wanglab/gogpt-training-data huggingface dataset:
Protein: Transforming acidic coiled-coil-containing protein 1 (Gastric cancer antigen Ga55) (Taxin-1) (O75410)
Organism: Homo sapiens (Human)
Function: Involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways. Might promote the nuclear localization of the receptors. Likely involved in the processes that promote cell division prior to the formation of differentiated tissues.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14767476}. Nucleus {ECO:0000269|PubMed:14767476}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21531210}. Midbody {ECO:0000269|PubMed:21531210}. Note=Nucleus during interphase. Weakly concentrated at centrosomes during mitosis and colocalizes with AURKC at the midbody during cytokinesis. {ECO:0000269|PubMed:21531210}.; SUBCELLULAR LOCATION: [Isoform 5]: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 10]: Cytoplasm {ECO:0000269|PubMed:20078863}.
Interaction partners:
- Cytoskeleton-associated protein 5
- U6 snRNA-associated Sm-like protein LSm7
- Fibroblast growth factor receptor 1
- YEATS domain-containing protein 4
- Centrosomal protein of 120 kDa
- Transforming acidic coiled-coil-containing protein 2
- Aurora kinase A
- Fibroblast growth factor receptor 3
- Spindle and centriole-associated protein 1
- Tudor domain-containing protein 7
Sequence:
MAFSPWQILSPVQWAKWTWSAVRGGAAGEDEAGGPEGDPEEEDSQAETKSLSFSSDSEGNFETPEAETPIRSPFKESCDPSLGLAGPGAKSQESQEADEQLVAEVVEKCSSKTCSKPSENEVPQQAIDSHSVKNFREEPEHDFSKISIVRPFSIETKDSTDISAVLGTKAAHGCVTAVSGKALPSSPPDALQDEAMTEGSMGVTLEASAEADLKAGNSCPELVPSRRSKLRKPKPVPLRKKAIGGEFSDTNAAVEGTPLPKASYHFSPEELDENTSPLLGDARFQKSPPDLKETPGTLSSDTNDSGVELGEESRSSPLKLEFDFTEDTGNIEARKALPRKLGRKLGSTLTPKIQKDGISKSAGLEQPTDPVARDGPLSQTSSKPDPSQWESPSFNPFGSHSVLQNSPPLSSEGSYHFDPDNFDESMDPFKPTTTLTSSDFCSPTGNHVNEILESPKKAKSRLITSGCKVKKHETQSLALDACSRDEGAVISQISDISNRDGHATDEEKLASTSCGQKSAGAEVKGEPEEDLEYFECSNVPVSTINHAFSSSEAGIEKETCQKMEEDGSTVLGLLESSAEKAPVSVSCGGESPLDGICLSESDKTAVLTLIREEIITKEIEANEWKKKYEETRQEVLEMRKIVAEYEKTIAQMIEDEQRTSMTSQKSFQQLTMEKEQALADLNSVERSLSDLFRRYENLKGVLEGFKKNEEALKKCAQDYLARVKQEEQRYQALKIHAEEKLDKANEEIAQVRTKAKAESAALHAGLRKEQMKVESLERALQQKNQEIEELTKICDELIAKLGKTD
