wanglab/gogpt-training-data huggingface dataset:
Protein: E3 SUMO-protein ligase PIAS1 (EC 2.3.2.-) (DEAD/H box-binding protein 1) (E3 SUMO-protein transferase PIAS1) (Gu-binding protein) (GBP) (Protein inhibitor of activated STAT protein 1) (RNA helicase II-binding protein) (O75925)
Organism: Homo sapiens (Human)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O88907}. Nucleus speckle {ECO:0000269|PubMed:12393906, ECO:0000269|PubMed:9177271}. Nucleus, PML body {ECO:0000250|UniProtKB:O88907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11672422}. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton (PubMed:11672422). Interaction with MSX1 is required for localization to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:O88907, ECO:0000269|PubMed:11672422}.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- Signal transducer and activator of transcription 1-alpha/beta
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Signal transducer and activator of transcription 3
- Signal transducer and activator of transcription 2
- Breast cancer type 1 susceptibility protein
- Androgen receptor
- Cellular tumor antigen p53
- SUMO-activating enzyme subunit 1
Sequence:
MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRNYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGTWAPMRSKKEVQEVSASYNGVDGCLSSTLEHQVASHHQSSNKNKKVEVIDLTIDSSSDEEEEEPSAKRTCPSLSPTSPLNNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPTTNGSSSGSNSSLVSSNSLRESHSHTVTNRSSTDTASIFGIIPDIISLD
Protein: Pleiotropic drug resistance protein 1 (ABC transporter G family PDR1) (Strigolactone transporter) (H6WS94)
Organism: Petunia hybrida (Petunia)
Function: Cellular strigolactone (SL) transporter required for the exudation of SL from the root to the soil. The presence of SL in the vicinity of the roots is required for development of symbiotic interactions with arbuscular mycorrhizal fungi (AMF). Transports SL in the above ground tissues and is required for the control of shoot branching. SL regulates plant shoot architecture by inhibiting the outgrowth of axillary buds. Involved in the regulation of shootward and outward directional strigolactone transport in roots. Due to its polar localization in root cells, mediates directional shootward strigolactone transport, as well as localized outward directional transport for exudation to the soil.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22398443, ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane (PubMed:22398443, PubMed:25683808, PubMed:27040840). Exhibits asymmetric localization in different root tissues (PubMed:25683808). In root tips, localizes at the apical membrane of hypodermal cells (PubMed:25683808). In the hypodermal passage cells localizes in the outer-lateral membrane (PubMed:25683808). {ECO:0000269|PubMed:22398443, ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}.
Interaction partners:
Sequence:
MEGGEELFRVSSARLSSSNVWRNSAMDVFSRSSREADDEEALKWAALEKLPTYLRIRRGILTEEEGQSREVDITKLDLVERRNLLERLIKITDEDNEKFLLKLKERIDRVGLDLPTIEVRFEHLSVDAEARVGSRALPTVFNFTVNILEDFLNYLHILPNRKQPLPILHDVSGIIKPGRMTLLLGPPSSGKTTLLLALAGKLDKDLKVSGRVTYNGHDMNEFVAQRSSAYISQYDLHIGEMTVRETLAFSARCQGVGAKYEILAELSRREKEANIKPDPDVDIFMKAAWNEGQEANVVTDYTLKILGLEICADTIVGDEMVRGISGGQRKRLTTGEMMVGPARALFMDEISTGLDSSTTYQIVNSIRQSIHILQGTAVISLLQPAPETYDLFDDIILLSDGQIVYQGPRENVLEFFEYMGFICPERKGVADFLQEVTSRKDQEQYWARREESYKFITVREFSEAFQAFHIGRKLGDELAVPFDKSKSHPAALTTKRYGVSKKELLKACTAREYLLMKRNSFVYIFKMIQLTLMASITMTLFLPTEMHRNTTIDGAVFLGALFYALIMIMFNGFSELALSIMKLPSFYKHRDLLFFPPWAYALPTWILKIPITLVEVAIWVCMTYYVIGFEADVGRFFKQLLLLICVNQMASGLFRLMGALGRNIIVANTFGSFVLLTVLVMGGFVLSRDDVKKWWIWGYWISPMMYAQNAIAVNEFLGKSWAHVPPNSTSTETLGVSFLKSRGIFPDARWYWIGAGALIGYVFLFNFLFAVALAYLNPFGKPQAVLSEETVAERNASKRGEVIELSSLGKSSSEKGNDVRRSASSRSMSSRVGSITAADLSKRRGMILPFEPLSITFDDIRYAVDMPQEMKAQGFTEDRLELLRGVSGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGTISISGYPKQQETFARIAGYCEQTDIHSPHVTVYESLQFSAWLRLPREVDTATRKMFIEEVMELIELIPLRDALVGLPGVNGLSTEQRKRLTVAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFDAFDELLLLKRGGEEIYVGPLGRQSSHLIKYFEGIDGVPKIKDGYNPATWMLEITSVAQEGALGNDFTELYKNSELYRRNKALIKELSVPASCSKDLYFPTKYSQSFFTQCMACFWKQHWSYWRNPPYTAVRIMFTFFIALMFGTIFWDLGSRRERQQDLLNAIGSMYIAVLFLGVQNATTVQPVIAIERTVFYRERAAGMYSAMPYAFGQVMIELPYLFLQTIIYGVIVYAMIGFEWTVAKFFWYLFFMYFTLLYFTLYGMMTVAVTPNQSIAAIISSAFYAVWNLFCGFIVPKTRMPVWWRWYYYICPISWTLYGLIASQFGDIQDRLDTNETVEQFIENFFDFKHDFVGYVALILVGISVLFLFIFAFSIKTFNFQKR
Protein: Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) (P62629)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P68104}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens. Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B. {ECO:0000250|UniProtKB:P68104}.
Interaction partners:
Sequence:
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGSASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (C6KRJ8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MMLMGSEGLLPPNWETAYTENGDKYFIDHNTGTTTWDDPRELPPGWEQVDDQNYGTFYVDHINRKTQYERPYGFGGSSATIDQPVKYGTLPSSTNHNHNNIYSHYNSGTLKSSSSPRDSGFDSSPTRYRKFGDPPETATSSADYDHHSKMFSRSSNPLFTTDPARLGGELISTKIVKGAKGLGFTLIGNDSSSRGDEFIQVKSVLSGGPAAANGVLRSGDILVRVNGRLLLGATQKEACDVFVAIPVNEAVDIQVCRGYELFIDPANRIVTENVYAAAKSRDLHEIDIFKGSEGFGFTIADNLNGQRIKKILFPSQCPNLMEGDTIVELDGRNVRPIPHTQLVDMLRERPIGYRGKLVVKRGSPKTRSRTPSAAFRYGEPQTNMMDSAAPLPVRSKTPAERQTSRTEEDQNVRNTLQRQPAVTSEWEGMSSAIPASRMRPSSTTLGFATPNYIPLSQYNQKPSDLITVSLIRKPVGFGFRLLGGVESKTPLSVGQIVIGGAAEEDGRLQEGDEIVEIDGHNVEGASHSEAVVLLEAAAQNKHVKLIVRRPSRTDPARRGSLNSAGPSGSYDVLLHRNENDGFGFVLMSSQHKNGSTVGQIQPGSPAARCGRLSVGDRVIAVNGIDILSLSHPDTISLIKDSGLSVRLTIAPPNTAGPVLPMVSATLGRNFTMNGHYESNYGLPPPPPSVYEKHPPPSYLAFDGLSINDRMSMNGNLIDVTLERGTKGFGFSIRGGQEFGSMPLFVLRIADDGPAKADGRLQVGDQLTTINGQSTKGMSHDDAIRIIKQHTMVNLTVLRNRLP
Protein: Transcription factor IBH1 (AtIBH1) (BHLH transcription factor zeta) (bHLH zeta) (Basic helix-loop-helix protein 158) (AtbHLH158) (bHLH 158) (Protein ILI1-BINDING BHLH 1) (bHLH transcription factor bHLH158) (Q9SKX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical and probable non DNA-binding bHLH transcription factor that acts as transcriptional repressor that negatively regulates cell and organ elongation in response to gibberellin (GA) and brassinosteroid (BR) signaling. Is able to form heterodimer with BHLH49, thus inhibiting DNA binding of BHLH49, which is a transcriptional activator that regulates the expression of a subset of genes involved in cell expansion by binding to the G-box motif. Binds and inhibits HBI1, a positive regulator of cell elongation that directly binds to the promoters and activated the two expansin genes EXPA1 and EXPA8, encoding cell wall loosening enzymes. The ability of IBH1 to inhibit BHLH49 and HBI1 is counteracted by binding to the antagonist bHLH transcription factor PRE1, restoring the transcriptional activity of BHLH49 and HBI1 and resulting in induction of cell elongation. Functions redundantly with IBL1/BHLH159 in a regulation node known as the incoherent feed-forward loop (FFL).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:23161888}.
