wanglab/gogpt-training-data huggingface dataset:
Protein: Coiled-coil domain-containing protein 87 (Q9NVE4)
Organism: Homo sapiens (Human)
Function: Plays a role in spermatogenesis, where it is important for normal sperm head morphology. Also required for the acrosome reaction and thus normal male fertility.
Interaction partners:
Sequence:
MMEPPKPEPELQRFYHRLLRPLSLFPTRTTSPEPQKRPPQEGRILQSFPLAKLTVASLCSQVAKLLAGSGIAAGVPPEARLRLIKVILDELKCSWREPPAELSLSHKNNQKLRKRLEAYVLLSSEQLFLRYLHLLVTMSTPRGVFTESATLTRLAASLARDCTLFLTSPNVYRGLLADFQALLRAEQASGDVDKLHPVCPAGTFKLCPIPWPHSTGFAQVQCSNLNLNYLIQLSRPPEFLNEPGRMDPVKELKSIPRLKRKKPFHWLPSIGKKREIDISSSQMVSLPSYPVAPTSRASPSPFCPELRRGQSMPSLREGWRLADELGLPPLPSRPLTPLVLATESKPELTGLIVAEDLKQLIKKMKLEGTRYPPLDSGLPPLLGVVTRHPAAGHRLEELEKMLRNLQEEEASGQWDPQPPKSFPLHPQPVTITLKLRNEVVVQAAAVRVSDRNFLDSFHIEGAGALYNHLAGELDPKAIEKMDIDNFVGSTTREVYKELMSHVSSDHLHFDQGPLVEPAADKDWSTFLSSAFLRQEKQPQIINPELVGLYSQRANTLQSNTKKMPSLPSLQATKSWEKWSNKASLMNSWKTTLSVDDYFKYLTNHETDFLHVIFQMHEEEVPVEIVAPARESLEIQHPPPLLEDEEPDFVPGEWDWNTVLEHRLGAGKTPHLGEPHKILSLQKHLEQLWSVLEVPDKDQVDMTIKYSSKARLRQLPSLVNAWERALKPIQLREALLARLEWFEGQASNPNRFFKKTNLSSSHFLEENQVRSHLHRKLNLMESSLVSLLEEIELIFGEPVIFKGRPYLDKMKSDKVEMLYWLQQQRRVRHLVSALKDPHQSTLFRSSAASL
Protein: Protein CHROMATIN REMODELING 35 (Protein DEFECTIVE IN MERISTEM SILENCING 1) (Protein DEFECTIVE IN RNA-DIRECTED DNA METHYLATION 1) (Q9SIW2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the chromatin-remodeling complex (DDR complex) that mediates RNA polymerases IV and V (Pol IV and Pol V) recruitment to chromatin. Cooperates with Pol IV and Pol V to regulates RNA- and RNAi- (RNA interference) directed non-CpG de novo DNA methylation on cytosine of genes targeted for silencing and enhancers, also known as siRNA-directed DNA methylation (RdDM), thus leading to epigenetic modification of the genome and promoting/maintaining heterochromatin. In collaboration with Pol V, mediates/maintains, in cis, methylation-associated self-silencing of exogenous transgene transcribing inverted-repeat (exo-IR) silencer (exo-Pdsi) to restrain exo-IR dsRNA accumulation and subsequent inappropriate silencing of active protein-coding genes (e.g. PDS) by exo-IR-derivating 24-nt siRNAs. Also required to mediate loss of CpG methylation when the silencing inducer is withdrawn. Required for the maintenance of retrotransposon large terminal repeats (LTRs) and transposable elements (TE) edges silencing mediated by cytosine methylation. Required for transcriptional repression of specific classes of pericentromeric 180-bp repeats by promoting condensation and histone H3 lysine 9 dimethylation (H3K9me2) at chromocenters. Required for basal resistance against the necrotrophic fungal pathogen Plectosphaerella cucumerina.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:16839878}. Note=Excluded from the nucleolus. Colocalizes with endogenous repeat loci. {ECO:0000269|PubMed:16839878}.