Protein: Transcription factor MYB39 (Myb-related protein 39) (AtMYB39) (Q8GWP0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
Sequence:
MGRSPCCDQDKGVKKGPWLPEEDDKLTAYINENGYGNWRSLPKLAGLNRCGKSCRLRWMNYLRPDIRRGKFSDGEESTIVRLHALLGNKWSKIAGHLPGRTDNEIKNYWNTHMRKKLLQMGIDPVTHEPRTNDLSPILDVSQMLAAAINNGQFGNNNLLNNNTALEDILKLQLIHKMLQIITPKAIPNISSFKTNLLNPKPEPVVNSFNTNSVNPKPDPPAGLFINQSGITPEAASDFIPSYENVWDGFEDNQLPGLVTVSQESLNTAKPGTSTTTKVNDHIRTGMMPCYYGDQLLETPSTGSVSVSPETTSLNHPSTAQHSSGSDFLEDWEKFLDDETSDSCWKSFLDLTSPTSSPVPW
Protein: SID1 transmembrane family member 1 (Q6AXF6)
Organism: Mus musculus (Mouse)
Function: In vitro binds long double-stranded RNA (dsRNA) (500 and 700 base pairs), but not dsRNA shorter than 300 bp. Not involved in RNA autophagy, a process in which RNA is directly imported into lysosomes in an ATP-dependent manner, and degraded.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLDCLRLALLCALPWLLRAAVPGHQEEPLAKSAELRRDPRDPARGADFDRVYSGVVSLSTENIYSFNHTSHPGQVTAVRVHVNSSSDNLDYPVLVVVRQQKEVLSWQVPLLFQGLYQRSYNYQEVSRTLCPSKATNETGPLEQLIFVDVASMAPHGAHYKLLVTKIKHFQLPTNVAFYFTASPSQPQYFLYKFPEDVDSVIIKVVSEKAYPCSVVSVQNIMCPVYDLDHNVEFNGVYQSMTKKAAITLQKKDFPDEQFFVVFVIKPEDYACGGSFSIQENENQTWNLQRSKNLKVTIVPSIKESVYVKSSLFSIFVFLSFYLGCLLVVLVHHVRFQRKSIDGSFGSSDGSGNMAVSHPITASTPEGSNYGAIDESSSSPGRQMSSSDGGQPCHSDTDSSVEESDFDTMPDIESDKNVIRTKMFLYLSDLSRKDRRIVSKKYKIYFWNIITIAVFYALPVMQLVITYQTVVNVTGNQDICYYNFLCAHPLGVLSAFNNILSNLGHVLLGFLFLLIVLRRDLLHRRALEAKDIFAMEYGIPKHFGLFYAMGIALMMEGVLSACYHVCPNYSNFQFDTSFMYMIAGLCMLKLYQTRHPDINASAYSAYASFAVVITLTVLGVVFGKNDVWFWIIFSAIHILSSLALSTQIYYMGRFKIDLGIFRRAAMVFYTDCIQQCSRPLYMDRMVLLIVGNLVNWSFAFFGLIYRPRDFASYMLGIFICNLLLYLAFYIIMKLRSSEKVLPLPVFCIAATAVVWAAALYFFFQNLSSWEGTPAESREKNRECVLLDFFDDHDIWHFLSATALFFSFLVLLTLDDDLDVVRRDQIPVF
Protein: Nucleolus and neural progenitor protein (Neural progenitor protein) (Q8R2U2)
Organism: Mus musculus (Mouse)
Function: May play a role in cortex development as part of the Notch signaling pathway. Downstream of Notch may repress the expression of proneural genes and inhibit neuronal differentiation thereby maintaining neural progenitors. May also play a role in preimplentation embryo development.
Subcellular location: Nucleus {ECO:0000269|PubMed:19906856}. Nucleus, nucleolus {ECO:0000269|PubMed:26178919}.