Interaction partners:
- Transcription factor PRE1
- Transcription factor BEE 2
- Transcription factor HBI1
- Transcription factor bHLH150
- Transcription factor PRE5
- Transcription factor bHLH49
- Protein BRASSINAZOLE-RESISTANT 1
- Transcription factor PRE3
- Transcription factor PRE6
- Transcription factor BEE 1
Sequence:
MASADKLINTDVPEKDVFAFHFLQSLSNLRKQNPFDTPDQKNYRVRKIKKAAYVSMARAAGGSSRLWSRALLRRADKDDNKIVRFSRRKWKISSKRRRSNQRAPVVEEAAERLRNLVPGGGGMETSKLMEETAHYIKCLSMQVKVMQCLVDGLSPK
Protein: Transcription initiation factor TFIID subunit 10 (Q5BH26)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR017246}.
Interaction partners:
- Transcription factor TFIID complex 145 kDa subunit, putative
- Transcription initiation factor TFIID subunit 13
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 7, putative
- Transcription initiation factor TFIID subunit 5
- SAGA-like transcriptional regulatory complex subunit Spt3, putative
Sequence:
MSDTKPPSTLPQSQPPPNSQDQSSEAIVVPKLEPDSDATALDTSIEQEAVMAGPSVNSAAAGPDAGAAPGAGVGDDQIGNPVQAPTSVDAAATSKKETSLREFLGKMDDYAPIIPDAVTAHYLTLAGLPPPGHGPNQTPPHLARLLALATQKFIADIAADSYQYARIRASNSSSASNPMGSLNAASGLGLAGAGGAGAGSAGGAGTGGAGETGKGGSKAGTHLGIQRPGFGGGGSGGSGQGRTVLTMEDLGMAVAEYGVSVKRGEFYR
Protein: 3-ketoacyl-CoA thiolase B, peroxisomal (EC 2.3.1.155) (EC 2.3.1.16) (EC 2.3.1.9) (Acetyl-CoA acyltransferase B) (Beta-ketothiolase B) (Peroxisomal 3-oxoacyl-CoA thiolase B) (Q8VCH0)
Organism: Mus musculus (Mouse)
Function: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs) (Probable). Plays an important role in fatty acid peroxisomal beta-oxidation (Probable). Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs (By similarity).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P09110}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000250|UniProtKB:P09110}.
