wanglab/gogpt-training-data huggingface dataset:
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) (Q54PC2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: An essential enzyme in glutathione (L-gamma-glutamyl-L-cysteinylglycine, GSH) biosynthesis, GSH is essential for growth and differentiation to prespore stage. Catalyzes the condensation of glutamate to cysteine.
Interaction partners:
- Glutathione synthetase
- 5-oxoprolinase
- Glutathione reductase
- Cytosol aminopeptidase
- Branched-chain-amino-acid aminotransferase
- Cysteine synthase
- Cystathionine gamma-lyase
- Kynurenine--oxoglutarate transaminase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
Sequence:
MGFIAEGNTLAWEDSVKYLEYIREHGVIQLLNIIKNNKDKVTEDFKWGDEVEYILINNDNYKLKLRANEILDLLMLEEKRNPTTVEHLWRPEYGRFMIEGTPGSPYIGLGKQLLSIQSNLKSRRENVEKYLKPNESILTITSYPRMGCKNFTDPQGEVKGPIAESKFLPDTVINPHFRFSTLTANIRKRRGGTVSINIPMYRDKNTPEYLDQICTYEKVPPILDDSDNSQTNISSPSNQPFNIYMDAMGFGMGCCCLQTTFQLPNIDDARTVYDQLAPISPLMLSLTAASSIFKGYLSDIDARWTIISQSVDDRNKEELGKAPLNNNKFVINKSRYDSIDSYIGSKSKSFRSEYNDLDLVYDKDVYQKLIENGVDSLLSKHFAHLFIRDPLVIYSDKIEIDDEKNTDHFENIQSTNWQTVRFKPPPPSSSIGWRVELRPMEVQLTDFQNSAFVVFSAILVKAIQDLKLNFYIPITKVDENLKTAHKRASVINDKFYFRKNIYNNTPNGSIENEYELMTINEIFNGKGGDNKGLIGVIRDYISTLDFDNETTELVNKYIKFISKRASGEIKSISTWTREFVQNHPAYNHDSIVNDEIQADYLQRCLDISNGTIYDSSIQGDKDDYYC
Protein: RNA binding protein La-like protein (Q9NIH4)
Organism: Trypanosoma brucei
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPLSSENKQKLQKQVEFYFSDVNVQRDIFLKGKMAENAEGFVSLETLLTFKRVNSVTTDVKEVVEAIRPSEKLVLSEDGLMVRRRDPLPESIQTDHQTVYVKPVPPTATLEQLTEFFSKHGTVQAVWRRYFAGKKDAPPESRTKPSVFVVFNSSEEAEAFQKAPPMYDDVQLTAEMKTTYLERKAEEIAAKKSSKTKNGGATDRAEKKTPPMPLGSSYRVSSCGEMESFATVKNLWPVEEQKGIRYVFMPDKESALLIFQDTQTGEKMVADLKSRGTTLNGKQPDIKKLEGDDEQKLLENVEKEIVDRAMQSANNRSGRGGRGGRGGRGHKRSRE
Protein: Glucose-6-phosphatase (EC 3.1.3.9) (F1QHF8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Phosphotransferase
- Hexokinase 2.
- Hexokinase 1.
- Hexokinase-2
- Glucose-6-phosphate 1-dehydrogenase
- Phosphoglucomutase 1
- ADP-dependent glucokinase
- Glucose-6-phosphatase
- Glucose-6-phosphate isomerase
- Aldose 1-epimerase
Sequence:
MDAVMDTMHGFGVSSTQYLQTHYKDAQGWFLFVSFAADLRNTFFIFFPIWFHLKESVGIKLIWVAVIGDWLNLVFKWILFGERPYWWVHETSYYMNSSAPHIEQYPMTCETGPGSPSGHAMGAAGVYYTLVTSILAIMLSKGKKSTSNSLYLRGSLWTLFWTVQICVCLSRVFIAAHFPHQVFAGVISGMIVAEAFNRQKWIYSASLKNYFNVTLFLLSFAVGLYVLLKALGVDLLWTLEKAQKWCANPAWVHLDTTPFASLLRNMGTLFGLGLGLHSPLYTESKKSSNAFVRITCIIASLLLLHLFDSIKPPTHTAALFYLLSFCKSATVPLVTVSIIPYCLSGALGLQSKKQL
Protein: Phospholipid-transporting ATPase NEO1 (EC 7.6.2.1) (P40527)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids (Potential). Leads to neomycin-resistance when overexpressed. Required for traffic between late Golgi and early endosomes.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:15314152, ECO:0000269|PubMed:31786280}; Multi-pass membrane protein {ECO:0000269|PubMed:15314152}. Golgi apparatus membrane {ECO:0000269|PubMed:12960419, ECO:0000269|PubMed:15314152, ECO:0000269|PubMed:31786280, ECO:0000269|PubMed:34645814}; Multi-pass membrane protein {ECO:0000269|PubMed:15314152}.