Interaction partners:
Sequence:
MAAAVRPGAEPWNRVRIPQAGNCSTLTVRDPSATLDICTAAVTKGCHLVTQSLKSQTLDAEVDVLCSVLYSNHNRLGHHKPHLALRQVEQCLKRLKHMNLEGSIEDLSQLLSANATQPGATENRVVPSQPVVEVVLMKVLGGCKLLLRLLDCCCKAFLLTVKHLGLKEFIILNLVMVGLVSRLWVLHKGLLRRLISLYEPLLSLRQEISSIHPMPYFKDFAFPSDITDFLGPSYLEVFKVKTPAASATKGVTKLLNKLFLMREQLPKMNEDTLDRLSKPSEQMTSNPQSTVDLGQPVKACKRTRKEKPLGFDLRAFCTRLGNKATQETNRDFKYSQSKLKTTKLPSQQLRTHWANDTVQRIRKTKTFAQLSEEIEMAIVWSRSKKLKTQATFLGNKLLKSNRFRHVESQGYSLTKKLQCMKTSLCNCLLRGSRTSTSEHPPRQRRSKYKVLSRQRKPQRKLQSTLLKETQQVPEGTLKNTRDSSAKRRCSGTVQRSDVCPNGKQVLRKLAKPDLKTKVVVHGNLTGGSRNESGFQAKTQMHTHNAPDTAKEADDIDDIFALMGV
Protein: Zinc finger and BTB domain-containing protein 38 (Zinc finger protein expressed in neurons) (Zenon) (Q5EXX3)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional regulator with bimodal DNA-binding specificity. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to E-box elements (5'-CACGTG-3'). Can also bind specifically to a single methyl-CpG pair. Represses transcription in a methyl-CpG-dependent manner. Plays an important role in regulating DNA-replication and common fragile sites (CFS) stability in a RBBP6- and MCM10-dependent manner; represses expression of MCM10 which plays an important role in DNA-replication (By similarity). Acts as a transcriptional activator. May be involved in the differentiation and/or survival of late postmitotic neurons.
Subcellular location: Nucleus {ECO:0000269|PubMed:15713629}. Chromosome {ECO:0000250|UniProtKB:Q8NAP3}. Note=Localizes to chromocenters. {ECO:0000250|UniProtKB:Q8NAP3}.
Interaction partners:
Sequence:
MTVMSLSRDLKDDFHSDTVLSILNEQRIRGILCDVTIIVEDTKFKAHSNVLAASSLYFKNIFWSHTICISSHVLELDDLKAEVFTEILNYIYSSTVVVRRQETVTDLAAAGKRLGISFLEDLSDRNFSNSPGPYVVCITEKGVVKEEKNEKRHEEPAVTNGPRITNAFSIIETENSNSMFSPLDLRASFKKVSDAMRTTSLCQERASVCPEAEPVRTLAEHSYAVSSITEAYRSQPLREHDSSSSSGKTGKENGEALTTKAKPCRKPKTQTQDSDSTTENMPLPLVTCPEVNQERSPQPAPILSHSEPPSSEGDVHFPREDENQPSETPGPPAAEVPPLVYNCSCCSKSFDSSTLLGAHMQLHKPTQDPFVCKYCNKQFTTLNRLDRHEQICMRSSHMPMPGGNQPFLENYPTIGQDGGSFTSPDSLVPESRIGELSSAGSALSDADHMVKFVNGQMLYSCVVCKRSYVTLSSLRRHANVHSWRRTYPCHYCNKVFALAEYRTRHEIWHTGERRYQCIFCLETFMTYYILKNHQKSFHAIDHRLSISKKTANGGLKPTVYPYKLYRLLPMRCKRAPYKSYRNSSYESAQGNRQRNESPPDTFVIPNLPSSEMPTLNFQDGRNSLTSSPAIPVETPSWQGTPTSAKVKNAEGLKWRKQALKTDLVDSAEVSISSIGNSVSTTLQAEPVCVSSGEHSASVISYSGLVPSVIVHSSQFSSVIKHSNAIACLANSNHQSPSQPVASPSLIKDSKPEADKASKLASRPKNSKEKKKTVPCNRGEITEEAKYVADLGGSSGKTTNVVEETSKIETYIAKPALPGTSTNSNVAPLCQITVKIGNEAIVKRHILGSKLFYKRGRKPKYQMQEETLPRESDPETRGDSPLGLCQADCVEMSEAFDEVSDQDSTDKPWRPYYNYKPKKKSKQLRKIRKVKWRKERGSRSPVGRRRYPAELDRAEMGRRRYPAELDRCAEVKLPPDKASEEEENKEMPKLQCELCDGDKAAGAGAEGKPHQHLTLKPYICELCAKQFQSSSTLKMHMRCHTGEKPYQCKTCGRRFSVQGNLQKHERIHLGVKEFICQYCNKAFTLNETLKIHERIHTGEKRYHCQFCFQGFLYLSTKRNHERRHVREHDGKGFACFQCPKICKTAAALRMHQKKHLFKTLTKQEETDDLCHENSDLLESQPCTDSEDSDQKDDIKKPLLKMSFE
