wanglab/gogpt-training-data huggingface dataset:
Protein: Secreted effector protein (A0A0F6B1Q8)
Organism: Salmonella typhimurium (strain 14028s / SGSC 2262)
Interaction partners:
Sequence:
MPLSVGQGYFTSSISSEKFNAIKESARLPELSLWEKIKAYFFTTHHAEALECIFNLYHHQELNLTPVQVRGAYIKLRALASQGCKEQFIIESQEHADKLIIKDDNGENILSIEVECHPEAFGLAKEINKSHPKPKNISLGDITRLVFFGDSLSDSLGRMFEKTHHILPSYGQYFGGRFTNGFTWTEFLSSPHFLGKEMLNFAEGGSTSASYSCFNCIGDFVSNTDRQVASYTPSHQDLAIFLLGANDYMTLHKDNVIMVVEQQIDDIEKIISGGVNNVLVMGIPDLSLTPYGKHSDEKRKLKDESIAHNALLKTNVEELKEKYPQHKICYYETADAFKVIMEAASNIGYDTENPYTHHGYVHVPGAKDPQLDICPQYVFNDLVHPTQEVHHCFAIMLESFIAHHYSTE
Protein: Outer envelope protein 61 (Tetratricopeptide repeat domain-containing protein 7) (B7ZWR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in protein import into the endoplasmic reticulum (ER). May function as chaperone docking protein during post-translational protein translocation into the ER. Chaperone receptor mediating Hsp70-dependent protein targeting to chloroplasts. Interacts specifically with some chloroplast precursors, but not with mitochondrial precursors. Able to select precursors for delivery to the chloroplast translocase independently of Hsp70.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Plastid, chloroplast outer membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Resides most likely exclusively in the ER membrane.
Interaction partners:
- Heat shock 70 kDa protein 4
- Protein FATTY ACID EXPORT 6
- Translocase of chloroplast 34, chloroplastic
- Outer envelope protein 64, mitochondrial
- Translocase of chloroplast 33, chloroplastic
- Protein TIC 22, chloroplastic
- At3g63160
- Protein TOC75-3, chloroplastic
- Translocase of chloroplast 159, chloroplastic
Sequence:
MFNGLMDPEMIRLAQDQMSRMTPADFARIQQQMMSNPDLMNMATESMKNMRPEDLKQAAEQLKHTRPEDMAEISEKMAKASPEDIAAMRAHADAQFTYQINAAQMLKKQGNELHSRGNFSDAAEKYLRAKNNLKEIPSSKGGAILLACSLNLMSCYLKTNQHEECIKEGSEVLGYDARNVKALYRRGQAYRDLGLFEDAVSDLSKAHEVSPEDETIADVLRDVKERLAVEGPGKASRGVVIEDITEENNVTSGENKKPSKEANGHAQGVKTDVDGLQALRDNPEAIRTFQNFISKTDPDTLAALSGGKAGDMSPDMFKTASSMIGKMSPEEIQKMVQTASSFKGDNPFAPTAPSTENGFTPTPDMLKLASDMMGKMSPEERERMFNMASSLKANAPASTSYGNAEASEPRESLGASGSSSGNSFVAPRSGFEPSIPSAPPADLQEQMRNQMKDPAMRQMFTSMIKNMNPEMMASMSEQFGMKLSQEDAAKAQQAMASLSPDALEKMMRWADRAQTGMEKAKKAKKWLFGKGGLIFAILMLVLAMVLHRLGYIGN
Protein: Cry2a protein (Cryptochrome circadian regulator 3a) (Q503J5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAPNSIHWFRKGLRLHDNPALQEAVRGADTVRCVYFLDPWFAGSSNLGVNRWRFLLQCLDDLDSNLRKLNSRLFVVRGQPANVFPRLFKEWKISRLTFEYDSEPFGKERDAAIKKLAMEAGVEVIVKTSHTLYNLDKIIELNGGQPPLTYKRFQTLISRMDPPEMPVETLSNSIMGCCVTPVSEDHGDKYGVPSLEELGFDIEGLPSAVWPGGETEALTRIERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYRKVKKTSTPPLSLYGQLLWREFFYTAATTNPRFDKMEGNPICVRIPWDKNPEALAKWAEAKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSVNAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDFIRRYLPILRGFPAKYIYDPWNAPDSVQAAAKCIIGVHYPKPMVNHAEASRLNIERMKQIYQQLSRYRGLGLLASVPSTHNGNGNGMAYSPGEQQSGTNTPAPAVSSGSVASGNRSGSILLNFDSEEHQGPSGIQQQHQQQQQQQQQQQLGYHHMPDSGHNSRFYKSNVSHDMAGHLLHKGGSVTGKRERESERDLDGEDESLSTSHKLQRQIAEVTSVYASSGNQSSMRS
Protein: Nigrocin-2JDb (B3A0M7)
Organism: Odorrana jingdongensis (Jingdong frog) (Rana jingdongensis)
Function: Has antibacterial activity against E.coli ATCC 25992 (MIC=15 uM), E.coli CIB 84492 (MIC=15 uM), S.aureus ATCC 25923 (MIC=8 uM) and S.aureus CIB 85462 (MIC=8 uM). Has antifungal activity against C.albicans (MIC=31 uM). Has hemolytic activity against rabbit erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:22917879}.
