wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic AMP-responsive element-binding protein 3-like protein 4 (cAMP-responsive element-binding protein 3-like protein 4) (Attaching to CRE-like 1) (ATCE1) (Acre1) (Transcript induced in spermiogenesis protein 40) (Tisp40) (mJAL) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3-like protein 4] (Q9D2A5)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator that may play a role in the unfolded protein response of the testis. Proposed to be involved in spermiogenesis. May be involved in regulating the maturation of sperm head nuclei. Alternatively proposed to be a paternally delivered transcription factor that may function in early zygotic gene activation. Increases the binding of CREM isoform Tau with CRE. The CREM isoform Tau-CREB3L4 heterodimer functions through CRE but not through UPRE and may recruit HIRA to CRE to regulate histone exchange.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16925989}; Single-pass type II membrane protein {ECO:0000269|PubMed:16925989}. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:16925989}; Single-pass type II membrane protein {ECO:0000269|PubMed:16925989}. Note=According to PubMed:16925989 is not observed within nuclei of haploid spermatids at any spermiogenic stage.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 4]: Nucleus. Note=Under ER stress the cleaved N-terminal cytoplasmic domain translocates into the nucleus.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Cyclic AMP-responsive element-binding protein 3
- cAMP-responsive element modulator
- Cyclic AMP-dependent transcription factor ATF-6 beta
- Cyclic AMP-responsive element-binding protein 5
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- CREB-regulated transcription coactivator 2
- Cyclic AMP-responsive element-binding protein 3-like protein 2
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Cyclic AMP-dependent transcription factor ATF-4
Sequence:
MELGCPELLEPPEDIFSTGSFLELGFNGPASKVPVTRGLQKSEPDDFLNLFIDPNMIHCSETSPGRDSGVSEDPGSPAQQASSSPALYEVVYDSGTLQGTQREAGPTFGLISIQIDQWTPALMVPDACTVSGLPSDSHRHILPRVSTRAPAPPAAMPSCQHHLFLTDEEKQLLAQEGITLPSHLPLTKAEERILKKIRRKIRNKQSAQDSRRRKKEYLDGLESRVAACSEQNQKLQRKVQELERQNIFLMEQVRQLQKLTAQTSSRAAQTSTCVLILLFSLALIILPSFSPFQGQSEARPEDYQLHGVISRNILTHENVTENLESPVLKSKLEELPEAPTTNGSTKTHLKMRVKARPPGQIRGMVHTDEM
Protein: Aminodeoxychorismate lyase (EC 4.1.3.38) (4-amino-4-deoxychorismate lyase) (ADC lyase) (ADCL) (Q03266)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Aminodeoxychorismate synthase
- Folic acid synthesis protein FOL1
