTYEKLTDIIPKSAVGELSEDSSNVLELIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVSQVNQPRGDCDGVQINVPITFQVKVTASECIQEQSFVIRALGFTDTVTVRVLPQCECRCGDSSKERTLCGNKGSMECGVCRCDAGYIGKHCECQTQGRSSQELEGSCRKDNSSIICSGLGDCICGQCVCHTSDVPNKKIYGQFCECDNMNCERFDGQVCGGEKRGLCFCSTCRCQEGFEGSACQCLKSTQGCLNLQGVECSGRGRCRCNVCQCDFGYQPPLCTDCPSCQVPCARYAKCAECLKFDTGPFAKNCSAECGTTKLLPSRMSGRKCNERDSEGCWMTYFLVQRDGRDNYDLHVEETRECVKGPNIAAIVGGTVGGVVLVGIFLLVIWKVLTHLSDLREYKRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAER
Protein: N,N'-diacetyllegionaminic acid synthase (EC 2.5.1.101) (Q5ZXH9)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates such as lipopolysaccharide (LPS) which could be a key determinant in the ability of L.pneumophila to inhibit the fusion of phagosomes with lysosomes. LPS contains a majority alpha2,4-linked homomer of legionaminic acid. Catalyzes the condensation of 2,4-diacetamido-2,4,6-trideoxymannose with phosphoenolpyruvate (PEP) to give N,N'-diacetyllegionaminic acid.
Interaction partners:
- CMP-N,N'-diacetyllegionaminic acid synthase
- UDP-N,N'-diacetylbacillosamine 2-epimerase
- 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC
- LPS biosynthesis protein, PseA-like
- GDP-perosamine synthase
- Acetyltransferase
- Imidazole glycerol phosphate synthase subunit HisH 1
- imidazole glycerol-phosphate synthase
- dTDP-glucose 4,6-dehydratase
Sequence:
MGSNRKINGIKPRGSSMTCFIIAEAGVNHNGDLQLAKELVYAAKESGADAVKFQTFKADTLVNKTVEKAEYQKNNAPESSTQYEMLKALELSEEDHYLLSELANSLGIEFMSTGFDEQSIDFLISLGVKRLKIPSGEITNVPYLQHCASKKLPLIISTGMCDLQEVRVAIDTVKPYYGNSLSDYLVLLHCTSNYPASYQDVNLKAMQTLADEFQLPVGYSDHTLGILVPTLAVGMGACVIEKHFTMDKSLPGPDHLASMDPEEMKNLVQSIRDAETVLGSGEKKPSDNELPIRALVRRSITLRRDLVKGAQISKEDLILLRPGTGIAPSEISNIVGSRLSMNLSAGTTLLWEHIEA
Protein: DNA damage-binding protein 1 (Zgc:63840) (Q6PGT6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSYNYVVTAQKPTAVNACITGHFTSAEDLNLLIAKNTRLEIYAVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFILTAKYNACILEYKQSGDSIDIITRAHGNVQDRIGRPSETGIIGIVDPECRMIGLRLYDGLFKVIPLDRENRELKAFNIRLEELQVIDVQFLYGCQAPTVCFIYQDPQGRHVKTYEVSLREKEFNKGPWKQENVEAEASMVIPVPEPFGGAIIIGQESITYHNGDKYLAVAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRLFMLLLEKEELMDGAVVLKDLHVELLGETSIAECLTYLDNGVVFVGSRLGDSQLVKLNVDSNDQGSYVGVMETFTNLGPIVDMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGIGIHEHASIDLPGIKGLWPLRSESSRDTDDMLVLSFVGQTRVLMLSGEEVEETELQGFVDNQQTFFCGNVAHQQLIQITSVSVRLVTQDSKALVSEWKEPQGRNISVASCNNTQVVLAVGRVLYYLQILSGELKQISSTEMEHEVACLDITPLGERTADSCICAVGLWTDISARLLKLPCFTPLHKEMLGGEIIPRSILMTTFEGSHYLLCALGDGALFYFGLDIQTGVLSERKKVTLGTQPTVLRTFRSLSTSNVFACSDRPTVIYSSNHKLVFSNVNLKEVNYMCPLNSEGYPDSLALANNSTLTIGTIDEIQKLHIRTVPLYESPKRICYQEVSQCFGVLSSRVEMQDASGTTAAVRPSASTQALSSSVSSSKLLPSSTSPHETSFGEEVEVHSLLVVDQHTFEVLHAHQFLQNEYALSMVSCKLGRDPAVYFIVGTAMVYPEEAEPKQGRIIVFHYTDGKLQTVAEKEVKGAVYSMVEFNGKLLASINSTVRLYEWTAEK
Protein: Possible acyl-CoA dehydrogenase FadE16 (O53926)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Phosphate ABC transporter substrate-binding protein
- Possible molybdopterin biosynthesis protein MoeX
- Probable integral membrane protein
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- Probable enoyl-CoA hydratase EchA3
- Probable transcriptional regulatory protein
- Probable fatty oxidation protein FadB
- Probable acyl-CoA dehydrogenase FadE18
- Probable acyl-CoA dehydrogenase FadE24
Sequence:
MATPGVVQEVVSVAAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTVAASPPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSADGAAGDVDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAVDIRIPDSYRLGEAGGGFGIMMQTVLPWFNLGNAAVSLGLATAATGAAVKHVGTARLEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLTHVLGVKASVNDAALTITESAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAVTGLPLF
Protein: Retinoblastoma-associated protein (pRb) (Rb) (pp105) (P33568)
Organism: Rattus norvegicus (Rat)
Function: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle. The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase. RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P13405}. Cytoplasm {ECO:0000250|UniProtKB:P13405}. Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization (By similarity). Localizes to the cytoplasm when hyperphosphorylated (By similarity). {ECO:0000250|UniProtKB:P06400, ECO:0000250|UniProtKB:P13405}.