Interaction partners:
Sequence:
GIFGKILGVGKKVLCGLSGMC
Protein: Endoglucanase (EC 3.2.1.4) (Cellulase) (Endo-1,4-beta-glucanase) (Spore germination protein 270-6) (P22699)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May digest the spore cell wall during germination, to release the enclosed amoeba.
Interaction partners:
- Endoglucanase
- cellulose 1,4-beta-cellobiosidase
- Uncharacterized protein
- Cellulose synthase catalytic subunit A
- Lysosomal beta glucosidase
- Endoglucanase
- Endoglucanase
- cellulase
- Galactose-binding domain-containing protein
- Glycoside hydrolase family 5 domain-containing protein
Sequence:
MKILKNCILLIIFGLLSTQLINADTDYCSLLENALMFYKMNRAGRLPDNDIPWRGNSALNDASPNSAKDANGDGNLSGGYFDAGDGVKFGLPMAYSMTMLGWSFIEYESNIAQCGLTSLYLDTIKYGTDWLIAAHTADNEFAGQVGDGNVDHSWWGPPEDMTMARPTYMLTTEAPGTEIAMEAASALAAASIAFKSSNPTYAATCLAHAKTLHNFGYTYRGVYSDSITNAQAFYNSWSGYKDDLVWGSIWLYKATQDSDYLTKAVADYASGGVGGMAQGNSHDWDNKAPGCCLLLSKLVPTTSTYKTDFEGWLNYWLPGGGVTYTPGGLAWIRQWGPARYAATAAFLGSLAGTEKGTDFTQKQVDYLIGNNPNQQSFVVGMGPNYPINPHHRAAHHSTTNDINNPVNNLYLLKGALVGGPGSNDEYTDDRTDYISNEVATDYNAGFVGALASLVNPSSTSVPTTTPTVTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETPTETVTPTPTVTPTETPSSGESLSIYKSGLKNDFQDWSWGEHSLTDTTNVESGETNSISFTPKAYGAVFLGCFECIDTDTYNNIEFDINGGSSGAQLLRITVVKNSKSVGSKLITDLNGGTPIEANSWTKIKASFIDDFKVSGKVDGIWIQDIKGDTQSTVYISNIIATA
Protein: Myosin-5 (AtMYA1) (Q39160)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables. Contributes to the trafficking of Golgi stacks, mitochondria and peroxisomes. Required for development of pavement cells, trichomes, and stigmatic papillae.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17288617, ECO:0000269|PubMed:17500056}. Note=Colocalizes with peroxisome, cytoplasmic vesicles and/or organelles.