Protein: Elongation factor P (EF-P) (P0A6N4)
Organism: Escherichia coli (strain K12)
Function: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS2
Sequence:
MATYYSNDFRAGLKIMLDGEPYAVEASEFVKPGKGQAFARVKLRRLLTGTRVEKTFKSTDSAEGADVVDMNLTYLYNDGEFWHFMNNETFEQLSADAKAIGDNAKWLLDQAECIVTLWNGQPISVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK
Protein: Major royal jelly protein 3 (MRJP-3) (Apalbumin 3) (Bee-milk protein) (Royal jelly protein RJP57-1) (RJP-1) (Q17060)
Organism: Apis mellifera (Honeybee)
Function: Secreted RNA-binding protein required to concentrate, stabilize and enhance environmental RNA bioavailability in the honeybee royal jelly. Acts as a RNA-aggregating protein: binds 18 nucleotides and longer single- and double-stranded RNA (ssRNA and dsRNA, respectively) in a non-specific manner. RNA-binding drives super-order assembly of oligomers into extracellular ribonucleoprotein granules that concentrate, protect and enhance RNA uptake granules, facilitating RNA transfer among bees.
Subcellular location: Secreted {ECO:0000269|PubMed:14709007, ECO:0000269|PubMed:15607658, ECO:0000269|PubMed:15693061, ECO:0000269|PubMed:31410279, ECO:0000269|PubMed:9791542}. Note=Incorporated into royal jelly. {ECO:0000269|PubMed:14709007, ECO:0000269|PubMed:15607658, ECO:0000269|PubMed:15693061, ECO:0000269|PubMed:31410279}.
Interaction partners:
Sequence:
MTKWLLLVVCLGIACQDVTSAAVNHQRKSANNLAHSMKVIYEWKHIDFDFGSDERRDAAIKSGEFDHTKNYPFDVDRWRDKTFVTIERNNGVPSSLNVVTNKKGKGGPLLRPYPDWSFAKYEDCSGIVSAFKIAVDKFDRLWVLDSGLVNNNQPMCSPKLLTFDLKTSKLVKQVEIPHNIAVNATTGMGELVSLAVQAIDRTNTMVYIADEKGEGLIMYQNSDDSFHRLTSNTFDYDPRYTKLTVAGESFTVKNGIYGIALSPVTNNLYYSPLLSHGLYYVDTEQFSNPQYEENNVQYEGSQDILNTQSFGKVVSKNGVLFLGLVGNSGIACVNEHQVLQRESFDVVAQNEETLQMIVSMKIMENLPQSGRINDPEGNEYMLALSNRMQKIINNDFNFNDVNFRILGANVDDLMRNTRCGRYHNQNAGNQNADNQNADNQNANNQNADNQNANKQNGNRQNDNRQNDNKQNGNRQNDNKQNGNRQNDNKQNGNRQNGNKQNDNKQNGNRQNDNKRNGNRQNDNQNNQNDNNRNDNQVHHSSKLH
Protein: Phospholipase DDHD1 (EC 3.1.1.111) (EC 3.1.1.32) (DDHD domain-containing protein 1) (Phosphatidic acid-preferring phospholipase A1 homolog) (PA-PLA1) (EC 3.1.1.118) (Phospholipid sn-1 acylhydrolase) (Q8NEL9)
Organism: Homo sapiens (Human)
Function: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid. Prefers phosphatidate (1,2-diacyl-sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol), PG) (By similarity). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system. Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (By similarity). Regulates mitochondrial morphology. These dynamic changes may be due to PA hydrolysis at the mitochondrial surface. May play a regulatory role in spermatogenesis or sperm function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15623529}.
