wanglab/gogpt-training-data huggingface dataset:
Protein: High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (EC 3.1.4.35) (O76083)
Organism: Homo sapiens (Human)
Function: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (By similarity).
Subcellular location: [Isoform PDE9A1]: Cell projection, ruffle membrane {ECO:0000269|PubMed:17090334}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17090334}. Golgi apparatus {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25799991}.; SUBCELLULAR LOCATION: [Isoform PDE9A2]: Cell projection, ruffle membrane {ECO:0000269|PubMed:17090334}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17090334}.; SUBCELLULAR LOCATION: [Isoform PDE9A3]: Cytoplasm {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}.; SUBCELLULAR LOCATION: [Isoform PDE9A17]: Cytoplasm {ECO:0000269|PubMed:17090334}. Endoplasmic reticulum {ECO:0000269|PubMed:17090334}.
Interaction partners:
- Adenine phosphoribosyltransferase
- GMP reductase 1
- Inosine triphosphate pyrophosphatase
- Hypoxanthine-guanine phosphoribosyltransferase
- Guanylate kinase
- GMP synthase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Guanylate cyclase soluble subunit alpha-2
- Atrial natriuretic peptide receptor 1
- Guanylate cyclase soluble subunit beta-1
Sequence:
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
Protein: Tip elongation aberrant protein Tea4 (Cell polarity protein tea4) (Win1-interacting SH3 domain protein) (O60132)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cell polarity factor essential for the bipolar localization and function of structures containing the cell-end marker tea1 during the normal cell cycle. Regulates cell polarity in complex with tea1 and together with the stress signaling MAPK cascade, contributes to cell polarity maintenance under stress conditions. Required for the localization of for3 at the cell tip specifically during initiation of bipolar growth. During the new end take off (NETO), formation of a protein complex that includes tea1, tea4 and for3 is necessary and sufficient for the establishment of cell polarity and localized actin assembly at new cell ends.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:15936270}. Note=Through it's binding with tea1, is transported by the cytoplasmic microtubule system and is localized at cell tips, microtubule plus ends and cytoplasmic dots.
Interaction partners:
- Tip elongation aberrant protein 1
- DYRK-family kinase pom1
- Serine/threonine-protein phosphatase PP1-1
- Formin-3
- Tip elongation aberrant protein 3
- Actin-interacting protein 3 homolog
- Rho guanine nucleotide exchange factor gef1
- Probable Rho-type GTPase-activating protein 4
- Tip elongation protein 1
- Serine/threonine-protein phosphatase PP1-2
Sequence:
MLHMNSASSADSMEIMESHFDPTQQNDSTIIESRYSPEEYLEQSFEIQRIISGENSEPQTVASQEISDSQEEDTTLTSSQFEDCGTEYNEVVEDDEFRSEDEDDFMDEEEEYALYEAELSSSPSIHEEVIDCNFVHAIRGFEATVEGQVDATKGDMMILLDDSNSYWWLVKMCKNLAIGYLPAEYIETPSERLARLNKYKNSETSNSQQSVTLPPLDIVEKTLEAPSPNFRIKRVTFTCSSNSSDDEMDSENDYEAMVNRTVAENGLEIEFSDSSDSSLSAEYRSESEDHVTDSPAYVDLTELEGGFNQFNSTSFQSTSPLGLEIVETEINGSSTTADSKNSHSPYSKFSSAYPDAENSNISKINISIAGNKELYGNATQSDPSLYSTWIANKHKTASSATVDSPLRRSLSVDAMQSNASFSSYSSTSNTDKSLRPSSYSAVSESSNFTHDVSRDNKEISLNAPKSIIVSQSDSFDTSNVTQDAPNDVEKEPISGQMPNNLSVQSLKQLEVYPIRHSVSIEMPSEKLLSPRLYSSSTPSSPTKGFQKDDEEDSENRKQADKVELSPSSLLRQMSLPVDSSSQSDAQCTTSSVYITAERKAFSQSSIDLSTLSNHHVNNEINRRSFAGGFTSLADELSEMRELLHESPAPLECNEEMVIPTPELDASSAIPSSSISHDEDLLPRKNTEESTSSSSFSSLITSPASLQYDENPFKQSVVAELNNNSSSVPFVDSAHASDIHAYDNDHVSTKNKEFNRRLREFILDPDSLSGLYWSVKSAGVRASRRVSRNIEGESVSSDLDDIFANVLKGLSDEMASLLNTNR
Protein: ROP-interactive CRIB motif-containing protein 7 (F4JLB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASFTNLSLLLLFLFTATLITSQQSDDDENASPQLALDPSEQEAVYRVLDSVNSAISWRTIFPDDICASPPDGVVCDNLYASQNGVATSVHVTEFHLGYLSDYTQNPPCSSNATLDPLLFTAFKHLRKLFFYKCFTDARASLPLTVPEDFGSVLEELVFIENPSLVGEIGAMIGNFTKLRRLVLTGNGFHGSIPGQIGDLVSLEEITLSRNSLTGGFPANATSRLKNLKVLDFSHNFINGNAPDSIGDLTELLKLDLSFNEFTGEVPSGVGNLKKLVFLDLSYNRFGNFGVPLFLAEMSSLREVHLSGNKLGGRIPAIWKNLEGISGIGFSRMGLEGNIPASMGSSLKNLCFLALDNNNLDGQIPEEFGFLDSAREINLENNNLTGKAPFSDSFRDRIGKKLKLSGNVNLQVKNSDPHLAGRALYSSARKVLPLIYFPATLLALYISITQ
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (O59924)
Organism: Candida albicans (Yeast)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00445}.
Interaction partners:
Sequence:
MVKAVAVVRGDSKVQGTVHFEQESESAPTTISWEIEGNDPNALRGFHIHQFGDNTNGCTSAGPHFNPFGKQHGAPEDDERHVGDLGNISTDGNGVAKGTKQDLLIKLIGKDSILGRTIVVHAGTDDYGKGGFEDSKTTGHAGARPACGVIGLTQ
Protein: Platelet glycoprotein 4 (Glycoprotein IIIb) (PAS IV) (PAS-4) (Platelet glycoprotein IV) (Q6DHC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}.
Interaction partners:
- Thrombospondin-1
- Thrombospondin 1a.
- Thrombospondin 2a.
- Thrombospondin 2b.
- Apolipoprotein Ba.
- Thrombospondin-3a
- Thrombospondin-4-B
- Cartilage oligomeric matrix protein
- Thrombospondin-3b
- Thrombospondin 4a
Sequence:
MTCCDQRCALITGAVLGALIALLGGILIPVGDMIIKNTVHKETVLENGTLAFDTWTSVDIAMYRQFWIFNVENPDKVLSEGSKPVLVQKGPYTYRVRYIPKTNITFNDNNTVSFVLPAGATFEPSMSVGSEEDVFTSLNLAVAGVYRLIGPKLADWLIRSSGSSLFQNRTVKELLWGYKDPMLNSLVGAFYPYNGTVDGPYTVFTGKDDINKVAIIERWQGETSVNYWNDSYCDKINGSDGSSFHPFLDKKEPLYFFSPDICRSISAEYEATVNLKGIDVYRYLLPVDALASPVSNPDNMCYCTDHEITRNCTLAGLLDITSCKGTPVFISLPHFLYASIELQQGVVGMNPNLDEHSIFLDVEPITGFTLRFSKRLQVNMMYGPSDDIALLNKIKEHTIIPILWLNETAVLDDETAKMFKNELISRMDMLEGLQIGLLVTGSAIFLGCMIGLIVVCSKPSKTNLS
Protein: T. brucei spp.-specific protein (Q57XL3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDGEGCTAERGEKEFDPIFDEAEKHHRRWLQRRTVGDDGNSDVVEEDRGVTTEFEELDESDVEMAVRREAENNKDGDIEVVNEEASPEPEAVEDDVKDDVSGKRFRKCDAVAARAWLKTLGTEDLAHDDNGAPQSIDAADEGEGEKSPSSVRSPVARGDVVGKFHARSLSREGRGTSSVIVDSAVEKENFREIISTLAPLKPLPTGIRPKTTQSSGMGDSGLGSDSGKVEANSSNQTNCMKEAEEEVGDHVEAIREGRGEQSDVGTEGSKTEESIGVEVEGDGGNETTGEEMDLR
Protein: HD/PDEase domain-containing protein (Q727L7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Antitoxin SocA-like Panacea domain-containing protein
Sequence:
MVKTVNWRDLLEPQTKIRDPLYGYIWVTDDELQIIDTPIFQRLRRVNQLALTKYVYPTAEHSRFVHSLGAMHCATQIFTGILNNTHSYHGIRAIDSANMLRRLRYAALLHDIGHIAFSHAAEKLILNPLQHEHLGQFIIANYSPISSILGEHIKPVISILADSVTQDNRLLHQIISGHLDADRADYLMRDSHACGVKYGEYDFERYMQAFGAINESNELKLFVHERDIFVIESFLVARHHYNMQVPYHRTRMGYDIILGRFLKEFLPKCDDAKLGLTVEEGAYTKVDLQKFEFFDDYSVFNHIKHEARTGNLWANMLLRQGHLCPVYDTTDSVDRGGKVFKKIIRRLKAKNFVEDDDFFQCRKEITASKLISTDEKENSLADTSRETIYVRTKSGKLVDIVKHSNIVRALRPVTIYRIYTSQKRKSEAEAVIADVCRKTQVDRRG
Protein: Alpha-defensin 1 (Cryptdin-1) (Defensin-related cryptdin peptide) (P11477)
Organism: Mus musculus (Mouse)
Function: Probably contributes to the antimicrobial barrier function of the small bowel mucosa. Has antibacterial activity against attenuated mutants of S.typhimurium.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MKKLVLLFALVLLGFQVQADSIQNTDEETKTEEQPGEEDQAVSVSFGDPEGTSLQEESLRDLVCYCRSRGCKGRERMNGTCRKGHLLYTLCCR
Protein: Meiosis-specific protein ISC10 (P32645)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Indispensable for spore formation.
Interaction partners:
- Spore wall maturation protein DIT1
Sequence:
MDVDERLHQDENQTHPFSQKKSSSFLIKEKAATKSKDLEHIRLRDLNFNHRKKLDDKKLAKQIPVKANFKKPNEIEARANLNSNELTDINLDYIPDSPSIEKISGPEDSIVVTPRNIIHLQSDSDIILEECEHNYDCSPFYRLFNYENRIEPDDYEAIINAIITDEIAGTYPVFERELEYQELKSLVRKRDYIMYYFLSRDYRGFFQLKEERTLFYRYPSIAYTSPLRYLDNGSETEQFTGDDDEELQSFDFENTSSVRTLDSNIWR
Protein: histone deacetylase (EC 3.5.1.98) (E5RQ39)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDTKDDFPLRKTESSVSSSSPGSGPSSPNNGPAGNVTENEASVLPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLSASNSLKDKQKCETQMLRQGVPLPGQYGSGIAASSSHAHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMEERATSKDSGTGKDSSACVEDTLGQVGAVKVKEEPVDSDEDAQMQEMECGEQAAFMQQTPLLESSHTRALSVHQARLAAAGIDGLEKHGLLSRTHSSPAPSMSPHPAADCPRQPASATGIAYDCLMLKHQCICGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTSPLDGQKLDPRTLLGDDSRKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESAAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGVGLGEGYNVNIAWTGGLDPPMGDVEYLEAFRTVVMPVAREFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLANGRVALALEGGHDLTAICDASEACINALLGNE
Protein: Cadherin domain-containing protein (Q8BY10)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
ITVSDKDTDVNGKVICFIEREVPFHLKAVYDNQYLLETSSLLDYEGTKEFSFKIVASDSGKPSLNQTALVRVKLEDENDNPPIFNQPVIELSVSENNRRGLYLTTISATDEDSGKNADIVYQLGPNASFFDLDRKTGVLTASRVFNREEQERFIFTVTARDNGTPPLQSQAAVIVTVLDENDNSPKFTHNHFQFFVSENLPKYSTVGVITVTDEDAGENKAVTLSILNDNENFVLDPYSGVIKSNVSFDREQQSSYTFDVKATDGGQPPRSSTAKVTINVMDVNDNSPVVISPPSNTSFKLVPLSAIPGSVVAEVFAVDIDTGMNAELKYTIVSGNNKGLFRIDPVTGNITLEEKPAPTDVGLHRLVVNISDLGYPRALHTLVLVFLYVNDTAGNTSYIYDLIRRTMETPLDRNIGDSGQPYQNEDYLTIMIAIVAGAMVVIVVIFVTVLVRCRHASRFKAAQRSKQGAEWMSPNQENKQN
Protein: Serine/threonine-protein kinase CBK1 (EC 2.7.11.1) (Cell wall biosynthesis kinase 1) (Q5AP53)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Serine/threonine-protein kinase required for wild-type hyphal growth and transcriptional regulation of cell-wall-associated genes. Involved in the biofilm formation through phosphorylation of the master regulator of biofilm formation BCR1.