Interaction partners:
- Protein MON2
- Phospholipid-transporting ATPase accessory subunit CDC50
- Scramblase ANY1
- Protein DOP1
- Phospholipid-transporting ATPase accessory subunit LEM3
- Phospholipid-transporting ATPase DRS2
- ADP-ribosylation factor-like protein 1
- Protein ERD1
- Phospholipid-transporting ATPase DNF1
- ATP phosphoribosyltransferase
Sequence:
MPNPPSFKSHKQNLFNSNNNQHANSVDSFDLHLDDSFDAALDSLQINNNPEPLSKHNTVGDRESFEMRTVDDLDNFSNHSSDSHRKSSNTDTHPLMYDNRLSQDDNFKFTNIASSPPSSSNNIFSKALSYLKVSNTKNWSKFGSPIELSDQHIEREIHPDTTPVYDRNRYVSNELSNAKYNAVTFVPTLLYEQFKFFYNLYFLVVALSQAVPALRIGYLSSYIVPLAFVLTVTMAKEAIDDIQRRRRDRESNNELYHVITRNRSIPSKDLKVGDLIKVHKGDRIPADLVLLQSSEPSGESFIKTDQLDGETDWKLRVACPLTQNLSENDLINRISITASAPEKSIHKFLGKVTYKDSTSNPLSVDNTLWANTVLASSGFCIACVVYTGRDTRQAMNTTTAKVKTGLLELEINSISKILCACVFALSILLVAFAGFHNDDWYIDILRYLILFSTIIPVSLRVNLDLAKSVYAHQIEHDKTIPETIVRTSTIPEDLGRIEYLLSDKTGTLTQNDMQLKKIHLGTVSYTSETLDIVSDYVQSLVSSKNDSLNNSKVALSTTRKDMSFRVRDMILTLAICHNVTPTFEDDELTYQAASPDEIAIVKFTESVGLSLFKRDRHSISLLHEHSGKTLNYEILQVFPFNSDSKRMGIIVRDEQLDEYWFMQKGADTVMSKIVESNDWLEEETGNMAREGLRTLVIGRKKLNKKIYEQFQKEYNDASLSMLNRDQQMSQVITKYLEHDLELLGLTGVEDKLQKDVKSSIELLRNAGIKIWMLTGDKVETARCVSISAKLISRGQYVHTITKVTRPEGAFNQLEYLKINRNACLLIDGESLGMFLKHYEQEFFDVVVHLPTVIACRCTPQQKADVALVIRKMTGKRVCCIGDGGNDVSMIQCADVGVGIVGKEGKQASLAADFSITQFCHLTELLLWHGRNSYKRSAKLAQFVMHRGLIIAICQAVYSICSLFEPIALYQGWLMVGYATCYTMAPVFSLTLDHDIEESLTKIYPELYKELTEGKSLSYKTFFVWVLLSLFQGSVIQLFSQAFTSLLDTDFTRMVAISFTALVVNELIMVALEIYTWNKTMLVTEIATLLFYIVSVPFLGDYFDLGYMTTVNYYAGLLVILLISIFPVWTAKAIYRRLHPPSYAKVQEFATP
Protein: Hap31p (Q5A6N7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Hap5p
- Transcriptional activator HAP2
- Hap43p
- Hap42p
Sequence:
MNQQNARDIELREQDRWLPIANVARIMKNTLPPTAKVSKDAKECMQECVSEFISFITSEASDKCLKEKRKTINGEDILYSMYDLGFENYAEVLKIYLAKYREARK
Protein: Outer capsid protein P8 (Structural protein P8) [Cleaved into: Outer capsid protein P8'; Small peptide 1 (Sp1)] (Q85439)
Organism: Rice dwarf virus (isolate Fujian) (RDV)
Function: Capsid protein which self-assembles to form the outer icosahedral capsid with a T=13 symmetry, about 70 nm in diameter and consisting of 780 molecules capsid proteins.
