wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein zfs1 (Multicopy suppressor of overexpressed cyr1 protein 4) (P47979)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Binds to specific AU-rich elements (ARE) in the 3'-untranslated region of target mRNAs and promotes their degradation. Binds to ARE present in the arz1 mRNA and stimulates the rate of arz1 mRNA decay. Required for coordination of septum formation with exit from mitosis. Involved in the mating response pathway. Induces sexual development and ascus formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:8534915}.
Interaction partners:
- GTPase-GDP dissociation stimulator arz1
- Transcription factor cbf12
- General negative regulator of transcription subunit 1
- Ribosomal RNA small subunit methyltransferase mra1
- Exosome complex component rrp43
Sequence:
MVYSPMSRPQVPLAFRQWPPYNYKSDPLVNSKLSQSTTSVNAGPSLISPSFLDSYANSSSLLHKPSTNLGSLKTSSLLASDEVFPSSVMPQLRPLDSSLSVSPEMDGWPWHHNSSSNPQGYAWTPSLLSSNATSYLHSGSSPHGNTSNHPSPISSLESLPSRSSTGSGSLDFSGLANLHDDSKSLAMSLNMAGVPVSVDENSQTSFPFVHGQPESTMSRKPKLCVQSKSMTNIRNSVAKPSLVRQSHSAGVIPIKPTASNASIRNAPSNLSKQFSPSGNSPLTEASKPFVPQPSAAGDFRQAKGSASHPHGSGSSNGVAPNGKRALYKTEPCKNWQISGTCRYGSKCQFAHGNQELKEPPRHPKYKSERCRSFMMYGYCPYGLRCCFLHDESNAQKSATIKQSP
Protein: Doublecortin domain-containing protein (Q385Q5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVELTVYEGHDVFLQNAVRLHIPCKVDTIEGLLSLVGRAVASSPGGPSAARRYRFVYSLDGSPLRSVDECLEVGTVIVSCTPGFQKRKHHVESPSNPVLDLLNRKGYETYSAAESRGLSATPPSHDGFVPISFQQHSVSRASPKYVFCDSNPGPIPNFSSIGGASVEWGGVSCRVGDERIVLPPTPSFDVPFPDMNLDISHAERVAAVKTLITLKLCGRSFLNDELLFEKELEEVFRPIVAEQASCPSWRDQTLDRPPPHVVVDGPPKSGVSTSLAYYSSMLVSSAASRYATFLILPLNFELLFDGSLGISSYSANRHLRGSKSANYNDARTQSLLLDVPFFYMTVVRALIDSVVAQRPSVRNCSTALVEMWEQLIKTTAGSGVRLNTCEVAHAVGHSALYRWETFAAPASQILRAAKLNPRDMKLRDAVLELVLVELVAQVASALHFSGVVYVVDGLRPLARSLCDRLRRPGGDAAVFLDRVAQRSWVHLAVGVDSLSTQVLESALLTRVRRVKLLRMLSVEYVTKMYGFPKAIHCGSNKYPLEMFLGTPGYLRMVHDLLRSCEGRKAHKGDSDGYAVRIEDLDVSNALLEFEAVRKLGQDTQKEMWSLS
Protein: Solute carrier family 13 member 1 (NaSi-1) (Renal sodium/sulfate cotransporter) (Na(+)/sulfate cotransporter) (Q07782)
Organism: Rattus norvegicus (Rat)
Function: Sodium:sulfate symporter that mediates sulfate reabsorption in the kidney and small intestine. Can also mediate the transport of selenate and thiosulfate.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:8765995}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sulfate transporter
Sequence:
MKLLNYAFVYRRFLLVVFTVLVLLPLPLIIRSKEAECAYILFVIATFWITEALPLSITALLPGLMFPMFGIMSSTHVASAYFKDFHLLLIGVICLATSIEKWNLHKRIALRMVMMVGVNPAWLTLGFMSSTAFLSMWLSNTSTAAMVMPIVEAVAQQITSAEAEAEATQMTYFNESAAQGLEVDETIIGQETNERKEKTKPALGSSNDKGKVSSKMETEKNTVTGAKYRSKKDHMMCKLMCLCIAYSSTIGGLTTITGTSTNLIFSEHFNTRYPDCRCLNFGSWFLFSFPVAVILLLLSWIWLQWLFLGFNFKEMFKCGKTKTLKEKACAEVIKQEYEKLGPMRYQEIVTLVIFIVMALLWFSRDPGFVTGWSVLFSEYPGYVTDSTVALVAGILFFLIPAKKLTKMTSTGDIIAFDYSPLITWKEFQSFMPWDIAILVGGGFALADGCQVSGLSSWIGSKLSPLGSLPVWLIILISSLIVTSLTEVASNPATITILFPILSPLAEAIHVNPLHILLPSTLCTSFAFLLPVANPPNAIVFSYGHLKVIDMVKAGLGVNILGVAVVMLGMFTWIEPMFNLHEYPSWAPDIVNQTMP
Protein: 14-3-3 protein epsilon (Suppressor of Ras1 3-9) (P92177)
Organism: Drosophila melanogaster (Fruit fly)
Function: Positively regulates Ras-mediated pathways. Acts downstream or parallel to Raf, but upstream of nuclear factors in Ras signaling. Three mutants have been isolated, that suppress the rough eye phenotype caused by mutated Ras1 (sev-Ras1 v12). Inhibits yki activity by restricting its nuclear localization. Together with pav, has a role in the inhibition of microtubule sliding during neurite outgrowth.