Subcellular location: Bud neck {ECO:0000269|PubMed:21593210}. Cell tip {ECO:0000269|PubMed:21593210}. Note=In yeast cells, localizes to the cell cortex of small- and medium-budded cells and to the bud neck in large-budded cells. During hyphal growth, is present at the tip of hyphae and in the region of the septum.
Interaction partners:
- CBK1 kinase activator protein MOB2
- Virulence protein SSD1
- Cas4p
- Tyrosine-protein phosphatase CDC14
- Mob1p
- Cell wall transcription factor ACE2
- Sog2p
- Hym1p
- Cell division control protein 42 homolog
- U3 small nucleolar RNA-associated protein 25
Sequence:
MNFDQLTDEQKQQLYLQHLQQQQQLQQQQQQLQQQQHQLQQQQQSYHLQQQQAAYQQQNQAQLQQDDSYMDEDTSELINQPPVQLDHGSPIRQQPQMSAFMPSPRFAQSESFDNHLNVDPNNTERFTSMDSMNFQPPASTFTQLGNGSSTNLSEISSGQNSLLSNHSVNNLPTALTSDTSPPVQQHPQFQPQQQQQQQQPQQQQIFQQQQQQQQQQQQPQQSRAVVNQSVSTEAANSDMTGSNTKYVYFERKPNLLSKTTQDKAASIKLTLENYYTSSVSHAIERNQRRLELENKIANEDIGSSEERKNRQLQNLGKKESQFLRLKRTKLALEDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFNKDQLAHVKAERDVLAGSDSPWIVALYYSFQDSQYLYLIMEFLPGGDLMTMLIRWEVFTEDITRFYIAECVLAIEAIHKLGFIHRDIKPDNILIDNRGHVKLSDFGLSTGFHKTHDSNYYNKLLEKEPSNTHLQPNQLTSGRNSVMVDAIHLTMSNRQTMQTWRKSRRLMAYSTVGTPDYIAPEIFIHQGYGQECDWWSLGAIMFECLIGWPPFCSENPHDTYRKILNWQESFQIPEDVHLSPEAEDLIKRFLTSAENRIGRYGGAEEIKQHPFFRGVDWDSIRDVQAPFVPRLSSMTDTRHFPTDDLASVPDNPAMSKAMEQRELDAKNGGGRKNPKEDLPFIGYTYSRFDYLTRKNAL
Protein: 2'-5'-oligoadenylate synthase 3 ((2-5')oligo(A) synthase 3) (2-5A synthase 3) (EC 2.7.7.84) (p100 OAS) (p100OAS) (Q9Y6K5)
Organism: Homo sapiens (Human)
Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- 2'-5'-oligoadenylate synthase 2
- 2'-5'-oligoadenylate synthase 1
- Interferon-induced GTP-binding protein Mx1
- Antiviral innate immune response effector IFIT1
- Signal transducer and activator of transcription 1-alpha/beta
- Interferon-induced, double-stranded RNA-activated protein kinase
- 2-5A-dependent ribonuclease
- Interferon alpha-inducible protein 6
- Antiviral innate immune response receptor RIG-I
- Interferon-induced protein with tetratricopeptide repeats 3
Sequence:
MDLYSTPAAALDRFVARRLQPRKEFVEKARRALGALAAALRERGGRLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYVDQRARRAEILSEMRASLESWWQNPVPGLRLTFPEQSVPGALQFRLTSVDLEDWMDVSLVPAFNVLGQAGSGVKPKPQVYSTLLNSGCQGGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQVCLQGLWKETLPPVYALELLTIFAWEQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLAQEAASCYDHPCFLRGMGDPVQSWKGPGLPRAGCSGLGHPIQLDPNQKTPENSKSLNAVYPRAGSKPPSCPAPGPTGAASIVPSVPGMALDLSQIPTKELDRFIQDHLKPSPQFQEQVKKAIDIILRCLHENCVHKASRVSKGGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPRRAEILDEMRAQLESWWQDQVPSLSLQFPEQNVPEALQFQLVSTALKSWTDVSLLPAFDAVGQLSSGTKPNPQVYSRLLTSGCQEGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGKGPAPASLPPAYALELLTIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHGSWELLAQEAAALGMQACFLSRDGTSVQPWDVMPALLYQTPAGDLDKFISEFLQPNRQFLAQVNKAVDTICSFLKENCFRNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGNKRAEIISEIRAQLEACQQERQFEVKFEVSKWENPRVLSFSLTSQTMLDQSVDFDVLPAFDALGQLVSGSRPSSQVYVDLIHSYSNAGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKISKGRGSLPPQHGLELLTVYAWEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNARWDLLAKEAAACTSALCCMGRNGIPIQPWPVKAAV
Protein: Large ribosomal subunit protein eL15 (60S ribosomal protein L15) (O17445)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL43
- Small ribosomal subunit protein eS4
- Large ribosomal subunit protein P2
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein eL20
- Ubiquitin-ribosomal protein eL40 fusion protein
- 40S ribosomal protein S24
Sequence:
MGAYRYMQELYRKKQSDVMRYLLRIRVWQYRQLTKLHRSPRPTRPDKARRLGYRAKQGFVIYRIRVRRGGRKRPVPKGCTYGKPKSHGVNQLKPYRGLQSIAEERVGRRLGGLRVLNSYWIAQDASYKYFEVILIDTHHSAIRRDPKINWICKHVHKHRELRGLTSAGKSSRGIGKGYRYSQTIGGSRRAAWKRKNREHMHRKR
Protein: Protein PAC2 (P39937)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for viability in the absence of the kinesin-related CIN8 mitotic motor. Seems to be involved in the assembly of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Chromosome instability protein 1
- Tubulin-specific chaperone A
- Tubulin-specific chaperone B
- Tubulin-specific chaperone C
- GTP-binding protein CIN4
- Tubulin beta chain
- Nuclear distribution protein PAC1
- Tubulin alpha-3 chain
- Tubulin alpha-1 chain
- Kinesin-like protein CIN8
Sequence:
MTYEIGDRLKIGGYFCTIKFIGVIKPWPSVKAYGVEWDDHSRGKHSGTIDDIHYFDVQIPNSGSFLKESKIKSPGVRRITFYEALSEKYGGSSNNINDLSIGNKRVEGLGFDELNARNKNYKKLRKIALRDSDVAILFQNQDELNRVIQNCVNVKDLDLSLNLFTNINSLCEFIEPLKNLESLNISQNKLLSGWDNLKEYDLSHIKTLRLSSCGLSYKHIGKLLKSFRTLKMLDLSYNNLTSAGIQNFENEIPCTLEELNISGNNLISFPLFPKNLTLKGLNVSNNQISRAPSIAIYSVESLDITDNKFKERSLIDDLNKTFPSLKNIHLSGNEFNYNGNYINVEEQATFYEVLARFDRVMVLNGSICDVKTRREAEMFFVSKVMNNELSYDTNLPRWSSLIKSYEIDMSKLSFNNERETRQSLVLKIKIRAGKKPSSDLDYWVLPSFTVRYVKSVICRKLNFDILNVKLFHENSEGMINEIKYNFRPISDFNVVNGDIIHVSSPVNNKSIQKVNSPS
Protein: Protein raptor homolog (Q55BR7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Protein LST8 homolog