Interaction partners:
- Triacylglycerol hydrolase DDHD2
Sequence:
MNYPGRGSPRSPEHNGRGGGGGAWELGSDARPAFGGGVCCFEHLPGGDPDDGDVPLALLRGEPGLHLAPGTDDHNHHLALDPCLSDENYDFSSAESGSSLRYYSEGESGGGGSSLSLHPPQQPPLVPTNSGGGGATGGSPGERKRTRLGGPAARHRYEVVTELGPEEVRWFYKEDKKTWKPFIGYDSLRIELAFRTLLQTTGARPQGGDRDGDHVCSPTGPASSSGEDDDEDRACGFCQSTTGHEPEMVELVNIEPVCVRGGLYEVDVTQGECYPVYWNQADKIPVMRGQWFIDGTWQPLEEEESNLIEQEHLNCFRGQQMQENFDIEVSKSIDGKDAVHSFKLSRNHVDWHSVDEVYLYSDATTSKIARTVTQKLGFSKASSSGTRLHRGYVEEATLEDKPSQTTHIVFVVHGIGQKMDQGRIIKNTAMMREAARKIEERHFSNHATHVEFLPVEWRSKLTLDGDTVDSITPDKVRGLRDMLNSSAMDIMYYTSPLYRDELVKGLQQELNRLYSLFCSRNPDFEEKGGKVSIVSHSLGCVITYDIMTGWNPVRLYEQLLQKEEELPDERWMSYEERHLLDELYITKRRLKEIEERLHGLKASSMTQTPALKFKVENFFCMGSPLAVFLALRGIRPGNTGSQDHILPREICNRLLNIFHPTDPVAYRLEPLILKHYSNISPVQIHWYNTSNPLPYEHMKPSFLNPAKEPTSVSENEGISTIPSPVTSPVLSRRHYGESITNIGKASILGAASIGKGLGGMLFSRFGRSSTTQSSETSKDSMEDEKKPVASPSATTVGTQTLPHSSSGFLDSAYFRLQESFFNLPQLLFPENVMQNKDNALVELDHRIDFELREGLVESRYWSAVTSHTAYWSSLDVALFLLTFMYKHEHDDDAKPNLDPI
Protein: Transcription factor 7 like 2 (D3Z9D1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Catenin beta-1
- Serine/threonine-protein kinase NLK
- Axin-2
- Junction plakoglobin
- Transcription factor 7 like 2
- Histone lysine acetyltransferase CREBBP
- histone acetyltransferase
- SRY-box transcription factor 17
- C-terminal-binding protein 1
- C-terminal-binding protein 2
Sequence:
MPQLNGGGGDDLGANDELISFKDEGEQEEKNSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPHLLGSPPQDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEAAHGKASALCPNGALDLPPATLQPSMVPSSSLAQPSTSSLHSHNSLAGTQPQPLSLVTKSLE
Protein: Sterile alpha motif domain-containing protein 3 (SAM domain-containing protein 3) (Q8N6K7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METWSVEQVCSWLVEKNLGELVHRFQEEEVSGAALLALNDRMVQQLVKKIGHQAVLMDLIKKYKQNTQGLKSPENPKKAALVMQTEAARDYRDEESSSPARHGEQMPSFYPAENLDNGLIDQRVLKQRRNVKQILARSKALQWTKSYVLPEFPYDVKCMLAEQKCPDHSMRIRIIEFLQADMTKYLEGSLYPSTQQYNDVVNALLQAHPFLDEDGCGFFLWKRALKDRFKYVRRPIEDDEQVIRNKCKFGHRRGQTRKSLADIRFDEIKLVQIKEEAVCFDSELDEHIKWFQQEYVKTEKDWREIDKRMSQTLEIRRKMIGSRTPLKDILKLFPFLKCPYQMFREFQLLTRTDIYKKTRHILESYSENILTSFSVVDNPINIVLQEKMKHYTDEDMLKYMKMTATCLLLPDVFGDDPSLFVIMNEQVQVSTPVLEVKNPFNMEVCEFSLYLERERLTKVDDCVTALAALVAAFHVFRIECPRRLSQTFNFLETLIFDMHSPYFPSLKEKENEVGFQHPLT
Protein: dTDP-fucosamine acetyltransferase (EC 2.3.1.210) (TDP-fucosamine acetyltransferase) (dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase) (P27832)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA).
