wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor tau subunit sfc3 (TFIIIC subunit sfc3) (Transcription factor C subunit 3) (Q9UST7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with sfc6 in DNA binding. Localizes to chromatin insulator sequence without recruiting RNA polymerase III and plays a role in nuclear organization.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transcription factor tau subunit sfc1
- Transcription factor tau subunit sfc6
- Transcription factor tau subunit sfc4
- Transcription factor IIIB 60 kDa subunit
- Putative transcription factor tau subunit sfc9
- Transcription factor tau subunit sfc7
- TATA-box-binding protein
- Transcription factor TFIIIB component B''
- Structural maintenance of chromosomes protein 4
- DNA-directed RNA polymerase III subunit rpc8
Sequence:
MDSLIRHCSEEIALDGSSGCSIDRLWEFAANFFFRQGIVQNLDDNYKTFVWPLILKEDGIEVWIEDEDATGLRSKMQEIPWNYQDITIELRARIRLFASEDRQWLTLTYKTKTDSKIQPLAFELLSCISRYRQEGVDRIQLCKETKQEPRSVYGRIQALEDASLISKVAINRSRAQTALLVLKRFESENSTINETVAQVSGKQIYNTEKIRSNICDAVQSSRNGICRHVDARAMVNLNHSRWERRYYARQVTYLHNNGYLRKCLTFVPNSPERCIRCLQFIKPYISSLDATEDDVDFTEVDDIPEDDELEEEEPLLPSKEEFDASFLQPLADVGPTLPQWSRFRPLEFQCFVLIRNAGFHGVITLQILSGLTGIRFNKPLFKLLGSLVEHRSSVPNHLSHMSITRFEDKTKKSRQYRYFTLQSQLNRLIRDGIPAETISKLLPHVHSLAGEFSPIDSSLFLNSLHHKGNMESNAEVSPDGMTLLPRKRGRPRKSANISVTSSPIRPSKNENNLPSLAISPVSEGFIQNATISTPSTSSNLSIAGSLTPSKTSRIYRGLAPLKNPEFNEDHVKKAEHLEPLLNVSSSVPSKNFTVSSPDHLKYGNTSSLQVSDSQSSIDLDSSFHYPVSVDSQLSHSTGSLMANFSSPTKKRRLESVDFIFLQRKGLILSYLVEQNGAFEISRKMFEDLADLKVRRNPETSRTVMDRRTFQQTLEKLMQEKKVRKLVIATNNGLGKLVRKDIVVQYDMKPDSPRFQQLRAQITTPEIEKQSTPEILKDVDVDFLKRNTSLSRRKSMPAEIKRHKESSETKPVDKEEVKKNEKEKDDPMRLAQQLLESLAPDFALHENTQQKSPVEKPKKLRKDRYASVEEFDYFSSTEHASKRSVKRFKNDFTSDEDETLIRAVVITQIYYGGTNRLIKWEAVQKCFPNRDIYALTRRYLSIRQHTKFKGLQQFLSENWQQMYKDAVSRKDLMPYPDSVDDFDPTPYVKASCRPYMISSSNLATTRLPRDLVDVYETYNIEVVKQETNFREMIFDPSLSVASKMNAYCDMPFTMPLSLNDKQNNEGDENCEKGQLFDAKSTIKSIVAIPDATYDARFSQERLMQYPEDILIAAHQELLDKRIITRVNSENSRLQPGRNFQFTEKFASSLKSPLPPFLLSQAKRFNKFLLEGFQNHKNHLFEETSNSGTLACILDLLSQGKLQISIVGSKFNEYGLSEGYRTRLLEHDNINVTLVLSGKESESKKNYGVTEKLATPPSHEPRLWLNGKCELIEMIWMNIEQSIVYQLLRKPGILRSQLTNLLFPGLEPREFNEVLDYFIAAGAAIEKDGLYLNHNYLFKLT
Protein: Partitioning defective 6 homolog alpha (PAR-6) (PAR-6 alpha) (PAR-6A) (Q9Z101)
Organism: Mus musculus (Mouse)
Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9NPB6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NPB6}. Note=Colocalizes with GTP-bound CDC42 or RAC1 at membrane ruffles and with PARD3 at epithelial tight junctions. Recruited to the centrosome by a microtubule and dynein-dynactin-dependent mechanism. {ECO:0000250|UniProtKB:Q9NPB6}.