- Ras-related GTP-binding protein A
- Ras-related GTP-binding protein
- Ragulator complex protein LAMTOR5 homolog
- Serine/threonine-protein kinase tor
- Serine/threonine-protein kinase atg1
- TAP42-like family protein
- Eukaryotic translation initiation factor 4E-1A-binding protein homolog
- Autophagy-related protein 101
- Protein pianissimo A
Sequence:
MDKSYNFSSSNLANSSGLHNSINSNNVNGVNNINNNNNNNNNNNNNNNNNNNNENVNNHNNVSNISNTHQQAKKKEKYNNNNNKNKPFFGEERHKDNATPDVQKTKIAKWRMRERMKTVSVALVLCLNIGVDPPDVIKTFPCARMECWFDPSTQPPQKALDLIGKTLQAQYEKWQSKARYKQSLDPTVEEVKKLCLSLRRNAKDERVLFHYNGHGVPKPTTNGEIWVFNRNFTQYIPLSIYELQTWMGTPSIYVFDCSAAGLIINWFNQFAEQRDKELERFSGNNQNNNQNNNQNSNQNNQNNTTNSTNGNTNGNNQQNNNNSNNNSSNNSNTNSPNMGSSNSVNNNQSGSSSSSSHQRDCILLAACSANEILPMNPDFPADMFTACLTTPIRIALRWFCSHSILTGITADMLDKIPGNLSSRRTPLGELNWIFTAVTDTIAWNVLPRHLFQKLFRQDLLVASLFRNYLLAERIMRSANCTPISCPRLPPTYQHAMWQAWDLAVDLVISQLPTLLADPNAEFKSSPFFTEQLTAFEVWLEFGSEHKDPPAQLPIVLQVLLSQAHRLRALVLLGKFLDLGPWAVNLALCVGIFPYVLKLLQSPAGDLRHILVFIWAKILALDKSCQLDLVKENGHAYFISVLSSPQIPADQRTMSAFVLSTICNNCRPGQNACLIGNLLPICLSQLNDPDPMVRRWMILCMAKMWENFEEAKWAAIKENAHEKLCLLLTDVSPEVRASAVVALGELIGGAEGSEQRTNIELNLALTLAVITADCSPMVRKELVISLSRIVSSYESNFVQVAQEIAQEERLRAVLEAKRLEESRKSKKRASVPKISDADHLNNNSDLYGNGSQSSVYGCLWKIILNLCTDPFDQVANRAQSIVKRISSKFSMEELMSHNLINRTNFNFNNLNGSMNGLNSSGSGFLNSSNGNLGASMNGSNLNSSNNNLGGSSGGGFGLNNSNSSIRNTFVNISRITNRDPRSPTKTKLGNQRSPILTSSTNNVGTNLNGNQLNLNNNNINNGNINNNNNNNSSINNNGNNINNNGNGNNNNINNNNGLGNQLANTFQSLSLSSGLGGNKTNKMSQSISSMNSSSQSLQNDFLMVSDSMPFEEDELYSDYYEWSCNYFSKPMMQSTGEDFESFESIEKKWKRQRNEMIIQESKEAVQNIIQQPPKSFSQMTIFAEPNGQPISHLQFHPFDNILVVSDGLENISVWNYDDGQRINTFNNCNMSGTRITSMKLVNDYDPSMIITAADDGVVRIWRGYESNDTLKMVSSWRAFPEFATTGNDPIGRLVLDWKGDSGLVLVSGETPDSPKIRIWDVERELGVQDIFIGTESVVTCMANEKRGPLFSAGFSDGLVKLFDQRIPGKYSCVSTLTEHKSYIVNVSMPASLGGKTVVSGSSTGEIKFWQHSYECSSTTIHNNDVISSFSVHEYAPLIACGSQNQRIKIMNFTGEDVCTIRYHDGFLGQRIGPVSCVAFHPYNILMGAGATDSIISIYNGDSKSKSNVDW
Protein: DNA repair protein XRCC1 (X-ray repair cross-complementing protein 1) (P18887)
Organism: Homo sapiens (Human)
Function: Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto-poly-ADP-ribosylated PARP1, limiting its activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:28002403}. Chromosome {ECO:0000269|PubMed:14500814}. Note=Moves from the nucleoli to the global nuclear chromatin upon DNA damage (PubMed:28002403). Recruited to DNA damage sites fowwing interaction with poly-ADP-ribose chains (PubMed:14500814). {ECO:0000269|PubMed:14500814, ECO:0000269|PubMed:28002403}.