- Dihydrofolate synthetase
- GTP cyclohydrolase 1
- 5-formyltetrahydrofolate cyclo-ligase
Sequence:
MSLMDNWKTDMESYDEGGLVANPNFEVLATFRYDPGFARQSASKKEIFETPDPRLGLRDEDIRQQIINEDYSSYLRVREVNSGGDLLENIQHPDAWKHDCKTIVCQRVEDMLQVIYERFFLLDEQYQRIRIALSYFKIDFSTSLNDLLKLLVENLINCKEGNSEYHEKIQKMINERQCYKMRVLVSKTGDIRIEAIPMPMEPILKLTTDYDSVSTYFIKTMLNGFLIDSTINWDVVVSSEPLNASAFTSFKTTSRDHYARARVRMQTAINNLRGSEPTSSVSQCEILFSNKSGLLMEGSITNVAVIQKDPNGSKKYVTPRLATGCLCGTMRHYLLRLGLIEEGDIDIGSLTVGNEVLLFNGVMGCIKGTVKTKY
Protein: Laminin subunit alpha 3 (D3ZN05)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MPPTVRWSAWSTGWLWIFGAALGQCLGYGSEQQRVAFLQHPGQNHLQASYMELRPSQGCRPGYYRDIKSFPAGRCVPCNCNGHSNRCQDGSGVCINCQHNTAGEHCERCQEGYYGSAIHGSCRVCPCPHTNSFATGCAVDGGAVRCACKPGYTGAQCERCAPGYFGNPQKFGGSCQPCNCNSNGQFGTCDPLTGDCVSQEPKDGSPAEECDDCDSCVMTLLNDLVSMGEELRLVKSRLQGLSVSTGALEQIRHVEMQAKDLRNQLLGFRSAISSHGSKMDGLEKELSHLNQEFETLQEKAQVNSRKAQTLYNNIDQTIQNAKELDMKIKNIIQNVHILLKQIARPGGEGMDLPVGDWSRELAEAQRMLRELRGRDFKKHLQEAEAQKMEAQLLLNRIRTWLESHQVENNGLLKNIRDSLNDYEAKLQDLRSVLQEAAAQGKQATGLNHENEGVLGAIQRQMKEMDSLKNDLTEHLATADASLLQTNSLLQRMDTSQKEYESLAAALNGARQELNDQVRELSRSGGKAPLVAEAEKHAQSLQELAKQLEEIKRNTSGDELVRCAVDAATAYESILNAIRAAEDAAGKAASASESAFQTVIKEDLPRRAKTLSSDSEELLNEAKMTRKRLQQEINPALNSLQQTLKTVSVQKDLLDANVTAVRNDLRGIQRGDIDSVVSGAKSMVRKANGITSEVLDGLSPIQTDLGRIKDSYGSTRHEDFNKALIDANNSVKKLTKKLPDLFVKIESINQQLLPLGNISDNVDRIRELIQQARDAANKVAIPMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPDLRENGGTEDMFVMYLGNKDASKDYIGMAVVDGQLTCVYNLGDREAEVQIDQVLTESESQEAVMDRVKFQRIYQFAKLNYTKEATSNKPKAPAVYDLEGGSSNTLLNLDPEDAVFYVGGYPPDFELPSRLRFPPYKGCIELDDLNENVLSLYNFKTTFNLNTTEVEPCRRRKEESDKNYFEGTGYARIPTQPNAPFPNFIQTIQTTVDRGLLFFAENQDNFISLNIEDGNLMVRYKLNSEPPKEKGIRDTINDGKDHSILITIGKLQKRMWINVNERSVRIEGEIFDFSTYYLGGIPIAIRERFNISTPAFQGCMKNLKKTSGVVRLNDTVGVTKKCSEDWKLVRTASFSRGGQMSFTNLDVPSTDRFQLSFGFQTFQPSGTLLNHQTRTSSLLVTLEDGHIELSTRDSNIPIFKSPGTYMDGLLHHVSVISDTSGLRLLIDDQVLRRNQRLPSFSNAQQSLRLGGGHFEGCISNVLVQRFSQSPEVLDLASKSTKKDASLGGCSLNKPPFLMLFKSPKRFNKGRIFNVNQLMQDAPQATRSTEAWQDGRSCLPPLNTKASHRALQFGDSPTSHLLFKLPQELLKPRSQFSLDIQTTSPKGLVFYTGTKDSFLALYVADGRVVFALGAGGKKLRLRSKERYHDGKWHTVVFGLNGGKARLVVDGLRAQEGSLPGNSTISPREQVYLGLPLSRKPKSLPQHSFVGCLRDFQLNSKPLDSPSARFGVSPCLGGSLEKGIYFSQGGGHVILANSVSLGPELKLTFSIRPRSLTGVLIHVGSQSGQRLSVYMEAGKVTTSVSSDAGGSVTSITPKQSLCDGQWHSVAVSIKQRILHLELDTDSSYTVAPLSFSPNSTRGSLHVGGVPDKLKMLTLPVWNSFFGCLKNIQVNHVPVPITEATEVQGSVSLNGCPDH