Interaction partners:
- Protein kinase C zeta type
- Cell division control protein 42 homolog
- Partitioning defective 3 homolog
- Protein kinase C iota type
- Protein PALS1
- Segment polarity protein dishevelled homolog DVL-2
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 1
- Ras-related C3 botulinum toxin substrate 3
- Glycogen synthase kinase-3 beta
Sequence:
MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRTSVRGFQEFSRLLCVVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEGDSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPSSVGPGPTDPDSDDDSSDLVIENRHPPCSNGLSQGPLCWDLQPGCLLPGAGSSLPSLDSREQANSGWGNGMRGDVSGFSL
Protein: Inducible T-cell co-stimulator ligand (cDNA FLJ77643, highly similar to Homo sapiens B7-like protein (B7H2), mRNA) (cDNA, FLJ95137, Homo sapiens B7-like protein (B7H2), mRNA) (A0N0L8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MRLGSPGLLFLLFSSLRADTQEKEVRAMVGSDVELSCACPEGSRFDLNDVYVYWQTSESKTVVTYHIPQNSSLENVDSRYRNRALMSPAGMLRGDFSLRLFNVTPQDEQKFHCLVLSQSLGFQEVLSVEVTLHVAANFSVPVVSAPHSPSQDELTFTCTSINGYPRPNVYWINKTDNSLLDQALQNDTVFLNMRGLYDVVSVLRIARTPSVNIGCCIENVLLQQNLTVGSQTGNDIGERDKITENPVSTGEKNAATWSILAVLCLLVVVAVAIGWVCRDRCLQHSYAGAWAVSPETELTGHV
Protein: 2-oxoglutarate and iron-dependent oxygenase domain-containing protein ICU11 (EC 1.14.11.-) (Protein INCURVATA 11) (Q3ED68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Participates in the epigenetic repression of flowering genes in association with CP2. Functions in the repression of several members of the MADS-box transcription factors family, including SEP3, during vegetative development via histone modification.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:29915151}.
Interaction partners:
Sequence:
MCNQTPLRSMALDSSGKQPEQQQQQQPRASSGNGEARLKLRRTPNEEHEPENYEDLPLDYSPSLFTSLERYLPEQLLNSTRIDKASFMRDLLLRYSPDTERVRVLRHKEYRDKIMSSYQRLHGEIYTLDPSSFFAPSFLGAFSRKSEPNFRSSMVESYPGIFTFEMFKPQFCEMLLAEVEHMEKWVYDSRSTIMRPNTMNNFGVVLDDFGFDSMLQKLVDDFISPIAQVLFPEVCGTSLDSHHGYIVEYGKDRDVDLGFHVDDSEVSLNVCLGKQFSGGELYFRGVRCDKHVNSDSTEKEVYDYSHVPGHAILHRGRHRHGARATTSGHRANLILWCRSSTFREMKNYQRDFSGWCGGCKLDKQRRQRDSINATKEILARKAAEKTLVELASKSCAE
Protein: Sperm-specific class P protein 31 (Q9XXL3)
Organism: Caenorhabditis elegans
Interaction partners:
- Anther-specific protein BCP1-like
- Regulator of microtubule dynamics protein 1
- MSP domain-containing protein
- Nematode Specific Peptide family, group D
Sequence:
MINIDPPSGDYPASGGSSTHYIVSESESRLAFKVKSSNNESYRVRPVYGFVDAKGKAKLEVNRLAGPAKEDKLVIQYAEVPADETDPKAPFAAGAQQGEVVVKMVAS
Protein: Branched-chain-amino-acid aminotransferase 2, chloroplastic (Atbcat-2) (EC 2.6.1.42) (Q9M439)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts 2-oxo acids to branched-chain amino acids. Shows activity with L-Leu, L-Ile and L-Val as amino donors and 2-oxoglutarate as an amino acceptor, but no activity for D-isomers of Leu, Ile, Val, Asp, Glu or Ala.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Dihydroxy-acid dehydratase, chloroplastic
- Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial
- 2-isopropylmalate synthase 2, chloroplastic
- 2-isopropylmalate synthase 1, chloroplastic
- Threonine dehydratase biosynthetic, chloroplastic
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 2, mitochondrial
- 3-methyl-2-oxobutanoate hydroxymethyltransferase 1, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial
- Cystathionine gamma-synthase 1, chloroplastic
Sequence:
MIKTITSLRKTLVLPLHLHIRTLQTFAKYNAQAASALREERKKPLYQNGDDVYADLDWDNLGFGLNPADYMYVMKCSKDGEFTQGELSPYGNIQLSPSAGVLNYGQAIYEGTKAYRKENGKLLLFRPDHNAIRMKLGAERMLMPSPSVDQFVNAVKQTALANKRWVPPAGKGTLYIRPLLMGSGPILGLGPAPEYTFIVYASPVGNYFKEGMAALNLYVEEEYVRAAPGGAGGVKSITNYAPVLKALSRAKSRGFSDVLYLDSVKKKYLEEASSCNVFVVKGRTISTPATNGTILEGITRKSVMEIASDQGYQVVEKAVHVDEVMDADEVFCTGTAVVVAPVGTITYQEKRVEYKTGDESVCQKLRSVLVGIQTGLIEDNKGWVTDIN
Protein: Calnexin (P35565)
Organism: Rattus norvegicus (Rat)
Function: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P24643}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P24643}; Single-pass type I membrane protein {ECO:0000255}. Melanosome membrane {ECO:0000250|UniProtKB:P27824}; Single-pass type I membrane protein {ECO:0000255}. Note=The palmitoylated form preferentially localizes to the perinuclear rough ER (By similarity). Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria (By similarity). {ECO:0000250|UniProtKB:P24643, ECO:0000250|UniProtKB:P27824}.
Interaction partners:
- Protein disulfide-isomerase A3
- Calreticulin
- Calreticulin
- Calreticulin
- TAP binding protein
- Endoplasmic reticulum chaperone BiP
- Endoplasmin
- UDP-glucose:glycoprotein glucosyltransferase 1
- Translocon-associated protein subunit alpha
- Beta-2-microglobulin
Sequence:
MEGKWLLCLLLVLGTAAIQAHDGHDDDMIDIEDDLDDVIEEVEDSKSKSDTSTPPSPKVTYKAPVPTGEVYFADSFDRGSLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTSELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIADPDAVKPDDWDEDAPSKIPDEEATKPEGWLDDEPEYIPDPDAEKPEDWDEDMDGEWEAPQIANPKCESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIISGDRRVVDDWANDGWGLKKAADGAAEPGVVGQMLEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQSNAMEYKKTDAPQPDVKDEEGKEEEKNKGDEEEEEEKLEEKQKSDAEEDGGTGSQDEEDSKPKAEEDEILNRSPRNRKPRRE
Protein: Oleosin (A0A1I9R3Y6)
Organism: Pinus elliottii (Slash pine)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:27889638}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Interaction partners:
Sequence:
MADQYHGVMQKIHDHTPNPTQILGFITLFVSGAILLLLTGLTLTGTVIGLVVLTPVLIFFSPILIPVATVLFVAVAGFLSAGGFGLAALSAISWLYNYIKGRHPPGADQIDYARMRIADTASHVKDYAREYGGYLQSKIQDAAPGA
Protein: Defective proboscis extension response 11, isoform B (Defective proboscis extension response 11, isoform C) (GH22307p) (Q8MRE6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dpr-interacting protein gamma
- Dpr-interacting protein beta, isoform C
- Enhancer of split m8 protein
- Common Dpr-interacting protein
Sequence:
MRSWKNRSRSEMQTLETRVRPLQGAQLTQLLLGGILCLTIASHTQTSAEAAGGRVSGPGAGTSEGAGTSSASAASTAISSDESGDPSSATAFSSLAQVSSLLPEASALSATSGLVEPYLDGYATSNVTTQIGTHAYLPCRVKQLGNKSVSWIRLRDGHILTVDRAVFIADQRFLAIKQPDKYWTLQIKYVQARDAGSYECQVSTEPKVSARVQLQVVVPRTEILGEPDRYVKAGSNVVLRCIVRGALEPPTFIMWYHGAEQLAADSRRHRTQLDPNLPEASGEGQSTIGSLIIESAKKRDTGNYTCSPSNSPSATVTLNIINGESSASAVTSSAATTRAYALSILALLLSVILIGVGHRT
Protein: Serendipity locus protein delta (Serendipity-delta) (P07664)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional activator that controls bicoid gene expression during oogenesis. Found in transcriptionally active cells. Binds to specific sites on polytene chromosomes of third instar larvae. Binds to the consensus DNA sequence 5'-YTAGAGATGGRAA-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:2081456}.