Subcellular location: [Outer capsid protein P8]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:16432031, ECO:0000269|PubMed:17174956}. Note=Found in the peripheral regions of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.
Interaction partners:
Sequence:
MSRQMWLDTSALLEAISEYVVRCNGDTFSGLTTGDFNALSNMFTQLSVSSAGYVSDPRVPLQTMSNMFVSFITSTDRCGYMLGKTWFNSDTKPTVSDDFITAYIKPRLQVPMSDTVRQLNNLSLQPSAKPKLYERQNAIMKGLDIPYSEPIEPCKLFRSVAGQTGNIPLMGILLTPPVAQQQPFFVAERRRILFGIRSNAAIPAGAYQFVVPAWASVLSVTGAYVYFTNSFFGTTIAGVTATATAADAATTFTVPTDANNLPVQTDSRLSFSLGGGNINLELGVAKTGFCVAIEGEFTILANRSQAYYTLNSITQTPTSIDDFDVSDFLTTFLSQLRACGQYEIFSDAMDQLTNNLITNYMDPPAIPAGLAFTSPWFRFSERARTILALQNVDLNIRKLMVRHLWVITSLIAVFGRYYRPN
Protein: Hepatocyte growth factor (Hepatopoietin-A) (Scatter factor) (SF) [Cleaved into: Hepatocyte growth factor alpha chain; Hepatocyte growth factor beta chain] (P14210)
Organism: Homo sapiens (Human)
Function: Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types. Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization.
Interaction partners:
- Hepatocyte growth factor receptor
- High affinity nerve growth factor receptor
- Interleukin-7
- Epidermal growth factor receptor
- Fibronectin
- Vascular endothelial growth factor receptor 2
- CD44 antigen
- Fibroblast growth factor 2
- Insulin-like growth factor 1 receptor
- Neuropilin-1
Sequence:
MWVTKLLPALLLQHVLLHLLLLPIAIPYAEGQRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISRCEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEGSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS
Protein: FAD-dependent monooxygenase aptC (EC 1.14.14.-) (Asperthecin synthesis protein C) (Q5B0C8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment. Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules. Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone. Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC. Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster. Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin.
Interaction partners:
Sequence:
MTLPVLIIGAGLSGLTTARLLTNAHIPCIVFEASPPSRTQGYAISLRDWGFNALLRALGNLPLSSLTRAVAPDRHIGGWGWLDQSWRNNQTGEIIMMPPKESKEKPTILRANRNALRQWIADAGVGEDEEIDVRYGHRLVGVQLLREGGDGNVVTAEFANGATYTGSLLIAADGVHSTVRTLILPAVKPEILPVLVYHGDFKLSREEYECVIRPHAGESTIVAGVGDGFNTPLTVCDVTSTTVHMDWTYSRPSIGDNDPLYNPNITSEEAKVIPEALIEEINAKKLGEPWSLFLNGEAMRRHRVFNWLTRCVSMERSDVNSCTGKGVVFVGDSWHAMPIFGGEGGNHAIFDGIELAKMLEVAWGRSKEDVQAAIGKYYDKSWRRCNDAVRRSKQRFYQLHRPISEWIEIAEKQKMRA
Protein: Inka box actin regulator 2 (E9PND8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTMESREMDCYLRRLKQELAPCFLSPLQMSMKEVGDGLQDQMNCMMGALQELKLLQVQTALEQLEISGGGPVPGSPEGPRTQCEHPCWEGGRGPARPTVCSPSSQPSLGSSTKFPSHRSVCGRDLAPLPRTQPHQSCAQQGPERVEPDDWTSTLMSRGRNRQPLVLGDNVFADLVGNWLDL
Protein: Type 3 secretion system secretin (T3SS secretin) (Outer membrane protein MxiD) (Q04641)
Organism: Shigella flexneri
Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Forms a ring-shaped multimeric structure with an apparent central pore in the outer membrane. Necessary for the secretion of Ipa invasins.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000269|PubMed:11717255, ECO:0000305|PubMed:8437520}. Note=Localization to the outer membrane requires MxiM/SctG. {ECO:0000269|PubMed:11717255}.