Protein: Contig An05c0060, genomic contig (EC 1.10.3.2) (A2QL29)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MWFSVSFLLSALAIPQVLGASIPSTSQPKACVNSPTNRACWRDGYNISTNYYEEVPDTGVTREYWFNVENTTAAPDGVELPVQLINGSFPGPTIIADWGDTVIVHVTNSLQNNGTGLHFHGIRQNWTDQMDGVPSITQCPIAPGQSYTYKWRAVEYGTGWYHSHFYVQAWDGVFGGIVINGPATANYDVDLGHLFLNDWYHKTADELVLQAATDGPPTPPNGLINGTNTYGNNGSRFETTFDAGTKYRLRLVNAAADNHFRFMIDNHTMEVIAADFVPIHPYNTTQLSIGMGQRYDIIVTAKQLTSGNFWLRAIPQEACSETDALNNIKGIIRYGNSSTADPTTSAWSYTDSCADESSSDLIPYVAINASDSFAYSTTEEVAIEVAENALLWTMNKTSFHTEWDYPTLMHVANHNYTWAAKERIIHLPYRDQWVYLVVHSPFAQDHPMHLHGHDFWVLASGYGDFDATKSDALTLVNAPRRDVAMMPASGYLVIAIKTNNPGAWLMHCHIAWHTSEGFAVQLLERAPEIAYDYEKLNDTCASWKSYVAAQDVVQHDSGV
Protein: Protein ADP-ribosyltransferase (EC 2.4.2.-) (Sirtuin class M) (SirTM) (A0A0H3JQ59)
Organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)
Function: Catalyzes specifically the mono-ADP-ribosylation of GcvH-L (SAV0324). This activity is dependent on prior lipoylation of the target protein. May be involved in the modulation of the response to host-derived oxidative stress. In contrast to other sirtuin classes, lacks protein deacylase activity, being unable to catalyze delipoylation, debiotinylation, deacetylation and desuccinylation of proteins.
Interaction partners:
Sequence:
MMQSSKWNAMSLLMDEKTKQAEVLRTAIDEADAIVIGIGAGMSASDGFTYVGERFTENFPDFIEKYRFFDMLQASLHPYGSWQEYWAFESRFITLNYLDQPVGQSYLALKSLVEGKQYHIITTNADNAFDAAEYDMTHVFHIQGEYILQQCSQHCHAQTYRNDDLIRKMVVAQQDMLIPWEMIPRCPKCDAPMEVNKRKAEVGMVEDAEFHAQLQRYNAFLEQHQDDKVLYLEIGIGYTTPQFVKHPFQRMTRKNENAIYMTMNKKAYRIPNSIQERTIHLTEDISTLITTALRNDSTTQNNNIGETEDVLNRTD
Protein: Solute carrier family 25 member 3 (Phosphate carrier protein, mitochondrial) (Phosphate transport protein) (F8VWR4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MFSSVAHLARANPFNTPHLQLVHDGLGDLRSSSPGPTGQPRRPRNLAAAAVEEQYSCDYGSGRFFILCGLGGIISCGTTHTALVPLDLVKCRMQVDPQKYKGIFNGFSVTLKEDGVRGLAKGWAPTFLGYSMQGLCKFGFYEVFKVLYSNMLGE
Protein: CASP-like protein 1E2 (AtCASPL1E2) (O23413)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:24920445}; Multi-pass membrane protein {ECO:0000269|PubMed:24920445}.
Interaction partners:
- EMBRYO DEFECTIVE 3147
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Putative acyl-activating enzyme 19
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 9
Sequence:
MEHEGKNNMNGMEMEKGKRELGSRKGVELTMRVLALILTMAAATVLGVAKQTKVVSIKLIPTLPPLDITTTAKASYLSAFVYNISVNAIACGYTAISIAILMISRGRRSKKLLMVVLLGDLVMVALLFSGTGAASAIGLMGLHGNKHVMWKKVCGVFGKFCHRAAPSLPLTLLAAVVFMFLVVLDAIKLP
Protein: Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase) (Q0TV31)
Organism: Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Function: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage. Acts on human and mouse erythrocytes, but not on rabbit or horse erythrocytes.
