wanglab/gogpt-training-data huggingface dataset:
Protein: Krueppel-like factor 9 (Basic transcription element-binding protein 1) (BTE-binding protein 1) (GC-box-binding protein 1) (Transcription factor BTEB1) (Q13886)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation.
Subcellular location: Nucleus {ECO:0000269|PubMed:22711835}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Progesterone receptor
Sequence:
MSAAAYMDFVAAQCLVSISNRAAVPEHGVAPDAERLRLPEREVTKEHGDPGDTWKDYCTLVTIAKSLLDLNKYRPIQTPSVCSDSLESPDEDMGSDSDVTTESGSSPSHSPEERQDPGSAPSPLSLLHPGVAAKGKHASEKRHKCPYSGCGKVYGKSSHLKAHYRVHTGERPFPCTWPDCLKKFSRSDELTRHYRTHTGEKQFRCPLCEKRFMRSDHLTKHARRHTEFHPSMIKRSKKALANAL
Protein: Nucleoporin NUP1 (Nuclear pore protein NUP1) (P20676)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). As one of the FG repeat nucleoporins NUP1 is involved in interactions with and guidance of nuclear transport receptors such as SRP1-KAP95 (importin alpha and beta) through the NPC. Like the closely related NUP2 it also plays an important role in disassembling and recycling SRP1-KAP95 to the cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1-KAP95-cargo complex in the nucleus, NUP1 binds through its C-terminus to KAP95, thus accelerating the release of KAP95 and, indirectly, of the nuclear localization signal (NLS)-containing cargo from the SRP1-KAP95-cargo complex.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.
Interaction partners:
- Nucleoporin NUP60
- Importin subunit beta-1
- Nucleoporin NUP2
- Nucleoporin NUP100/NSP100
- Protein MLP2
- Nucleoporin NUP57
- Protein MLP1
- Nucleoporin NUP159
- Nucleoporin NUP145
- Nucleoporin NUP116/NSP116
Sequence:
MSSNTSSVMSSPRVEKRSFSSTLKSFFTNPNKKRPSSKKVFSSNLSYANHLEESDVEDTLHVNKRKRVSGTSQHSDSLTQNNNNAPIIIYGTENTERPPLLPILPIQRLRLLREKQRVRNMRELGLIQSTEFPSITSSVILGSQSKSDEGGSYLCTSSTPSPIKNGSCTRQLAGKSGEDTNVGLPILKSLKNRSNRKRFHSQSKGTVWSANFEYDLSEYDAIQKKDNKDKEGNAGGDQKTSENRNNIKSSISNGNLATGPNLTSEIEDLRADINSNRLSNPQKNLLLKGPASTVAKTAPIQESFVPNSERSGTPTLKKNIEPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATSSAGAVFKSSVEMGKTDKSTKTAEAPTLSFNFSQKANKTKAVDNTVPSTTLFNFGGKSDTVTSASQPFKFGKTSEKSENHTESDAPPKSTAPIFSFGKQEENGDEGDDENEPKRKRRLPVSEDTNTKPLFDFGKTGDQKETKKGESEKDASGKPSFVFGASDKQAEGTPLFTFGKKADVTSNIDSSAQFTFGKAATAKETHTKPSETPATIVKKPTFTFGQSTSENKISEGSAKPTFSFSKSEEERKSSPISNEAAKPSFSFPGKPVDVQAPTDDKTLKPTFSFTEPAQKDSSVVSEPKKPSFTFASSKTSQPKPLFSFGKSDAAKEPPGSNTSFSFTKPPANETDKRPTPPSFTFGGSTTNNTTTTSTKPSFSFGAPESMKSTASTAAANTEKLSNGFSFTKFNHNKEKSNSPTSFFDGSASSTPIPVLGKPTDATGNTTSKSAFSFGTANTNGTNASANSTSFSFNAPATGNGTTTTSNTSGTNIAGTFNVGKPDQSIASGNTNGAGSAFGFSSSGTAATGAASNQSSFNFGNNGAGGLNPFTSATSSTNANAGLFNKPPSTNAQNVNVPSAFNFTGNNSTPGGGSVFNMNGNTNANTVFAGSNNQPHQSQTPSFNTNSSFTPSTVPNINFSGLNGGITNTATNALRPSDIFGANAASGSNSNVTNPSSIFGGAGGVPTTSFGQPQSAPNQMGMGTNNGMSMGGGVMANRKIARMRHSKR
Protein: Uncharacterized protein C15A10.07 (O13727)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSVVFRTVEDPELKSICTTFTSSISAEFDSNTLVCDLVETDLFTEEGTSQIFTFKKNVLILPANVPEGIELRILEENVSLPLKEFEPIKVPAGAHCFLSWEKVPLRKRIKIISSSQPDDNDEESTWPGVFIKFGVENSSSAEFGEPLKSQIEIPDDQKLIVQ
Protein: Protein MLP2 (Myosin-like protein 2) (P40457)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Together with the closely related MLP1, involved in the structural and functional organization of perinuclear chromatin. MLP1/MLP2 associate with the nuclear pore complex and form filamentous structures along the nuclear periphery. Has a role in the localization of Esc1 to nucleolar regions. Together with MLP1, mediates tethering of the some telomeres to the nuclear periphery, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing. MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring. Plays a role in the incorporation of components into the spindle pole body. Involved in double-strand break repair, probably also mediated by the YKU70/YKU80 (HDF1/HDF2) heterodimer.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus, nuclear pore complex {ECO:0000269|PubMed:24152732}. Note=Nuclear periphery, excluded from nuclear envelope adjacent to nucleolus.
Interaction partners:
- Nucleoporin NUP60
- Nucleoporin NUP2
- Nucleoporin NUP1
- Protein MLP1
- Nucleoporin NSP1
- Nucleoporin NUP53
- Nucleoporin NIC96
- Nucleoporin NUP133
- Nucleoporin ASM4
- Spindle pole body component 110
Sequence:
MEDKISEFLNVPFESLQGVTYPVLRKLYKKIAKFERSEEEVTKLNVLVDEIKSQYYSRISKLKQLLDESSEQKNTAKEELNGLKDQLNEERSRYRREIDALKKQLHVSHEAMREVNDEKRVKEEYDIWQSRDQGNDSLNDDLNKENKLLRRKLMEMENILQRCKSNAISLQLKYDTSVQEKELMLQSKKLIEEKLSSFSKKTLTEEVTKSSHVENLEEKLYQMQSNYESVFTYNKFLLNQNKQLSQSVEEKVLEMKNLKDTASVEKAEFSKEMTLQKNMNDLLRSQLTSLEKDCSLRAIEKNDDNSCRNPEHTDVIDELIDTKLRLEKSKNECQRLQNIVMDCTKEEEATMTTSAVSPTVGKLFSDIKVLKRQLIKERNQKFQLQNQLEDFILELEHKTPELISFKERTKSLEHELKRSTELLETVSLTKRKQEREITSLRQKINGCEANIHSLVKQRLDLARQVKLLLLNTSAIQETASPLSQDELISLRKILESSNIVNENDSQAIITERLVEFSNVNELQEKNVELLNCIRILADKLENYEGKQDKTLQKVENQTIKEAKDAIIELENINAKMETRINILLRERDSYKLLASTEENKANTNSVTSMEAAREKKIRELEAELSSTKVENSAIIQNLRKELLIYKKSQCKKKTTLEDFENFKGLAKEKERMLEEAIDHLKAELEKQKSWVPSYIHVEKERASTELSQSRIKIKSLEYEISKLKKETASFIPTKESLTRDFEQCCKEKKELQMRLKESEISHNENKMDFSSKEGQYKAKIKELENNLERLRSDLQSKIQEIESIRSCKDSQLKWAQNTIDDTEMKMKSLLTELSNKETTIEKLSSEIENLDKELRKTKFQYKFLDQNSDASTLEPTLRKELEQIQVQLKDANSQIQAYEEIISSNENALIELKNELAKTKENYDAKIELEKKEKWAREEDLSRLRGELGEIRALQPKLKEGALHFVQQSEKLRNEVERIQKMIEKIEKMSTIVQLCKKKEMSQYQSTMKENKDLSELVIRLEKDAADCQAELTKTKSSLYSAQDLLDKHERKWMEEKADYERELISNIEQTESLRVENSVLIEKVDDTAANNGDKDHLKLVSLFSNLRHERNSLETKLTTCKRELAFVKQKNDSLEKTINDLQRTQTLSEKEYQCSAVIIDEFKDITKEVTQVNILKENNAILQKSLKNVTEKNREIYKQLNDRQEEISRLQRDLIQTKEQVSINSNKILVYESEMEQCKQRYQDLSQQQKDAQKKDIEKLTNEISDLKGKLSSAENANADLENKFNRLKKQAHEKLDASKKQQAALTNELNELKAIKDKLEQDLHFENAKVIDLDTKLKAHELQSEDVSRDHEKDTYRTLMEEIESLKKELQIFKTANSSSDAFEKLKVNMEKEKDRIIDERTKEFEKKLQETLNKSTSSEAEYSKDIETLKKEWLKEYEDETLRRIKEAEENLKKRIRLPSEERIQKIISKRKEELEEEFRKKLKENAGSLTFLDNKGSGEDAEEELWNSPSKGNSERPSAVAGFINQKNLKPQEQLKNVKNDVSFNDSQSMVTNKENNIVDSSAAGNKAIPTFSFGKPFFSSNTSSLQSFQNPFTASQSNINTNAPLRTLNIQPEVAVKAAINFSNVTDLTNNSTDGAKITEIGSTSKRPIESGTSSDPDTKKVKESPANDQASNE
Protein: Cytochrome P450 monooxygenase aba2 (EC 1.-.-.-) (Abscisic acid biosynthesis cluster protein 2) (A0A384JQH2)
Organism: Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLLSIKDLSEKYIMLLDVKDLSTLKTTVAVLVTVALIAQVLWKIFFHPLSAFPGPWFNRISEIPGSWVIATGKQHSYYRKLHEKYGPVVRVAPNELSFIGDRAWDDIYGVQKKGPNFEKSPIFIGAVSPLDGQTGISLAPNEAHTRQRRALAHVFSNTALLQQEEIMRSHVDKLVGQLKKTIAENRPINFSNWYTYTTFDMMGDLCFAEPFGCLDQGGATEWSTSVINVFKSAAWDQSIRRVAGVNTWLQKLMVKLLIPSKAANWRKVHFQNSREKTLRRLADGNREHKDFIYHILKNKEAKNSLSETEIILNMVLLISAGTETTASLLTGWTYFICTHPEVYKRLTDEIRGRFNSEQDITWETVKDLPYLHATLSEALRLYSPAPANQQRIVPPGGSVIDGHFVPGKTTVAVAPWAAINSSLNFKDPQKFIPERWLGDERFVNDKLNASQPFSLGPRGCIGKNLSFFEMRLITSRLLWNFDVSLVTTGEHGETNKLWDMDGAGKYMKVYQTWNKPDMWVMLKEVPR
Protein: Anaphase-promoting complex subunit CDC27 (Anaphase-promoting complex subunit 3) (Cell division control protein 27) (P38042)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- APC/C activator protein CDC20
- Anaphase-promoting complex subunit CDC23
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit SWM1
- Cyclin-dependent kinase 1
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 11
- APC/C activator protein CDH1
Sequence:
MAVNPELAPFTLSRGIPSFDDQALSTIIQLQDCIQQAIQQLNYSTAEFLAELLYAECSILDKSSVYWSDAVYLYALSLFLNKSYHTAFQISKEFKEYHLGIAYIFGRCALQLSQGVNEAILTLLSIINVFSSNSSNTRINMVLNSNLVHIPDLATLNCLLGNLYMKLDHSKEGAFYHSEALAINPYLWESYEAICKMRATVDLKRVFFDIAGKKSNSHNNNAASSFPSTSLSHFEPRSQPSLYSKTNKNGNNNINNNVNTLFQSSNSPPSTSASSFSSIQHFSRSQQQQANTSIRTCQNKNTQTPKNPAINSKTSSALPNNISMNLVSPSSKQPTISSLAKVYNRNKLLTTPPSKLLNNDRNHQNNNNNNNNNNNNNNNNNNNNNNNNIINKTTFKTPRNLYSSTGRLTTSKKNPRSLIISNSILTSDYSITLPEIMYNFALILRSSSQYNSFKAIRLFESQIPSHIKDTMPWCLVQLGKLHFEIINYDMSLKYFNRLKDLQPARVKDMEIFSTLLWHLHDKVKSSNLANGLMDTMPNKPETWCCIGNLLSLQKDHDAAIKAFEKATQLDPNFAYAYTLQGHEHSSNDSSDSAKTCYRKALACDPQHYNAYYGLGTSAMKLGQYEEALLYFEKARSINPVNVVLICCCGGSLEKLGYKEKALQYYELACHLQPTSSLSKYKMGQLLYSMTRYNVALQTFEELVKLVPDDATAHYLLGQTYRIVGRKKDAIKELTVAMNLDPKGNQVIIDELQKCHMQE
Protein: Glucosamine 6-phosphate N-acetyltransferase (EC 2.3.1.4) (Glucose-6-phosphate acetyltransferase 1) (AtGNA1) (Phosphoglucosamine acetylase) (Phosphoglucosamine transacetylase) (Protein LIGNESCENS) (Q9LFU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22329777}; Peripheral membrane protein {ECO:0000269|PubMed:22329777}.
Interaction partners:
- Glutamine--fructose-6-phosphate aminotransferase 1
- Phosphoacetylglucosamine mutase
- Probable hexokinase-like 2 protein
- Hexokinase-1
- Hexokinase-like 1 protein
- Hexokinase-3
- Hexokinase-2
- Hexokinase-4
- UDP-N-acetylglucosamine diphosphorylase 1
- UDP-N-acetylglucosamine diphosphorylase 2
Sequence:
MAETFKIRKLEISDKRKGFIELLGQLTVTGSVTDEEFDRRFEEIRSYGDDHVICVIEEETSGKIAATGSVMIEKKFLRNCGKAGHIEDVVVDSRFRGKQLGKKVVEFLMDHCKSMGCYKVILDCSVENKVFYEKCGMSNKSIQMSKYFD
Protein: Colicin E3 immunity protein (Colicin E3 chain B) (ImmE3) (Im3) (Microcin-E3 immunity protein) (P02984)
Organism: Escherichia coli
Function: This protein inhibits the 16S RNA hydrolyzing activity of colicin E3 by binding with high affinity to the C-terminal catalytic domain of E3. This protein is able to protect a cell, which harbors the plasmid ColE3 against colicin E3.
Interaction partners:
Sequence:
MGLKLDLTWFDKSTEDFKGEEYSKDFGDDGSVMESLGVPFKDNVNNGCFDVIAEWVPLLQPYFNHQIDISDNEYFVSFDYRDGDW
Protein: GDNF family receptor alpha-4 (GDNF receptor alpha-4) (GDNFR-alpha-4) (GFR-alpha-4) (Persephin receptor) (Q9GZZ7)
Organism: Homo sapiens (Human)
Function: Receptor for persephin. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor. May be important in C-cell development and, in the postnatal development of the adrenal medulla.