Interaction partners:
- Transcription factor E2F1
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 2
- Histone deacetylase 1
- G1/S-specific cyclin-D1
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- E2F transcription factor 3
- Cyclin-A2
- cyclin-dependent kinase
- E2F transcription factor 4
Sequence:
MPPKAPRRTAAAEPPPPPPPPPEDDPAQDSDPEELPLIRLEFEKIEEPEFIALCQKLKVPDHVRERAWLTWEKVSSVDGILEGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKSIETSVYKFFDLLKEIDTSTKVDNAVSRLLKKYNVLCALYSKLERTCGLIYLTQPSSGLSTEINSMLVLKVSWITFLLAKGEVVQMEDDLVISFQLMLCVLDYFIKLSPPALLREPYKTAATPINGSPRTPRRGQNRSARIAKQLESDTRTIEVLCKEHECNVDEVKNVYFKNFIPFISSLGIVSSNGLPELESLSKRYEEVYLKSKDLDARLFLDHDKTLQTDTIDSFETERTPRKSNPDEEANMVTPHTPVRTVMNTIQQLMVILNSASDQPSENLISYFSNCTVNPKENILKRVKDVGHIFKEKFASAVGQGCIDIGAQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSMLQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKVEANLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDGEGPDHLESACSLSLPLQSNHTAADMYLSPIRSPKKRTSTTRVNSAANTETQAASAFHTQKPLKSTSLSLFYKKVYRLAYLRLNTLCARLLSDHPELEHIIWTLFQHTLENEYELMKDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGSDEADGSKHLPAESKFQQKLAEMTSTRTRMQKQKLNDSMEISNKEEK
Protein: Probable NAD(P)H-dependent D-xylose reductase xyl1 (XR) (EC 1.1.1.307) (Q5BGA7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway (By similarity).
Interaction partners:
- Probable D-xylulose reductase A
- L-arabinitol 4-dehydrogenase
- D-xylulose reductase
- D-xylulose reductase
- L-arabinitol 4-dehydrogenase
- Zinc-dependent alcohol dehydrogenase, putative
- Sorbitol/xylitol dehydrogenase, putative
Sequence:
MSPPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYEAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKRSDLFIVSKLWNSFHDGERVEPIARKQLSDWGIDYFDLYIVHFPVSLKYVDPEVRYPPGWENAEGKVELGKATIQETWTAMESLVDKGLARSIGISNFSAQLLLDLLRYARIRPATLQIEHHPYLTQERLVTFAQREGIAVTAYSSFGPLSFLELSVKQAEGAPPLFEHPVIKDIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPARLLQNLDVVGFDLEDGELKAISDLDKGLRFNDPPNYGLPITIF
Protein: Auxin-binding protein 1 (ABP1) (P33487)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin receptor that controls cell elongation and cell division. Involved in embryonic morphogenesis. Acts on the cell cycle, endocycle, cell plate formation, and cell expansion and contributes to the control of auxin-related gene expression. Controls root meristem size and mediates auxin responsiveness. Involved in activation of ROP GTPases in response to auxin and regulation of clathrin-mediated endocytosis in roots. Acts as a positive factor in clathrin recruitment to the plasma membrane, thereby promoting endocytosis. Upon auxin binding, restricts the internalization of PIN proteins by inhibiting clathrin-mediated endocytosis. Involved in the regulation of polar auxin transport. Behaves as a negative regulator of the SCF(TIR1/AFB) signaling pathway, protecting AUX/IAA repressors from degradation. Regulates the expression of cell wall remodeling genes via an SCF(TIR1/AFB)-dependent pathway. Involved in the modulation of hemicellulose xyloglucan structure. Required for rapid auxin-mediated re-orientation of microtubules to regulate cell elongation in roots and dark-grown hypocotyls as well as asymmetric growth during gravitropic responses. Involved in the shade avoidance response. Forms with TMK1 a cell surface auxin perception complex that activates ROP signaling pathways. ABP1 sensing of auxin is important for the ABP1-TMK1 complex formation. Interacts functionally with phytochrome to regulate growth.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:24578577, ECO:0000305|PubMed:7517789}. Cell membrane {ECO:0000269|PubMed:24578577, ECO:0000303|PubMed:16649105}; Peripheral membrane protein {ECO:0000303|PubMed:16649105}. Note=In plasmolyzed cells, observed in strands connecting the apoplast and the plasma membrane. {ECO:0000269|PubMed:24578577}.