Subcellular location: Secreted.
Interaction partners:
- Cardiolipin synthase
- Cardiolipin synthase
- Diacylglycerol kinase/PAP2 family protein
- Cardiolipin synthase
- Phosphatidylserine decarboxylase proenzyme
- CDP-diacylglycerol--serine O-phosphatidyltransferase
Sequence:
MKRKICKALICAALATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEAFYTDILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFSDAYKPENIKIIANGKVVVDKDINEWISGNSTYNIK
Protein: RE31022p (Serpin 4) (Serpin 42Da, isoform K) (Serpin 42Da, isoform L) (Q8MM39)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADAAHQEFARRLALFSINVYGKLSGQKPGENIVFSPFSIQTCAAMARLGAENETATQLDQGLGLASSDPEQIAHSFHQVLAAYQDSQILRIANKIFVMDGYQLRQEFDQLLSKQFLSAAQSVDFSKNVQAAATINNWVEQRTNHLIKDLVPADVLNSESRLVLVNAIHFKGTWQHQFAKHLTRPDTFHLDGERTVQVPMMSLKERFRYADLPALDAMALELPYKDSDLSMLIVLPNTKTGLPALEEKLRLTTLSQITQSLYETKVALKLPRFKAEFQVELSEVFQKLGMSRMFSDQAEFGKMLQSPEPLKVSAIIHKAFIEVNEEGTEAAAATGMVMCYASMLTFEPQPVQFHVQHPFNYYIINKDSTILFAGRINKF
Protein: RNA-binding protein Pasilla (A0A0B4KGY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion (By similarity). Plays a role in long-term memory formation by processing the unspliced Orb2-isoform A (Orb2A) mRNA and thereby controlling Orb2A protein abundance.
Subcellular location: Nucleus {ECO:0000269|PubMed:11784037, ECO:0000269|PubMed:28525754}. Cytoplasm {ECO:0000269|PubMed:28525754}. Note=Localizes to synaptoneuropil region of neurons. {ECO:0000269|PubMed:28525754}.
Interaction partners:
- RNA-binding Fox protein 1, isoform H
- Heterogeneous nuclear ribonucleoprotein A1
Sequence:
MESIMKVAMDKAAEQLIQQFGFDYLQQQLQLQHQNQHNSSPQQPQHQQLEPENEHLTYQYQQSKPTHMQQLACNYQPRHSTTTSSPSSTHSLASGGGSSSNSSNSSSSDSSSINISHISNISNISNIGNISNSNHSNAAYSLAVHSYQKQIESPANPSHVPHHQMDLSPLSENGSPNGTPGAQTPTATASGNTAAALASAAAAAAAATSGGNGSSITNCNSNNSSSSSNAQQQLQLGNYKTNSCWCYGESVCSGIEVEIENNNNNHIHHGETTYHMKILVPAVASGAIIGKGGETIASLQKDTGARVKMSKSHDFYPGTTERVCLITGSTEAIMVVMEFIMDKIREKPDLTNKIVDTDSKQTQERDKQVKILVPNSTAGMIIGKGGAFIKQIKEESGSYVQISQKPTDVSLQERCITIIGDKENNKNACKMILSKIVEDPQSGTCLNVSYADVSGPVANFNPTGSPYATNQNAINSSTASLNSTLGTTIGGANSAASLLVNGTGINLSINLGSPNPAPNLAVATQLLEHIKVAMRGSGYSETVTNEVVAALSVLAKYGVLGMGVGVSHTNGAHSTLGNFLGVTTLDQQTAAAASAATASNVFGAVGQVNLEQYAAAVASAAAASRPTQSQLDAAAVQFDPFRHLGSATAPAATPVSLNNNSFGLTATTGTATTAQLGGLSKSPTPGDLSSKDSKNVEVPEVIIGAILGPSGRSLVEIQHVSGANVQISKKGIFAPGTRNRIVTITGQPSAIAKAQYLIEQKINEEETKRARQIPLTTVVN
Protein: UPF0674 endoplasmic reticulum membrane protein C2G5.01 (O94280)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein C18B11.08c
- Protein transport protein sec61 subunit beta
- Probable protein transport protein Sec61 subunit gamma
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL39
Sequence:
MINKKLLFLVFALAKGVLADEEDEYEEDYNMNPELENPGMFKHVDWRDFRLEFVILACFFLYVFSFITQKKKNQKIASRWYGSLQSSFRQQFAQYGPGPNSSPIIYDSPTEFSSYLTGRLNVKNVYTTLQLFPRQDLLAYSLNQIVEILLGNVMSSVLPVADRFQFDLTLADQNLKAERFVFAIVHKDCMRILREIRYDLSFTRISSSPYLPETHVLMSENNECSQAIFEIPEFMSSINECIENLEYFIVTDQPSVPPATEKDYVTKPRIEASIRIKKITSLSGLSNATGSALFNSLLLVADSCPKFQWRPEVSKKLTSARKLAFEQVVHASAAKAAKKKVKSSGDISKLSESDQKKRMERERQRKMRRRAKKM