Subcellular location: [Isoform GFRalpha4a]: Cell membrane {ECO:0000269|PubMed:11116144}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11116144}.; SUBCELLULAR LOCATION: [Isoform GFRalpha4b]: Cell membrane {ECO:0000269|PubMed:11116144}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11116144}.; SUBCELLULAR LOCATION: [Isoform GFRalpha4c]: Secreted {ECO:0000269|PubMed:11116144}.
Interaction partners:
- Persephin
- Artemin
- Neurturin
- Glial cell line-derived neurotrophic factor
- Proto-oncogene tyrosine-protein kinase receptor Ret
- GDNF family receptor alpha-3
- GDNF family receptor alpha-1
Sequence:
MVRCLGPALLLLLLLGSASSVGGNRCVDAAEACTADARCQRLRSEYVAQCLGRAAQGGCPRARCRRALRRFFARGPPALTHALLFCPCAGPACAERRRQTFVPSCAFSGPGPAPPSCLEPLNFCERSRVCRCARAAAGPWRGWGRGLSPAHRPPAAQASPPGLSGLVHPSAQRPRRLPAGPGRPLPARLRGPRGVPAGTAVTPNYVDNVSARVAPWCDCGASGNRREDCEAFRGLFTRNRCLDGAIQAFASGWPPVLLDQLNPQGDPEHSLLQVSSTGRALERRSLLSILPVLALPALL
Protein: Calcium-transporting ATPase 9, plasma membrane-type (EC 7.2.2.10) (Ca(2+)-ATPase isoform 9) (Q9LU41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell or into organelles.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Cation/H
- Cyclic nucleotide-gated ion channel 18
- Defensin-like protein 90
- Receptor-like protein kinase ANXUR1
- Receptor-like protein kinase ANXUR2
- Protein MODIFYING WALL LIGNIN-1
- Glutamate receptor 2.8
- 2-oxoglutarate
- GPI-anchored protein LORELEI
Sequence:
MSTSSSNGLLLTSMSGRHDDMEAGSAKTEEHSDHEELQHDPDDPFDIDNTKNASVESLRRWRQAALVLNASRRFRYTLDLNKEEHYDNRRRMIRAHAQVIRAALLFKLAGEQQIAFGSSTPAASTGNFDIDLEKLVSMTRNQNMSNLQQYGGVKGVAEKLKSNMEQGINEDEKEVIDRKNAFGSNTYPKKKGKNFFMFLWEAWQDLTLIILIIAAVTSLALGIKTEGLKEGWLDGGSIAFAVLLVIVVTAVSDYRQSLQFQNLNDEKRNIQLEVMRGGRTVKISIYDVVVGDVIPLRIGDQVPADGVLISGHSLAIDESSMTGESKIVHKDQKSPFLMSGCKVADGVGNMLVTGVGINTEWGLLMASISEDTGEETPLQVRLNGLATFIGIVGLSVALVVLVALLVRYFTGTTQDTNGATQFIKGTTSISDIVDDCVKIFTIAVTIVVVAVPEGLPLAVTLTLAYSMRKMMADKALVRRLSACETMGSATTICSDKTGTLTLNQMTVVETYAGGSKMDVADNPSGLHPKLVALISEGVAQNTTGNIFHPKDGGEVEISGSPTEKAILSWAYKLGMKFDTIRSESAIIHAFPFNSEKKRGGVAVLRGDSEVFIHWKGAAEIVLACCTQYMDSNGTLQSIESQKEFFRVAIDSMAKNSLRCVAIACRTQELNQVPKEQEDLDKWALPEDELILLAIVGIKDPCRPGVREAVRICTSAGVKVRMVTGDNLQTAKAIALECGILSSDTEAVEPTIIEGKVFRELSEKEREQVAKKITVMGRSSPNDKLLLVQALRKNGDVVAVTGDGTNDAPALHEADIGLSMGISGTEVAKESSDIIILDDNFASVVKVVRWGRSVYANIQKFIQFQLTVNVAALIINVVAAMSSGDVPLKAVQLLWVNLIMDTLGALALATEPPTDHLMHRTPVGRREPLITNIMWRNLLVQSFYQVAVLLVLNFAGLSILGLNHENHAHAVEVKNTMIFNAFVMCQIFNEFNARKPDEMNVFRGVNKNPLFVAIVGVTFILQIIIVTFLGKFAHTVRLGWQLWLASIIIGLVSWPLAIVGKLIPVPKTPMSVYFKKPFRKYKASRNA
Protein: FACT complex subunit SSRP1 (Facilitates chromatin transcription complex subunit SSRP1) (Recombination signal sequence recognition protein 1) (Structure-specific recognition protein 1) (T160) (Q08943)
Organism: Mus musculus (Mouse)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA. Also acts as a transcriptional coactivator for p63/TP63.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q05344}. Chromosome {ECO:0000250|UniProtKB:Q05344}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q05344}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q05344}.