Interaction partners:
Sequence:
MKKFNIKSLTLLIVLLPLIVNANNIDSHLLEQNDIAKYVAQSDTVGSFFERFSALLNYPIVVSKQAAKKRISGEFDLSNPEEMLEKLTLLVGLIWYKDGNALYIYDSGELISKVILLENISLNYLIQYLKDANLYDHRYPIRGNISDKTFYISGPPALVELVANTATLLDKQVSSIGTDKVNFGVIKLKNTFVSDRTYNMRGEDIVIPGVATVVERLLNNGKALSNRQAQNDPMPPFNITQKVSEDSNDFSFSSVTNSSILEDVSLIAYPETNSILVKGNDQQIQIIRDIITQLDVAKRHIELSLWIIDIDKSELNNLGVNWQGTASFGDSFGASFNMSSSASISTLDGNKFIASVMALNQKKKANVVSRPVILTQENIPAIFDNNRTFYVSLVGERNSSLEHVTYGTLINVIPRFSSRGQIEMSLTIEDGTGNSQSNYNYNNENTSVLPEVGRTKISTIARVPQGKSLLIGGYTHETNSNEIISIPFLSSIPVIGNVFKYKTSNISNIVRVFLIQPREIKESSYYNTAEYKSLISEREIQKTTQIIPSETTLLEDEKSLVSYLNY
Protein: Fibroblast growth factor (FGF) (Q4R0X9)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MDPCSSLFSYVFMHLFVLCLQAQVTVQSPPNFTQHVREQSLVTDQLSRRLVRTYQLYSRTSGKHVQILDNKKINAMAEDGDVHAKLIVETDTFGSRVRIKGAATGFYICMNKKGKLIGKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPKGHQTTEPHRRFEFLNYPFNRRSKRTRNSSARVRP
Protein: Riparin-1.2 (P86125)
Organism: Crinia riparia (Streambank froglet) (Flinders Ranges froglet)
Function: Induces mouse splenocyte proliferation through binding to CCK-BR.
Subcellular location: Secreted {ECO:0000269|PubMed:16470724}.
Interaction partners:
Sequence:
FLPPCAYKGTC
Protein: LD48048p (Q8SZY6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQQAYAQYMQQLTLRSTLPGSNQSGLPPPTQPLLPSVPLIAGRNFGEVQQVAGAAAAPAAQVPADPQINGAPQNRNFPNIQEEPEMHDWLDSFFSFTRLAIFVTVLYFNSSALRCLLVVLIAGAIYLYHIGVLRRRRERNNNNINRNNNAGDAAAFAAVQQIQRMMDAAVQRENNDPQAANEPGAVPAAGPAAAGEQDAIDAPPAGAPVAPASAANPEPTDVSAEAVEPPNANNSVISVVRTFVITFFTSLLPEAPAL
Protein: WD_REPEATS_REGION domain-containing protein (Q18403)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- CXXC-type zinc finger protein 1
- RNA polymerase II subunit A C-terminal domain phosphatase ssup-72
- pre-mRNA 3' end processing protein pfs-2
- Retinoblastoma-binding protein homolog 5
- Set1/Ash2 histone methyltransferase complex subunit ash-2
- Cleavage and polyadenylation specificity factor subunit 3
- Cleavage and polyadenylation specificity factor subunit 4
- Probable cleavage and polyadenylation specificity factor subunit 2
- Probable cleavage and polyadenylation specificity factor subunit 1
- Pre-mRNA polyadenylation factor Fip1 domain-containing protein
Sequence:
MTMKEVEITAESLAKLTPAKQPNDTTTRVNSLSYGLKGDHMIMSTDDDSMFLYDMNTGLRSRSVNSKKYGCSHVKFASDSMCALHGSTKVDNTIRYLSLTDNKYIRYFQGHDKLVTGINVSPMDDMFLSVAEDKTIRLWDLKTHNCIGLMNLSATPIATFDPEGLLFAAGLDNNIIKLYDLRSFDKGPFSSFGPLENEDNVEWTAMRFSPCGKYIMICTNSSQLLLVDAFTGLIKFTLEEHQNAQKIPLMASFTPESSHIMVGSSDGYIYFYDVETGEIALKTLAPNNQTCHIAEFSPQHFVAATADTKLTLWCASDELKAQAQQS
Protein: Pseudouridylate synthase TRUB1 (EC 5.4.99.-) (TruB pseudouridine synthase homolog 1) (tRNA pseudouridine 55 synthase TRUB1) (Psi55 synthase TRUB1) (EC 5.4.99.25) (Q8WWH5)
Organism: Homo sapiens (Human)
Function: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs and tRNAs. Mediates pseudouridylation of mRNAs with the consensus sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes the major pseudouridine synthase acting on mRNAs. Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs. Promotes the processing of pri-let-7 microRNAs (pri-miRNAs) independently of its RNA pseudouridylate synthase activity. Acts by binding to the stem-loop structure on pri-let-7, preventing LIN28-binding (LIN28A and/or LIN28B), thereby enhancing the interaction between pri-let-7 and the microprocessor DGCR8, which mediates miRNA maturation.