Protein: PAN2-PAN3 deadenylation complex subunit Pan3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) (Q640Q5)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.
Subcellular location: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:18625844}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250|UniProtKB:Q58A45}. Nucleus {ECO:0000250|UniProtKB:Q58A45}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q58A45}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000250|UniProtKB:Q58A45}.
Interaction partners:
- PAN2-PAN3 deadenylation complex catalytic subunit Pan2
- Polyadenylate-binding protein 1
- Trinucleotide repeat-containing gene 6C protein
Sequence:
MNSGGGGGLPPPSAAASPSSSSLAAAVAVAVAASSGVGGVPGGPAAAAGVKLKYCRYYAKDKTCFYGEECQFLHEDPAAGAAPGLGLHSNSVPLALAAAAGAAFPPGALPGGGAGPPAGPKKPELGVPGAATAGGGLDGPRVAIPGMDGGALTDASLTESYFSTSFIGVNGFGSPVETKYPLMQRMTSSSSSPSLLNDSAKPYTGHDLLTSSASSLFNDFGALNISQRRKPRKYRLGMLEERLVPMGSQARKAKNPLGCLADRCESGVPVSMVWWDRVPENNLQTPNPTASEFIPKGGSTSRLSNVSQSNMSAFSQVFSHPSMGSPATAGLAPGMSLSAGSSPLHSPKITPHTSPAPRRRSHTPNPASFMVPPSASTPANNPAPQPPSSGQVIQKETVGGTTYFYTDTTPAPLTGMVFPNYHIYPPTAPHVAYMQPKANAPSFFMADELRQELINRHLITMAQIDQADMPAVPTEVDSYHSLFPLEPLPPPNRIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTKCMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFAYDFHAGGETMMSRHFNDPNSDAYFTKRKWGQHDGPLPRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITSKTRLRVNCVGVFDVLTFDNSQNNNPLALMAQYQQADLISLGKVVLALACNSLAGIQRENLQKAMELVTINYSSDLKNLILYLLTDQNRMRSVNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQVTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQELIAAANGQL
Protein: Transcription repressor OFP6 (Ovate family protein 6) (AtOFP6) (Q3EAL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor that regulates multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription repressor OFP18
- Transcription repressor OFP15
- Transcription repressor OFP16
- Transcription repressor OFP14
- Transcription repressor OFP11
- Transcription repressor OFP12
- Transcription repressor OFP17
- BEL1-like homeodomain protein 1
Sequence:
MATKSKKKILKTVSVVDISCGNCIKPTFASIFNFFSKKPKRPSSTYRHCHSSISSATPSSTPLATASVAVEKDSDDPYLDFRQSMLQMILENQIYSKDELRELLQCFLSLNSHYHHGIIVRAFSEIWEDVSSAAASAVEASPLITRHVSRASRDYYNYY
Protein: AP-3 complex subunit mu (Adaptor protein complex AP-3 subunit mu) (Adaptor protein-3 mu-adaptin) (Adaptor-related protein complex 3 subunit mu) (At-muD-Ad) (Mu3-adaptin) (Protein ZIG SUPPRESSOR 4) (F4I562)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the AP-3 complex, an adaptor-related complex which seems to be clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole. It also functions in maintaining the identity of lytic vacuoles and in regulating the transition between storage and lytic vacuoles.