Interaction partners:
- LEAF RUST 10 DISEASE-RESISTANCE LOCUS RECEPTOR-LIKE PROTEIN KINASE-like 2.7
- Myosin-binding protein 1
- Myosin-binding protein 2
- Myosin-binding protein 3
- Myosin-binding protein 7
- WPP domain-interacting tail-anchored protein 2
Sequence:
MAAPVIIVGSHVWVEDPHLAWIDGEVTRIDGINVHVKTKKGKTVVTNVYFPKDTEAPSGGVDDMTKLSYLHEPGVLRNLETRYELNEIYTYTGNILIAVNPFQRLPHIYETDMMEQYKGIALGELSPHVFAIGDAAYRAMINEGKNNSILVSGESGAGKTETTKMLMRYLAFLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTLRNNNSSRFGKFVEIQFDKNGRISGAAIRTYLLERSRVCQISDPERNYHCFYLLCAAPPEDIKKYKLENPHKFHYLNQSSCYKLDGVDDASEYLETRRAMDVVGISNEEQEAIFRVVAAILHLGNIDFGKGEEIDSSVIKDKDSRSHLNMAAELLMCNAQSLEDALIRRVMVTPEEIITRTLDPDNAIASRDTLAKTIYSHLFDWIVNKINTSIGQDPRSKSIIGVLDIYGFESFKCNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYTKEEIAWSYIEFIDNQDVLELIEKKPGGIISLLDEACMFPKSTHETFSQKLFQTFKEHERFAKPKLSRTDFTISHYAGEVTYQSNHFIDKNKDYIVAEHQALFTASNCKFVAGLFHALHEDSSRSSKFSSIGSRFKQQLHSLMESLNGTEPHYIRCIKPNNVLKPGIFENFNVIHQLRCGGVLEAIRISCAGYPTRLAFYDFLDRFGLLAPEVLEGNYDDKVACQMILDKKSLTDYQIGKTKIFLRAGQMAELDARRAEVLGNAARVIQRQFRTCMARKNYRSIRNAAIVLQSFLRGEIARAVHKKLRIEAAALRVQKNFRRYVDRKSFVTTRSSTIVLQTGLRAMIARSEFRLRRQRKAAIVLQAHWRGRQAFSYYTRLQKAAIVTQCAWRCRLARRELRMLKMAARDTGALKDAKNKLEQRVEELSLRLHLEKRLRTDLEEAKVQEVAKLQEALHTMRLQLKETTAMVVKEQEAARVAIEEASSVNKEPVVVEDTEKIDSLSNEIDRLKGLLSSETHKADEAQHAYQSALVQNEELCKKLEEAGRKIDQLQDSVQRFQEKVFSLESENKVLRQQTLTISPTTRALALRPKTTIIQRTPEKDTFSNGETTQLQEPETEDRPQKSLNQKQQENQELLLKSISEDIGFSEGKPVAACLIYKCLIHWRSFEVERTSIFNRIIETIASAIEMQENSDVLCYWLSNSATLLMFLQRTLKAGATGSITTPRRRGMPSSLFGRVSQSFRGSPQSAGFPFMTGRAIGGGLDELRQVEAKYPALLFKQQLTAFLEKIYGMIRDKMKKEISPLLASCIQVPRTPRSGLVKGRSQNTQNNVVAPKPMIAHWQNIVTCLNGHLRTMRANYVPSLLISKVFGQIFSFINVQLFNSLLLRRECCSFSNGEYVKTGLAELEKWCHDATEEFVGSAWDELKHIRQAVGFLVIHQKPKKSLKEITTELCPVLSIQQLYRISTMYWDDKYGTHSVSTEVIATMRAEVSDVSKSAISNSFLLDDDSSIPFSLDDISKSMQNVEVAEVDPPPLIRQNSNFMFLLERSD
Protein: Autophagy-related protein 8g (Autophagy-related ubiquitin-like modifier ATG8g) (AtAPG8g) (Protein autophagy 8g) (Q9LZZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8LEM4}.