Subcellular location: Nucleus {ECO:0000269|PubMed:28073919, ECO:0000269|PubMed:33023933}. Cytoplasm, cytosol {ECO:0000269|PubMed:28073919}. Note=Catalyzes pseudouridylation of mRNAs in the nucleus. {ECO:0000269|PubMed:28073919}.
Interaction partners:
- Nucleolar protein 56
- Pseudouridylate synthase 1 homolog
- H/ACA ribonucleoprotein complex subunit 3
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit 1
- tRNA pseudouridine
- Pseudouridylate synthase 7 homolog
- H/ACA ribonucleoprotein complex subunit 2
- rRNA 2'-O-methyltransferase fibrillarin
- tRNA
Sequence:
MAASEAAVVSSPSLKTDTSPVLETAGTVAAMAATPSARAAAAVVAAAARTGSEARVSKAALATKLLSLSGVFAVHKPKGPTSAELLNRLKEKLLAEAGMPSPEWTKRKKQTLKIGHGGTLDSAARGVLVVGIGSGTKMLTSMLSGSKRYTAIGELGKATDTLDSTGRVTEEKPYDKITQEDIEGILQKFTGNIMQVPPLYSALKKDGQRLSTLMKRGEVVEAKPARPVTVYSISLQKFQPPFFTLDVECGGGFYIRSLVSDIGKELSSCANVLELTRTKQGPFTLEEHALPEDKWTIDDIAQSLEHCSSLFPAELALKKSKPESNEQVLSCEYITLNEPKREDDVIKTC
Protein: Matrin-type domain-containing protein (A0A178VXZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDREWGSKPGSGGAASGQNEAIDRRERLRRLALETIDLAKDPYFMRNHLGSYECKLCLTLHNNEGNYLAHTQGKRHQTNLAKRAAREAKDAPTKPQPLKRNVSVRRTVKIGRPGYRVTKQYDPELQQRSLLFQIEYPEIEDNIKPRHRFMSSYEQKVQPYDKSYQYLLFAAEPYEIIAFKVPSTEVDKSTPKFFSHWDPDSKMFTLQVYFKPTKPEPNKPQSAVGANGLPPPPPPPPHQAQPPPPPPSGLFPPPPPPMANNGFRPMPPAGGFGHPNM
Protein: FACT complex subunit SSRP1 (Facilitates chromatin transcription complex subunit SSRP1) (High mobility group B protein 8) (Nucleosome/chromatin assembly factor group D 08) (Nucleosome/chromatin assembly factor group D 8) (Protein NUCLEAR FUSION DEFECTIVE 8) (Recombination signal sequence recognition protein 1) (Q05153)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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. Binds specifically to double-stranded DNA (Probable). Required for karyogamy during female gametophyte development, when the two polar nuclei fuse to form the diploid central cell nucleus.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:15546350}. Chromosome {ECO:0000269|PubMed:15546350}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.