Interaction partners:
- DNA ligase 3
- Aprataxin and PNK-like factor
- Aprataxin
- Bifunctional polynucleotide phosphatase/kinase
- Poly [ADP-ribose] polymerase 1
- DNA repair nuclease/redox regulator APEX1
- DNA polymerase beta
- N-glycosylase/DNA lyase
- DNA ligase 1
- Poly [ADP-ribose] polymerase 2
Sequence:
MPEIRLRHVVSCSSQDSTHCAENLLKADTYRKWRAAKAGEKTISVVLQLEKEEQIHSVDIGNDGSAFVEVLVGSSAGGAGEQDYEVLLVTSSFMSPSESRSGSNPNRVRMFGPDKLVRAAAEKRWDRVKIVCSQPYSKDSPFGLSFVRFHSPPDKDEAEAPSQKVTVTKLGQFRVKEEDESANSLRPGALFFSRINKTSPVTASDPAGPSYAAATLQASSAASSASPVSRAIGSTSKPQESPKGKRKLDLNQEEKKTPSKPPAQLSPSVPKRPKLPAPTRTPATAPVPARAQGAVTGKPRGEGTEPRRPRAGPEELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSQRYLMAGPGSSSEEDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQKPPTPEETKAASPVLQEDIDIEGVQSEGQDNGAEDSGDTEDELRRVAEQKEHRLPPGQEENGEDPYAGSTDENTDSEEHQEPPDLPVPELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNEKQKLLPHQLYGVVPQA
Protein: Peroxisomal membrane protein PEX14 (Peroxin-14) (AtPEX14) (Peroxisome biogenesis protein 14) (Pex14p) (Protein PEROXISOME DEFECTIVE 2) (Q9FXT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:11060021}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q642G4}.
Interaction partners:
- Peroxisome biogenesis protein 5
- Peroxisome biogenesis protein 12
- Peroxisome biogenesis protein 7
- Peroxisome biogenesis factor 10
- Peroxisomal ATPase PEX6
- Peroxisomal membrane protein 13
- Peroxisome biogenesis protein 19-2
- Peroxisome biogenesis protein 19-1
- Peroxisome biogenesis protein 16
- Peroxisomal ATPase PEX1
Sequence:
MATHQQTQPPSDFPALADENSQIPEATKPANEVQQATIAQDPPTSVFKNSEPIREDQIQNAIKFLSHPRVRGSPVIHRRSFLERKGLTKEEIDEAFRRVPDPPPSSQTTVTTSQDGQQAVSTVQPQAMQPVVAAPAPLIVTPQAAFLSRFRWYHAILAVGVLAASGAGTAVFIKRSLIPRFKSWVQRIMLEEETDPLKKADAKPSLAEEAVAAAKAASAAASDVARVSQEMMITKNEERKYFEDLTHLLGVQVQEMKSLSNNIRKLEGQSNNIPKIYSADQEVYNGSVTTARKPYTNGSNVDYDTRSARSASPPAAPADSSAPPHPKSYMDIMSMIQRGEKPSNIREINDMPPNPNQPLSDPRIAPKSKPWDYGQAPQDESSNGQWWQQKNPRSTDFGYETTTAARFTANQNETSTMEPAAFQRQRSWVPPQPPPVAMAEAVEAIRRPKPQAKIDQEAAASDGQSGVSDELQKITKFSESGGDGSGGIKIAEIQEETEQQHISQEGN
Protein: Somatostatin receptor subtype 3 (Q6YEX9)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDTPGYPSLVPTTSEPGNASSAWSLDAVLGNGSSAPSVAGLAVRGILIPLVYLVVCVVGLLGNSLVIYVVLRQTASPSVTSIYILNLALADELFMLGLPFLAAQNALSYWPFGSLMCRLVMAVDGINQFTSIFCLTVMSVDRYLAVVHPTRSARWRTAPVARMVSAAVWVASAVVVLPVVVFSGVPRGMSTCHMQWPEPAAAWRAGFIIYTAALGFFGPLLVICLCYLLIVVKVRSAGRRVRAPSCQRRQPSERRVTRMVVAVVALFVLCWMPFYVLNIINVVCPLPEEPAFFGLYFLVVALPYANSCANPILYGFLSYRFKQGFRRVLLRPSRRVRNQEPPVGPPEKTEEEEEDGGEHEKGGAGNQGERKEMNGRVIQITQPGPSGQERPPSGTATKEHQFLPQEPSAGDKSGPLHISYL