Interaction partners:
- 14-3-3 protein zeta
- Raf homolog serine/threonine-protein kinase Raf
- Transcriptional coactivator yorkie
- MAP/microtubule affinity-regulating kinase 3
- non-specific serine/threonine protein kinase
- Gigas, isoform A
- AT08303p
- Forkhead box protein O
- Ras-like protein 1
- M-phase inducer phosphatase
Sequence:
MTERENNVYKAKLAEQAERYDEMVEAMKKVASMDVELTVEERNLLSVAYKNVIGARRASWRIITSIEQKEENKGAEEKLEMIKTYRGQVEKELRDICSDILNVLEKHLIPCATSGESKVFYYKMKGDYHRYLAEFATGSDRKDAAENSLIAYKAASDIAMNDLPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQAEEVDPNAGDGEPKEQIQDVEDQDVS
Protein: Homoserine dehydrogenase (HDH) (HSD) (EC 1.1.1.3) (Q5B998)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in osmoadaptation.
Interaction partners:
- Aspartokinase
- Aspartate-semialdehyde dehydrogenase
- Homoserine kinase
- Threonine synthase
- Histidine biosynthesis trifunctional protein
- Histidinol dehydrogenase
- Homoserine O-acetyltransferase
- Homocysteine S-methyltransferase
- Cystathionine beta-lyase
- ACT domain-containing protein
Sequence:
MSAPIYLGVIGVGGVGTAFLNQLARLPNAPKLILLARSSQTLLSPTPSYSPTIPAAEWKTAVETPSLTKSGALTPDEIATYLASAPGRSILVDNTSDPALASNYPVFLRKGISVVTPNKKGFSSDLSLWKEIFAAAAEGKALVYHESTVGAGLPVISTLKDLVNTGDEVTRIEGVFSGTLSFLFNTFAPASGSSSAKWSEVVSQAKELGYTEPDPRDDLNGMDVARKLTILARIAGLDVQSPDSFPIESLIPAELTSLPSSADGIAQFMARLPEFDSQMAAIKEGAEKAGKVVRYVGSVDVAKKEVRVGLQQFDKDSAIAGLKGSDNIISFYTRRYGSNPLIVQGAGAGGDVTAMGVTADLLKVIERL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I6GLD8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASDSPARSLDEIDLSALRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHGQRPATEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKRGEKDETEYEYSGSEEEEEENDSGEPSSILNLPGESTLRRDFLRLQLANKERSEALRRQQLEQQQRENEEHKRQLLAERQKRIEEQKEQRRRLEEQQRREKELRKQQEREQRRHYEEQMRREEERRRAEHEQEYIRRQLEEEQRQLEILQQQLLHEQALLLEYKRKQLEEQRQAERLQRQLKQERDYLVSLQHQRQEQRPLEKKPLYHYKEGMSPSEKPAWAKEVEERSRLNRQSSPAMPHKVANRISDPNLPPRSESFSISGVQPARTPPMLRPVDPQIPQLVAVKSQGPALTASQSVHEQPTKGLSGFQEALNVTSHRVEMPRQNSDPTSENPPLPTRIEKFDRSSWLRQEEDIPPKVPQRTTSISPALARKNSPGNGSALGPRLGSQPIRASNPDLRRTEPVLESSLQRTSSGSSSSSSTPSSQPSSQGGSQPGSQAGSSERTRVRANSKSEGSPVLPHEPSKVKPEESRDIPRPSRPADLTALAKELRELRIEETNRPLKKVTDYSSSSEESESSEEEEEDGESETHDGTVAVSDIPRLIPTGAPGKNEQYNMGMVGTHGLETSHADTFGGSISREGTLMIRETAEEKKRSGHSDSNGFAGHINLPDLVQQSHSPAGTPTEGLGRVSTHSQEMDTGAEYGMGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAAALFTSELLRQEQAKLNEARKISVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYNLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGDLEGCIHYKVVKYERIKFLVIALKNAVEIYAWAPKPYHKFMAFKSFADLQHKPLLVDLTVEEGQRLKVIFGSHTGFHVIDVDSGNSYDIYIPSHIQGNITPHAIVILPKTDGMEMLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIHSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVFFMTLNRNSMMNW
Protein: Gem-associated protein 8 (Gemin-8) (Protein FAM51A1) (Q9NWZ8)
Organism: Homo sapiens (Human)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
Subcellular location: Nucleus, gem {ECO:0000269|PubMed:16434402}. Cytoplasm {ECO:0000269|PubMed:16434402}. Note=Found in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
Interaction partners:
- Gem-associated protein 2
- Gem-associated protein 6
- Gem-associated protein 7
- Probable ATP-dependent RNA helicase DDX20
- Gem-associated protein 5
- Serine-threonine kinase receptor-associated protein
- Survival motor neuron protein
- Gem-associated protein 4
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
Sequence:
MAAVKASTSKATRPWYSHPVYARYWQHYHQAMAWMQSHHNAYRKAVESCFNLPWYLPSALLPQSSYDNEAAYPQSFYDHHVAWQDYPCSSSHFRRSGQHPRYSSRIQASTKEDQALSKEEEMETESDAEVECDLSNMEITEELRQYFAETERHREERRRQQQLDAERLDSYVNADHDLYCNTRRSVEAPTERPGERRQAEMKRLYGDSAAKIQAMEAAVQLSFDKHCDRKQPKYWPVIPLKF
Protein: Protein YeeZ (P0AD12)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS19
- Uncharacterized HTH-type transcriptional regulator YeeY
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS13
Sequence:
MKKVAIVGLGWLGMPLAMSLSARGWQVTGSKTTQDGVEAARMSGIDSYLLRMEPELVCDSDDLDALMDADALVITLPARRSGPGDEFYLQAVQELVDSALAHRIPRIIFTSSTSVYGDAQGTVKETTPRNPVTNSGRVLEELEDWLHNLPGTSVDILRLAGLVGPGRHPGRFFAGKTAPDGEHGVNLVHLEDVIGAITLLLQAPKGGHIYNICAPAHPARNVFYPQMARLLGLEPPQFRNSLDSGKGKIIDGSRICNELGFEYQYPDPLVMPLE
Protein: LD47843p (Sarcolemma associated protein, isoform A) (Sarcolemma associated protein, isoform D) (Q9W5R5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FGFR1 oncogene partner 2 homolog
- Connector of kinase to AP-1, isoform E
- AT25231p
- CTTNBP2 N-terminal-like protein
- Serine/threonine-protein phosphatase PP2A
- MOB kinase activator-like 4
- Cerebral cavernous malformation 3
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Ubiquitin-ribosomal protein eS31 fusion protein
- Probable 2-oxoadipate dehydrogenase complex component E1 homolog
Sequence:
MVLVCNEWLKNNVDEDQTSSSLSPTPASGAVGSTALNRTGTTDTATELPQTTRYPSGEEPAVKPEEAQYALNMETEKNLEQDNFFHIMDIKEDMADSNNEASTKNQENNNMELCDSNTVCIDRRPAEVSQHAMNMAMNSVLNANNTGVGVRVTTACSLFSPLGVLNNSALQREVASECGTLQVSSVPPTSGVDLDIGLESAPTPCKGAAKIVLLCEPKSHKFETRSILLQPNQDCKVGRLIAKSKAGEGNAIFDCKVLSRNHAILWYTPDGKFWVKDTKSSNGTFINDNKLGSDPAELHYGDIVKFGVEVIENSRQEVHGCILARVALFLPNGQEAISVEAEQMMLTVPNRISFDEVQRLSSFLQEAAQREKSLKAKLSSLQGVLDNTRKNSAMCWQSMITEDQLLHKINILEKKLQMMEKNIPENALRNEIVKLLEDKTTYQLTAKEALRKVYQERCDAMQMLSKMEMAYATSENECGILRAQVLTLKQTLTDFNTRLEELQQEYMEFKKESVRQEQEAKEQESRSLEVLNGKLTTQELELKELRLQVSRIHRDLSESDTEHLKERIVLKNLDTINLDDYDHAQDRALNERDDNESSDDDILSVSPAKNVLSETKKRKLKLSNPDLEEGNYKSNVLRLLKNSDLGKGEEGSSVLKAIFNGDDEAFECKVKEEEDMANDSVPTEFVSRNTSEIVDHFKNHSSTTHTILEDSAATKLSAPNAESKEKLVDVEENLNIPNALPTEQAIDMLQEECDTYKKKTAHLTSEIHFLQGQIELLKKQLEKGVDHNFATNLQEEENSLPRETLELIDNRDSTEGVWNEDIATINNPNVENEEELIVYKELLENSELNNMQLRKEISELHLKHKHIPFSKQELLCRFLPLGCVAIGLLIYFLSSRI
