wanglab/gogpt-training-data huggingface dataset:
Protein: Coatomer subunit epsilon-1 (Epsilon-coat protein 1) (Epsilon-COP 1) (Q9SA78)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta-1
- Coatomer subunit alpha-2
- Coatomer subunit beta'-1
- Coatomer subunit alpha-1
- Coatomer subunit zeta-3
- Coatomer subunit delta
- Coatomer subunit beta'-2
- Coatomer subunit beta'-3
- Coatomer subunit beta-2
- Coatomer subunit gamma
Sequence:
MASMAGPDHLFNLRNHFYLGAYQAAINNSEIPNLSQEDIVERDCLVHRAYIALGSYQLVISEIDEAAATPLQAVKLLAMYLSSPENKESTISSLREWLADPTVGNNAIIRLIAGTIFMHEEDYNEALKHTHSGGTMDLHALNVQIFIKMHRSDFAEKQLRVMQQIDEDHTLTQLASAWLNLAVGGSKIQEAYLIFQDFSEKYPMTSLILNGKAVCCMHMGNFEEAETLLLEALNKDAKDPETLANLVVCSLHVGKSSSRYLNQLKLSHPEHVLVKRAASAEDNFERALQSFA
Protein: Histone deacetylase 6 (A0A2R8YDE6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKKLGQAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLIQEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNSYSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQKHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATPAGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSAQASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSRTGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCHSAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLNGAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMFEDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEGGYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVEDREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSETAVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGAILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQTPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEAAGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKNIAHQNKFGEDMPHPH
Protein: Eukaryotic translation initiation factor 6 (eIF-6) (B(2)GCN homolog) (B4 integrin interactor) (CAB) (p27(BBP)) (P56537)
Organism: Homo sapiens (Human)
Function: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity. In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis (By similarity). Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC. Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth (By similarity).
Subcellular location: Cytoplasm. Nucleus, nucleolus. Note=Shuttles between cytoplasm and nucleus/nucleolus.
Interaction partners:
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL30
- GTP-binding protein 4
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL34
- 60S ribosomal export protein NMD3
- Large ribosomal subunit protein eL6
Sequence:
MAVRASFENNCEIGCFAKLTNTYCLVAIGGSENFYSVFEGELSDTIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDTVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAQPSTIATSMRDSLIDSLT
Protein: PPi-type phosphoenolpyruvate carboxykinase 3 (EhPEPCK3) (PPi-PEPCK3) (EC 4.1.1.38) (Diphosphate-dependent phosphoenolpyruvate carboxykinase 3) (PEP carboxyphosphotransferase 3) (C4LWQ8)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Inorganic pyrophosphate (PPi)-dependent phosphoenolpyruvate carboxykinase, which regulates the carbon flow of the central metabolism by fixing CO(2) to phosphoenolpyruvate to produce oxaloacetate. Can also produce pyruvate and diphosphate from phosphoenolpyruvate and phosphate.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:C4LY96}.