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit delta
- AP3-complex subunit beta-A
- AP-3 complex subunit sigma
- At1g76620/F14G6_22
- DUF547 domain-containing protein
- Electron transporter
- DUF547 domain-containing protein
- AP-1 complex subunit gamma-1
- AP-4 complex subunit epsilon
- AP-1 complex subunit gamma-2
Sequence:
MLQCIFLISDSGEVMLEKQLTGHRVDRSICAWFWDQYISQGDSFKALPVIASPTHYLFQIVRDGITFLACSQVEMPPLMAIEFLCRVADVLSEYLGGLNEDLIKDNFIIVYELLDEMIDNGFPLTTEPSILKEMIAPPNLVSKMLSVVTGNASNVSDTLPSGAGSCVPWRPTDPKYSSNEVYVDLVEEMDAIVNRDGELVKCEIYGEVQMNSQLTGFPDLTLSFANPSILEDMRFHPCVRYRPWESHQVLSFVPPDGEFKLMSYRVKKLKNTPVYVKPQITSDSGTCRISVLVGIRSDPGKTIESITLSFQLPHCVSSADLSSNHGTVTILSNKTCTWTIGRIPKDKTPCLSGTLALEPGLERLHVFPTFKLGFKIMGIALSGLRIEKLDLQTIPPRLYKGFRAQTRAGEFDVRL
Protein: Large ribosomal subunit protein uL10m (39S ribosomal protein L10, mitochondrial) (L10mt) (MRP-L10) (Q3MHY7)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069, ECO:0000269|PubMed:11551941}.
Interaction partners:
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL4m
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein bL9m
- MRPL41 protein
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL40
Sequence:
MAAAVAGMLRGGLLPQAGRLPTHQFIRYGSKAVTRHRRVMHFERQKLMAVTEYIAPKPVVNPRCLPPPPSPPQEETGLIRLLRREIAAVFRDNRMIAVCQNVAMSAEDKLLMRHQLRKHKILMKVFPNQILKPFLEDSKYQNLLPLFVGHNLLLVSEEPKVKEMVRILKSVPFLPLLGGCIDDTILSRQGFINYSKLPSLALAQGELVGGLTLLTARTHSLLQHHPLQLTALLDQYARQQHEGDPVVPASAQPDPPNPVQDS
Protein: Serine-protein kinase RsbW (EC 2.7.11.1) (Anti-sigma-B factor) (Sigma-B negative effector RsbW) (P17904)
Organism: Bacillus subtilis (strain 168)
Function: Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
Interaction partners:
- Phosphoserine phosphatase RsbX
- Phosphoserine phosphatase RsbU
- Anti-sigma-B factor antagonist
- RNA polymerase sigma-B factor
- Serine/threonine-protein kinase RsbT
- RsbT antagonist protein RsbS
- RsbT co-antagonist protein RsbRA
- Phosphoserine phosphatase RsbP
- RNA polymerase sigma-F factor
- Anti-sigma F factor antagonist
Sequence:
MKNNADYIEMKVPAQPEYVGIIRLTLSGVASRMGYTYDEIEDLKIAVSEACTNAVQHAYKEDKNGEVSIRFGVFEDRLEVIVADEGDSFDFDQKQQDLGPYTPSHTVDQLSEGGLGLYLMETLMDEVRVQNHSGVTVAMTKYLNGERVDHDTTIKNYETN
Protein: Polyadenylate-binding protein (PABP) (E7ERJ7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU362004}.