Interaction partners:
- Receptor protein kinase TMK1
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Rac-like GTP-binding protein ARAC3
- Rac-like GTP-binding protein ARAC4
- CRIB domain-containing protein RIC4
- Auxin transporter protein 1
- CCG-binding protein 1
- Monocopper oxidase-like protein SKU5
- F-box protein SKP2A
- Auxin efflux carrier component 2
Sequence:
MIVLSVGSASSSPIVVVFSVALLLFYFSETSLGAPCPINGLPIVRNISDLPQDNYGRPGLSHMTVAGSVLHGMKEVEIWLQTFAPGSETPIHRHSCEEVFVVLKGSGTLYLAETHGNFPGKPIEFPIFANSTIHIPINDAHQVKNTGHEDLQVLVIISRPPIKIFIYEDWFMPHTAARLKFPYYWDEQCIQESQKDEL
Protein: Sodium channel and clathrin linker 1 (Sodium channel-associated protein 1) (Q96NL6)
Organism: Homo sapiens (Human)
Function: Adapter protein that links SCN10A to clathrin. Regulates SCN10A channel activity, possibly by promoting channel internalization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23348840}. Note=Localizes to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane.
Interaction partners:
- Centrosomal protein of 83 kDa
- Fas-binding factor 1
- Centrosomal protein of 164 kDa
- Centrosomal protein of 89 kDa
- Sodium channel protein type 10 subunit alpha
- Ninein
- Centrosomal protein kizuna
- Clathrin heavy chain 1
- Leucine-rich repeat-containing protein 45
- Outer dense fiber protein 2
Sequence:
MAAEIDFLREQNRRLNEDFRRYQMESFSKYSSVQKAVCQGEGDDTFENLVFDQSFLAPLVTEYDKHLGELNGQLKYYQKQVGEMKLQLENVIKENERLHSELKDAVEKKLEAFPLGTEVGTDIYADDETVRNLQEQLQLANQEKTQAVELWQTVSQELDRLHKLYQEHMTEAQIHVFESQKQKDQLFDFQQLTKQLHVTNENMEVTNQQFLKTVTEQSVIIEQLRKKLRQAKLELRVAVAKVEELTNVTEDLQGQMKKKEKDVVSAHGREEASDRRLQQLQSSIKQLEIRLCVTIQEANQLRTENTHLEKQTRELQAKCNELENERYEAIVRARNSMQLLEEANLQKSQALLEEKQKEEDIEKMKETVSRFVQDATIRTKKEVANTKKQCNIQISRLTEELSALQMECAEKQGQIERVIKEKKAVEEELEKIYREGRGNESDYRKLEEMHQRFLVSERSKDDLQLRLTRAENRIKQLETDSSEEISRYQEMIQKLQNVLESERENCGLVSEQRLKLQQENKQLRKETESLRKIALEAQKKAKVKISTMEHEFSIKERGFEVQLREMEDSNRNSIVELRHLLATQQKAANRWKEETKKLTESAEIRINNLKSELSRQKLHTQELLSQLEMANEKVAENEKLILEHQEKANRLQRRLSQAEERAASASQQLSVITVQRRKAASLMNLENI
Protein: Dynein axonemal intermediate chain 4 (WD repeat-containing protein 78) (E9PYY5)
Organism: Mus musculus (Mouse)
Function: Plays a critical role in the assembly of axonemal dynein complex, thereby playing a role in ciliary motility.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30060180}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30060180}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6GPB9}.