Interaction partners:
- Pyruvate, phosphate dikinase
- Pyruvate kinase
- PPi-type phosphoenolpyruvate carboxykinase 2
- PPi-type phosphoenolpyruvate carboxykinase 1
- Malate dehydrogenase
- Malate dehydrogenase
- Malate dehydrogenase
Sequence:
MFNQEQGTDYPVLNKKKLESLANLKLAMGGHEYPTDDLTQQGLKLAGPLLEEVEESEVNHTTAPIDARLQTFLNSYFAECGEEVPKIPDDTFILDREGLGRVLSFPPHKQEFFCETMKSYKIKQGVLHNPAKDKRTTVGVFHICQSDVPVPADKIECPKIAFLRMLKAAFYGAPDDHLIIPYTAECKEPTRSWVSLYMRPVVVPGVKGVKGFEHEKATEMHFFVPGNMVSCLDFVESVFGNAGNPRLSKNDAALDPLGWTGHSGMAILAPHLTRMTKKECGLPHISQATERQKRERMCWEKEDELYNDGKTFKMYCRDASGVICTIIADNYFGYCKKEVKTQISYSANLYGFAEEEHAGGAIARPSYDLGESCDASKYAEGYKFSEMVEKNKHSIIVKEEGYAVDKKYPEGIIYVPEDSVFTIEDASIKFNHNGKEESILLTPKVNYVLPNGYTIILHDTMTSRRWTLRGILPQYTLCHKPCTVSGGGKSEISKSIRDAVIEGSVFVNNKEEDFKAVQKVFDHDFSKRYANGEVKPIHILDPNVTLGTVVELLTPSHLFTKEHNDYISSISPLIVELVMTIKSLYREDWKGDWQSRITVDKINGNEGNELKYRGANLSSQYLRVGFERDETTWRVFQLRKDFFPAAKLQMEDDITASVIVPTKLLKTPINNMQKKACKIVKNCELRLFQRPDDAVFRGFDKQTEYDFSIPGHFISNYQPMTREEAKDFTKDVVRLYQYTEPMRKCLQDFVAGKDEAKYIVSSSYTRLVPEGDKLVGSKNPRYLQRRPDMLDPEYTYMTFKAIQLYRKISDEEPLYTPVDAVLSGRRNNPPQVAKNGMKLRPLSVFAPLHYFELPELLMECITSMTGASPSMFGAGSEGALTKGPFNSLPAVVDLNNYLLGMICCGYSGFVSSASYCGPHYKVAHDISLLIPEIWSKMIRYEQEPKYLIEHGYLEPCPDVTYNGKTYSGKRLGYRITTAFANHFLRTLFSMPNSVMPEDFLKPELQDLAIYADSYEYMSQTDKGIAMNYVKDGTVEGACPPLKALIYIMANGEYNGMTRESKEFREMFDPEVVLNSEWYKERLVTRQKLEVAKLNKDLAYLNKTIAEKPRLAETLNKQIAAVKEELQYVSSEEYLHDINGSIGTDPYPYKCMKH
Protein: ATP-dependent permease MDL1, mitochondrial (ABC transporter MDL1) (Multidrug resistance-like protein 1) (P33310)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mediates export of peptides with molecular masses of 2100 to 600 daltons generated upon proteolysis of mitochondrial inner membrane proteins.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11251115, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:11251115, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
Sequence:
MIVRMIRLCKGPKLLRSQFASASALYSTKSLFKPPMYQKAEINLIIPHRKHFLLRSIRLQSDIAQGKKSTKPTLKLSNANSKSSGFKDIKRLFVLSKPESKYIGLALLLILISSSVSMAVPSVIGKLLDLASESDGEDEEGSKSNKLYGFTKKQFFTALGAVFIIGAVANASRIIILKVTGERLVARLRTRTMKAALDQDATFLDTNRVGDLISRLSSDASIVAKSVTQNVSDGTRAIIQGFVGFGMMSFLSWKLTCVMMILAPPLGAMALIYGRKIRNLSRQLQTSVGGLTKVAEEQLNATRTIQAYGGEKNEVRRYAKEVRNVFHIGLKEAVTSGLFFGSTGLVGNTAMLSLLLVGTSMIQSGSMTVGELSSFMMYAVYTGSSLFGLSSFYSELMKGAGAAARVFELNDRKPLIRPTIGKDPVSLAQKPIVFKNVSFTYPTRPKHQIFKDLNITIKPGEHVCAVGPSGSGKSTIASLLLRYYDVNSGSIEFGDEDIRNFNLRKYRRLIGYVQQEPLLFNGTILDNILYCIPPEIAEQDDRIRRAIGKANCTKFLANFPDGLQTMVGARGAQLSGGQKQRIALARAFLLDPAVLILDEATSALDSQSEEIVAKNLQRRVERGFTTISIAHRLSTIKHSTRVIVLGKHGSVVETGSFRDLIAIPNSELNALLAEQQDEEGKGGVIDLDNSVAREV
Protein: Exported protein family 4 (Q8IJ10)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNFFHVIILDVGIVICLYLIIYKNSDIKWKKHINCCKYHFYFFSSKRCLLQHMVEEPFEKKDKSGVLLKDKNTEEGRKKERQKPMCIKSINKKKKKNNNNNNNNVLKNLNNEEINKQRNMTNERIRNKNKNDKGVENISSNTQMEEKNIICKDINSNVILNQNEINDDQMVQKIKENFVKDLMKNENKEIFKQIETINSVGTMAKIKNSLYSIIFKGSNFWKGLGIYLGTLSGAALGQLILAGILQFGTFSVMNFSIYFSAVPSFIAFSSFVGIILLSIIIVICLLVWLWPSRGKLMGKDKTENKSDT