Interaction partners:
- Boundary element associated factor
- Transcription factor Ouib
Sequence:
MDTCFFCGAVDLSDTGSSSSMRYETLSAKVPSSQKTVSLVLTHLANCIQTQLDLKPGARLCPRCFQELSDYDTIMVNLMTTQKRLTTQLKGALKSEFEVPESGEDILVEEVEIPQSDVETDADAEADALFVELVKDQEESDTEIKREFVDEEEEEDDDDDDEFICEDVDVGDSEALYGKSSDGEDRPTKKRVKQECTTCGKVYNSWYQLQKHISEEHSKQPNHICPICGVIRRDEEYLELHMNLHEGKTEKQCRYCPKSFSRPVNTLRHMRMHWDKKKYQCEKCGLRFSQDNLLYNHRLRHEAEENPIICSICNVSFKSRKTFNHHTLIHKENRPRHYCSVCPKSFTERYTLKMHMKTHEGDVVYGVREEAPADEQQVVEELHVDVDESEAAVTVIMSDNDENSGFCLICNTNFENKKELEHHLQFDHDVVLK
Protein: Defensin-like protein CAL1 (OsCPT1) (Pathogen-related protein 12) (OsPR12) (Protein CADMIUM ACCUMULATION IN LEAF 1) (Q6K209)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plant defensin-like protein involved in accumulation of cadmium (Cd) in rice leaves. Mediates Cd efflux from cytosol into extracellular spaces via chelation. This drives Cd secretion from xylem parenchyma cells into the xylem vessels, hence lowering Cd levels in cytosol meanwhile promoting Cd translocation from roots to shoots.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:29440679}.
Interaction partners:
Sequence:
MAPSRRMVASAFLLLAILVATEMGTTKVAEARHCLSQSHRFKGMCVSSNNCANVCRTESFPDGECKSHGLERKCFCKKVC
Protein: Teleost multiple tissue opsin b (A0A2R8Q4C0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
- SKI-like proto-oncogene a.
- COP9 signalosome complex subunit 9
- NAD kinase b.
Sequence:
MWQQCSCALGELQNHRNDGLENSPKLKWITKHSRYKTKLIKSFTQAIINGAMIESNVSRSCEWCAGGGEGTGAHLDENHSDHSLSPTGHLVVAVCLGFIGTFGFLNNTLVLVLFCRYKVLRSPMNCLLISISVSDLLVCVLGTPFSFAASTQGRWLIGRAGCVWYGFINSFLGVVSLISLAVLSYERYCTMMGSTQADSTNYRKVVIGIAFSWIYSMVWTLPPLFGWSCYGPEGPGTTCSVNWAARTPNNVSYIVCLFVFCLILPFIVIVYSYGRLLQAITQVSRINTVVSRKREQRVLFMVVTMVVCYLLCWLPYGIMALLATFGHPGLVTPAASIVPSLLAKSSTVINPIIYIFMNKQFCRCFHALIMCTTPERGSSFKNSSKVTKTLRTVRRANGQNVTFAVASAVHRTPYSDRQKSSSEGEKLPPATGQGTSKPVVSLVAYYNG
Protein: Uncharacterized protein C24B10.03 (Q9P7K2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDADDFGKKDLENGNESPKKPIFMKDWKNSQPNEQGRWLHLDARMNRNIEDLEISNYNLRLMNEQLESQLLSLNVKPVVSFAEQGKSSESKTDEEGFILNSASNVLDNFISIVNELVQHAEDVLDDLG
Protein: Probable septum site-determining protein MinC (Q55901)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization (By similarity).