Interaction partners:
- Dynein axonemal intermediate chain 3
- Dynein, axonemal, heavy chain 9
- Dynein, axonemal, heavy chain 10
- Dynein, axonemal, heavy chain 6
- Dynein axonemal intermediate chain 7
- Dynein axonemal heavy chain 2
- Dynein axonemal heavy chain 1
- Dynein axonemal heavy chain 3
- Dynein axonemal heavy chain 5
- Thioredoxin domain-containing protein 3
Sequence:
MHSSPTSTRKQASFAASASAQPRKSISFINPSKSSAGKGYAASNPNKLAVSRTMGFLTDMKPAEKLNVPSAKTVQVLDSKGVDVTPRPLYHPDPHAASAKPNKLLTSQEGSLGSDYISSYSLYQNTLNPSMLGQYTRSVLGSSSVSKSSISTTESMSEDLEDSSYKRDRLASFTDVRVLRSTAEAAISKEELEKTIEIILTETETLRFFDLPTVMFSTESEEAEKIIEKNKKYETLCRNRLGNDLYVERMMQTFNGAPKNKEVQCEKIILEEKGVVATTWDLYDSYNIPETLLAAKRSGYSSKGSLPAKDRDPKIQDSESSSLMDIENVILAKVQEDEEDNSEAILKSDKLHQDLFYMERVLMENVFQPKLAAYRQLPVYKEHEPEEPEETLQVENLKVAEDEPKKEDEEEVEMELELEIATEQSTIPANLERLWSFSCDLTKGLNVSSLSWNKANPDLLAVGYGNFGFREQKKGMACCWSIKNPMWPERIYQSSYGVTSVDFSNSSPNLLAVGYHNGTVAIYNVQSSHNIPVLDSSESPQKHLGPVWQVQWIEQDRGTTGDDKREILVSISADGRISKWIIRKGLDCHDLMRLKRTTATGGKKGGEKEKKGEALISRQAPGMCFAFHPKDTNIYLAGTEEGLIHKCSCSYNEQYLETYRGHKGPVYKVTWNPFCPDVFLSCSADWGVMIWHQDTVKPFLSFYPTTYVVYDVSWSPKSAYIFAAANENRVEIWDLQISTLDPLIVNVANPGIKFTTVLFAKETDCLLVGDSDGQVAVYELRNMPTASDTSRGDVINILLGPKTNHTG
Protein: Dipeptidyl-peptidase 8-like serine peptidase (Q38AR6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPTLPLSKYIDELKALEGLLAVDGKPRMLKFVGDQLYWLQGMDQELYSVNIADHNATPSRVIDRCRKGCTAAEGKEGSTVETKEEELLRERLRSRVTGISSYRVRCRDGAVFFTSGANIFLYRPASGKPPLKVLDYIGDEELKQRFSSEKKPFLCIEYFSHLANDAGACDSTKERADVISFVYSNNLYIATVVEGSGEASHSREPPLRVNVECVTTFGDELHSCGDADYIIQEEFGRYTGHYATAEYVLFSYTDVSMLREVMLIDGSTDSGVEKMPYCRVGDPNARTVLVVYERRTKRYRVVPSSAIAAIAPWAEYMPRFGFKDEHTIYFSVLSRTQEKMSLLSCRINSLPVVDAEALASCFSEAARDTDVAAVAAGTTLATRAATVNLTTEWHQHIPWAWVDVQPGVALHLCGKYEVLVRHANESESAHSHVYARAQGGDEGSWRPLTCGAWNVRAGGLIVKDDRVFFLANARNRLESVLYSVVINLDAGPVSAEELTQLTPSGEHVYSFAVLNNTLCYVSSTATTPAELHISSINNPGSRWVVPTRHLWDDTSEKAVTPRTTLEGLTVPHIINIVNRRGVPLSGRLFVSPHAALGKLNPLAMYIYGGPHAQLVYDSDFDGACKPIFQMLASFGISVLVADGQMSNANGLRDHSICKHSMGSFETSDYVDWVRHMTNCKELPCGFCADPERVAIFGWSYGGYATLLAMSQAPDVFKIGFAGAPVGDWTLYDTGYTERYMGLLHTNADGTSGSKGDATAKCAISDAYTRSAIKAFASNFPEELNRVFIAHGLLDENVHFCHTSVVVNAMIDAGKPCCSVVYPGERHSLRKKKASRLHHDAMLAKTLMEVL