Protein: Prismalin-14 (Q6F4C6)
Organism: Pinctada fucata (Akoya pearl oyster) (Pinctada imbricata fucata)
Function: Displays inhibitory activity against calcium carbonate precipitation, binds calcium and affects crystallization of calcium carbonate in vitro. May be involved in calcification of the prismatic layer of the shell.
Interaction partners:
Sequence:
MRSLLVLLALAACASAQYFFRGGDDDNGFFGGDDDNGYFGYFPRFSYPIYRPIYRPIYYPQIIRPFYGYGYGGFNGGYGGLGLYGGYGGFGGYGYRPFSYGYNPFSYGYYGFGDDDGGFDD
Protein: Ragulator complex protein LAMTOR5 (Hepatitis B virus X-interacting protein) (HBV X-interacting protein) (HBX-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5) (O43504)
Organism: Homo sapiens (Human)
Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway. Down-regulates hepatitis B virus (HBV) replication.
Subcellular location: Lysosome {ECO:0000269|PubMed:22980980}. Cytoplasm, cytosol {ECO:0000269|PubMed:12773388}.
Interaction partners:
- Ras-related GTP-binding protein C
- Ras-related GTP-binding protein B
- Ragulator complex protein LAMTOR2
- Regulatory-associated protein of mTOR
- Ras-related GTP-binding protein A
- Ragulator complex protein LAMTOR4
- Neutral amino acid transporter 9
- Ragulator complex protein LAMTOR3
- Ras-related GTP-binding protein D
- Ragulator complex protein LAMTOR1
Sequence:
MEATLEQHLEDTMKNPSIVGVLCTDSQGLNLGCRGTLSDEHAGVISVLAQQAAKLTSDPTDIPVVCLESDNGNIMIQKHDGITVAVHKMAS
Protein: C-X-C chemokine receptor type 3 (CXC-R3) (CXCR-3) (Interferon-inducible protein 10 receptor) (IP-10 receptor) (CD antigen CD183) (O88410)
Organism: Mus musculus (Mouse)
Function: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of mesangial cells through a heterotrimeric G-protein signaling pathway. Probably promotes cell chemotaxis response (By similarity). Binds to CCL21.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Platelet factor 4
- C-X-C motif chemokine 9
- C-X-C motif chemokine 10
- C-C motif chemokine 5
- Stromal cell-derived factor 1
- C-C motif chemokine 2
- C-X-C motif chemokine 13
- C-C motif chemokine 4
- C-C motif chemokine 3
- C-C motif chemokine 20
Sequence:
MYLEVSERQVLDASDFAFLLENSTSPYDYGENESDFSDSPPCPQDFSLNFDRTFLPALYSLLFLLGLLGNGAVAAVLLSQRTALSSTDTFLLHLAVADVLLVLTLPLWAVDAAVQWVFGPGLCKVAGALFNINFYAGAFLLACISFDRYLSIVHATQIYRRDPRVRVALTCIVVWGLCLLFALPDFIYLSANYDQRLNATHCQYNFPQVGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRFRAMRLVVVVVAAFAVCWTPYHLVVLVDILMDVGVLARNCGRESHVDVAKSVTSGMGYMHCCLNPLLYAFVGVKFREQMWMLFTRLGRSDQRGPQRQPSSSRRESSWSETTEASYLGL
Protein: Kin of IRRE-like protein 2 (Kin of irregular chiasm-like protein 2) (Nephrin-like protein 3) (Q6UWL6)
Organism: Homo sapiens (Human)
Function: May regulate basal insulin secretion.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q7TSU7}; Single-pass type I membrane protein {ECO:0000255}. Note=Localized along the sites of the cell contacts. Colocalizes with E-Cadherin and beta-catenin. {ECO:0000250|UniProtKB:Q7TSU7}.
