wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein mnm-2 (Q17895)
Organism: Caenorhabditis elegans
Function: Required in the M3 pharyngeal motor neuron to guide the growth cone of the sister M2 motor neuron during axon development.
Subcellular location: Nucleus {ECO:0000269|PubMed:17916347}.
Interaction partners:
Sequence:
MSVEASRTCFLIDSLLNKKPKEELETEEEDEEEDEEEELSSSEVTSENDMETESASSSASSVGQPKPDFSAFHKIFSNLDFAKLAAVKRNGHHQPMLFRPECFFPLELSKHLHLVQQTFQMNVLQNLGHTLPLPFVPMLKNVAPAQKRLNNKRASYVDHSQKGNLKKYRCDVCDKTFSRSNTLITHKRIHTGEKPFKCEHCGRAFRQPGNLTRHRLTHTTVKPYVCGLCDKAFNRASNLHTHMRTHTNV
Protein: At1g16790 (Ribosomal protein-like protein) (Q6NQG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKQPATPNAAEETKSEQKQKSKKFPTPTELISHYQKRGLEPAEASIKVIEDLQNALVRVVSSSRNASSKDKLVTDARKIDAINGRLAVVDAKLETKPGYVETFALGLASGATLNGISAVWPHVTRGIGQIWSAVRIGTDPSSTS
Protein: 3-ketoacyl-CoA synthase 18 (KCS-18) (EC 2.3.1.199) (Protein FATTY ACID ELONGATION 1) (Very long-chain fatty acid condensing enzyme 18) (VLCFA condensing enzyme 18) (Q38860)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to fatty acids elongation and stockage in developing seeds. Active on both saturated and mono-unsaturated acyl-CoAs of 16 and 18 carbons. Required for the elongation of C18 to C20 and of C20 to C22 fatty acids. Mediates also the synthesis of VLCFAs from 20 to 26 carbons in length (e.g. C20:1, C20, C22:1, C22, C24:1, C24, C26). Has no activity with polyunsaturated C18:2 and C18:3 or with acyl-CoAs having 22 carbons or longer chain length.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:12135493}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Delta
- Acyl-lipid omega-3 desaturase
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
- Diacylglycerol O-acyltransferase 1
- Biotin carboxylase, chloroplastic
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Diacylglycerol O-acyltransferase 3
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
Sequence:
MTSVNVKLLYRYVLTNFFNLCLFPLTAFLAGKASRLTINDLHNFLSYLQHNLITVTLLFAFTVFGLVLYIVTRPNPVYLVDYSCYLPPPHLKVSVSKVMDIFYQIRKADTSSRNVACDDPSSLDFLRKIQERSGLGDETYSPEGLIHVPPRKTFAASREETEKVIIGALENLFENTKVNPREIGILVVNSSMFNPTPSLSAMVVNTFKLRSNIKSFNLGGMGCSAGVIAIDLAKDLLHVHKNTYALVVSTENITQGIYAGENRSMMVSNCLFRVGGAAILLSNKSGDRRRSKYKLVHTVRTHTGADDKSFRCVQQEDDESGKIGVCLSKDITNVAGTTLTKNIATLGPLILPLSEKFLFFATFVAKKLLKDKIKHYYVPDFKLAVDHFCIHAGGRAVIDELEKNLGLSPIDVEASRSTLHRFGNTSSSSIWYELAYIEAKGRMKKGNKAWQIALGSGFKCNSAVWVALRNVKASANSPWQHCIDRYPVKIDSDLSKSKTHVQNGRS
Protein: Serpentine receptor class gamma-47 (Protein srg-47) (O17699)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- non-specific serine/threonine protein kinase
- Serpentine receptor class gamma
Sequence:
MSEILIVPLKEKMSERTLWLTIVQMFYGTITVVFMLILLFLFQFSKKFSYSFYRILQLDLITNILCNLNSLFSVRFQNHLMFLPVLEFLENSIPGFLSISSRGKFLFFHLQFFTALSMNIHRISSVTHPVGHGEFWTKYFKLYYVILCGISIFFTSVLPLESHRIEMENGTLIEISNHSMTTWTLNIYAIYSSVYFIILLLVGIISIFYISRKVEQVSTRSREVARKLSLITLVYGFLYSGILLWSILMALNRYFQFCPPSFGYIFNMSLGISSDLITLSLPYILLIFDVGIRKLFCRKRRKVGAMNVP