Protein: Protein Ac76 (Q06690)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Plays an essential role in budded virion (BV) and occluded derived virion (ODV) development. Participates in intranuclear microvesicle formation, ODV envelopment, and subsequent embedding of virions into occlusion bodies.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:20484514}. Host nucleus {ECO:0000269|PubMed:20484514}.
Interaction partners:
Sequence:
MNLYLLLGALAIFSLVYDKKENSIFLYLLILFLVFIIVSPAIISKNTESTVEDIPSHKAKSVRKKLEIEQALDAILNKNTSSID
Protein: Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (IP210) (Iron-responsive protein-like) (IRP-like) (Major iron-containing protein) (MICP) (Probable 2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (RNA-binding protein) (P37032)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate (By similarity).
Interaction partners:
- Isocitrate dehydrogenase
- Citrate synthase
- Superoxide dismutase
- Citrate synthase
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL36
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein bL28
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein bS16
Sequence:
MKVGQDSLSTKSQLTVDGKTYNYYSLKEAENKHFKGINRLPYSLKVLLENLLRFEDGNTVTTKDIKAIADWLHNKTSQHEIAFRPTRVLMQDFTGVPAVVDLAAMRTAIVKMGGNADKISPLSPVDLVIDHSVMVDKFASADALEVNTKIEIERNKERYEFLRWGQKAFSNFQVVPPGTGICHQVNLEYLGKTVWNSENDGQLYAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGFKLSGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGPGLNDLPLADRATISNMAPEYGATCGFFPVDKETIKYLELTGRDKHTIALVEAYAKAQGMWYDKDNEEPVFTDSLHLDLGSVEPSLAGPKRPQDKVNLSSLPVEFNNFLIEVGKEKEKEKTFAVKNKDFQMKHGHVVIAAITSCTNTSNPSVLMAAGLVAKKAIEKGLQRKPWVKSSLAPGSKVVTDYLRHAGLQTYLDQLGFNLVGYGCTTCIGNSGPLPDDISHCVAEHDLVVSSVLSGNRNFEGRVHPQVRANWLASPPLVVAYALCGTTCSDLSREPIGQDKEGNDVYLKDIWPSNEEIAAEVAKVSGTMFRKEYAEVFKGDAHWQAIQTSSGQTYEWNPDSTYIQHPPFFENLSLKPEPLKPIKQAYVLALFGDSITTDHISPAGSIKASSPAGLYLKSKGVDEKDFNSYGSRRGNHEVMMRGTFANIRIRNEMTPGQEGGVTRYVPTGETMSIYDAAMRYQENQQDLVIIAGKEYGTGSSRDWAAKGTNLLGVKAVITESFERIHRSNLIGMGILPLQFKEGTTRKTLKLDGSERISIEISDKLTPGAMVPVTIERQDGDIEKIETLCRIDTADELEYYKNGGILQYVLRKISS
Protein: Type II methyltransferase M.PvuII (M.PvuII) (EC 2.1.1.113) (Modification methylase PvuII) (N-4 cytosine-specific methyltransferase PvuII) (P11409)
Organism: Proteus hauseri
Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-CAGCTG-3', methylates C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.