Interaction partners:
- Nephrin
- Podocin
- Na
- Tyrosine-protein kinase ITK/TSK
Sequence:
MLRMRVPALLVLLFCFRGRAGPSPHFLQQPEDLVVLLGEEARLPCALGAYWGLVQWTKSGLALGGQRDLPGWSRYWISGNAANGQHDLHIRPVELEDEASYECQATQAGLRSRPAQLHVLVPPEAPQVLGGPSVSLVAGVPANLTCRSRGDARPTPELLWFRDGVLLDGATFHQTLLKEGTPGSVESTLTLTPFSHDDGATFVCRARSQALPTGRDTAITLSLQYPPEVTLSASPHTVQEGEKVIFLCQATAQPPVTGYRWAKGGSPVLGARGPRLEVVADASFLTEPVSCEVSNAVGSANRSTALDVLFGPILQAKPEPVSVDVGEDASFSCAWRGNPLPRVTWTRRGGAQVLGSGATLRLPSVGPEDAGDYVCRAEAGLSGLRGGAAEARLTVNAPPVVTALHSAPAFLRGPARLQCLVFASPAPDAVVWSWDEGFLEAGSQGRFLVETFPAPESRGGLGPGLISVLHISGTQESDFSRSFNCSARNRLGEGGAQASLGRRDLLPTVRIVAGVAAATTTLLMVITGVALCCWRHSKASASFSEQKNLMRIPGSSDGSSSRGPEEEETGSREDRGPIVHTDHSDLVLEEEGTLETKDPTNGYYKVRGVSVSLSLGEAPGGGLFLPPPSPLGPPGTPTFYDFNPHLGMVPPCRLYRARAGYLTTPHPRAFTSYIKPTSFGPPDLAPGTPPFPYAAFPTPSHPRLQTHV
Protein: BHLH transcription factor (Os05g0103000 protein) (cDNA clone:J013044E05, full insert sequence) (Q75M33)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MESLCGQLEHEHEQQLHQSSSSSLLPYCFLSAPEPLPVPGFPAGCSNLEEKAAAAMAAYEYESSSCSSLDPTSMPMVYSPIVLQPQECPLSFVFDNAAAAAGDNKWVPGIQGSCPCSLGSTQDMDASWGKSRKHKRSNVGLKGLEEKKARRVVLHQHDDDVKKKAKEAAGGEPPAGYIHVRARRGQATDSHSLAERVRREKISERMKMLQSLVPGCDKVTGKALMLDEIISYVQSLQNQVEFLSMKLASLSPLMYEFGPGIDMHPDVLRQLAKMPHEMVQCMGQMGSTGISLQGLGGGPTGFAQDGSSHINMVVMQVGEQGQQQGSLHQVEMSSHCFFH
Protein: DNA/pantothenate metabolism flavoprotein C-terminal domain-containing protein (Q57ZB4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Flavoprotein domain-containing protein
- Pantothenate kinase subunit, putative
- Kynurenine aminotransferase, putative
- aspartate transaminase
- Aspartate aminotransferase
Sequence:
MSAEGLSRFFTENLTEEGRSDLNQWEAKTLEFAQRVNRDGCEGVAFITSGGTAVPLEVHAVRFVTNFSSGGRGAVLVEELLARGWACILLRSKTSQLPFRRLVDNMTTEQFFAELNAPQKSCDVSAAIEAYTKYKSRFLEIPYYTVVEYLYLFSLLTGTLSHRAECLRQTPMMLLAAAAVSDYYIPESRLSHHKMSGGDGLTIQFNNVPKILDLISEEWHGSSRAAPRYLITFKLETEEEQLKAKALRNLGLYRCDAVVANMLQNYRERVLVFWNGEEQNPTLLHRSPNGSVESLMIDHVLQRIKNHAKGCGMQYKLEGRRR
Protein: DnaJ homolog 1, mitochondrial (P35191)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in mitochondrial biogenesis and protein folding.