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (Q386S1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase, putative
- Phosphoglycerate mutase protein, putative
- Phosphotransferase
- Phosphotransferase
- Glucose-6-phosphate isomerase
- Pyruvate kinase
Sequence:
MSLSALRSKRTVNDIWPVRYKRFFVLTDPQNIIGETTDGLATLTTISYLLEREAAVVVASSFGDLKGIPLSFSRGQREEAIEIFRTEGGMGYTNYFNSLPINLKAEVLKVANGCETPVDSVTLSPVEVNGAFAALSIRQKAAALHNVFPRVEFSQCSTYAFVRELTNRFPTVPVKFSPDPLNAPISQLKPGEILVLENLKFYQNEISPNHEERVAMAEVLASYCDYCVNESFATVCAVHASNTELPKILYHGAAGFSMEKELAFFLSFLAHPPRPIVVVVAGRQSSKKLRMIRSLVGKVDKILVAGALIMPFLAAKGLTTDKSFNNSERVERRRLNEAAEVEELSVPCVGFAQEIITLCEKNGVELVFPVDHVVTRRITKATEDSAAIVESIAVPSDVYAVDCSANTIALFTKCIRPCQCVFWTGTFGCTRMGYSEGTYAFARALAQQGKLSIVSGNSTACVVRQLGLTSQFSHISSGGSTCLDALQGHHLPGVEMLSDIPVAVDVRSCILADDLLRSLPLFSNCSSHQLKAVAQKFVRRVHACGDYLTYYGDKHACMWVVASGGLVARSGDTTLTLPSRYIGRGQTVGMYGFITQSFATDTIQAAEDETVTYQLTFSSLQDLFNEQSDLAAQLLQNVSETLRVMAIEEYREQSSIMNVLRRAALCSRFPTFLAIPKDWGFMEDVIQDIISGTVLSGITQICTGQTALSSPRTFSLGLGSSTSRGHMVHCLCRVVLRDLLYHKLIEYGIMPATCISSIILSPFRLRAMGMMWSDVTCKAMLDEALLLAVEMCSPIAAHGTFLVVQRRIEVLLRRKCATIVKFFLTALVDVGFGFVLFPLTFHRRTSEAISLPDLFRSSVFKRHQWKVVLLLVLRCVVHVLLNGVRRVHRFWVIKRKSESGCNLTPQRLPRVTK
Protein: small monomeric GTPase (EC 3.6.5.2) (Q95SY7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MLKDDKLAQHVPTLHPTSEELSIGNMRFTTFDLGGHTQARRVWKDYFPAVDAIVFLIDAWDRGRFQESKNELDSLLTDEALSNCPVLILGNKIDKPGAASEDELRNVFGLYQLTTGKGKVARADLPGRPLELFMCSVLKRQGYGEGFRWLAQYID
Protein: Calponin-homology (CH) domain-containing protein (D0IMZ7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAQPKRLDQEEEVVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEKREDGDNKEETPKQKLLNWIRNRLPGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATKPIIMKPKVQATISNLDKILQVNDPREFDLKLSRDGFKPKVSIRDEDGQDIHLSLKKVEDKENAYKVKFTPTKIGFIHVDVAANDVHTFETQTIPEASVICQVVPIARLLDYNKTAKVGDDVKFAVVDAIEGPVEAIVVDPTGKEHRMVILDGTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRGKPKNSFKVWGRGIAPEGIRKNDVVGVHVESLDPEENIANANISLEVLKPSDGSHLPVSVGYNDESQSMDFEYSPKQAPDDLEVLVKVAGEVIESHKIHVAPESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPSKAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHIQDSPFVLRVTEPIEGLKPSATRVTGIDESKVYNVGEKIPFRVDTRLCGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAGVSVPGAPFSVKVKEPTDASKLKIFGPGVDGPVYSKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGEEISPIEINVKPNVDVSGIRVEGLENENLLIGSHLRPTINIGKLEPKSKGLQLIDEVNGKRYNVPMKINPDGTYSTDTPLMEVGEHKLQLLFDEIPVKEAVVEVIKGTDVNKCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPAKAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGKDEQKEHVKGSPFKAVVDYKKDPSQITISGLDQPNYRLNQPINFVIDTSKTKDLPVKATVPSDFAQLQPVVSRSPSNPRHHNVRFVPSGKPNVSIPIEIIYDGLKIDEKLVKVLPEVEPQLIKILHDKKKDSLTTTPITTNASHEGHVPFDVRDCGNVKKIESRVFGPDGKERLNHVRSTEQNGIYDVSFPTDMAGEYCVVFYINGQEVAARVPVMAEKIGRKEDVIKEEIVFHPEIAEHSPTVLTYNHPIDAKKKKAHPAIQVLAAKPDAVRLEHIQELVDNGHRVADRIVFTATKLGTNTLDVFYGGEHVDHVEYEAIGKLEYERIQAERAKVVVEKEDDVDKYEKQYKFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVDAYGDGWATVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPAKSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDSPFRVLVMGEGQKRSHLSVGSTSEVALPITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRDGKLVPKAPFKIKVDKTQVGDASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPSKAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHHVKDSPLTVQCTGKSAGRVIQTIQKDVEQHGICLPDQESHLFLKLLNTSPMDITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPFQFTVGSFSEGGAHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPSKATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQHIPDSPFKVYIAPATGEVRKLELAQFHGQGIPAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGESYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRVGGKDLCDPTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKGYKVRYTPLAPGSYFASVKYNGIHAPGSPFKIPVEGKELGGNGYNETSHVKIDAVAKTSKGTVAVVPEYQGDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKEIPGSPFAIEP
Protein: Fibroblast growth factor receptor (EC 2.7.10.1) (F8W9L4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNLVLWGPALGDLHAGGLPVPRHPCGGALQAAEGGPPHGQARQLHTRPVHDHAGVLACRALPEAHLQAAGGGPGPCPYRDVHRRVPGPVGAFRAVLPGWPGHPQLQLLRGRLRVCPRPAAPGPTQQWGLADVKGHWSPTM
Protein: Protein SPT3 (Positive regulator of Ty transcription) (P06844)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SPT3 is required for recruitment of TATA-binding protein (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are required for the initiation of Ty transcription from the delta promoter. SPT3 regulates Ty1 as well as the mating factor genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit ADA2
- SAGA complex subunit SPT7
- SAGA complex subunit NGG1
- SAGA complex subunit SPT20
- Histone acetyltransferase GCN5
- Ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF10
- SAGA complex/transcription factor TFIID complex subunit TAF9
Sequence:
MMDKHKYRVEIQQMMFVSGEINDPPVETTSLIEDIVRGQVIEILLQSNKTAHLRGSRSILPEDVIFLIRHDKAKVNRLRTYLSWKDLRKNAKDQDASAGVASGTGNPGAGGEDDLKKAGGGEKDEKDGGNMMKVKKSQIKLPWELQFMFNEHPLENNDDNDDMDEDEREANIVTLKRLKMADDRTRNMTKEEYVHWSDCRQASFTFRKNKRFKDWSGISQLTEGKPHDDVIDILGFLTFEIVCSLTETALKIKQREQVLQTQKDKSQQSSQDNTNFEFASSTLHRKKRLFDGPENVINPLKPRHIEEAWRVLQTIDMRHRALTNFKGGRLSSKPIIM
Protein: Cell division protein SepF (P73376)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Cell division protein that is part of the divisome complex and is recruited early to the Z-ring. Probably stimulates Z-ring formation, perhaps through the cross-linking of FtsZ protofilaments. Its function overlaps with FtsA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01197}. Note=Localizes to the division site, in a FtsZ-dependent manner. {ECO:0000255|HAMAP-Rule:MF_01197}.