Interaction partners:
- Septum site-determining protein MinD
- Cell division protein FtsZ
- Cell division protein SepF
- Putative cell division topological specificity factor
- Penicillin-binding protein
- Sll0445 protein
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MSDDTPHPEWQLVPQGNFVRLSLTLPTVTTAPDSPSLVFSHQQLEQSLGNYLRIMAGRWQDQTLVRLAVNNQLLDARQLQAIAAGLKEQNLTLQWVETNRRQTAVAAASAGLSVDQTMADKPLVDPSETPSLPKPLVVRHTLRSGGEIRHGGDVVIIGDVNPGSSIVADGDILIWGCLRGMAHAGAKGNDQAVIMILRLAACQIRIGDRLARVGADAVDRREPEIAYITSEGIRLTPVRQFQRSALL
Protein: Ribosome biogenesis protein NOP53 (Nucleolar protein 53) (Q12080)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Late-acting factor in the nuclear maturation of 60S ribosomal subunits, which is required for normal acquisition of export competence. Required for the export of the large subunit. Acts to stimulate the RNase activity of the exosome complex, and may recruit the exosome to 7S pre-rRNA for processing. Associates with numerous RNAs including the 27S and 7S pre-rRNAs and the box H/ACA snoRNA snR37. Also interacts (via N-terminal region) with the mature 25S rRNA and the mature 5.8S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15686447, ECO:0000269|PubMed:16043506, ECO:0000269|PubMed:16128814}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16043506}. Note=Does not shuttle from the nucleus to the cytoplasm (PubMed:16043506). {ECO:0000269|PubMed:16043506}.
Interaction partners:
- Probable metalloprotease ARX1
- Large ribosomal subunit protein uL24A
- Large ribosomal subunit protein uL29A
- Large ribosomal subunit protein uL30A
- Protein SDA1
- Large ribosomal subunit protein uL18
- 27S pre-rRNA
- Nucleolar GTP-binding protein 1
- Large ribosomal subunit protein eL19A
- Nucleolar GTP-binding protein 2
Sequence:
MAPTNLTKKPSQYKQSSRKGKKAWRKNIDLSDVEQYMEKKIDHEITHGTSDITSLQNDALFHVDVEGDEILKNKLIKRKQIKKVLKSKEILDAVKTNSKIAALNHHKNSSGNPNKIQGVSKHELKKLMALAGRVHGESKIKNRVAKDGLVKTTAGDLWGEESNSKKQKVKLPSGIKLDVEKKDQIPEELLKKSTTSWSTASVRPSTLDIEPIAVKEFTEIPHAGKSYNPNNKAWSELINKEYKEEKAREDERIALEKYKERIRHLMETLDDNEEEESSSNEEEEEEEEENENENESTQCSGSDKEIKLSINKPVKNKKKTKYQRNKAKRHEEKVKLQQELKELRQRVKDLEEVINSEETEILSAIESDSNKVKKSKKNKKHKLGTKYSVIDERLEIKFSDELSDSLRKLKPEGNLLYDTVRKLQSSGKVETRVPVRKGRKYKQKITEKWTHKDFK
Protein: Smad-related protein daf-14 (Abnormal dauer formation protein 14) (F5GUE5)
Organism: Caenorhabditis elegans
Function: Probably an atypical receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta-like daf-7 signaling. Plays a role in TGF-beta-like daf-7 signaling in regulating entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions; partially redundant with R-SMAD daf-8.
Interaction partners:
- Cell surface receptor daf-4
- Cell surface receptor daf-1
- Ski protein homolog
- Dauer larva development regulatory growth factor daf-7
- Protein dbl-1
- Serine/threonine-protein kinase receptor sma-6
- Smad protein daf-8
- TGF-beta family profile domain-containing protein
- Mothers against decapentaplegic homolog
- Dwarfin sma.