Interaction partners:
- Protein RDM1
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- DNA-directed RNA polymerase V subunit 1
- DNA-directed RNA polymerases IV and V subunit 2
- DNA-directed RNA polymerases IV and V subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerase IV subunit 1
- DNA-directed RNA polymerase V subunit 5A
- Protein argonaute 4
- Endoribonuclease Dicer homolog 3
Sequence:
MGFVYIVMTGYYKNVHKRKQNQVDDGPEAKRVKSSAKVIDYSNPFAVSNMLEALDSGKFGSVSKELEEIADMRMDLVKRSIWLYPSLAYTVFEAEKTMDNQQVVEGVINLDDDDDDDTDVEKKALCVVPSSSEIVLLDSDDEDNERQRPMYQFQSTLVQHQKNQGDVTPLIPQCSFEEVDLGRGKEMPSAIKAIVEGQTSRGKVLPIENGVVNEKGVYVGVEEDDSDNESEAADEDLGNIWNEMALSIECSKDVARETSHKEKADVVEDCEHSFILKDDMGYVCRVCGVIEKSILEIIDVQFTKAKRNTRTYASETRTKRFGESDNELKFSEEGLMIGGLAAHPTHAAEMKPHQIEGFQFLCSNLVADDPGGCIMAHAPGSGKTFMIISFMQSFLAKYPQAKPLVVLPKGILPTWKKEFVRWQVEDIPLLDFYSAKAENRAQQLSILKQWMEKKSILFLGYQQFSTIVCDDTTDSLSCQEILLKVPSILILDEGHTPRNEDTNLLQSLAQVQTPRKVVLSGTLYQNHVKEVFNILNLVRPKFLKLDTSKSAVKRILAYTPCDVRGRLTGSNSDMASMFNETVEHTLQKSEDFTVKIKVIQDLREMTKKVLHYYKGDFLDELPGLADFTVVLNLSPKQLNEVKKLRREKRKFKVSAVGSAIYLHPKLKVFSDKSDDVSDTTMDEMVEKLDLNEGVKAKFFLNLINLCDSAGEKLLVFSQYLIPLKFLERLAALAKGWKLGKEVFVLTGNTSSEQREWSMETFNSSPDAKIFFGSIKACGEGISLVGASRILILDVPLNPSVTRQAIGRAFRPGQKKMVHAYRLIAGSSPEEEDHNTCFKKEVISKMWFEWNEYCGYQNFEVETIDVDEAGDTFLESPALREDIRVLYKR
Protein: Transcriptional repressor p66-beta (GATA zinc finger domain-containing protein 2B) (p66/p68) (Q8VHR5)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A. Targets MBD3 to discrete loci in the nucleus. May play a role in synapse development.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q8WXI9}. Nucleus {ECO:0000250|UniProtKB:Q8WXI9}. Chromosome {ECO:0000250|UniProtKB:Q8WXI9}. Note=Speckled nuclear localization requires both CR1 and CR2 regions. Localizes to sites of DNA damage. {ECO:0000250|UniProtKB:Q8WXI9}.
Interaction partners:
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- Histone deacetylase 1
- Chromodomain-helicase-DNA-binding protein 4
- Histone deacetylase 2
- DNA helicase
- Metastasis-associated protein MTA2
- Transcriptional repressor p66 alpha
- Metastasis-associated protein MTA1
- Metastasis-associated protein MTA3
Sequence:
MDRMTEDALRLNLLKRSLDPADERDDVLAKRLKMEGHEAMERLKMLALLKRKDLANLEVPHELPTKQDGSGVKGYEEKLNGNLRPHGDNNRTAGRPGKENINDEPVDMSARRSEPDRGRLTPSPDIIVLSDNEASSPRSSSRMEERLKAANLEMFKGKGMEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKENVVQKTPVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGIEPQNMRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPPKPGIVRTTTPNMNPAISYQPQSSSSVPCQRTTSSAIYMNLASHIQPGTVNRVSSPLPSPSAMSDAANSQAAAKLALRKQLEKTLLEIPPPKPPAPLLHFLPSAANSEFIYMVGLEEVVQSVIDSQGKNCASLLRVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVKALQQEQEIEQRLQQQAALSPTTAPAVSSVSKQETIMRHHTLRQAPQPQSSLQRGIPTSARSMLSNFAQAPQLSVPGGLLGMPGVNIAYLNTGIGGHKAPSLADRQREYLLDMIPPRSISQSISGQK
Protein: Rho guanine nucleotide exchange factor TIAM1 (T-lymphoma invasion and metastasis-inducing protein 1) (TIAM-1) (Q13009)
Organism: Homo sapiens (Human)
Function: Guanyl-nucleotide exchange factor that activates RHO-like proteins and connects extracellular signals to cytoskeletal activities. Activates RAC1, CDC42, and to a lesser extent RHOA and their downstream signaling to regulate processes like cell adhesion and cell migration.