Interaction partners:
- Protein NBR1 homolog
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy-related protein 3
- Cysteine protease ATG4a
- Cysteine protease ATG4b
- Serine/threonine-protein kinase ATG1b
- Serine/threonine-protein kinase ATG1c
- Autophagy-related protein 16
- Beclin-1-like protein
- Serine/threonine-protein kinase ATG1a
Sequence:
MSNVSFRQDHDFEKRKAEALRIREKYSDRVPVIVEKSEKSDIPNIDKKKYLVPADLTVGQFVYVIRKRIQLSAEKAIFIFVDNVLPPTGAMMSTIYDENKEEDGFLYVTYSGENTFGSSMT
Protein: Ubiquitin carboxyl-terminal hydrolase 12 (EC 3.4.19.12) (Deubiquitinating enzyme 12) (Ubiquitin specific peptidase 12) (Ubiquitin thioesterase 12) (Ubiquitin-hydrolyzing enzyme 1) (Ubiquitin-specific-processing protease 12) (O75317)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR20 and WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2. In complex with WDR48, acts as a potential tumor suppressor by positively regulating PHLPP1 stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:30466959}. Cytoplasm {ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:30466959}. Cell membrane {ECO:0000269|PubMed:30466959}. Note=Translocates from the nucleus to the cytosol on TCR stimulation, while it translocates into the nucleus in IFN signaling. USP12/WDR20/WDR48 complex is localized mainly to the plasma membrane (PubMed:30466959). {ECO:0000269|PubMed:26811477, ECO:0000269|PubMed:30466959, ECO:0000269|PubMed:31899788}.
Interaction partners:
- WD repeat-containing protein 48
- WD repeat-containing protein 20
- Polyubiquitin-C
- PH domain leucine-rich repeat-containing protein phosphatase 1
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- PH domain leucine-rich repeat-containing protein phosphatase 2
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Dystrophia myotonica WD repeat-containing protein
Sequence:
MEILMTVSKFASICTMGANASALEKEIGPEQFPVNEHYFGLVNFGNTCYCNSVLQALYFCRPFREKVLAYKSQPRKKESLLTCLADLFHSIATQKKKVGVIPPKKFITRLRKENELFDNYMQQDAHEFLNYLLNTIADILQEERKQEKQNGRLPNGNIDNENNNSTPDPTWVHEIFQGTLTNETRCLTCETISSKDEDFLDLSVDVEQNTSITHCLRGFSNTETLCSEYKYYCEECRSKQEAHKRMKVKKLPMILALHLKRFKYMDQLHRYTKLSYRVVFPLELRLFNTSGDATNPDRMYDLVAVVVHCGSGPNRGHYIAIVKSHDFWLLFDDDIVEKIDAQAIEEFYGLTSDISKNSESGYILFYQSRD
Protein: Sister chromatid cohesion protein PDS5 homolog A-A (Q4QXM3)
Organism: Xenopus laevis (African clawed frog)
Function: May regulate sister chromatid cohesion during mitosis and couple it to DNA replication.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q29RF7}.
Interaction partners:
Sequence:
MEFPTQPKLVDGKSIIYPPGVKEITDKISNDEVVKRLKMVVKTYMDMDQDSEEEKQQYLPLALHLSSEFFLRNPNKDVRLLVACCLADIFRIYAPEAPYTSHDKLKEIFLFITRQLKGLEDTKSPQFNRYFYLLENLAWVKSYNICFELEDCNEIFIQLFKTLFSVINNSHNQKVQMHMLDLMSSITMEGDGVTQEQLDSILINLISAHKNLNKQAFDLAKVLLKRTAQTIEPCIANFFNQVLVLGKSSVSDLSEHVFDLIQELFAIDPHLLLSVMPQLEFKLKSNDGEERLAVVRLLAKLFGSKDSDLATQNRPLWQCFLGRFNDIHVPVRLESVKFASHCLMNHPDLAKDLTEFLKVRSHDPEEAIRHDVIVTIITAAKKDLFLVNDQLLGFVRERTLDKRWRVRKEAMMGLAQLYKKYCLHGEGGKDAAEKVSWIKDKLLHIYYQNSIDDKLLVEKIFAQQLVPHNLETEERMKCLYYLYASLDPNAVKALNEMWKCQNMLRSHVRELLDLHKQPTSEANTTAMFAKLMTVAKNLPDPGKAQDFVKKFNQVLGEDEKLRSQLEVLISPSCSCKQADVCVRDIARKVANPKQPTNPFLEMVKFLLERIAPVHIDSEAISALVKLMNKSIEGTADDEEEGVSPDSAIRAGLELLKVLSFTHPTSFHSDETYESLLQCLRMEDDKVAEAAIQIFRNTGHRIETDLPQIRSALIPILHQKAKRGTPHQAKQAVHCIHSIFSNKEVQLAQIFEPLSRSLNADVPEQLVTPLVSLGHISMLAPDQFASPMKSVVANFIVKDLLMNDRSNGDKNGKLWCPDEEVSPEVLAKGQAIKLLVRWLLGMKNNQSKSANSTLRLLSAMLVSEGDLTEQKRISKSDMSRLRLAAGAAIMKLAQEPCYHEIITPEQFQLCALVINDECYQVRQIFAQKLHKALVKLQLPLEYMAIFALCAKDPVKERRAHARQCLLKNISIRREYIKQNPVSNEKLLSLLPEYVVPYMIHLLAHDPDFTKPQDIDQLRDIKECLWFMLEVLMTKNENNSHAFMKKLCENIKQTRDAQAPDDPKANEKLFTVCDVALCVVYNKSAPCHSESSKDPVLPLTFFTQPDKDFSSKSYITDEARNLLLTGKPKPMTVLGMVNKPLNATGRRPYSRSTGSEISNNVSINSESDASVANRQSSEVPEIGVSENDENPVRLISVPPAKTETVKNKEVNLDQTAPSNTGTERGKKRSAASAGAENIRKESEEKKADNISATPTPKPRRGRPPKSESQGSAAKNDETSKPSGRGRKRAAANQESSGAQEAANAKVPKQDSTAKKTAQRQIDLHR
Protein: Spanin, inner membrane subunit (i-spanin) (Lysis protein Rz) (P00726)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is due to local fusion between the inner and outer membrane performed by the spanin complex.
Subcellular location: Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04137, ECO:0000269|PubMed:18713319}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04137, ECO:0000269|PubMed:18713319}; Periplasmic side {ECO:0000255|HAMAP-Rule:MF_04137, ECO:0000269|PubMed:18713319}.
Interaction partners:
Sequence:
MSRVTAIISALVICIIVCLSWAVNHYRDNAITYKAQRDKNARELKLANAAITDMQMRQRDVAALDAKYTKELADAKAENDALRDDVAAGRRRLHIKAVCQSVREATTASGVDNAASPRLADTAERDYFTLRERLITMQKQLEGTQKYINEQCR
Protein: Spore coat protein SP85 (Cellulose-binding protein SP85) (Prespore protein 14E6) (Prespore protein B) (P54704)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
Subcellular location: Spore wall {ECO:0000269|PubMed:17416892}. Note=Accumulates in prespore vesicles coordinately with other coat proteins.
Interaction partners:
- Spore coat protein SP65
- Spore coat protein SP70
- Spore coat protein SP60
- Spore coat protein SP96
- Prespore vesicle protein
- Prespore-specific protein A
Sequence:
MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPPTYPPTYPPTQPPRASCDNVRCPRGYHCECNHWENVARCVRNEEPTHRPKPPHHGCRPDSCARGEKCICVRGKIYCIPKTTCDQVRCPRKHHCECNRKGQVFCVPDCPKLTCKQVGCPENHECVSRRGELHCVYVRPPTGRWGDDLSDLGYNQASVEAAIDAYEAQRGQRPHNNIPSNNLHQENNDNLGDGFYDGVEIGFADGGFDVNDLNGF
Protein: MKIAA4015 protein (Q5DTS4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
PCLCFYSGSQEERFAPGWNRDYPPPPLKSHAQERHSGNFPGRDSLPFDFQGHSGPPFANVEEHSFSYGGRDGPHGDYQGGEGPGHDFRGGDFSSSDFQSRDSAQLDFRNRDIHSGDFRDREGPPMDYRGGDGTPMDYRGRETPHMNYRDRDSHTVDFRSRDVPPTDFRGRGTYDLDFRGREGSHSDFRGRDLSDLDFRSRDQSRSDFRNRDVSDLDFRDKDGTQVDFRGRGSATTDLDFRNRDTPHSDFRGRHRTRTYQDFRGREVGPCMEFKDREMPPMDPKVLDYIQPSPQEREHSGMNMNKREESIHDHAMERPAFGVQKGEFEHSETREGETQSGTFEHESQSDFQNSQSPVQEQDKPKLSGGEQQSSDAGLFKEEGDLDFLGQQDTDYRSIEYCDVDHRLPGNQIFGYGQSKSFSQGKMSRDAQQDLQDQDYRTGPSEEKPNRLIRLSGVPENATKEEILNAFRTSDGIPVKDLQLKEYNTGYDYGYVCVEFSLLEDAIGCMEANQGTLMIHDKEVTLEYVPSPDFWYCKRCKASTGGHQSSCSFCKGPKEEVKQELVSYPQPQKTSIPVPSEKQPNQPRPADKEHELRKREEGQESRLGHQKRDTERYFPHSRREGLTFRRDREKEPWSGDSRQDGESKTIMLKRIYRSTPPEVIVEVLEPYVHLTTANVRIIKNRTGPMGHTYGFIDLDSHAEALRVVKILQNLDPPFSIDGKMVAVNLATGKRRNDSGDHSDHMHYYQGKKYFRDRRGGNRNSDWSSDTNRQGQQSSSDCYIYDSTTGYYYDPLAGTYYDPNTQQEVYVPQDPESPDEEEIKEKKSTSQGKSNSKKETSKRDGKEKKDRGMTKFQESTSEGKPPLEDVFKKPLPPTVKKEESPPPPKVVNPLIGLLGEYGGDSDYEEEEEEEQAPPVQPQPQPREEMTKKENEDDKLTDWNKLACLLCRRQFPNKEVLTKHQQLSDLHKQNLEIHRKIKQSEQELAYLERREREGRFKEKGNDRREKLQSFDSPERKRIKYSRETDSDRNPVDKEDTDTSSKGGCAQQATGWRKGAGLGYSHPGLGSSEEIEGRMRGPGGGPPGRTSKRQSNETYRDAVRRVMFARYKELD