Sequence:
MSNEQEDFGSLFNNQGELGIMDDFAEFGFQTTTTPTNWAAAGNYMYPDQVHLPASINNPNMPINDWLEDAPMPDCYNVPSTSTDENNDPFPFSNISSQSSLKPKTPEKAVVEVRPTGNEMLDPEPKYPKEEKPWCTIFYYELTVRLGKAFEAKVPTITIDGATGASDECRMSLTSQPSSRNSKSSQIRNTVGAGIQLAYENGELWLTVLTDQIVFVQCPFLNQTLNKPLKYVFRLQNKGDQKRMKIFDKEQFEQEKTLALGPLTEKEVADERMRIFSNIRVSFCKGFGETYSRLKVVNLPCWIEIILHEPADEYDTVFRINNERPEIGSRS
Protein: Calmodulin-like protein 5 (Calmodulin-like skin protein) (Q9NZT1)
Organism: Homo sapiens (Human)
Function: Binds calcium. May be involved in terminal differentiation of keratinocytes.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Nitric oxide synthase 3
- Ryanodine receptor 2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Ryanodine receptor 1
- Nitric oxide synthase 1
- Calcium/calmodulin-dependent protein kinase kinase 2
- Calcium/calmodulin-dependent protein kinase type IV
- GTPase KRas
- Myosin light chain kinase, smooth muscle
Sequence:
MAGELTPEEEAQYKKAFSAVDTDGNGTINAQELGAALKATGKNLSEAQLRKLISEVDSDGDGEISFQEFLTAAKKARAGLEDLQVAFRAFDQDGDGHITVDELRRAMAGLGQPLPQEELDAMIREADVDQDGRVNYEEFARMLAQE
Protein: H/ACA ribonucleoprotein complex non-core subunit NAF1 (Q19788)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Putative H/ACA ribonucleoprotein complex subunit 4
- Putative H/ACA ribonucleoprotein complex subunit 2-like protein
- Putative H/ACA ribonucleoprotein complex subunit 3
- ADP-ribosylation factor-related protein 1
- C2H2-type domain-containing protein
- TruB_N domain-containing protein
- Probable H/ACA ribonucleoprotein complex subunit 1-like protein
- RRM domain-containing protein
- Small nuclear ribonucleoprotein associated homolog 13
- Protein SHQ1 homolog
Sequence:
MEEETIKVENLDDSITIDRNPVPLAFCARPTLPAKIGMKTEDGIVDQLLDLVDPITVVNPTEIRQAPSLKSFGCDTESEFEFSGDDSDFENINDLRAGALDSDEEFDRLVKFSAKIIEKTHKSEYPDENGKKQRKPKKSQKTRNVHEYDDMPPLENLSIECKGQLLEFGFVSKVVDCQVVIISTCTEVLDFDSFLFDQKGNALGQIYDIFGQVKNPQYVIRFNSCEEASMIPIDMKVYYAPTEEQFSKTPFKGLNLAAANRDAIKSLNRRIDHQEAVAKAGETMAQVGIGSDVEFSDDEAEKEFKRTTYTQPASQMSRGFDSNRGRKRDRRGGQKVRFSAQNPPARSDNLGPIPQQPSAPPPPARPAQSTESNPYAEFGCHSGFNGRFGI
Protein: ADP-ribosylhydrolase ARH1 (EC 3.2.2.19) (ADP-ribose-L-arginine cleaving enzyme) ([Protein ADP-ribosylarginine] hydrolase) (ADP-ribosylarginine hydrolase) (hARH1) (P54922)
Organism: Homo sapiens (Human)
Function: Specifically acts as an arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins.