Interaction partners:
- FACT complex subunit SPT16
- RNA polymerase-associated protein LEO1
- Transcription elongation factor SPT5
- RNA polymerase-associated protein CTR9 homolog
- Transcription elongation factor SPT6
- RNA polymerase-associated protein RTF1 homolog
- Parafibromin
- Transcription elongation factor SPT4-A
- RNA polymerase II-associated factor 1 homolog
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MAETLEFNDIFQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGINPGYDDYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDREEKKREQLKRAKMAKDRKSRRKSSEAKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARREYEKAMKEYEGGRGDSSKRDKSKKKKKVKAKMEKKSTPSRGSSSKSSSRQLSDSFKSKEFVSSDESSSGENKSKKKRRRSEDSEEELASTPPSSEDSASGSDE
Protein: ADP-ribosylation factor-like protein 14 (ADP-ribosylation factor 7) (Q8N4G2)
Organism: Homo sapiens (Human)
Function: GTPase that recruits MYO1E to MHC class II-containing vesicles via the effector protein ARL14EP and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells.
Subcellular location: Cytoplasmic vesicle {ECO:0000269|PubMed:21458045}. Note=Colocalizes with MHC II-containing cytoplasmic vesicles.
Interaction partners:
- PH and SEC7 domain-containing protein 4
- ARL14 effector protein
Sequence:
MGSLGSKNPQTKQAQVLLLGLDSAGKSTLLYKLKLAKDITTIPTIGFNVEMIELERNLSLTVWDVGGQEKMRTVWGCYCENTDGLVYVVDSTDKQRLEESQRQFEHILKNEHIKNVPVVLLANKQDMPGALTAEDITRMFKVKKLCSDRNWYVQPCCALTGEGLAQGFRKLTGFVKSHMKSRGDTLAFFKQN
Protein: Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (Molybdenum cofactor biosynthesis protein C) (P0A738)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Interaction partners:
- Molybdenum cofactor biosynthesis protein B
- Molybdopterin synthase sulfur carrier subunit
- Molybdopterin synthase catalytic subunit
- GTP 3',8-cyclase
- Molybdopterin molybdenumtransferase
- Molybdopterin adenylyltransferase
- Molybdopterin-synthase adenylyltransferase
- Molybdenum cofactor guanylyltransferase
- Molybdopterin-guanine dinucleotide biosynthesis adapter protein
- Molybdate-binding protein ModA
Sequence:
MSQLTHINAAGEAHMVDVSAKAETVREARAEAFVTMRSETLAMIIDGRHHKGDVFATARIAGIQAAKRTWDLIPLCHPLMLSKVEVNLQAEPEHNRVRIETLCRLTGKTGVEMEALTAASVAALTIYDMCKAVQKDMVIGPVRLLAKSGGKSGDFKVEADD
Protein: Serine/threonine-protein kinase MRK1 (EC 2.7.11.1) (P50873)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Phosphoglucomutase 2
Sequence:
MTDVLRSLVRKISFNNSDNLQLKHKTSIQSNTALEKKKRKPDTIKKVSDVQVHHTVPNFNNSSEYINDIENLIISKLIDGGKEGIAVDHIEHANISDSKTDGKVANKHENISSKLSKEKVEKMINFDYRYIKTKERTIHKRVYKHDRKTDVDRKNHGGTIDISYPTTEVVGHGSFGVVVTTVIIETNQKVAIKKVLQDRRYKNRELETMKMLCHPNTVGLQYYFYEKDEEDEVYLNLVLDYMPQSLYQRLRHFVNLKMQMPRVEIKFYAYQLFKALNYLHNVPRICHRDIKPQNLLVDPTTFSFKICDFGSAKCLKPDQPNVSYICSRYYRAPELMFGATNYSNQVDVWSSACVIAELLLGKPLFSGESGIDQLVEIIKIMGIPTKDEISGMNPNYEDHVFPNIKPITLAEIFKAEDPDTLDLLTKTLKYHPCERLVPLQCLLSSYFDETKRCDTDTYVKAQNLRIFDFDVETELGHVPLVERPAIEERLKHFVSAPSSSL
Protein: Senescence associated gene 20 (Protein WOUND-INDUCED 12) (AtWI-12) (Q94AK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable E3 ubiquitin-protein ligase RHG1A
- At1g71190
- Protein SENESCENCE-ASSOCIATED GENE 21, mitochondrial
- Senescence-associated protein 13
- Senescence-specific cysteine protease SAG12
- Senescence-associated carboxylesterase 101
- Serine/threonine-protein kinase PBL36
Sequence:
MRVLTGGVSPSSSSFEFVPLSVVSFGSTVIAEGCDAATSISWIHAWTVANGIITQVREYSNTSLTVTRIGNVVAGRRSAEIAPPSHCSSVWESQFSGRAGKPVPGLVLAI
Protein: Lectin-like protein (Apoplastic EDS1-dependent protein 9) (SA-induced legume lectin-like protein 1) (Q9LZF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a positive role in the effector-triggered immunity (ETI) response. Involved in salicylic acid (SA)-mediated processes occurring in ETI response, but is not involved in the autophagy process. Promotes systemic rather than local immunity. Essential for systemic acquired resistance (SAR), but not necessary for immune signaling downstream of SA. May act in parallel with SA.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:24006883, ECO:0000269|PubMed:24755512}. Cell membrane {ECO:0000269|PubMed:24006883}. Note=Tightly bound to the apoplastic side of the plasma membrane. {ECO:0000269|PubMed:24006883}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase family protein
- Amino acid transporter AVT1J
- Curculin-like
- Pentatricopeptide repeat
- Putative small RNA degrading nuclease 4
- Uncharacterized protein At1g21520
- Acetyl-CoA:benzylalcohol acetyltranferase-like protein
- At2g05540/T20G20.11
- Immune-associated nucleotide-binding protein 8
- Probable lysophospholipase BODYGUARD 3
Sequence:
MKIHKLCFLALLLAHTTSAVNLNLNLKTSELVFLGDAELGPASDGVSRSGALSMTRDENPFSHGQSLWSTPVPFKPSSNSSSPYPFETSFTFSISTRIKPAPGHGLAFVVVPSIESDGPGPAGYLGIFNKTNNGNPKNHIFAVEFDVFQDKGFGDINDNHVGININSVTSVVAEKAGYWVQTGIGKMKHWSFKEFKLSNGERYKAWIEYRNSKVTVTLAPETVKKPKKPLIVAHLDLSKVFLQNMYPGFSGAMGRGVERHDIWSWTFQNSAKRI