Subcellular location: Mitochondrion.
Interaction partners:
- Import motor subunit, mitochondrial
- Mitochondrial DnaJ homolog 2
- Mitochondrial import inner membrane translocase subunit TIM14
- Heat shock protein 78
- GrpE protein homolog
- Heat shock protein SSC3, mitochondrial
- J-type co-chaperone JAC1, mitochondrial
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Heat shock protein 60, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM44
Sequence:
MAFQQGVLSRCSGVFRHHVGHSRHINNILYRHAIAFASIAPRIPKSSFHTSAIRNNEAFKDPYDTLGLKKSATGAEIKKAYYKLAKKYHPDINKEPDAEKKFHDLQNAYEILSDETKRQQYDQFGPAAFGGGGAAGGAGGGSGSPFGSQFHDFSGFTSAGGSPFGGINFEDLFGAAFGGGGRGSGGASRSSSMFRQYRGDPIEIVHKVSFKDAVFGSKNVQLRFSALDPCSTCSGTGMKPNTHKVSCSTCHGTGTTVHIRGGFQMMSTCPTCNGEGTMKRPQDNCTKCHGEGVQVNRAKTITVDLPHGLQDGDVVRIPGQGSYPDIAVEADLKDSVKLSRGDILVRIRVDKDPNFSIKNKYDIWYDKEIPITTAALGGTVTIPTVEGQKIRIKVAPGTQYNQVISIPNMGVPKTSTIRGDMKVQYKIVVKKPQSLAEKCLWEALADVTNDDMAKKTMQPGTAAGTAINEEILKKQKQEEEKHAKKDDDNTLKRLENFITNTFRKIKGDKKN
Protein: BZIP domain-containing protein (A7RN55)
Organism: Nematostella vectensis (Starlet sea anemone)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
EYEYNPLPIGKKARRKFVPDQEKDDRYWARRVKNNVAARRSRDMRRQKEIEISMKWKQLEKENARLREELQQLKDRASELEKKLSEKQAGH
Protein: Uncharacterized protein (J9VW60)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Interaction partners:
Sequence:
MSLDEMPHPSGIVADDRPASDDEDSLEDEGPPELTFPPFPKLPSGALLIAFSESDVKGAWVPPFSANREEDGKNFATPHDHQGLPLVEMERPYTGLNHTFEERENHKKMKRRAANDRRKENPNATQTTRSRTKKASESRLKEEDCWKIGDPLSGWHEPSGTSRTRFEISSPPFSRLIHATADFISSRDAELQYKYNKRLFDIIRDLFGIRTTFIGRHWPGSGPNATIYASRRRRYETGLAPVLLPSQRYGQYGNRPPRLEETCVLLREPESSVRQFMTFARKEVETAWEFEPALKLATMTAAFISFLTHHNVFPEPALHSAFKKAAAIARSGPGKLIRARELENILVRGTRWNRASWAVWGGSHSGPEPGGPEKESQWGSLSTELKASEEKIKPGDPDEAKTGDSDEAGGWTVDEILDKRLDPPTKEDAINVVHSLIQPFSIDDIHLIQNIEFSNRIIIAVLPPQPAEAGAPAYISKCYRFVTIKSPLQPTFKKSLPTQTNRDSAEDEDGEEETDKEQSIPEPEEMVIWVEAEDLAGKGGGVGYVGMSLQGRWGLMGLKEDRGKSAKYGQWWAFKTSDFVLPAM
Protein: CREB-regulated transcription coactivator, isoform B (M9PFU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Cyclic AMP response element-binding protein B