Interaction partners:
- Peroxisomal bifunctional enzyme
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MHRLQVVLGHLAGRPESSSALQAAPCSAGFLQASASDVVVVHGRRTPIGRASRGCFKDTTPDELLSAVLTAVLQDVKLKPEQLGDISVGNVLQPGAGAIMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMTLSQRGNHGNISSRLLENEKARDCLIPMGITSENVAERFGVSRQKQDAFALASQQKAASAQSRGCFHAEIVPVTTTVLNDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN
Protein: Chromatin assembly factor 1 subunit FAS2 (CAF-1 subunit FAS2) (CAF-1 p60 homolog) (Protein FASCIATA 2) (Q9SXY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the chromatin assembly factor complex (CAF-1) involved in chromatin assembly following DNA replication and DNA repair. Required for several aspects of development, including seedling growth and leaf hair differentiation. Plays a critical role in the organization of shoot apical meristem (SAM) and root apical meristem (RAM) during postembryonic development by facilitating stable maintenance of gene expression states. Seems not required to maintain transcriptional repression of heterochromatic genes. Involved in heterologous recombination.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone-binding protein MSI1
- Chromatin assembly factor 1 subunit FAS1
- Histone chaperone ASF1B
- Probable histone chaperone ASF1A
- WD-40 repeat-containing protein MSI4
- Proliferating cellular nuclear antigen 1
- Proliferating cell nuclear antigen 2
- Histone H4
- WD-40 repeat-containing protein MSI5
- Histone H3.1
Sequence:
MKGGTIQISWHDGKPVLTVDFHPISGLLATAGADYDIKLWLINSGQAEKKVPSVSYQSSLTYHGCAVNTIRFSPSGELLASGADGGELFIWKLHPSETNQSWKVHKSLSFHRKDVLDLQWSPDDAYLISGSVDNSCIIWDVNKGSVHQILDAHCHYVQGVAWDPLAKYVASLSSDRTCRIYANKPQTKSKGVEKMNYVCQHVIMKADQQRGDETKTIKTHLFHDETLPSFFRRLSWSPDGSFLLIPAGSFKVSPTSEAVNATYVFSRKDLSRPALQLPGASKPVVVVRFCPVAFKLRGSSSEEGFFKLPYRLVFAIATLNSVYIYDTECVAPIAVLAGLHYAAITDITWSPNASYLALSSQDGYCTLVEFEDKELGEAVSISVGKKPVDGEEKKHDLEKGDELMTETTPDESKKQAELEQNEESKQPLPSKITTDGKEKEHIMQKTDDEVMTETRHEEENQPLQSKVNTPVSNKPARKRITPMAIDP
Protein: Small ribosomal subunit protein eS19B (40S ribosomal protein S19b) (Q7KS38)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein uL5
- Ribosomal protein S30, isoform A
- 40S ribosomal protein S15
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS10A
- 40S ribosomal protein S27
- Small ribosomal subunit protein uS14
Sequence:
MPGVTVKEIDQHVLTKNMAAFLKKSGKIFVPEQAVYMKTGKFKETAPTDDDWFYTRCASIMRHLYLRSPAGVGAFTKVYSGRKRNGVRPSKHCRSSDGCIRKALQALEAANMVERHPDGGRKLTPQGQRNLDRIANKIVAKQRERSAPVSMIITT
Protein: Protein serine/threonine kinase activating protein (Q5A5B4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- non-specific serine/threonine protein kinase
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM3
- DNA replication initiation factor
- Serine/threonine-protein kinase RAD53
- Origin recognition complex subunit 2
Sequence:
MSKVEEHESVNNLKRKFPSLAKPRQPLKETNSNIPSPHKRAKIESPSKQQSTQQPQQQPQPQPQPQPQQEKATHKPKKSSHQSKNNDKLAGDEMHEWQQSWRRIMKSSIVYFEGDQQSLEYRKAHKLLRLVGCKVTPFYDNNVTIIISKRPYDSKTEYSPHDIFSNVSKASIKVWNYDKVFRFLKHLGINIQTGVDELAVNTHTILPPSLTNNNEKPDLYNLLKEEKIYGSTDRDPNAKRDDLHYLGKNYLYVYDLTQTVRPIAIREWSDHYPVMQLSLDGKCPFIEDPTDQNSERKRLKRLRKFEANQAHREALRLATYKMINGISMSVHGFTATSTSTDKVDEEEDSTVKEPSEDPRFRQPLNRNSSCMQSKAFEAMASGYNGASNAVQPSMDSNLNSAAAMAGGNGLGPALSQVPSKQLNNLKRRILMKKKTTNTTEKKDKEHASGYCENCRVKYTNFDEHIMTNRHRNFACDDRNFQDIDELIASLRERKSLGNVISNGDYV
Protein: BLOC-1-related complex subunit 6 (Lysosome-dispersing protein) (Lyspersin) (Q96GS4)
Organism: Homo sapiens (Human)
Function: As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor.
Subcellular location: Lysosome membrane {ECO:0000305|PubMed:25898167}.