Protein: Caprin-1 (Cytoplasmic activation- and proliferation-associated protein 1) (GPI-anchored membrane protein 1) (GPI-anchored protein p137) (GPI-p137) (p137GPI) (Membrane component chromosome 11 surface marker 1) (RNA granule protein 105) (Q60865)
Organism: Mus musculus (Mouse)
Function: May regulate the transport and translation of mRNAs of proteins involved in synaptic plasticity in neurons and cell proliferation and migration in multiple cell types. Binds directly and selectively to MYC and CCND2 RNAs. In neuronal cells, directly binds to several mRNAs associated with RNA granules, including BDNF, CAMK2A, CREB1, MAP2, NTRK2 mRNAs, as well as to GRIN1 and KPNB1 mRNAs, but not to rRNAs (By similarity).
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:17210633}. Cytoplasm, cytosol {ECO:0000269|PubMed:14764709, ECO:0000269|PubMed:17210633}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q5M9G3}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14444}. Note=Mediates formation and localizes to cytoplasmic ribonucleoprotein membraneless compartments (By similarity) (PubMed:17210633). Associated with RNA granules (PubMed:17210633). At the leading edge of migrating fibroblasts, colocalizes with DDX3X (By similarity). {ECO:0000250|UniProtKB:Q14444, ECO:0000269|PubMed:17210633}.
Interaction partners:
- Ras GTPase-activating protein-binding protein 1
- Ras GTPase-activating protein-binding protein 2
- Fragile X messenger ribonucleoprotein 1
- Cytotoxic granule associated RNA binding protein TIA1
- RNA-binding protein FXR1
- Ubiquitin carboxyl-terminal hydrolase 10
- Nucleolysin TIAR
- Ubiquitin-associated protein 2-like
- Eukaryotic initiation factor 4A-I
- RNA-binding protein FXR2
Sequence:
MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDDVRTDLKQGLSGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKALKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPTVEDQVAEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFSSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQSDPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPQVHSESRLAQSNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPMDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPANEPETLKQQSQYQATYNQSFSSQPHQVEQTELQQDQLQTVVGTYHGSQDQPHQVPGNHQQPPQQNTGFPRSSQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYSQSQFTAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN
Protein: DExH-box ATP-dependent RNA helicase DExH2 (EC 3.6.4.13) (DEIH-box RNA/DNA helicase) (EC 3.6.4.12) (F4IDQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May function as an ATP-dependent RNA/DNA helicase. Binds DNA in vitro in a non-specific manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:10471743}.