Sequence:
MANPRKFSEKIALQKQKQAEGTAEFERIMKEVYATKRDEPPANQKILDGLVGGQEVSQSSPGAGNGTGGGGSGSGSGASGGGASPDGLGGGGGSPTAYRESRGRSVGVGPMRRPSERKQDRSPYGSSSTQQTLDNGQLNPHLLGPPTAESLWRRSSSDSALHQSALVAGFNSDVNSMGANYQQQQHQQQQQPGQPRSHSPHHGINRTMSPQAQRRKSPLLQPHQLQLQQLQQQQQQMQHQHQLHQQLQMQQLQQHQQQHQQQQQQQNTPYNNAKFTNPVFRPLQDQVNFANTGSLPDLTALQNYGPQQQQQQSQQQPSQQQQQLQQTLSPVMSPHNHRRERDQSPSPFSPAGGGGGAGPGSPYQQQQHSPTGNTQQQQQQHQQPSNSPHLSFTNLATTQAAVTTFNPLPTLGPHNATDYRQPPNPPSPRSSPGLLSSVSATDLHSSAPASPIRQQQQAHQQQQQQQQAQQQQQQFDNSYNSLNTSFHNQFEIFSLGDSNSSPEQQGFANNFVALDFDDLSGGGGGGPSGGGGSNGGGLTNGYNKPEMLDFSELSGSPEASGNNNHMRRGVSNLNNNGLSNGVVGSTHNGSTNLNGAGNNNSSSGGGTAQDPLGITTSPVPSPLGCPSSPLPIPIPMSAQSSPQQQHHHHQQQQQQHHQQQHHQQQQLSLSLHHSPHHSPMHSPHHGNSPLSSSSPVSHNACSNSNVVMNHQQQQQQHHHQQHHHQGSSQSHTPTTANIPSIIFSDYSSNADYTREIFDSLDLDLGQMDVAGLQMLSDQNPIMIADPNIEDSFRRDLNXYYEEAVAAIESGVLLEEDYQALLGSEALADEQVVTVEAAGAAAAVVTVEEAATVSEKDKKDLEVVELLVSGVMDDLVDSSDLDEEVRNFFF
Protein: Protein inturned (Inturned planar cell polarity effector homolog) (PDZ domain-containing protein 6) (Q059U7)
Organism: Mus musculus (Mouse)
Function: Plays a key role in ciliogenesis and embryonic development. Regulator of cilia formation by controlling the organization of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules. Plays a key role in definition of cell polarity via its role in ciliogenesis but not via conversion extension. Has an indirect effect on hedgehog signaling. Proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20067783}. Cell surface {ECO:0000250|UniProtKB:Q2I0E5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29038301}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:29038301}. Note=Enriched at the apical surface in ciliated cells (By similarity). Localizes at the transition zone, a region between the basal body and the ciliary axoneme (PubMed:29038301). Recruited to the centriole in a TTBK2-dependent manner (PubMed:29038301). {ECO:0000250|UniProtKB:Q2I0E5, ECO:0000269|PubMed:29038301}.