Interaction partners:
- SNARE-associated protein Snapin
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- KxDL motif-containing protein 1
- BLOC-1-related complex subunit 7
- BLOC-1-related complex subunit 5
- BLOC-1-related complex subunit 8
- Ragulator complex protein LAMTOR4
- Ragulator complex protein LAMTOR2
- Ragulator complex protein LAMTOR3
Sequence:
MESSRGRPGPETDLLAVAEHQALVFGGGPGRTSSEPPAGLRVSGEEETENVGGANRHPRTSPKTSSCGVVHRPEREALENEPGPQGTLSGAGSRRGAPGAEHEPSLSSRHKNPAPPEGKPSSGRDCRRGGPGGGMDVEQQEEEDNDEEAAAGSRAGRSFSSRLQDSRSLDGLSEACGGAGSSGSAESGAGGGRRATISSPLELEGTVSRHGDLTHFVANNLQLKIRLSGAPPPPPSAPARPCPAPAPTPTPAIPPIDPEVLRDLERLSRELGGRVDRLLRGLGGAVQELTALSVGCIQTYRDAVDSLGEAVDMSIKGMYTLLARCEELERALQPVQGLARQVRDIRRTLEVLEALCK
Protein: Unconventional myosin-VI (Unconventional myosin-6) (A0A8I5ZWC2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}.
Interaction partners:
Sequence:
MEDGKPVWAPHPTDGFQMGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNCSLMYLNEATLLHNVKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSDTIKSYQGKSLGTMPPHVFAIADKAFRDMKVLKMSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDRIVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEERNYHIFYRLCAGASEDIREKLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYVKAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCNLKNKSAPSLEYCAELLGLDQDDLRVSLTTRVMLTTAGGTKGTVIKVPLKVEQANSARDALAKTVYSHLFDHVVDRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEVKLVGILDILDEENRLPQPSDQHFTSVVHQKHKDHFRLTIPRKSKLAVHRNLRDDEGFIIRHFAGAVCYETTQFVEKNNDALHMSLESLICESRDKFIRALFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMPEKLARLDPRLFCKALFKALGLNEVDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKRVNLWLVCSRWKKVQWCSLSVIKLKNKIKYRAEACIKMQKTIRMWLCKRRHKPRIDGLVKVGTLKKRLDKFNEVVSALKDGKPEVNRQIKDLEISIDALMAKIKSTMMTREQIQKEYDALVKSSEDLLSALQKKKQQEEEAERLRRIQEEMEKERKRREEDEQRRRKEEEERRMKLEMEVKRKQEEEERKKREDDEKRIQAEVEAQLARQREEESQQQAVLAQECRDRELALRIAQNESELISDEAQGDTALRRGPAVQATKAAAGTKKHDLSKWKYAELRDTINTSCDIELLAACREEFHRRLKVYHAWKSKNKKRNTETEQRAPKSVTDYAQQNPAAQLPARQQEIEMNRQQRFFRIPFIRPADQYKDPQNKKKGWWYAHFDGPWIARQMELHPDKPPILLVAGKDDMEMCELNLEETGLTRKRGAEILPRQFEEIWERCGGIQYLQSAIESRQARPTYATAMLQNLLK
Protein: Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (3-demethylubiquinone 3-O-methyltransferase) (EC 2.1.1.-) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) (O74421)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000269|PubMed:24911838}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190, ECO:0000269|PubMed:16823372}.
Interaction partners:
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein coq9
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein coq4, mitochondrial
- Atypical kinase COQ8, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis protein coq11
- Protein sly1
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MNSMNILNKVKNVKSYTRLVRQGFLSQQRNHSVSVNEVDHFNELAKTWWDWDGGSRLLHLMNSTRLDFMTEVFRERNCFSGKKILDIGCGGGILSESMARLGASVTAVDASPMAIEVAKKHASLDPVLNGRLEYIHGSVEGSQLPTTFDVVTCMEVLEHVEQPRDFLFSLMEKVKPNGRLVLSTISRTLLARLLTITLAEHVLRIVPVGTHTFEKFIRADELSNFLKEQNWIINDIRGVCYNPLKQQWTLDKPGSSGLGLSCNYFLSAQKPMSA
Protein: Receptor-type tyrosine-protein phosphatase U (R-PTP-U) (EC 3.1.3.48) (Receptor-type protein-tyrosine phosphatase psi) (R-PTP-psi) (B3DK56)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. Functions in somitogenesis. Functions as a regulator of the biochemical clock responsible for the segmentation of the presomitic mesoderm.