Subcellular location: Cell junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Detected at the boundary between cells with actin-rich protrusions (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction. {ECO:0000250}.
Interaction partners:
- Cell division control protein 42 homolog
- Partitioning defective 3 homolog
- CD44 antigen
- Ankyrin-3
- Ankyrin-1
- GTPase KRas
- Ras-related C3 botulinum toxin substrate 1
- Nucleoside diphosphate kinase A
- GTPase HRas
- Ankyrin-2
Sequence:
MGNAESQHVEHEFYGEKHASLGRKHTSRSLRLSHKTRRTRHASSGKVIHRNSEVSTRSSSTPSIPQSLAENGLEPFSQDGTLEDFGSPIWVDRVDMGLRPVSYTDSSVTPSVDSSIVLTAASVQSMPDTEESRLYGDDATYLAEGGRRQHSYTSNGPTFMETASFKKKRSKSADIWREDSLEFSLSDLSQEHLTSNEEILGSAEEKDCEEARGMETRASPRQLSTCQRANSLGDLYAQKNSGVTANGGPGSKFAGYCRNLVSDIPNLANHKMPPAAAEETPPYSNYNTLPCRKSHCLSEGATNPQISHSNSMQGRRAKTTQDVNAGEGSEFADSGIEGATTDTDLLSRRSNATNSSYSPTTGRAFVGSDSGSSSTGDAARQGVYENFRRELEMSTTNSESLEEAGSAHSDEQSSGTLSSPGQSDILLTAAQGTVRKAGALAVKNFLVHKKNKKVESATRRKWKHYWVSLKGCTLFFYESDGRSGIDHNSIPKHAVWVENSIVQAVPEHPKKDFVFCLSNSLGDAFLFQTTSQTELENWITAIHSACATAVARHHHKEDTLRLLKSEIKKLEQKIDMDEKMKKMGEMQLSSVTDSKKKKTILDQIFVWEQNLEQFQMDLFRFRCYLASLQGGELPNPKRLLAFASRPTKVAMGRLGIFSVSSFHALVAARTGETGVRRRTQAMSRSASKRRSRFSSLWGLDTTSKKKQGRPSINQVFGEGTEAVKKSLEGIFDDIVPDGKREKEVVLPNVHQHNPDCDIWVHEYFTPSWFCLPNNQPALTVVRPGDTARDTLELICKTHQLDHSAHYLRLKFLIENKMQLYVPQPEEDIYELLYKEIEICPKVTQSIHIEKSDTAADTYGFSLSSVEEDGIRRLYVNSVKETGLASKKGLKAGDEILEINNRAADALNSSMLKDFLSQPSLGLLVRTYPELEEGVELLESPPHRVDGPADLGESPLAFLTSNPGHSLCSEQGSSAETAPEETEGPDLESSDETDHSSKSTEQVAAFCRSLHEMNPSDQSPSPQDSTGPQLATMRQLSDADKLRKVICELLETERTYVKDLNCLMERYLKPLQKETFLTQDELDVLFGNLTEMVEFQVEFLKTLEDGVRLVPDLEKLEKVDQFKKVLFSLGGSFLYYADRFKLYSAFCASHTKVPKVLVKAKTDTAFKAFLDAQNPKQQHSSTLESYLIKPIQRILKYPLLLRELFALTDAESEEHYHLDVAIKTMNKVASHINEMQKIHEEFGAVFDQLIAEQTGEKKEVADLSMGDLLLHTTVIWLNPPASLGKWKKEPELAAFVFKTAVVLVYKDGSKQKKKLVGSHRLSIYEDWDPFRFRHMIPTEALQVRALASADAEANAVCEIVHVKSESEGRPERVFHLCCSSPESRKDFLKAVHSILRDKHRRQLLKTESLPSSQQYVPFGGKRLCALKGARPAMSRAVSAPSKSLGRRRRRLARNRFTIDSDAVSASSPEKESQQPPGGGDTDRWVEEQFDLAQYEEQDDIKETDILSDDDEFCESVKGASVDRDLQERLQATSISQRERGRKTLDSHASRMAQLKKQAALSGINGGLESASEEVIWVRREDFAPSRKLNTEI