Interaction partners:
Sequence:
MMTLNLQTMSSNDMLNFGKKPAYTTSNGSMYIGDSLELLESFPDESISLVMTSPPFALQRKKEYGNLEQHEYVDWFLSFAKVVNKKLKPDGSFVVDFGGAYMKGVPARSIYNFRVLIRMIDEVGFFLAEDFYWFNPSKLPSPIEWVNKRKIRVKDAVNTVWWFSKTEWPKSDITKVLAPYSDRMKKLIEDPDKFYTPKTRPSGHDIGKSFSKDNGGSIPPNLLQISNSESNGQYLANCKLMGIKAHPARFPAKLPEFFIRMLTEPDDLVVDIFGGSNTTGLVAERESRKWISFEMKPEYVAASAFRFLDNNISEEKITDIYNRILNGESLDLNSII
Protein: LONGIFOLIA protein (Q0WNQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- At5g26910
- tRNA
- RB1-inducible coiled-coil protein
- DUF3741 domain-containing protein
- GPI-anchored adhesin-like protein
- tRNA
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Methyl-coenzyme M reductase II subunit gamma, putative
- Serine-rich adhesin for platelets-like protein
Sequence:
MAAKLLHSLADDSADLQKQIGCMNGIFQIFDRHHVLTGRRKSLTLGNGNAININYERDSVDTIYQQKETFQDSNIGGNVKEKRRVSTESSRVSFSSSCSSSPSSSEFNRGVQPDASAYDRANFQESPTSDPEMTEGNGFSHLGLDLRDVVRDSMYREARGLLSKTPMTREEVVRQSRREDSPRPYGLKQSTPMDLNESFRVLARLRETSQHYNELGMKDAPRYSVDSHDTLKSRQKLKELPRLSLDSRERATRNSSVDPKSSKLSESFSESCSSSSKKRPPSVVAKLMGLETLPGSPLGRDIHQFGLNKTNISDQNDDPFSRSLREKNLNRAIRFSPSSPRSLGKDPASPRWRNSDFVMKPLSNTRFPVEPAPWKHADRNRVLQKQASMPVKAKPYEAPNFPPTVYSEMERRLNDLEFKHSGKDLRALKQILESMQSKGFLDTEKQQQSTNFAVQRDYERENSATSNHAMSSRTRVQSSSSNQVYQSPIVIMKPAKLVEKAGIPASSLIPIHSLTGIKKIRREKPDDKGTSASNSKRVTKDCSPGNRRAESCTSSFDKKSDSRNVRSSSKKPQQVSKESASKSSGSVSPRLQQKKLEYDKRSRPPTPPDSSKSRKPSNQQLVESTSPGGRRRPKGQKSLQQVDDQLSQASNESRTSSHGICTQSETEASACVEKSTEADGGKSPSVIEAAKAVVSNLMQNKSSPRFSEDGLSANLSLVALEHPSPISVLDASTYRETEPSPVKTQGNVAHDFGDENCEDQWNPAYSFSETTSSFSPEINRKKLQNVEHLVQKLRRLNSSHDEASQDYIASLCENADPTTDHRYISEILLASGLLLRDLGSGLTTFQLHPSGHPINPELFFVLEQTKGSSTTHLLHKEESKVLKNEKLNRKLVFDLVNEILVEKLASVEATTNPLMKSYAKVTKKAVSAQQLLKELCSAIETQQKQATKRSENFLLEEEDDFLKSILAEDVTIRSGNWADFSGEMSGLVLDVERLVFKDLVNEIVHAETSRLQAKSGRRRTLFADQ
Protein: AN1-type zinc finger protein 1 (Zinc finger AN1-type-containing protein 1) (Q8TCF1)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of cytoplasmic stress granules (SGs) turnover. SGs are dynamic and transient cytoplasmic ribonucleoprotein assemblies important for cellular protein homeostasis when protein production is suspended after acute exogenous stress. Associates with SGs and is involved in the efficient and specific arsenite-induced clearance process of SGs through the recruitment of the ubiquitin-selective ATPase VCP and the 26S proteasome. This process requires both complexes for efficient degradation of damaged ubiquitinated SG proteins during recovery from arsenite stress, and hence avoiding aberrant cytoplasmic SGs degradation via autophagy.