Interaction partners:
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- Glucose-1-phosphate thymidylyltransferase 2
- Lipid III flippase
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
- dTDP-glucose 4,6-dehydratase 2
- UDP-N-acetylglucosamine 2-epimerase
- UDP-N-acetyl-D-mannosaminuronic acid transferase
- Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- Probable ECA polymerase
Sequence:
MPVRASIEPLTWENAFFGVNSAIVRITSEAPLLTPDALAPWSRVQAKIAASNTGELDALQQLGFSLVEGEVDLALPVNNASDSGAVVAQETDIPALRQLASAAFAQSRFRAPWYAPDASSRFYAQWIENAVRGTFDHQCLILRAASGDIRGYVSLRELNATDARIGLLAGRGAGAELMQTALNWAYARGKTTLRVATQMGNTAALKRYIQSGANVESTAYWLYR
Protein: PAN2-PAN3 deadenylation complex catalytic subunit PAN2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2) (A1Z7K9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic 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.
Subcellular location: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03182}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03182}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_03182}.
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit PAN3
- Polyadenylate-binding protein
- Protein Gawky
- poly
- 5'-3' exoribonuclease 1
- poly
- Not1, isoform H
- GH03795p
- Protein painting of fourth
Sequence:
MDYVYCGTDPIGASEDILSVYDAGSAPGNGHFSPSFNGFNIGTTDPEYVELVPVLADGGEHFGVSSVAFDDYEELLWMGNQGGHVTSYYTNSMQKYTSFQVHATDIVRDISTLDSGVLALTQTSLRHQIRRGLPKFTFKSNNMKEMVSMLQLSPHRLVMAGLQDELIDFDLRTLKETRIEHVGAGGCTVLRKNSRYLFAGDQLGTVTLRDLNSLSVQHTIKTHTNILSDFSVQGNLLISCGYSGRQNNLAIDRFLMVYDLRMLRLIAPIQVMIDPQMLKFLPSLTSQLAVVSSYGQVQLVDTVELSEPRVSMYQINTNGSQCLSFDISSSSQAMAFGDQSGHINMIAAVQTPQPQFNLYSRSTEFADVVPQLPMVSITDTNFPLSSVMLPHLTTGTQWFSDWPEELLRYRYHRPKTIDPEVLSNMKMQGPIGYSPNPRTARRNQIPYVIEQGGVCSPNGNGTAAATKAENGVKIIPRRYRKVELKYTKLGTQDFDFDQHNQTCFAGLEATLPNSYCNAMLQILYFTDALRVKLLEHSCIKEFCLSCELGFLFNMLDKSTASSPCQASNFLRSFRTVPEASALGLILTDRSSNVNLISLIQNWNRFILHQMHYEIFDSSKNASTYSGSVQTSTNAENAGSSETSGSSDLYDSISDENSKEDDRERSKINAETDISKIFGTKQICINRCIKCQEEKIKESILLACNLSYPNHIKDSDQYFNFGTILKRSLSSEKSIQAFCERCKKFSPTNQSVKVTSLPQILSINCGLNNEKDITFLKRQLNRCSEKTTVDAAASLSTSKPCRYGANCSRSDCHFMHPDRKSPSHTSQPNAVNNSPNGRQKSWFPLTFTMGINDQGEVQVQTQSDASSGKSEQEEETEKPPTKGLDNNRMYALHAVVCQVDDGTQKNLVSLINVQRPYHTMKLAESADDPQSQWYIFNDFSISPVSPQESVWFTLDWKVPCILFYRHVEDDSESASTTSSTVTESEETIPSESSSGSPTNLSNPFLEEIVSPMLGNLSADATLQPLQSDEMPQSGDLVAMDAEFVTLNPEENEIRPDGKTATIKPCHMSVARISCIRGQGPAEGVPFMDDYISTQEKVVDYLTQFSGIKPGDLDANFSKKRLTALKYSYQKLKYLVDVGVIFVGHGLKNDFRVINIYVPSEQIIDTVHLFHMPHHRMVSLRFLAWHFLGTKIQSETHDSIEDARTTLQLYKHYLKLQEEKKFANALKNLYERGKQLQWKVPED