Protein: T. brucei spp.-specific protein (Q57U60)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGRLSSCELPEPRRSEIMSAAGRRSQLALAVNRTLDRKSLFYTSSNTHNTAVDAAGSSRISGINEHKLDTCTNTTIRDVVKCAINRGSGITDSATAVRALSVLPSETLMSSSRPSELLSHCPLSGSLRERGADPLRSMQPTSQLSFMTCSSAGPRISAGKRVSAPPRVEPTVSCRISTMQISPRLSCIADRSGAVARSDIAVGGRSALVGVHSPQPRVINSGRVAYGTYTRRSTENDGVAPARCAPAISSTSSSARIAAIRSEKSVLPPAAIATTTATPTKTTPVTPVSASSSASIHFAVSRTAAPRNGAAADNSGSGTRAAPDVSAFRNSRLSDHEGAQQLISPEKQARDADGCTGAKGVSRRLSFDDGAVKMGSNSLDFSKDSTKASSRVNGADKPEQTTVSLSANTQQWREESRTTLTPVRRPTAPPTFISTLDPCPVNVNEGVVTTTKSSADEVVLGKHVQENDVRAHGRERQTVNVSRLHSYAGAPVHETGQKPFIRESVCGTDSDRSQSNVVSSRISQGDIRFCSALRPKFDMCSGRYGDKVAQVKMSRCHSAGSRLLPASRESGGTLFNDERNTSFGARSRARASDQVGCNSHKEANGSSHAASLVSTTAGGRLERAERRPIPPASQWKGTCFPASLTAVDRASGSNTYAATTAKRASSTDAQTSEGCGAFLRGLKLASSGAADSMEPQVIPPTFSKDTETTLTFTRCVTEFCTTILQERDRRHDAEAGAEVKACHPTRKSGSMDVTSLCFSRCASGRIVPQSREWPRRADPTSQKRLSCPSVPLRRSATAPSWRCRMSTREETTCPIRAPSPTNTTTSSTASVLLRVRNVLDERRARIQASLQEWRNGTSEAGGNAAKAVVLARVDQSNHQQLKFNRGGGSGSGSSGGCYGISSSNTPGEMTERVDKSHERSEEEEHTPLQAPLHGDESHMQQKRYVLLASESVASPKRINSSDHHGTDDSEGNDTNHISVGGDAARRGEQHVDCDNCVSDGYEADYCDDDDDDDCGESSHSDEDPWWFFEYFWSGPAIVVVPPAFVPPLNFAKLLIPDDGTALKKYAIPLPTPMPLSPTRANRTVPTDFVAPPAFNPPHSSAACSGSRRRRLAEVKQTETSVEAKRERGVSVKILLLETAERRSRRLRHQEEIASRWALQEQRAEELRCQGL
Protein: Protocadherin 9 (A0A0A6YY09)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDLRDFYLLAALIACLRLDSAIAQELIYTIREELPENVPIGNIPKDLNISHINAATGTSASLVYRLVSKAGDAPLVKVSSSTGEIFTTSNRIDREKLCAGASYAEENECFFELEVVILPNDFFRLIKIKIIVKDTNDNAPMFPSPVINISIPENTLINSRFPIPSATDPDTGFNGVQHYELLNGQSVFGLDIVETPEGEKWPQLIVQQNLDREQKDTYVMKIKVEDGGTPQKSSTAILQVTVSDVNDNRPVFKEGQVEVHIPENAPVGTSVIQLHATDADIGSNAEIRYIFGAQVAPATKRLFALNNTTGLITVQRSLDREETAIHKVTVLASDGSSTPARATVTINVTDVNDNPPNIDLRYIISPINGTVYLSEKDPVNTKIALITVSDKDTDVNGKVICFIEREVPFHLKAVYDNQYLLETSSLLDYEGTKEFSFKIVASDSGKPSLNQTALVRVKLEDENDNPPIFNQPVIELSVSENNRRGLYLTTISATDEDSGKNADIVYQLGPNASFFDLDRKTGVLTASRVFNREEQERFIFTVTARDNGTPPLQSQAAVIVTVLDENDNSPKFTHNHFQFFVSENLPKYSTVGVITVTDEDAGENKAVTLSILNDNENFVLDPYSGVIKSNVSFDREQQSSYTFDVKATDGGQPPRSSTAKVTINVMDVNDNSPVVISPPSNTSFKLVPLSAIPGSVVAEVFAVDIDTGMNAELKYTIVSGNNKGLFRIDPVTGNITLEEKPAPTDVGLHRLVVNISDLGYPKALHTLVLVFLYVNDTAGNTSYIYDLIRRTMETPLDRNIGDSGQPYQNEDYLTIMIAIVAGAMVVIVVIFVTVLVRCRHASRFKAAQRSKQGAEWMSPNQENKQNKKKKRKKRKSPKSSLLNFVTIEESKPDDAVHEPINGTISLPAELEEQGIGRFDWGPAPPTTFKPNSPDLAKHYKSASPQPAFHLKPDTPVSVKKHHVIQELPLDNTFVGGCDTLSKRSSTSSDHFSASECSSQGGFKTKGPLHTRQCNSYSKNDNIPVTHQKCPGSTSFHIRENEESHSEPQDEFYDQASPDKRTEADGNSDPNSDGPLGPRGLAEATEMCTQECLVLGHSDNCWMPPGLGPYQHPKSPLSTFAPQKEWIKKDKLVNGHTLTRAWKEDTNRNQFNDRKQYGSNEGHFNNGGHMADIPLANLKSYKQAGGTIESPKEHQL
Protein: Uncharacterized protein (Q584T8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ubiquitin-like domain-containing protein