Subcellular location: Cytoplasm, Stress granule {ECO:0000269|PubMed:29804830}. Note=Colocalizes with TIA1, G3BP1, VCP and 26S proteasome in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment in a VCP-independent manner (PubMed:29804830). Not localized in SGs in response to other heat- oxidative- or osmotic-induced stress treatments. Colocalizes with VCP in cytoplasmic speckles (PubMed:29804830). {ECO:0000269|PubMed:29804830}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
Sequence:
MAELDIGQHCQVEHCRQRDFLPFVCDDCSGIFCLEHRSRESHGCPEVTVINERLKTDQHTSYPCSFKDCAERELVAVICPYCEKNFCLRHRHQSDHECEKLEIPKPRMAATQKLVKDIIDSKTGETASKRWKGAKNSETAAKVALMKLKMHADGDKSLPQTERIYFQVFLPKGSKEKSKPMFFCHRWSIGKAIDFAASLARLKNDNNKFTAKKLRLCHITSGEALPLDHTLETWIAKEDCPLYNGGNIILEYLNDEEQFCKNVESYLE
Protein: Dipeptidyl carboxypeptidase (EC 3.4.15.5) (Peptidyl-dipeptidase Dcp) (P24171)
Organism: Escherichia coli (strain K12)
Function: Removes dipeptides from the C-termini of N-blocked tripeptides, tetrapeptides and larger peptides.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:8226676}.
Interaction partners:
Sequence:
MTTMNPFLVQSTLPYLAPHFDQIANHHYRPAFDEGMQQKRAEIAAIALNPQMPDFNNTILALEQSGELLTRVTSVFFAMTAAHTNDELQRLDEQFSAELAELANDIYLNGELFARVDAVWQRRESLGLDSESIRLVEVIHQRFVLAGAKLAQADKAKLKVLNTEAATLTSQFNQRLLAANKSGGLVVNDIAQLAGMSEQEIALAAEAAREKGLDNKWLIPLLNTTQQPALAEMRDRATREKLFIAGWTRAEKNDANDTRAIIQRLVEIRAQQATLLGFPHYAAWKIADQMAKTPEAALNFMREIVPAARQRASDELASIQAVIDKQQGGFSAQPWDWAFYAEQVRREKFDLDEAQLKPYFELNTVLNEGVFWTANQLFGIKFVERFDIPVYHPDVRVWEIFDHNGVGLALFYGDFFARDSKSGGAWMGNFVEQSTLNKTHPVIYNVCNYQKPAAGEPALLLWDDVITLFHEFGHTLHGLFARQRYATLSGTNTPRDFVEFPSQINEHWATHPQVFARYARHYQSGAAMPDELQQKMRNASLFNKGYEMSELLSAALLDMRWHCLEENEAMQDVDDFELRALVAENMDLPAIPPRYRSSYFAHIFGGGYAAGYYAYLWTQMLADDGYQWFVEQGGLTRENGLRFREAILSRGNSEDLERLYRQWRGKAPKIMPMLQHRGLNI
Protein: Entericidin A (P0ADB4)
Organism: Escherichia coli (strain K12)
Function: Acts as antidote to the effect of entericidin B.
Subcellular location: Cell membrane; Lipid-anchor.
Interaction partners:
- Entericidin B
Sequence:
MMKRLIVLVLLASTLLTGCNTARGFGEDIKHLGNSISRAAS
Protein: Selenoprotein BthD (dSelM) (Q9VYB0)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in a redox-related process. Required for survival and specifically for salivary gland morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14612395}. Secreted {ECO:0000269|PubMed:14612395}. Note=Secreted into the salivary gland lumen.