Interaction partners:
Sequence:
MEKYVAAMVLSAAGDALGYYNGKWEFLQDGEKIHRQLAQLGGLDALDVGRWRVSDDTVMHLATAEALVEAGKAPKLTQLYYLLAKHYQDCMEDMDGRAPGGASVHNAMQLKPGKPNGWRIPFNSHEGGCGAAMRAMCIGLRFPHHSQLDTLIQVSIESGRMTHHHPTGYLGALASALFTAYAVNSRPPLQWGKGLMELLPEAKKYIVQSGYFVEENLQHWSYFQTKWENYLKLRGILDGESAPTFPESFGVKERDQFYTSLSYSGWGGSSGHDAPMIAYDAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFKGVSPSNYEKLEYRNRLEETARALYSLGSKEDTVISL
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (Q9VTH1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Fragile X messenger ribonucleoprotein 1 homolog
- 26S proteasome non-ATPase regulatory subunit 4
- Sodium/potassium-transporting ATPase subunit alpha
- Protein cycle
Sequence:
MNGGGGGEDDQHLPGVSSASGSAAGAVGGRATPEMKRSAVRSLIKRYFHQLQSGCGNANCSNANCASSGKVAPMTPNEVAARALQLFSQDAQLCEAFTSEANSPQDVDMLSPNDSSSSSSGSSTSTITSASTTTTTSRQSQSTPAAVVVPVSSPYLTQSVPQLDIAGAEHSSGDSEPCTPTLAPVHSLDANSLIALYEQCRAADSYDRICHAIGVVFSSVDRLGKSFIRSAEPAASSSLQELLANSPGALNKEQLRTLEGEHDKDEDSTQQVDEQSESAANATATAESVESEAEPEEEDDDVCSSQSSDTLVDLPGLRRVQRLLFGCQIRAITEKLTSSVIQLSDWVIYMRTDWERVIHCLVICFDLATNTNNSVVDMDYLDRVLPKLCQAASAMPVPAQARLARIWAAHCSDQLHSLIAACQQQITLQVLLDEESMRENESIISVTKVLKIVFYANILASELERPSCRVPLEDRTEAATASGSAAVEDDLFVYNSLLEPHMPKFAEDQFEKELQVSAIDCRKPLIPLEEFYNEALSENIQMHHDYLSYKTLAMESEIGSGHANYFSFMLYAFILTPSTKVDALYYDSRMRMYSERYSSLHSILNNIGQVGQEDNPRPDLKLTVRRDQLINDALIGLEMVAMSNPKDLKKQLVVEFVGEQGIDEGGVSKEFFQLIVEEIFNPAFGMFIQQEETNNMWFNATPFENGAQFTLIGIIIGLAIYNNVTLAVNFPMVVYRKLIGYCGTFADLSDWSPALYKSLKSMLDYQGQDMEEVFEQTFKISYSDVFGDVVQHELVPNGQDVLVGQHNKELFVNLYSDFLLNTNIEQQFNAFRKGFEMVTDESPLKLLFRPEEIEMLVCGSREFDFVELENSTVYEGGYTEKSQYIQDFWSIVHAMPSEDKHKLLEFTTGSARVPVGGLKCLRLLITRHGPDSDRLPTSHTCFNVLLLPEYSSREKLEERLMKAINYSKGFGML
Protein: ATP-dependent RNA helicase DBP6 (EC 3.6.4.13) (DEAD box protein 6) (P53734)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9528757}.
Interaction partners:
- Ribosome assembly protein 3
- Nucleolar pre-ribosomal-associated protein 2
- Nucleolar pre-ribosomal-associated protein 1
- Ribosome biogenesis protein ERB1
- Ribosome biogenesis protein MAK21
- 60S ribosome subunit biogenesis protein NOP8
- Nucleolar complex protein 2
- ATP-dependent RNA helicase HAS1
- 25S rRNA
- Ribosome biogenesis protein YTM1
Sequence:
MFASRFDPSQLTAPAASAPEGIVGTTPPAIVPLKRQATESDNEEYGSHQDSDESSNSSSEEDEDRMQVDYGASEEDSSEVEEEESKPSTHSTVLSRFKQTVSLQERLGASDIAESKEDEGIEDEAASTHQLKQIPQPEFVKNPMNLNTNSLQFKSTGWLNTEKIYYDNSLIKPFSDYANELEAKLLQNICKNFSTNTFPIQSIILDSILPVLNFTLNVSKRNFTRRIGDILVNAATGSGKTLAYSIPIVQTLFKRQINRLRCIIIVPTKLLINQVYTTLTKLTQGTSLIVSIAKLENSLKDEHKKLSNLEPDILITTPGRLVDHLNMKSINLKNLKFLIIDEADRLLNQSFQGWCPKLMSHLKTDKLDTLPGNVIKMIFSATLTTNTEKLNGLNLYKPKLFLKQTDKLYQLPNKLNEFNINIPTAKSVYKPLILLYSICQFMAHSPIAAKILIFVKSNESSIRLSKLLQLICESRSQSSVLKNLQNLAVSINSVNSNNSKAENKKIVANFSHHSESAGITILITTDIMSRGIDINDITQVINYDPPMSSQQYVHRVGRTARANELGSAYNLLVGRGERTFFDDLNKDLDRDGKSVQPLELDFTLLESDSELYTSSLESLKNYHNNTAQA