- Manganese/iron superoxide dismutase C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Ribosomal protein S9
Sequence:
MLRRCPCVWPDGPTKSSVSIGTAFTLQKRFLKIAKSAFGFYLARRGQRKYPFLRRPHIKNTHSMNPSAPYFWSFMTAKSQMAFLPEENYITGDWTGKFFVSKRQVYTLQHATSGAKVRVKSFPSIFEFNSPSRWNIGKEMNTLTKPRMDLIDEQMLTKKQRLDYVRAGLLPK
Protein: Receptor tyrosine-protein kinase let-23 (EC 2.7.10.1) (Lethal protein 23) (P24348)
Organism: Caenorhabditis elegans
Function: Tyrosine-protein kinase receptor which, upon binding ligand lin-3, activates 2 signaling cascades: the let-60/Ras and MAP kinase signaling pathway and the let-60-independent phospholipase C-mediated Ca(2+) signaling pathway. Each pathway regulates distinct functions. By activating let-60/Ras, regulates larval development, induction of vulva cell precursors during vulva development, male spicule formation and posterior development of the epidermis. Probably by activating phospholipase plc-3 and inositol 1,4,5-trisphosphate receptor itr-1 signaling cascade downstream of ligand lin-3, plays a role in ovulation by promoting ovulatory gonadal sheath cell contractions. Probably by regulating neuronal transmission in ALA neurons, mediates, independently of let-60/Ras, the decrease in pharyngeal pumping and locomotion during the quiescent state that precedes each larval molt, downstream of lin-3 and upstream of plc-3.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:32053105}; Single-pass type I membrane protein {ECO:0000269|PubMed:10359617}. Basolateral cell membrane {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:32053105}; Single-pass type I membrane protein {ECO:0000269|PubMed:10359617}. Note=Basolateral and apical membrane of cell junctions in epithelial vulval precursor cells. {ECO:0000269|PubMed:10359617}.
Interaction partners:
- Protein lin-3
- E3 ubiquitin-protein ligase CBL
- Sex muscle abnormal protein 5
- SHC-transforming protein homolog 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma plc-3
- Ras protein let-60
- Son of sevenless homolog
- Protein lin-7 homolog
- Protein let-756
- Signal transducer and activator of transcription 1
Sequence:
MRYPPSIGSILLIIPIFLTFFGNSNAQLWKRCVSPQDCLCSGTTNGISRYGTGNILEDLETMYRGCRRVYGNLEITWIEANEIKKWRESTNSTVDPKNEDSPLKSINFFDNLEEIRGSLIIYRANIQKISFPRLRVIYGDEVFHDNALYIHKNDKVHEVVMRELRVIRNGSVTIQDNPKMCYIGDKIDWKELLYDPDVQKVETTNSHQHCYQNGKSMAKCHESCNDKCWGSGDNDCQRVYRSVCPKSCSQCFYSNSTSSYECCDSACLGGCTGHGPKNCIACSKYELDGICIETCPSRKIFNHKTGRLVFNPDGRYQNGNHCVKECPPELLIENDVCVRHCSDGHHYDATKDVRECEKCRSSSCPKICTVDGHLTNETLKNLEGCEQIDGHLIIEHAFTYEQLKVLETVKIVSEYITIVQQNFYDLKFLKNLQIIEGRKLHNVRWALAIYQCDDLEELSLNSLKLIKTGAVLIMKNHRLCYVSKIDWSSIITSKGKDNKPSLAIAENRDSKLCETEQRVCDKNCNKRGCWGKEPEDCLECKTWKSVGTCVEKCDTKGFLRNQTSMKCERCSPECETCNGLGELDCLTCRHKTLYNSDFGNRMECVHDCPVSHFPTQKNVCEKCHPTCYDNGCTGPDSNLGYGGCKQCKYAVKYENDTIFCLQSSGMNNVCVENDLPNYYISTYDTEGVIETHCEKCSISCKTCSSAGRNVVQNKCVCKHVEYQPNPSERICMDQCPVNSFMVPDTNNTVCKKCHHECDQNYHCANGQSTGCQKCKNFTVFKGDIAQCVSECPKNLPFSNPANGECLDYDIASRQRKTRMVIIGSVLFGFAVMFLFILLVYWRCQRIGKKLKIAEMVDMPELTPIDASVRPNMSRICLIPSSELQTKLDKKLGAGAFGTVFAGIYYPKRAKNVKIPVAIKVFQTDQSQTDEMLEEATNMFRLRHDNLLKIIGFCMHDDGLKIVTIYRPLGNLQNFLKLHKENLGAREQVLYCYQIASGMQYLEKQRVVHRDLATRNVLVKKFNHVEITDFGLSKILKHDADSITIKSGKVAIKWLAIEIFSKHCYTHASDVWAFGVTCWEIITFGQSPYQGMSTDSIHNFLKDGNRLSQPPNCSQDLYQELLRCWMADPKSRPGFEILYERFKEFCKVPQLFLENSNKISESDLSAEERFQTERIREMFDGNIDPQMYFDQGSLPSMPSSPTSMATFTIPHGDLMNRMQSVNSSRYKTEPFDYGSTAQEDNSYLIPKTKEVQQSAVLYTAVTNEDGQTELSPSNGDYYNQPNTPSSSSGYYNEPHLKTKKPETSEEAEAVQYENEEVSQKETCL
Protein: Cyclin-dependent protein kinase inhibitor SMR4 (Protein SIAMESE-RELATED 4) (Q1JPP8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle. Acts as a potent cell cycle inhibitor.
Interaction partners:
- Cyclin-dependent protein kinase inhibitor SMR7
- Putative cyclin-D7-1
- SUPPRESSOR OF GAMMA RESPONSE 1
- Wee1-like protein kinase
- Cyclin-dependent protein kinase inhibitor SMR2
- Ribonucleoside-diphosphate reductase small chain C
- Cyclin-dependent kinase inhibitor 6
- Cyclin-dependent kinases regulatory subunit 2
- Cyclin-dependent protein kinase inhibitor SMR11
- Transcription factor MYB3R-5
Sequence:
MEVVERKTEMAEEGCTTPRSTMYRIPVASVCPPPPRKKLMVVRKRDPPRNGYFQPPDLETLFYAQPRREACA
Protein: Peroxisomal targeting signal receptor (PTS1 receptor) (PTS1R) (Peroxin-5) (Peroxisomal protein PAH2) (Q01495)
Organism: Pichia angusta (Yeast) (Hansenula polymorpha)
Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35056}. Peroxisome matrix {ECO:0000250|UniProtKB:P35056}. Note=Cycles between the cytosol and the peroxisome matrix. Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol. Cys-9 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15, resetting PEX5 for a subsequent import cycle (By similarity). {ECO:0000250|UniProtKB:P35056, ECO:0000250|UniProtKB:P50542}.