Interaction partners:
- Cell division protein FtsZ
- Probable septum site-determining protein MinC
- Penicillin-binding protein
- Pyridoxal phosphate homeostasis protein
- Sll0445 protein
- Sll1252 protein
- Ssl0353 protein
- Ycf19 protein
- Sll0446 protein
- Slr0580 protein
Sequence:
MILTKLKDFVGISEHDEYEEDYDEEMEFPQSVASQPPAEEVAPPPRISREPLSLNNETSIGTGVRNNVIGMPGINNSVAEVVVVEPHSFDEMPQVIQTLRERKSVVLNLNVMDPEEAQRAVDFVAGGTFAMDGHQERIGESIFLFTPNCVKVSSLAGRSQESNETSSSVSSDNFPTWGYETSRLAQ
Protein: Protein Daple (Coiled-coil domain-containing protein 88C) (A0A2R8QCI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Positive regulator of Wnt signaling, acting synergistically with dvl2 (By similarity). Functions upstream of ctnnb1/beta-catenin in the canonical Wnt pathway, and also activates jnk in the Wnt/planar cell polarity (PCP) pathway (By similarity). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits. This promotes apical cell constriction and subsequent bending of the neural plate during neurulation via arhgef18 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell junction {ECO:0000250|UniProtKB:Q9P219}. Note=Enriched at apical cell junctions. {ECO:0000250|UniProtKB:Q9P219}.
Interaction partners:
Sequence:
MDITVSELMSNFMDSPLVVWVKTFGPLGFSSEDKLSMFMDLVDGVFLHKIMTHIDPSPMNQRVNKQVNNDVNLRIQNLNTVIRHIKNYYQEHLQQLIVMNLPNVLAIAKDPLSGKSMEEMKRMLLLILGCAVQCDRKEEIIEKIKLLDIETQAAIVTHIQEVTHNQENVLDLQWMEVAEIPAEQLDPLSRTMAFHLRKLIDERDESAELVIELTQERDYLQSQQPSGLLGFPSPERTSLSPITLLSKEDRQHLAVELADTKAKLRRSRQELEEKTEQLIDAKNEIERLDSDIQKLKQENTQLLAEARSVRAYRDEVDSLRERAGKVDRLETELSRFKEKLNDVHFYKTRIEELREDNLTLLETKSMLEEQLTGARGRCDKLHELEKENLQLRSKLHDIEIDRDSDKKRLEELLEENMLLEISQKQSMNESAHLGWELEQLAKNNEVNEARKSFVFELNESASSRLLKLEKENQCLQSTIQELREASINMEEGQLHSLELEKENQSLSKKLERLQSQLDQEKQTTQDMENLGEELIKEKQRMEKTLETIQAEKDRQISELEQEKEHLTQAVSSLRKRAQANSEARVREVETENRILHQTISETGGKLARLEAEKRQVTKELESLRERGERCEELEREVPRLERVREQLQREAAALKIGSERAEALERENATLEQDNRRLKKLADTAQNATLRLAVLEKDHQQLEEENLEQRRALETLRPAAARLAQLQQEHAELEREHEEMCRTMEELRSQAKRSERLEKSCGSLSLENQRLQQTLENSSTKMQGLESELRQNEAEMKDLQRELEGLRQKVTWAETLEKENRGMEQELSQLEKEKKQLEKEARRFRQQLEVKEAALEENCLRLASMEKEGTALSKELGRVKEAAGRLKELERENKDLQKQATMDKKTLATLREELVNEKLRVQQQCNELEKLSHELEKIGLNREKLLQEEHSCEDNKYKILETKIESALKKTLELREEKIQSLESRLEESSSLNQQLRTELTTVKKNLEALKQRHEEEAAHSEISQQTLGQTRSLPDKEKWEMEQREATAELLKLKDRLIDVEKNVRQRHVSIDIHRVIFSIVICFCDSLQNAALQTEKYLLKDQLKQIDSQNAQLNAQTLALQKQAASLQEHNTSLHKETAKLQVENSTLSSQSSSLMAQYGALQAQLQTLESEAESLQKQREEASAARDRVTQDHERLLGVHERQASEYEQLIAQHAALKASQRALEQENRTLENKYMVLLKQKDAMEALEESLQRDRESLGEEIRKNTLILGENRSLREEVDRVSHMHTQLRQEYDSLQLQTKELKTSLNESQLELNRWQARYDQLKEQHQGLDISMTKLDNHCELLTRLKGNLEEENHHLLSQIQMLSQQNQTLLERTMESKELYHEEQKQYIDKLNSLRRQKEKLEEKIMDQYKFYDPTPKKSRQWVGAKAIAKFIKPKKESSRERPDAPRERIRSAPDIPLPEIPTCIDCPESAPPPPPPPLPPRQSRPSLDSMNSQSVEENHVQSPTLSSPALNGRVLNESGGSRSRDGYRSIGGGSESMNGYEELLRWRSREPGGATCSTPLSRNSHNAPGFTSSSSLRPGRRPKGLVSEEDLRHHSPDAGFGSGVHGNTGHRPSSAEFSRNTSSSNSPVSSKGSLDCLQGRSASLSSDDVVGLAHEGSRLSQSSLLPRSSTLPCDSPSASRPSQRPASRRPSSPGSEMVTLEEFLQESNALSPPTVQTGSREDLMTDYFTRSTRPVPLRDGAKTPTNYVTPTVKTTPPELDARTPKPGHSVKPSVRLTDTSTPPSHSQTLPNRGAGLRPSALQQSSPRGSVGGSASLSRTFSLASADLLRSNGPDSYRTEAASPNQNDVVMRRPGAVARERPMSARVTGSSPLPGDPGHISVDPRRLSLAQPRDEFSLVSPPPLHSSSMSLQAEREYVGSGSSRAGAARSGSAQPRGAPHRGEVAMVTPVRAVPALRLNDLEEEPQEQREAESPLLKKADTTNLSYASKEQPTSKPASPDPNNDPQTVWYEYGCV
Protein: KH domain-containing, RNA-binding, signal transduction-associated protein 2 (Sam68-like mammalian protein 1) (SLM-1) (mSLM-1) (Q9WU01)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion (By similarity). Binds both poly(A) and poly(U) homopolymers. Phosphorylation by PTK6 inhibits its RNA-binding ability. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. Regulates cell-type specific alternative splicing of NRXN1 at AS4 and acts synergystically with SAM68 in exon skipping. In contrast acts antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its phosphorylation by FYN inhibits its ability to regulate splice site selection (By similarity). May function as an adapter protein for Src kinases during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10077576, ECO:0000269|PubMed:15471878}.
Interaction partners:
- Protein-tyrosine kinase 6
Sequence:
MGEEKYLPELMAEKDSLDPSFVHASRLLAEEIEKFQGSDGKKEDEEKKYLDVISNKNIKLSERVLIPVKQYPKFNFVGKLLGPRGNSLKRLQEETGAKMSILGKGSMRDKTKEEELRKSGEAKYAHLSDELHVLIEVFAPPGEAYSRMSHALEEIKKFLVPDYNDEIRQEQLRELSYLNGSEESGRGRGIRGRGIRITPTAPSRGRGGAVPPPPPPGRGVLTPRGTTVTRGALPVPPIARGVPTPRARGTAAVPGYRAPPPPAHDAYEEYGYDDGYGGEYDDQTYEAYDNSYVTPTQSVPEYYDYGHGVNEDAYDSYAPEEWATTRSSLKAPPPRSARGGYREHPYGRY
Protein: Cullin, putative (Q57YJ8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TATA-binding protein interacting
- Ubiquitin, putative
- Ubiquitin-conjugating enzyme E2, putative
- Polyubiquitin, putative
- Ubiquitin-conjugating enzyme E2, putative
- S-phase kinase-associated protein, putative
- SKP1 component dimerisation domain-containing protein
- RING-type domain-containing protein
- RING-type domain-containing protein
- PCI domain-containing protein
Sequence:
MLEEDLEAIRRMKADFEAIGELTDNEFRSDTTISKRMNHYSTVYNAATRITGYDDPRDPMGSGAEELLYVDFQEMLTRYLLKHSNLSAPSEMELFARILKVWERYKVMMKWNVNAFAYLSRFYIVNFSKPPLRQVALRIFHEQVLKKYVPTVVRVTHELLTAERKGEGVNREDVREAIELLSSVTVEQRQEIYNEQFLKQYLELTKDYYVALVAEWGESSSHTELLRQIEGAYNDEDVRCSYYFPPEDKRAVMVQVEEVLLDSSVVLDKLLKSKDGFIAKLKSREKNLLKLYYNLLSRRQKALACLADLTRDGITAEGSEKLRQYDNKERDIDFKSCVVDIMKLQDEFLTLSSECFDGDTAMLKAVKEGIERVYADGVRLTETVKRFVPMSELLAHYADSIIQGSGCSSSQEEELDRVIAALSYVTDRDTFLAHSRDLLAQRILSPKKKFDDNIERSFAHRISHCCGVSSTCYLEGMLHDVDVAEGFRAADKLEAMGVKLPFAFDALVLKKGIWPPRIHSENFTPPPIISEALHSFEAAYLQGTRGRVLTWSYSNSSGDVHAAFKKGPKTLVMPGLQCWVLLAFNGANQLTVDDVVGRFGMTFDDAKPVLLSLVKASILIRESNFPTVSLHDIFIVNDNFTSKLKKMKIAMGRDQNIVAAQSEEVAREVEEDRKPAIDACLVRIMKSRRVLEHSMLVEECKERLLPTFSADPKLVKQRIEELIRKEFIERDANTPGLYRYAA