Interaction partners:
- Glycine-rich selenoprotein
Sequence:
MPPKRNKKAEAPIAERDAGEELDPNAPVLYVEHCRSURVFRRRAEELHSALRERGLQQLQLQLNALGAPRRGAFELSLSAGGMGKQEQVALWSGLKRGPPRARKFPTVEEVYDQIVGILGDQQESKEQTNTQKSSKIDLPGSEAIASPKKSESTEEAQENKAPTSTSTSRKSKKEQKSEEEPTQVDSKEAKQSKELVKTKRQPKAQKKQAKASESQEEVAEDKPPSSQKRKRTTRSSTDEATAGAKRRR
Protein: Thyroid hormone receptor interactor 11 (H3BJG4)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
ELSDYEERIEELENLLQQGGSGVTVTDHSKVYEMQNTIQILQMEKVESTKQIEDLENKIKEIHKRLSSAEHDQEVWKKEQERLEVEKREMTEQCERLKLELSEAQQSALRQSDAAVEEETILPHSSSVAEVLRLQQALTDAENEIMRLRSLNQEELQISLSKLSSEYEVIKSTATRDLDLFSQVHDLKHNLEAKEQELNQSIHENEILMAELEELDKQNQEATKHVILIKDQLSKQQSEGDSVIKKLKEELAGEKQRTHQLEDDKMNIIKELTVQKEKLTHSEQALSDLQLTKQKLEDKVEDLVDQLSKSEKNNFDIQKENHELREHIRQNEEELSTVRSELTQSQTQGSSRNVKDDLLKERETQVQNLKQNLSEVEQLNEHLEQVAFDLRTENEELLEAYEEVRNQLEESVAGNKQISLEKTAMLEWEKAPLETELCRAEKRVLEEERKYEQTVQELSSACSPDTSALQLEQERLIQLNQEKDFEIAELKKSIEQMDTDHKRTKETLSSSLEEQKQLTQLINEKEICIVKLKEKSSELQKELDKCAQTLRKNETLRQTIEEKDRSLGSMKEENNHLQEELERLREQQSRVVPAPEPRTLDSTTELESELSQLHRIKGHLEEEIKHHQKMIEDQNQSKLQLLQSLQEQKKELDEFKYQHEQMSISHTRLFLEKDEEIKNLQKTIEQIKAQLHEERQDSQTENSDIFQETKVQSLSIEHGSEKHDLSKAETERLVKGIKERELEIKLLNEKNTSLTKQIDQLSKDEVGKLTQIIQQKDLEIQALHARISSASYSQDVVYLQQQLHAYAMEREKVMVILNEKTRENSQLKTEYHKVIDIISAKEAALIKLQDENKKMSTRFESSGQDMFKETIQNLSRIIREKDIEIDALSQKCQTLLTVLQTSGTGSEAGGVNSNQFEELLQERDKLKQQVKKMEEWKQQVMTTVQNMQHESAQLQEELHQLQAQVSVDSDNNSKLQVDYTGLIQSYEQNETKLKNFGQELAQVQHSIGQLCNTKDLLLGKLDIMSPQLSSGSSLTSQAAEPLRASQSSEPHESSQLLQQEVDDLRKSLQEKDATIRTLQENNHRLSDSVAASSEVERKEHEQADSEIKQLKEKQEVLQNLLKEKDLLIKAKSDQLHSSNENLANKVNENELLRQAVTNLKERILILEMDISKLKGENEKIVDASKGKETEYQALQETNMKFSMMLREKEFECHSMREKALAFEQLLKEKEQGKAGELNQLLNAVKSMQEKTVTFQQERDQVMLALKQKQMETSTLQNEVQRLRDKESRLNQELQRLRDHLLESEDSHTREALAAEDREAKLRKKVSVLEEKLVSSSNAMENASHQASVQVESLQEQLNMVSKQRDETALQLSVSQEQVKQYALSLANLQMVLEHFQQEEKAMYSAELEKQNHLLAEWKKKAESLEGKVLSLQERLDEANAALDSASRLTEQLDLKEEQIEELKKQNELHQEMLDDAQKKLMSLVNSTEGKVDKVLMRNLFIGHFHTPKHQRHEVLRLMGSILGVKREEMEQLFAEDQGGVTRWMAGWLGGGSKSVPNTPLRPNQQSVFNSSFSELFVKFLETESHPSVPPPKLSVHGLKPLDSPGRRKADTGIPESFRDTAESRAGRRTDVNPFLAPRSAAVPLINPAGHGPGGPGHLLLKPISDVLPTFTPLPVSPDNSAGVVLKDLLKQ