Interaction partners:
Sequence:
MSFLGGSECAANANPLAQFFKQSQHDTSLEQSLRNSAHDTHQNAQIRAPVAMNEAERAHMEQFMNQSTPFNFQPMANELRMIQPDLQTQTTPALRGPRAQNPVPLQIPGQAQPQVSGWSSEFQNTATSQVTHSPSPVSQVRMRSMGMAPRLHLRPFSSANGPIQASSMTNSVMQEDTSQQVDWEQQFKEMEEMEEMEEATAAMQQPAEETVSAQESAFDQVWDNIQETYADNMLSNDEFQAQWEKDFEKYAQTRLNYGEYTFEENNQFRNNLDAYEIGIKLMESGAKLSEAALAFEAAVEQNPGHVDAWLRLGQVQTQNEKELAGIAALEKCLELSPQNLVALMTLAISYINEGYDNAAFATLERWIETKYPEVAERARNANPDIQADDRFSLNKRVTQLFIKAAQLSPEGANMDSEVQTGLGVLFYSMEEYSKTLDCFQAAIEHNPNDALAWNRLGASLANSNKPEQAIEAYSRTLQLNPNFVRARYNLGVSFINMGMYRDAVDHLLTGLSMHEVESLDGSSSVARSNQSTSLIETLKRAFLAMDRRDLIDKVKPGLNVESFRKTYDI
Protein: 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CPDase) (EC 3.1.4.37) (P53314)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- tRNA ligase
- tRNA 2'-phosphotransferase
- Probable ADP-ribose 1''-phosphate phosphatase YML087W
- ADP-ribose 1''-phosphate phosphatase
Sequence:
MAIALWYCPPQGSVAYETLQMLIFSFQTLFPDSPVFEPHVTVTSHLVCNSKDDVNKILTSCVAAIQSIRSHQTAKKGRKGQVSHAVAAPLVSFNGCSVGKQYFKKIVLECNKNKILYGVAQVMREMYVEIDPETRSSRAATWVHEEFHPHVSLLYSDIHPVSQASLRVVQQRIEDALDVQLVPREKRKGSGNADGSNEVQMRWDFDVSSSLSWNIPGTFKVVNCVGPVQEWEVLGRVDV
Protein: Claudin-4 (B9EL29)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MASAGFQMLGTALGIIGWIGAIVVCALPQWKVTAFIGENIITAQTTWQGIWMNCVVQSTGQMQCKVYDSMLALPQDLQAARALIIISIMMGLVGILLSVAGGKCTNCVEDERTKSRIGVGSGVVFIIAGVLCLIPVCWSANTIIRDFYNPMLNSSQKMELGAALYIGWGAAALMIIGGGFLCANCPPKEDNYPTRYSAARSTAPRDYV
Protein: Heat-shock protein 12.1 (SHSP domain-containing protein) (G5EE65)
Organism: Caenorhabditis elegans
Interaction partners:
- SHSP domain-containing protein
- J domain-containing protein
- Heat shock protein 90
- Heat shock protein Hsp-12.2
- MAP kinase-activated protein kinase mak-2
Sequence:
MHTIPITTDSAASWDWPLQHNDGVVKVTNTSEKFEVGLDAGFFGPNDIDVKVNGIEIIIHLRHDLLQNRPTEYGIVNREVHRTYKLPEDVDPSTVRSHLNSSGVLTITANKL
Protein: Arrestin C-terminal-like domain-containing protein (Q20577)
Organism: Caenorhabditis elegans
Interaction partners:
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- Patterned Expression Site
- Arrestin C-terminal-like domain-containing protein
- Neuropeptide-like protein 32
Sequence:
MEHMDHFGIVFDSPRGYAPGQTVTGQVVLRSNEPITARFLKICIHGAAHTKWSEGERRYRTNCEGKEESYTEIVHYSAEVDYVSGETIAWSARNGTEKLPSGHHVFPFAFPLPIECPPSFEGFHGHVRYSVRVELDRPWKFNKNEREDFKVIPNFDLNHLPLGNVPRMMKDVKDIGQIFKKGIVTITVTIPKAGYAPGEYLPITIDIDNASKRAATFVRAELHQHSHYNASKNHGLLCTHSSYHEHHKDESKRIAEARKSIKIAPKTAGREMLRMKIPKSPPTFTSPIISIEYCLSVRLDTLTTLNNTLHCEFDIIIGTVPITESIVEPTVTTFPSDPPVLERLDS
Protein: GH23377p (Q961H4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELRKIFNDDNETLSTLCKVLANMSLVPDAVEHFFTSGWVGALAEWQQCPDLRLQVISAKTMANLDHDDPNQCTYPPNVYPLHPRVRTRRKPKADIVFVHGLLGGVFITWRQRDRKPTELGLYGKNAFYTSETDDVFLVGEQKRLSGGKLKPGEAVKNVNGNQKTETIKDPVLKASKKVEEQRLNISDAATKEFVETLRNEAELDSDWEVVHPDVPLNANEECEGKFSVCGSEWRNQDTSEEYTNCWPMEWLPDDYPDSRILGIDYTSAVTEWSANFTKYCPCEKGQGHIDVRANTLLDRISASDVGNDRPIVWIGHSMGGLLTKLILLKSLDSQEPKVQQLTKNTKGIVFLGTPHRGSPIAKWKQHMQMILSPSIEVKEMEENSPKLLEMHRRFMGCLHTLLRHVKVVSVAEGSPTMLTSFKFPLRIVTEESSKIDFGDFYLLKDDHLSLSKPIYRQSFLYQRLLHVIREAIKERSDPKDQDGQSQSTSNQDVVLVKIVAALLEGAKGLFESLPRVALRFST
Protein: Protein ROD1 (Resistance to o-dinitrobenzene protein 1) (Q02805)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mediates resistance to o-dinitrobenzene, calcium and zinc.