Protein: Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (EC 3.4.22.-) (MALT lymphoma-associated translocation) (Paracaspase) (Q9UDY8)
Organism: Homo sapiens (Human)
Function: Protease that enhances BCL10-induced activation: acts via formation of CBM complexes that channel adaptive and innate immune signaling downstream of CARD domain-containing proteins (CARD9, CARD11 and CARD14) to activate NF-kappa-B and MAP kinase p38 pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Mediates BCL10 cleavage: MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion. Involved in the induction of T helper 17 cells (Th17) differentiation. Cleaves RC3H1 and ZC3H12A in response to T-cell receptor (TCR) stimulation which releases their cooperatively repressed targets to promote Th17 cell differentiation (By similarity). Also mediates cleavage of N4BP1 in T-cells following TCR-mediated activation, leading to N4BP1 inactivation. May also have ubiquitin ligase activity: binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16123224}. Nucleus {ECO:0000269|PubMed:16123224}. Note=Shuttles between the nucleus and cytoplasm. Found in perinuclear structures together with BCL10. {ECO:0000269|PubMed:16123224}.
Interaction partners:
- Caspase recruitment domain-containing protein 9
- B-cell lymphoma/leukemia 10
- TNF receptor-associated factor 6
- Caspase recruitment domain-containing protein 11
- Caspase recruitment domain-containing protein 10
- Caspase-8
- NF-kappa-B essential modulator
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Caspase recruitment domain-containing protein 14
Sequence:
MSLLGDPLQALPPSAAPTGPLLAPPAGATLNRLREPLLRRLSELLDQAPEGRGWRRLAELAGSRGRLRLSCLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPESFQRSVDGVSESKLQICVEPTSQKLMPGSTLVLQCVAVGSPIPHYQWFKNELPLTHETKKLYMVPYVDLEHQGTYWCHVYNDRDSQDSKKVEIIIGRTDEAVECTEDELNNLGHPDNKEQTTDQPLAKDKVALLIGNMNYREHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMRNAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGKQALEIRSSLSEKRALTDPIQGTEYSAESLVRNLQWAKAHELPESMCLKFDCGVQIQLGFAAEFSNVMIIYTSIVYKPPEIIMCDAYVTDFPLDLDIDPKDANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLVFTVCLSYQYSGLEDTVEDKQEVNVGKPLIAKLDMHRGLGRKTCFQTCLMSNGPYQSSAATSGGAGHYHSLQDPFHGVYHSHPGNPSNVTPADSCHCSRTPDAFISSFAHHASCHFSRSNVPVETTDEIPFSFSDRLRISEK
Protein: DNA-directed RNA polymerase II subunit GRINL1A (DNA-directed RNA polymerase II subunit M) (Glutamate receptor-like protein 1A) (P0CAP2)
Organism: Homo sapiens (Human)