Interaction partners:
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Protein: Polycomb complex protein BMI-1 (Polycomb group RING finger protein 4) (Q5T8Z2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
YFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRLDRKVNKDKEKSKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKISHQRDGLTNAGELESDSGSDKANSPAGGIPSTSSCLPSPSTPV
Protein: Rhamnosyltransferase 2 (Q9I4K5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable major facilitator superfamily
- 3-
- Rhamnosyltransferase chain B
- HTH-type quorum-sensing regulator RhlR
- ATP-dependent RNA helicase RhlB
- Glucose-1-phosphate thymidylyltransferase
- Acyl-homoserine-lactone synthase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-glucose 4,6-dehydratase
- dTDP-4-dehydrorhamnose reductase
Sequence:
MDRIDMGVLVVLFNPGDDDLEHLGELAAAFPQLRFLAVDNSPHSDPQRNARLRGQGIAVLHHGNRQGIAGAFNQGLDALFRRGVQGVLLLDQDSRPGGAFLAAQWRNLQARNGQACLLGPRIFDRGDRRFLPAIHLDGLTLRQLSLDGLTTPQRTSFLISSGCLLTREAYQRLGHFDEELFIDHVDTEYSLRAQALDVPLYVDPRLVLEHRIGTRKTRRLGGLSLSAMNHAPLRRYYLARNGLLVLRRYARSSPLALLANLPTLTQGLAVLLLERDKLLKLRCLGWGLWDGLRGRGGALETNRPRLLKRLAGPAVASVASGKAKA
Protein: Protein CNGC15c (Cyclic nucleotide-gated ion channel protein 15 c) (A0A072VMJ3)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations. Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors. Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise to sustained Ca(2+) oscillations. May function during fertilization in both female and male gametophytic Ca(2+) signaling.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:27230377}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGFDNPRSERFEDDPEISKIPTTSGVKVKYHIDGTQIPEQSSKKSRKNETRNKFLKTRVLSRVFSEDYERVKKRVLVLDPRGQLIHRWNKIFLVACLVSLFVDPLFFYLPVVREEVCIDIGKTLEVILTVVRSFGDLFYIVQICMKFRTAYVAPSSKVFGRGELVLTYSKIALRYFSKGFWLDFIAALPLPQVLIWIIIPTLRGSTMANTKNVLRFFIIFQYIPRLYLIFPLSSQIVKATGVVTETAWAGAAYNLMLYMLASHILGACWYLLSIERQEACWKSVCNMEKSNCQYGFFNCHSIKDAPRVAWFIASNVTNLCSPNAGFYPFGIYADAMTSKVTSSPFFNKYFYCLWWGLRNLSSLGQGLLTSTFIGEIMVAIVVATLGLVLFALLIGNMQTYLQSITVRLEEWRVKRTDTEQWMHHRQLPPELRESIRKYNQYKWVATRGVEEEDLLKGLPLDLRREIKRHLCLELVRGVPLFDQMDERMLDAICERLKPALCTEGTYLVREGDPVNEMLFIIRGHLDSYTTNGGRDGFFNSCRIGPGDFCGEELLTWALDPRPSVILPSSTRTVKAFSEVEAFALIAEDLKFVASQFRRLHSKQLRHKFRFYSHQWRTWAACFIQAAWRRHKKRKEAAELRAKENLVAASEAENEIAKKYGKGFVVYGTRVARSTRKGVNMHSGTNSGVVSSLQKPTEPDFSDE