Interaction partners:
- AP-2 complex subunit sigma
- AP-2 complex subunit mu
- Calcium sensing receptor, chloroplastic
- Nucleolar-like protein
- F18K10.11 protein
- Nucleolar protein
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- At4g01000
- rRNA biogenesis protein RRP5
- U3 small nucleolar RNA-associated protein 18 homolog
Sequence:
MAKKKKDTKHTRLCEATGAWATKVLEDFRASGNDSYVFEQQLTNSERGIIHQMCRTMGLRSKSNGSGEERRLSLFKGDGISKSDKRRMYEARNQKEKEGDGISKSYSKHRYETRFQKAGGIRKTRISPKKLKCVSFPPEAKAVLHDLFTRYPPCDGDTTGTSLGIYTTGNVNSNWKDDFFKKPHMTKHDIENNVVSLSSRLKKERHFREIFEARSKLPIASFRDAIISAVESNQVVLIAGETGCGKTTQVPQYLLDHMWHSKKEACKIICTQPRRISAISVSDRISWERGETIGRTVGYKVRLQSEGGRESSVVFCTNGILLRVLIGKGVNSSVPDITHIIVDEIHERDSYSDFMLMILRDLLPSNPHLRLILMSATLDAERFSEYFGGCPVVRVPGFTYPVRTFFLDDALSVLNSDKNSHLLSAVKRDFKDEDKVSLDEAIDLAWTNDEFDCLVDLVSSEGSHEAYNYQNSTTGLTPLMVFAGKGRVSDVCKLLSVGADCTLKSKEGITALELAEKENQFETAQIIREHAGNIQSNSQQAQDLLDKYMATIKPEEVDVGLIVKLMKKICSDSKDGAILVFLPGWEEISKTKEKLLDDRFFAHSAKFIILCLHSRVPAEEQKKVFNRPPRGCRKIVLATNIAESAVTIDDVVYVIDSGRMKEKSYDPYNDVSTLQSSWVSKANAKQRAGRAGRCQAGICYHLYSKLRAASLPEYRVPEVMRMPVDELCLQVKMLDPNCNVNDFLQKLMDPPVAQSIENALIILKDIGALTPEEELTELGQKFGQLPVHPRISKMIYFAILVNCLDPALILACAADEKDPFTMPLSPGDRKKAAAAKHELASLYGDHSDHLATVAAFQCWKNAKASGQAKEFCSKYFISQVVMKRLDDLCRKLQGELNRHGVIPSSSSNCSLNAHDPGILRAVIAVGLYPMLGRMCPLSKNRTRSVIETIAGAKVRVPSLSNNVDMSSTKFDEALIVFDEITRGDWGVVIRSCTVLPTIPVLLFSREIAVSTTESYDAVKSDDEEDHKVGNVGDAMDIDKEVGRPGEKIMLGPENSVKVVVDRWLPFKVTAFEIAQMYILRERLMASILFKVKHPKENLPPHLGASMYAIASVLSYDSLAQSSVQTVAVQPITSVVDATSPRDDIPSTNPNELREHDPNTTPMGSKLELANKLGLGNMEESLPSNFADGNEQPDPNTSPVEDVSAATKQKKMQSESKRCKSLNNVDLGNIEENFGNMEENPPSDLAIGNEQTLPKLASNLDMGNMEENTPSDLANGNEKTEPNSANSMDLGNMEENTPSDLANGNKKKEPKSVSKLDLGSEKVSIPSNLVNGNEQHDLNIAPGEDASAAKQPEKKRSRSKKRKSGNNLDLGKMEKSKPSDLANENEQTEPKSANNLDLGNMKENTPSDLANENEQTELRLPNNSDYGNMEESLPLNLANGDEQPDPTTAPMEAAKQPKKKRSRSKKCKSVNNLDLGNMEENKPSDLANGNEQKDPESVNRLDPGKEKESIPSNLVSGNEQPDSNTAPAKKPKKKKRKLANNFDSVNNMEEKMPSTNVLSQGNKSGLIEEKPSIPSDQ
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform (PP2A subunit B isoform B55-delta) (PP2A subunit B isoform PR55-delta) (PP2A subunit B isoform R2-delta) (PP2A subunit B isoform delta) (Q6NY64)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55-delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P56932}.