Subcellular location: Membrane {ECO:0000269|PubMed:8621680}; Peripheral membrane protein {ECO:0000269|PubMed:8621680}. Note=Membrane-associated or associated to a complex that cofractionates with plasma membrane.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Carbon catabolite-derepressing protein kinase
- Arrestin-related trafficking adapter 6
- Protein LDB19
- Ubiquitin ligase-binding protein BUL1
- Carboxylic acid transporter protein homolog
- Ubiquitin ligase-binding protein BUL2
- Protein ECM21
- Transcription factor CSR2
- pH-response regulator protein palF/RIM8
Sequence:
MFSSSSRPSKEPLLFDIRLRNLDNDVLLIKGPPDEASSVLLSGTIVLSITEPIQIKSLALRLFGRLRLNIPTVLQTVHGPHKRYSKFERNIYSHFWDDFNIKSYFQNLYDNHNNGKITISSKSSTNLAALPKRKRALSTASLISSNGQTSASKNYHTLVKGNYEFPFSAIIPGSLVESVEGLPNAAVTYALEATIERPKQPDLICKKHLRVIRTLAIDAVELSETVSVDNSWPEKVDYTISIPTKAIAIGSSTMINILIVPILKGLKLGPVRISLVENSQYCGSYGGVINQERMVAKLKLKDPLKHVAQIKKKRSLNEAADEGVDTDTGEFQDKWEVRALLNIPASLTKCSQDCRILSNIKVRHKIKFTISLLNPDGHISELRAALPVQLFISPFVPVNVKTSDVIERTLKTFGPSYQVTSQHDNSFSSKNFVDDSEEDVIFQRSASALQLSSMPTIVSGSTLNINSTDAEATAVADTTMVTSLMVPPNYGNHVYDRVYGEVTNEDETSASASSSAVESQAIHNIQNLYISDSNNSNNPILAPNPQIKIEDDSLNNCDSRGDSVNNSNLNLVNSNLTISENWNNNSPSANRYNNIINAGLNSPSLTPSFAHLSRRNSYSRQTSSTSLKNDLELTDLSRVPSYDKAMKSDMIGEDLPPAYPEEELGVQENKKIELERPQILHHKSTSSLLPLPGSSKSSNNLKRSSSRTHLSHSPLPRNNSGSSVSLQQLARNNTDSSFNLNLSFTSAKSSTGSRHFPFNMTTSFTSNSSSKNNSHFDKTDSTSDANKPREEENYTSATHNRRSRSSSVRSNNSNSPLRQGTGSFANLMEMFTKRDRS
Protein: Unconventional myosin (Q8T6M0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFNFMKKSAGDEDKERRKREKKLRKEAKGTSGGPGMGGVTGVTGSMSTDELLRLDEVRRSLKIRGRRKEKEKLPSGITADYSADFFAALNADANGGSNGGAVGAADPEQDRGNEEIVASVMTHIESRASNGAGVSVNYSEVTHSLLSGGLKNRFLPPIPPKPPKRGILKGSRSNMTNVHEEISFAGSAGGAGGTPEMLLRNTFQNESLYEGAARGAGSIGSNSSQHGTSFTSVESLRSDGEQTGGQQRAMTLPANARYGALPQGNSQGSHLHVLTSPSPSADSLTDTTNSSFATPPFSLSPVGESQGIDRWARVHAFEDVELPLPPVQLVKLPPPRQLVIRRQKSPRQDFGFSLRKAICLDRTESLTSPIFRPVIFAEPGAGGGATGLLPGDRLIKVNGTPVGELPREIIIEMIRNSGEAVTVEVQPVAELVELSKRCMAPSTATVEEIDHSITNGNCNTLRRSASKRFKRQSRHENGNGGGEEGGAKGVGHDLEADVADASQPERVWLVHRGGFTAAIRLPTASSGRDEENKLSLRLLHNGEQLTVDEDDVEKQNSPALDLVEDICELKYLNEASVLHCLRQRYASNLIHTKAGPTLLVVNPMAPLSLYSEKVVSM