Interaction partners:
- Protein PAF1 homolog
- Protein CTR9 homolog
- Protein LEO1 homolog
- Protein RTF1 homolog
- FACT complex subunit SPT16
- Protein CDC73 homolog
- Transcription elongation factor SPT6 homolog
- FACT complex subunit
- Histone H4
- Transcription elongation factor SPT6-like
Sequence:
MADGHSFNNISLSGRGGKNPGLLKINSGGIQWKKQGGGKAVEVDRSDIVSVSWTKVTKSNQLGVKTKDGLYYKFVGFRDQDVPSLSSFFQSSYGKTPDEKQLSVSGRNWGEVDLHGNTLTFLVGSKQAFEVSLADVSQTQLQGKNDVTLEFHVDDTAGANEKDSLMEISFHIPNSNTQFVGDENRPPSQVFNDTIVAMADVSPGVEDAVVTFESIAILTPRGRYNVELHLSFLRLQGQANDFKIQYSSVVRLFLLPKSNQPHTFVVISLDPPIRKGQTMYPHIVMQFETDTVVESELSISDELMNTKFKDKLERSYKGLIHEVFTTVLRWLSGAKITKPGKFRSSQDGFAVKSSLKAEDGVLYPLEKGFFFLPKPPTLILHDEIDYVEFERHAAGGANMHYFDLLIRLKTDHEHLFRNIQRNEYHNLYTFISSKGLKIMNLGGAGTADGVAAVLGDNDDDDAVDPHLTRIRNQAADESDEEDEDFVMGEDDDGGSPTDDSGGDDSDASEGGVGEIKEKSIKKEPKKEASSSKGLPPKRKTVAADEGSSKRKKPKKKKDPNAPKRAMSGFMFFSQMERDNIKKEHPGIAFGEVGKVLGDKWRQMSADDKEPYEAKAQVDKQRYKDEISDYKNPQPMNVDSGNDSDSN
Protein: Diacylglycerol kinase zeta (DAG kinase zeta) (EC 2.7.1.107) (EC 2.7.1.93) (104 kDa diacylglycerol kinase) (DGK-IV) (Diglyceride kinase zeta) (DGK-zeta) (O08560)
Organism: Rattus norvegicus (Rat)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group (By similarity). The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization (By similarity). Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity). Regulates RASGRP1 activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:8855332}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13574}. Cell membrane {ECO:0000250|UniProtKB:Q13574}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q13574}.
Interaction partners:
- Lipoprotein lipase
- Sorting nexin-27
- Disks large homolog 4
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Phospholipase D1
- Phosphatidate cytidylyltransferase 2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
- Phospholipase D2
Sequence:
MEPRDPSPEARSSDSESASASSSGSERDADPEPDKAPRRLTKRRFPGLRLFGHRKAITKSGLQHLAPPPPTPGAPCGESERQIRSTVDWSESAAYGEHIWFETNVSGDFCYVGEQYCVAKMLPKSAPRRKCAACKIVVHTPCIGQLEKINFRCKPSFRESGSRNVREPTFVRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRRSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHNLRILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDRWDLRAEPNPEAGPEERDDGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCIVFLNIPRYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVLLTTAKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSTAPLHSDQQPVPEQLRIQVSRVSMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPMCHPLSSKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLPASPCSPTPGSLQGDAALPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDHQSRTLLHHAVSTGSKEVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Protein: Keratin, type 1 cytoskeletal 11 (Type I keratin 11) (Q5K2P6)