Protein: Lysosomal protein transmembrane 5 (Q6P9Z7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Lysosomal-associated transmembrane protein 4B
- Lysosomal-associated transmembrane protein 4A
- Leukocyte surface antigen CD53
- NCK associated protein 1 like
- Coronin-1A
- Integrin beta
- Tyrosine-protein phosphatase non-receptor type 6
- E3 ubiquitin-protein ligase NEDD4
- small monomeric GTPase
- Tyrosine-protein kinase HCK
Sequence:
MASRAVPVRQTCCCFNVRVATVALAIYHIVMSVLLFIEHVVEVARGKVSCRFSKMPYLRLADLLSSFLLIGVLFIISLSLLFGVVKNREKYLIPFLSLQIMDFLLCLLTLLGSYIELPAYLKFARPRPGPSKVPLMTLQLLDFCLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEGMPRSQFINMMLIFSVAFITVLILKVYMFKCVWTCYRFMKHMNSAVEDSSSKLFLKVALPSYEEALSLPTKTPEGDLAPPPYSEV
Protein: Calcium-dependent secretion activator (H9G2V3)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MLGASSSEEEDDDFQEDHDSLPIAQVKKRSLLSGAMTPRSSSPAPSDSVSQTNSLKRNNSSSQGRRKDSVQSQTPARSARIMSNVSKPIMQNSQEFDGDEEEGEEGSTTVVGSGDECGGPALSKEEQERMKAEREEEDHKKNLQMYMFLARCIAYPFNGQQTGDMARRQMKVNKQELARIRERFTLFLKGETNIAADEAFTKAIQSYFEVFLKSERVQKVVHAGGFSQHDFREVFRLNIEKRVRSLPDIEGLSKDTVLNSWLAKFDAIIKGDETDQNRNARGRSRNPQNAMSADAVLGKEQLYDVFQQILGVKKFEHQIIFNALQLDNPDEQAAAIRREFATREEALKDPIKMKRLTPKFVVKDMETLYMDEVRMSINTLIGNLETVPVTTRGATVGKRKDKSRLKRRTSSGSLNKGDSEDGDVTLTKSDVSLALSMEVVVMEVQGLKSVQPSKIVYCTMEVDGHKLQTDHAEASKPKWDTQGDFSTKNPLPVVKVKLYTEVKSMIAFEDKELGKVIIQPTPNCARSPEWYTMTLPKSSQDQNLKIRIAIRVEKPPNLKYCGYCYCIGRNAWKKWKKRFFCLVQVSQYAFAVCSFRQKKADPTEFIQLDGFTIDYMPESDPELSAQGGKHFFTAIKEGDELKFATDDENERHLWVQALYRATGQAYKPVPPKQSTIAPKAQGFQDKASKHGMDAMIQADSINFDHDHFYSDVQRLTLDFRINEPICSLGWFSPGQAFVLEEYSARYMVRGCFRHVTLLSNLLDKADDGLLIDPALIHYSFAFCASHVHGNRCMPDRQGPEGVGTVTLEEKEKFQEIKERLRVLLEKQITNFRYCFPFGRPEGALKGTLGLLERVLMKDVVSPVPPEEVRAVIRKCLEDAALVNYTRICNEAKIEQRMGIDVSPAQRIEDMIRVTEFCIDLLKENEEHHGEAFAWFSDLLSDHSEIFWSLYSVDLDSALEVQPHDSWDSFPLFQMLNDFLLSESSLKGGIFHNKIVQQFQPLVVRYIDLMEHSIAQAIDKGFSKEKWESRKEGCATSEDIYWKLDALHTFVIDLNWPEEDFRKYLQTKMKSLTSDMISKVSDCTFTAFDSWMQRAKKSTDYMLPSEVCVQINVMFSSKSRAVRVTVDSGEYKYQSKLDETLETMLKTMESCIQEKLHGVLESVLSRLARYDEGNPIGAILNIAPKPASIFNKLKTMAGDTSAQATTTARQPLTAQQSSGQIGNSYVTFFHGCTELLRQVIIDEIWVNGLFEHWYDNQMKSINEWLTERLQQSLSATQYISLSTIVKKVYQDFSLQGIDEERLNSKTYQSISRRLQLEESNSHIQEAAINGSAQGSVFPTSLGNATAAVSNMSSMVEGAGAKMFSLFK