Interaction partners:
- Protein phosphatase 2, regulatory subunit A, beta a
- Protein phosphatase 2
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase.
- Tcp1 protein.
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit delta
Sequence:
MAGVGGGNDFQWCFSQVKGAIDEDVAEADIISTVEFNYSGELLATGDKGGRVVIFQREQESKNRPLSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAHFLLSTNDKTIKLWKISERDKRAEGYNLKDEDGRLRDPFRITSLRVPVLMPMDLMVEASPRRIFANAHTYHINSISVNSDYETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAECHPHQCNVFVYSSSKGTIRLCDMRAAALCDRHSKFFEEPEDPSSRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKVWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSAIMTGSYNNFFRMFDRNTRRDITLEASRESSKPRAMLKPRKVCTGGKRKKDEISVDSLDFNKKILHTAWHPKENVIAVAATNNLYIFQDKMN
Protein: Wolframin (O76024)
Organism: Homo sapiens (Human)
Function: Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store. Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:23035048}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:23035048}. Note=Co-localizes with ATP6V1A in the secretory granules in neuroblastoma cell lines. {ECO:0000269|PubMed:23035048}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- CDGSH iron-sulfur domain-containing protein 2
- Cyclic AMP-dependent transcription factor ATF-6 beta
- Sodium/potassium-transporting ATPase subunit beta-1
- X-box-binding protein 1
- ATP-binding cassette sub-family C member 8
- Gap junction beta-2 protein
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- Protein diaphanous homolog 1
- ATP-sensitive inward rectifier potassium channel 11
Sequence:
MDSNTAPLGPSCPQPPPAPQPQARSRLNATASLEQERSERPRAPGPQAGPGPGVRDAAAPAEPQAQHTRSRERADGTGPTKGDMEIPFEEVLERAKAGDPKAQTEVGKHYLQLAGDTDEELNSCTAVDWLVLAAKQGRREAVKLLRRCLADRRGITSENEREVRQLSSETDLERAVRKAALVMYWKLNPKKKKQVAVAELLENVGQVNEHDGGAQPGPVPKSLQKQRRMLERLVSSESKNYIALDDFVEITKKYAKGVIPSSLFLQDDEDDDELAGKSPEDLPLRLKVVKYPLHAIMEIKEYLIDMASRAGMHWLSTIIPTHHINALIFFFIVSNLTIDFFAFFIPLVIFYLSFISMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYAHFLLSVFFVIFSFPIASKDCIPCSELAVITGFFTVTSYLSLSTHAEPYTRRALATEVTAGLLSLLPSMPLNWPYLKVLGQTFITVPVGHLVVLNVSVPCLLYVYLLYLFFRMAQLRNFKGTYCYLVPYLVCFMWCELSVVILLESTGLGLLRASIGYFLFLFALPILVAGLALVGVLQFARWFTSLELTKIAVTVAVCSVPLLLRWWTKASFSVVGMVKSLTRSSMVKLILVWLTAIVLFCWFYVYRSEGMKVYNSTLTWQQYGALCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTDIDNSAESAINMLPFFIGDWMRCLYGEAYPACSPGNTSTAEEELCRLKLLAKHPCHIKKFDRYKFEITVGMPFSSGADGSRSREEDDVTKDIVLRASSEFKSVLLSLRQGSLIEFSTILEGRLGSKWPVFELKAISCLNCMAQLSPTRRHVKIEHDWRSTVHGAVKFAFDFFFFPFLSAA