Organism: Protopterus aethiopicus (Marbled lungfish)
Interaction partners:
Sequence:
MSYSSFSIAQGSRVPSLSGTRSSSSYSLKSDLIPQSRRSHSVYGTPGSIRISSPSMPSAIVSSYSSTLSSALPSSSYGGNSYSSSTSFSSGGTDFLLGTSGKEAMQNLNDRLADYLARVRSLEDRNRELEQKIREWYEKQGAGTKRKDFSHYFKIIADLQNQINAGNMENARILLKIDNAKLAADDFKQKWEAEQALRLGVEADIHGLRKILDEMTLARTDLEMQIEGHKEEKAYLIKSHDEDMKALRSQLGGQVNVEVDAAPAEDLTKKLEIIRQRYEQLAEKNRKESEDWFIKKSEELNKNMASSTEALQTSKTEINELRRTIQGLEIELQSQQSMKGALEGQLADTEHRYSSTLMNLQNIINQKEAELSNIRADIESQASKYKILLDVKTRLENEISTYRTLLEGDAGRSHSSSHLSSTVSKDKVPVSSPNVITKVRTIVEEKINGQVISKKEYEGSPDQLSYY
Protein: Zinc transporter 2 (ZRT/IRT-like protein 2) (Q9LTH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates zinc uptake. May also transport copper and cadmium ions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP-dependent DNA helicase homolog MER3
- DNA mismatch repair protein MSH5
- DNA mismatch repair protein MSH4
- TPR repeat-containing protein ZIP4
- Copper transporter 2
- Crossover junction endonuclease MUS81
- Probable zinc transporter 8
- Zinc transporter ZTP29
- Copper transporter 5
- Metal-nicotianamine transporter YSL2
Sequence:
MALSSKTLKSTLFFLSIIFLCFSLILAHGGIDDGDEEEETNQPPPATGTTTVVNLRSKSLVLVKIYCIIILFFSTFLAGVSPYFYRWNESFLLLGTQFSGGIFLATALIHFLSDANETFRGLKHKEYPYAFMLAAAGYCLTMLADVAVAFVAAGSNNNHVGASVGESREDDDVAVKEEGRREIKSGVDVSQALIRTSGFGDTALLIFALCFHSIFEGIAIGLSDTKSDAWRNLWTISLHKVFAAVAMGIALLKLIPKRPFFLTVVYSFAFGISSPIGVGIGIGINATSQGAGGDWTYAISMGLACGVFVYVAVNHLISKGYKPREECYFDKPIYKFIAVFLGVALLSVVMIWD
Protein: Paxillin (Q6R3L1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDDLDALLADLESTTSHISKQGVFLPEETPYSCPRGSDSYQDVSSPPRVISPPAETLNGSWVEKPESKHSSTQSFNSAPKSSSPRVSQSEEEHVYSFPNKQKSIESPTAVMNSSLGSNLSELDRLLLELNAVQHSTPSFPAEETYPPKPASNTQRYVPENGVSSVVKAAPPKIEKPKRNIPAKVIEEVRPSVESLLNQLESSVPAAVPVSSVPMVSELRGVQEETPAQQQARISASSATRELDELMASLSDFKVQSNIMAQGKSSPTSVPKQGNKLDNMLGSLQSDLNRLGVQTVAKGVCGACKKPIAGQVVTAMGRTWHPEHFVCTQCQEEIGSRNFFERDGQPYCEKDYHSLFSPRCYYCSGPILDKVVTALDKTWHPEHFFCAQCGSFFGPEGFHEKEGKAYCRKDYFDMFAPKCGGCARAILENYISALNSLWHPECFVCRECFTPFVNGSFFEHEGQPYCEAHYHERRGSLCSGCQKPITGRCITAMGKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQSCFVKLFS
Protein: RE18826p1 (Tequila, isoform C (EC 3.4.21.-)) (Q9VST9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMAKWLLGLWLAILLVDRPGAKAYRSGSGYHSEQSEPVGLSATGNAHSSYGGDQQQPIYHRDSACPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVVCPSAESASTRLGRLRQLDSEPKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKDLAKCGSGTGAVRDDTSGTGYPALPFDDLGCPPGTRGLRPHPHDVHKYLRCGIGVKPQVEQCPRGHIFDGSSSVCVYSDSPRTSSSSFTSAEIQVNYLLCPVGAVGQFVHPFDQTKFLSCKDGKSAVQNCQPNYVFSISRRYCQLKAQLAFTDYVTLIISEISYEYSLILNACPGNINGIFLYPYDAKKYVQCSSGGRMSILSCGPQMAFSVSQRSCLPSHQVHISDRVQFWQEVQVQTTYTSQDLRGNVQSQLSSLRSCPPNVQKNYPYPFHAGHYVRCQYGALEIICCPTGQLYSLSQRQCVPRSLLSAHDYLDYSYISAELSTEFMVDRSTLSCPPQAQGLYLHPFDCTKYVRCWNQQTFIESCVVCAYAILRTIK