Protein: DShc protein (FI07258p) (SHC-adaptor protein) (Q9V3C8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein son of sevenless
- Epidermal growth factor receptor
- Growth factor receptor-bound protein 2
- Tyrosine-protein kinase
- Tyrosine-protein kinase receptor torso
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Adapter molecule Crk
- Tie-like receptor tyrosine kinase
- Insulin-like receptor
- RAC serine/threonine-protein kinase
Sequence:
MPKNGDAGNRSGSGTTSDGCIYPDDVIMGVGVAFNVRYTGCVEVKTSMKSLDFETRTQLARECINRVCEAAGLKSAGKRRLTNFISDRPSMQHAGTNIIINVSSRALSLSNVETGEVIANHNMPRISFASGGDNDTLDFLAYIAKNEDEWRACYVLECAGGQSEDLIVTIGKAFALRFNALSRLNDPSADCNINQSCKENVKEYYNDLPNKLPPEVPEPQQQQVQQPLHPHAPRVAQLNLKKPRDRLSSNLIDLNSPPPDQTTNKLGHFDPLQATTAANSVLPSVRDVFDGPQCPLTAEVWFHAGISRPISERLLQQDGDFLVRESQGKRGQYVLTGLEGKTPKHLLLIDPEGVVRTKDRIFDSISHLINYHWAHALPIISEDSELVLRNPVRRPQQDQAASPITSASS
Protein: General transcription factor 3C polypeptide 5 (TF3C-epsilon) (Transcription factor IIIC 63 kDa subunit) (TFIIIC 63 kDa subunit) (TFIIIC63) (Transcription factor IIIC subunit epsilon) (Q9Y5Q8)
Organism: Homo sapiens (Human)
Function: Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters.
Subcellular location: Nucleus.
Interaction partners:
- General transcription factor 3C polypeptide 4
- General transcription factor 3C polypeptide 3
- General transcription factor 3C polypeptide 1
- General transcription factor 3C polypeptide 6
- General transcription factor 3C polypeptide 2
- Transcription factor IIIB 90 kDa subunit
- Transcription factor TFIIIB component B'' homolog
- Transcription factor IIIB 50 kDa subunit
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC1
Sequence:
MAAEAADLGLGAAVPVELRRERRMVCVEYPGVVRDVAKMLPTLGGEEGVSRIYADPTKRLELYFRPKDPYCHPVCANRFSTSSLLLRIRKRTRRQKGVLGTEAHSEVTFDMEILGIISTIYKFQGMSDFQYLAVHTEAGGKHTSMYDKVLMLRPEKEAFFHQELPLYIPPPIFSRLDAPVDYFYRPETQHREGYNNPPISGENLIGLSRARRPHNAIFVNFEDEEVPKQPLEAAAQTWRRVCTNPVDRKVEEELRKLFDIRPIWSRNAVKANISVHPDKLKVLLPFIAYYMITGPWRSLWIRFGYDPRKNPDAKIYQVLDFRIRCGMKHGYAPSDLPVKAKRSTYNYSLPITVKKTSSQLVTMHDLKQGLGPSGTSGARKPASSKYKLKDSVYIFREGALPPYRQMFYQLCDLNVEELQKIIHRNDGAENSCTERDGWCLPKTSDELRDTMSLMIRQTIRSKRPALFSSSAKADGGKEQLTYESGEDEEDEEEEEEEEEDFKPSDGSENEMETEILDYV
Protein: Gap junction protein (B3DHR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
- Tight junction protein 1a
- Neurobeachin b.