Function: Isoform 1 appears to be a stable component of the Pol II(G) complex form of RNA polymerase II (Pol II). Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. Isoform 1 may play a role in the Mediator complex-dependent regulation of transcription activation. Isoform 1 acts in vitro as a negative regulator of transcriptional activation; this repression is relieved by the Mediator complex, which restores Pol II(G) activator-dependent transcription to a level equivalent to that of Pol II.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000305}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase II subunit RPB11-a
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MCSLPRGFEPQAPEDLAQRSLVELREMLKRQERLLRNEKFICKLPDKGKKIFDSFAKLKAAIAECEEVRRKSELFNPVSLDCKLRQKAIAEVDVGTDKAQNSDPILDTSSLVPGCSSVDNIKSSQTSQNQGLGRPTLEGDEETSEVEYTVNKGPASSNRDRVPPSSEASEHHPRHRVSSQAEDTSSSFDNLFIDRLQRITIADQGEQQSEENASTKNLTGLSSGTEKKPHYMEVLEMRAKNPVPQLRKFKTNVLPFRQNDSSSHCQKSGSPISSEERRRRDKQHLDDITAARLLPLHHMPTQLLSIEESLALQKQQKQNYEEMQAKLAAQKLAERLNIKMRSYNPEGESSGRYREVRDEDDDWSSDEF
Protein: Uncharacterized protein C21C3.14c (Q9P7L0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKIERYFKAIARAFIITFLFSLILQDNGVLARKAKKQDKGAALKSIYDYHVRPYGTVVQSQIAKASPIVDAAKQATVNVKSYYDEHAKPKVENIRYEVNEVIDKKVAPCIKAFNEKARKIGSKVLDGDNLRELYTTGKERIHFFIVDVLIPFFQRVVQEVRTISRDIAEKLQYFWEIHAIPAYHHYKPIIQRGAMDGYMQLRYVFFPAAKATITQMIETSIRFLRTFLDMHIKPQLQHIYESVVEEKSEAFASATSSKILSEMSASMASSSAHYTSSPTILSRTKSVETPVPMEAAEEEPATEYSIPSSVTFNSQNDCFSNAMNYLEHEYETLVSTFTLSVSEHWEDLLRKATDSCQKELEAFEEISNLRVLAVENSLGNLIQKAEESNYDQAIMDLFEYVKDSILRVHERAIKLRTLSDSIRADVAENIEMGINSIREQAAASSEVALAACSGIKHNAEQVNKLNALIQKVYSYITAESEKVGNRYGETLDNVIKQHLSRIGSVASSAVQRLTAVKNSHKLKMVDRSSAELPNFDYLVSDQVHKIVEINDEHADCDDVNFSTASFEIYERSIPTHGADSERKILKRDSLLNEDDEIFNDLNSDKTIKTNQATSTSSSNTQEISYTGTLNDNINEGLSTFPSIDIPASEADNVYSILPIDVSTSEAEGAYSILPIDVPKSVAEETYSFLPSDVPKSEAEKVYSILPIDVPQSVAEETYSFKPSDIPESEAEKIYSILPIDVKDPSLEKDGHVIDSSNLQTDSVKDYSEVSRADNLDASSDTIFSVLHAENEASITKEVHSTPLSDVASSEAEKVYTILPIEVPTDPLPNYSSDVESELTSD
Protein: Folate transporter 1 (PfFT1) (Q8IBB7)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cell membrane {ECO:0000269|PubMed:21998306}; Multi-pass membrane protein {ECO:0000255}. Note=In intraerythrocytic stage parasites, localizes to the plasma membrane and some intracellular vesicular structures. {ECO:0000269|PubMed:21998306}.
Interaction partners:
- GTP cyclohydrolase 1
- Vacuolar protein sorting-associated protein VTA1, putative
- Protein YOP1, putative
Sequence:
MEDDDFSIKDKKENYETCSTETISSYISINEKCQLIEKDINDDNHENPYMIFNKISSSLIAMLQGVEVLCNLSIIYLLKDNYHLHPASLSIVMCFIKIPWSIKLVWAVISDNYPIFGYRRKYYLLLGSFLCILSLICLGLITHNNLFITILLLFIYFFGSSLCNVIGEAQVVESNRNCSINSSARNVSLFFAFRKLSFAIMSYLSGYLLLLISKKHIFLIGSFLPICVFTSGFFIIEKRNYTKSSIKDQIKCIYSIIKLSYLKNFIIFIFIMMSTPSCGNTLFFYITNELKFSPNLLGKMAMFQSLASFISIISYMLFFTKIDIRKLLLYSTIIITPFCLLPLVVIKKVNYFLFIPNTLFFITDTVLIEFIAEFQTMPILVLCSRLIPEGFESTIYSLLLSSNNFASIISSFLSSLLTYSLNITSTNFTNLPYMIIICCLTNIIPIFFLYILPNHSQKKNLQHSNSHTQKYYSYPSTDYISSQKSDSSEITKFSADMQIDDITLE