Interaction partners:
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Ciliogenesis and planar polarity effector 2
- Protein fuzzy homolog
- Mitotic spindle assembly checkpoint protein MAD2A
- Intraflagellar transport protein 43 homolog
- Cell division cycle protein 16 homolog
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 5
Sequence:
MAGLARGDSRGRPPELPGDLSSQEEEEEEGDSDAGASSLGSYSSASSDTDVEPEWLDSVQKNGELFYLELSEDEEESLLPETQTANHVNHVRFSDKEVIIEEDDSRERKKSEPKLRRFTKILKSKSLLPRRHHKKSSSNNGPVSILKHQSSQKTGVTVQQRYKDVTVYINPRKLTAIKAREQVKLLEVLVGIIHQTKRSWKRSAKQADGERLVVHGLLPGGSAMKSGQVLVGDVLVAVNDVDVTSENIERVLSCIPGPMQVKLTFENAYAVKRETAQPQKKKAQSSTQDLVKLLCGSEADAVQHSTLSIPHISMYLTLQLQSEAAREEQEILYHYPVSEASQKLKSVRGIFLTLCDMLESVTGTQVTSSSLHLNGKQIHVAYLKESDKLLLIGLPAEEVPLPQLRNMIEDVAQTLKFMYGSLDSAFCQVENAPRLDHFFSLFFERALRPGKLHLSGSPSAQQYAAASAVLLDNLPGVRWLVLPQELKVELDTALSDLEAADFEELSEDYYDMRRLYTILGSSLFYKGYMVCSHLPKDDVIEIAAYCRQHCLLPLAAKQRIGQLIIWREVFPRHHLQPPSDSDPEAFQEPEGRYFLLVVGLRHYLLCVLLEAGGCASKATGNPGPDCIYVDQVRATLHQLEGVDSRIEEQLATSPGPCLSCADWFLAAPREKADSLTTSPILSRLQGPSKTAASPTCRRTFFSDYSFKARKPSPSRIGGGREPTEGEESAGLSPHATPDAVRKQRESEGSDDNVALLKLARKKSTLPNPFHLGTSKKELSEKELEVYDIMKLTSGPENTLFHYVALETVQGIFITPTHEEVAQLGGSVHSQLIKNFHQCCLSIRAFFQQTLKEEKKKALSDGEHSEPTNSVSSLSPVKEHGVLFECSPENWTDQKKTPPVMSYWVVGRLFLNPKPQELYVCFHDSVSEIAIEMAFKLFFGLTL
Protein: Proline-, glutamic acid- and leucine-rich protein 1 (Modulator of non-genomic activity of estrogen receptor) (C9JFV4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLLPSLSPRVQPAFTQCARPQPPPHAPSPVGGRRGVFASSRHATTGTRGKMAAAVLSGPSAGSAAGVPGGTGGLSAVSSGPRLRLLLLESVSGLLQPRTGSAVAPVHPPNRSAPHLPGLMCLLRLHGSVGGAQNLSALGALVSLSNARLSSIKTRFEGLCLLSLLVGESPTELFQQHCVSWLRSIQQVLQTQDPPATMELAVAVLRDLLRYAAQLPALFRDISMNHLPGLLTSLLGLRPECEQSALEGMKACMTYFPRACGSLKGKLASFFLSRVDALSPQLQQLACECYSRLPSLGAGFSQGLKHTESWEQELHSLLASLHTLLGALYEGAETAPVQNEGPGVEMLLSSEDGDAHVLLQLRQRFSGLARCLGLMLSSEFGAPVSVPVQEILDFICRTLSVSSKNISLHGDGPLRLLLLPSIHLEALDLLSALILACGSRLLRFGILIGRLLPQVLNSWSIGRDSLSPGQERPYSTVRTKVYAILELWVQVCGASAGMLQGGASGEALLTHLLSDISPPADALKLRSPRGSPDGSLQTGKPSAPKKLKLDVGEAMAPPSHRKGDSNANSDVCAAALRGLSRTILMCGPLIKEETHRRLHDLVLPLVMGVQQGEVLGSSPYTSSRCRRELYCLLLALLLAPSPRCPPPLACALQAFSLGQREDSLEVSSFCSEALVTCAALTHPRVPPLQPMGPTCPTPAPVPPPEAPSPFRAPPFHPPGPMPSVGSMPSAGPMPSAGPMPSAGPVPSARPGPPTTANHLGLSVPGLVSVPPRLLPGPENHRAGSNEDPILAPSGTPPPTIPPDETFGGRVPRPAFVHYDKEEASDVEISLESDSDDSVVIVPEGLPPLPPPPPSGATPPPIAPTGPPTASPPVPAKEEPEELPAAPGPLPPPPPPPPPVPGPVTLPPPQLVPEGTPGGGGPPALEEDLTVININSSDEEEEEEEEEEEEEEEEEEEEEDFEEEEEDEEEYFEEEEEEEEEFEEEFEEEEGELEEEEEEEDEEEEEELEEVEDLEFGTAGGEVEEGAPPPPTLPPALPPPESPPKVQPEPEPEPGLLLEVEEPGTEEERGADTAPTLAPEALPSQGEVEREGESPAAGPPPQELVEEEPSAPPTLLEEETEDGSDKVQPPPETPAEEEMETETEAEALQEKEQDDTAAMLADFIDCPPDDEKPPPPTEPDS
Protein: Cip1-interacting zinc finger protein (CDKN1A-interacting zinc finger protein 1) (Nuclear protein NP94) (Zinc finger protein 356) (Q9ULV3)
Organism: Homo sapiens (Human)
Function: May regulate the subcellular localization of CIP/WAF1.
Subcellular location: Nucleus.
Interaction partners:
- Cyclin-dependent kinase inhibitor 1
- Anoctamin-3
- THAP domain-containing protein 1
- DNA replication licensing factor MCM3
- Enhancer of rudimentary homolog
- Guanine nucleotide-binding protein G
Sequence:
MFSQQQQQQLQQQQQQLQQLQQQQLQQQQLQQQQLLQLQQLLQQSPPQAPLPMAVSRGLPPQQPQQPLLNLQGTNSASLLNGSMLQRALLLQQLQGLDQFAMPPATYDTAGLTMPTATLGNLRGYGMASPGLAAPSLTPPQLATPNLQQFFPQATRQSLLGPPPVGVPMNPSQFNLSGRNPQKQARTSSSTTPNRKDSSSQTMPVEDKSDPPEGSEEAAEPRMDTPEDQDLPPCPEDIAKEKRTPAPEPEPCEASELPAKRLRSSEEPTEKEPPGQLQVKAQPQARMTVPKQTQTPDLLPEALEAQVLPRFQPRVLQVQAQVQSQTQPRIPSTDTQVQPKLQKQAQTQTSPEHLVLQQKQVQPQLQQEAEPQKQVQPQVQPQAHSQGPRQVQLQQEAEPLKQVQPQVQPQAHSQPPRQVQLQLQKQVQTQTYPQVHTQAQPSVQPQEHPPAQVSVQPPEQTHEQPHTQPQVSLLAPEQTPVVVHVCGLEMPPDAVEAGGGMEKTLPEPVGTQVSMEEIQNESACGLDVGECENRAREMPGVWGAGGSLKVTILQSSDSRAFSTVPLTPVPRPSDSVSSTPAATSTPSKQALQFFCYICKASCSSQQEFQDHMSEPQHQQRLGEIQHMSQACLLSLLPVPRDVLETEDEEPPPRRWCNTCQLYYMGDLIQHRRTQDHKIAKQSLRPFCTVCNRYFKTPRKFVEHVKSQGHKDKAKELKSLEKEIAGQDEDHFITVDAVGCFEGDEEEEEDDEDEEEIEVEEELCKQVRSRDISREEWKGSETYSPNTAYGVDFLVPVMGYICRICHKFYHSNSGAQLSHCKSLGHFENLQKYKAAKNPSPTTRPVSRRCAINARNALTALFTSSGRPPSQPNTQDKTPSKVTARPSQPPLPRRSTRLKT