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Cyclin-dependent kinase 1
- Tight junction protein 1b
- Neurobeachin
Sequence:
MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVGIVGEKVYEDEQIMFICNTLQPGCNQACYDKAFPISHIRYWVFQIILVCTPSLCFITYSVHQSAKHKDQRYTLLHGPYIDHGHGPSRKLRNINGILVHPESKDDRECLDLKDIPNIPAGVTYSKSAKIRQQEGISRFYVIQVVFRNVLEIGFLAGQYFLYGFNVPAMFECDRYPCVKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKTAIRGVQARRKSICEIRKKDVSHLSSVPNLGRTQSSESAYV
Protein: F-actin-capping protein subunit beta (P34686)
Organism: Caenorhabditis elegans
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A9XFX6}.
Interaction partners:
- F-actin-capping protein subunit alpha
- Probable dynactin subunit 2
- Actin-related protein 10
- Actin
- Dynactin subunit 4
- Dynactin subunit 6
- Dynactin subunit 1
- Dynactin subunit 5
- Twinfilin
- CARMIL pleckstrin homology domain-containing protein
Sequence:
MGEQQLDCALDLMRRLPPQHCDKNLTDLIDLCPHLVDDLLSTIDQPLKIAADRETGKQYLLCDYNRDGDSYRSPWSNTYDPPLEDGQLPSEKRRKMEIEANAAFESYRDLYFEGGVSSVYFWDLDNGGFAGIVLIKKEGDGAKNITGCWDSIHVIEITERARQAHYKLTSTIMLWLQTNKSSSGVMNLGGSLTRQHEMDAPINDQNTHLANMGRMIEDQESKMRLTINEIYFGKTKKVMSDLRSTEKQSELEKQDEIVRELNNAMANRGN
Protein: Neuroepithelial cell transforming gene 1 (Neuroepithelial cell-transforming gene 1 protein) (Q5RKM4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVAYDEPCVVPIKRTLQKIDYQNQAYKELEEPCTKRVRPLGRVTSLANLISPVKNGAVRRFGQTLQASFRGDGRSPGVPQQKPCSKAAAPTPPKRRNSTLWSETLDVHQKGTFSTKEIKRQEAIFELSRGEQDLIEDLKLARKAYHDPMLKLSIMSEEELTAIFGDLDAYIPLHEDLLDQLAKATGTDGTVRQIGKIVVDWLPRLNAYRAYCSNQLAAKALLDQKKQDPRVQDFLQRCLESPFSRKLDLWSFLDIPRSRLVKYPLLLKEILRHTPPDHPDKGSLEQAISVIQAVLADINMKKGESECQYYIDKLEYLEDKQKDPRIEQCKSLLCHGELRNKSGTKLHVFLFTEVLILTRPVTRNDRHCFQVYRQPIPVQDLVLEDLQDGDVRMGGSFRGAFSNADKAKNIFRVRFQDASQGQSHTLQVNDVFHKQQWLNCLRNAMSTQKDLTLSENEPLTTPATDVCAKRRSSSVSTVIQMDEMDENCPRAAASAPSSPSSEEHPSPTPSATSTLSSSSSSSSISAPIPSRKSKKDKRSLCPLGKRKETMV