Subcellular location: Cell junction {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Mast/stem cell growth factor receptor kita
- XK-related protein
- RAP2C, member of RAS oncogene family.
Sequence:
MNTCAFLLILAVQIHADSVEGPTAGCTFDEDSDPSLCEFSQGEEDDFDWQLFRAHASPHSTSDLLRGSYMMVNSSQHAAGQRAQLLLQTLSENDTHCVQFSYFLYSRDGHSPGALRVYVRVNGGPLGIPVWNVSGSRGRQWHQVELAVSTFWPNEYQILLEATVDRKGYIAVDDILLLNYPCYKAPHFSRLGDVEVNAGQNATFQCVAAGRPSEAEKFLLERHNGEVSSGGSVKHLGRNRFAVSFQLEDVQKPEQDLYRCVTQSSRGSGVSNFAELIVKVPPSPIAPPQLLRAGSTYLIIQLNTNSILGDGPIIRREIEYRASLAPWSEILGVNMVTYKLWHLDPDTEYHISVLLTRPGEGGTGPPGPPLISRTKCAEPMRALRGLRASEIQSRQLTLQWEVPAFNLTRCHTYSVSLCYRYTTAGGGGGHNTTVRECLAVEHNTSRFTLRDLPPFHTIQIRLALANTEGKKEGKEVMFQTEEDIPGGIAPESLTFTPLEDMIFLKWEEPVEPNGLITQYEISYQSIESSDPGINVPGPRRTVSKLKNETYHMFSNLHPGTTYLISVRARTAKGFGQTALTEITTNISAPTFDYGDMPSPLSETENTITVLLRPAQGRGAPVSTYQVVVEEEAGRKVKRELGIQDCFPIPTSHGEAQARGAPHYYTAELPPSSLSEATPFTVGDNHTYNGYWNSPLDPRKNYLVYFQAMSNFRGETRINCIRIARKAACKDHQRALEVTQRSEEMGLILGVCAGGLVVLILLLGAIIIIIKKGRDYYSYSYYPRKPGNMNKTPITYRQEKSNMMGSMERSFTDQSTLQEDERMALSFMDTHTCSTRSDPRSSMNESSSLLGGSPRRQCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFDGWDINKKKDKTKGRHDTLMGYDRHRVKLHPLLGDPNSDYINANYIDGYHRSNHFIATQGPKQETVYDFWRMVWQENCFSIVMITKLVEVGRVKCCKYWPDESEMYGDIKITLLKTETLAEYTVRTFALERRGYSAKHEVCQFHFTSWPEHGVPYHATGLLAFIRRVKTSTPLDAGPVVVHCSVGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLCGETAIPVNEFALAYKEMLRVDSQSNSSQLREEFQTLNSVTPHLDVEECSIALLPRNREKNRSMDVLPPDRALAFLVTTEGESNNYINAALMDSFHRPAAFIVTPHPLPGTTSDFWRLVFDYGCTSVVMLNQLNQSNSAWPCVQYWPEPGLQQYGPMQVEFLSMSADEDIITRLFRVKNVTRLQEGQLVVCQFQFLRWSAYRDVPDSKKAFLNLLASVQKWQRECGEGRTVVHCLNGGGRSGTYCASNILMEMIQYQNIVDVFYAVKTLRNAKPNMVETLEQYRFCYELVLEYLDCLEVR
Protein: Glycosomal membrane protein, putative (Q383C6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
Sequence:
MSEFQRFVKLLEQTDGRDKILKAFSGVFKALGSLDTCQSRSSAFGAVGKSIGDARCLLRMAKWVGDVPKMQNTIQDCRAKGKVNMKEVLKFLRVLCNFLYVLGDNVAFVARYNLLALRHKSIHLKAKTAQFWGFFLAAVLDVVALYGALQKRASDPATSKKEMKAALISFVKDASDTLVTMAFVGYLREVWRPSATTSGALTAVAGGVATYLNWNKIK