wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisome biogenesis protein 20 (Peroxin-20) (Q6C6R8)
Organism: Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Function: Coreceptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase. Acts via its interaction with PEX7, promoting association between PEX7 bound to cargo proteins and the PEX13-PEX14 docking complex. PEX20 along with PEX7 and PTS2-containing cargo proteins are tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex. PEX20 coreceptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (By similarity). Also mediates peroxisomal import of proteins that do not contain PTS1- or PTS2-type peroxisomal targeting signals, such as acyl-CoA oxidases (Aox) izozymes. Import of acyl-CoA oxidases (Aox) izozymes is independent of PEX7.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9679140}. Peroxisome matrix {ECO:0000269|PubMed:9679140}. Note=Cycles between the cytosol and the peroxisome matrix. Following binding to cargo proteins in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 retrotranslocation channel. Cys-4 of PEX20 is then monoubiquitinated by PEX2, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by release of bound cargo in the peroxisome matrix (By similarity). {ECO:0000250|UniProtKB:P50542, ECO:0000250|UniProtKB:Q2VUH8}.
Interaction partners:
- YALI0E15818p
Sequence:
MASCGPSNALQNLSKHASADRSLQHDRMAPGGAPGAQRQQFRSQTQGGQLNNEFQQFAQAGPAHNSFEQSQMGPHFGQQHFGQPHQPQMGQHAPMAHGQQSDWAQSFSQLNLGPQTGPQHTQQSNWGQDFMRQSPQSHQVQPQMANGVMGSMSGMSSFGPMYSNSQLMNSTYGLQTEHQQTHKTETKSSQDAAFEAAFGAVEESITKTSDKGKEVEKDPMEQTYRYDQADALNRQAEHISDNISREEVDIKTDENGEFASIARQIASSLEEADKSKFEKSTFMNLMRRIGNHEVTLDGDKLVNKEGEDIREEVRDELLREGASQENGFQSEAQQTAPLPVHHEAPPPEQIHPHTETGDKQLEDPMVYIEQEAARRAAESGRTVEEEKLNFYSPFEYAQKLGPQGVAKQSNWEEDYDF
Protein: Gamma-crystallin C (Gamma-C-crystallin) (Gamma-crystallin 2-1) (P02529)
Organism: Rattus norvegicus (Rat)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Gamma-crystallin D
- Alpha-crystallin A chain
- Gamma-crystallin A.
Sequence:
MGKITFYEDRGFQGRCYECSSDCPNLQTYFSRCNSIRVDSGCWMLYERPNYQGHQYFLRRGDYPDYQQWMGFSDSIRSCRLIPHTGSHRMRLYEKEDHKGVMMELSEDCSCIQDRFHLSEVRSLHVLEGCWVLYEMPNYRGRQYLLRPQEYRRYHDWGAVDAKAGSLRRVVDLY
Protein: Spalt-related protein (P91639)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MCSIFRNRINYRGTGGTRSGSGERERDRDRDRDRDRDRERDRDTLLAKELDADSNNNGTEPQMEAEAVPESDTERETAEERGEEQEPENSNEALDLSLISSGGRESLPGSGHVSLEALQHTKVAVAQFAATAMAGNHQSADLAMVQSTIFNVQRQHLMQLQLIQHLQSQLKRAEAAALGRHSHSDEEEEEPEPEPEPKKQPTNGLKEELELEQGPESEQDHESRREENSKTDKRGTEDRKAEPEGYQSMMCDISSSLASSIITNHDPPPAPNEPNCLEMLQRRTEEVLDSASQSLHAAQMQEEYSEYASKEAQSRGEIFKHRCKYCGKIFGSYSALQIHLRSHTGERPFVCNVCGSKFTTKGNLKVHYQRHTQIFPPMLLPPGVAPNVGHSGQGQVQGEQYPIRLPFAPPVAPVGQEQHQNQVEEPEEIPVPQAEDLSKPMVKEKEKSHSPVECVKTPKEVKTDASLPSSEKPEKEISKPVVTSSRRNGSVRKRQTSAVSPPQEDRERDLVEHMNIAKLVRRSSASRESQPAEYSLAQMERIIDKSWEDLIEIDKTSETSKLQQLVDNIENKLTDPNQCIFCQKVMSCRSSLQMHIRTHTGERPFRCKICGRAFATKGNLKAHMSIHKIKPPMRSQFKCPVCHQKFSNGIILQQHIRIHTMDDGSGGQGVPAANPGEAERLGIEDQNSNKSLGTSDTLDFSTTISDHSGQRSESSQGGDFDEFMTMDSTDDSRDNSSAATATPHPLERERDREKERERRIPNDCSDERSHSNPDLTGGRSESGEMPAMDLSSPSSNSGRIFATGLANGATGGGSGNGGLPMLGMPMPPNLLLMAAAREEMHALGHAHAKFPLLPFGPLGFMGLHPPPNVCNLCFKMLPSLAALESHLQSEHAKEPATGHAQRPHCSDAGSPYGAKLTLNPNLFAKKPPSSSSSSSGEKLPESSNPPFPAENPPATPIKEDPDQEQLMVEEGASAGEGSGTGATSNYPQEAGDAEQSLMKMQLHAHRFPASPLDFQQALMSAGPPTSSLDPPVNNKHFCHVCRRNFSSSSALQIHMRTHTGDKPFQCNVCQKAFTTKGNLKVHMGTHMWTNPTSRRGRRMSLELPMRPGPNSGQGHPGSSAEQEFMQRRPELFFPYLPPFFNGLPPKPGELSPGAFPNIPPPPFANGGKYPYPPGLLGFPGFLAQHPYGLERRSSSKSPTPEPAQSPALREEEGSGNIWHPLSRIKVENNQNESMGGFNEQEDHAETDATGGDNDESESRDAEK
Protein: Sm-like protein LSM1B (AtLSM1b) (Q8LFL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. LSM1A and LSM1B are essential for the formation of the cytoplasmic LSM1-LSM7 complex which regulates developmental gene expression by the decapping of specific development-related transcripts. Required for P-body formation during heat stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}. Cytoplasm, P-body {ECO:0000269|PubMed:23221597}. Note=Translocates from cytosol to P-bodies upon heat stress. {ECO:0000269|PubMed:23221597}.
Interaction partners:
- Sm-like protein LSM4
- Sm-like protein LSM5
- Sm-like protein LSM2
- Sm-like protein LSM3A
- Sm-like protein LSM3B
- Sm-like protein LSM6A
- Sm-like protein LSM7
- mRNA-decapping enzyme subunit 2
- Sm-like protein LSM36B
- Sm-like protein LSM8
Sequence:
MSWAGPEEIYLSTSLASYLDRKLLVLLRDGRKLMGTLRSFDQFANAVLEGACERVIVGEQYCDIPLGLYVIRGENVVLIGELDTEREELPPHMIRVSEAEIKRAQKVEREASELRGTMRKRMEFLDFD
Protein: Doublesex and mab-3-related transcription factor 2a (Doublesex- and mab-3-related transcription factor 2a) (Terra) (Q9W7K3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00070}.
Interaction partners:
- Telomerase reverse transcriptase
- Forkhead box protein L2
- TERF1
- DNA helicase
Sequence:
MTDLSGTEFEIDVEGLETESDDQAVFTGPGEDDTGSKDDDKSDRLNLGSGDQRKLSRTPKCARCRNHGVVSCLKGHKRFCRWRDCQCANCLLVVERQRVMAAQVALRRQQATEDKKGITGKQIPVERRNIYQRHIRPSTMLAKSILEGYRPVQNDPFLGANPALPPPLSDRMRKRRAFADKELETIMLEREYKERELLESTQSNSASLFMPGSMVHAAEYNSYKTAFSSASAPSTVEPSPKDLCGFLPGCLDLSLQYAATGGTTANVELISSNVSVATTYRQYPLSPRFVMWPRGSSSISDALLYQQCLLNATAVQNLKPGAVWDPKMMSSTESHPPEQDAPASRLEGSRVAPESSDLQPGPREAQTGLGHNGGARSAFSPPKRTYGQVFSPQAGSHEHVINNMSKDTAKHTLSMKLNSFHSLIQQTLNDKNPDTNRPYCKELLEEAAKKFREGTAKDTVGLKSSERAAKDFVAKPRCSKVTAGESLSFSVEAILKRPALSLNRKSQ
Protein: Baculoviral IAP repeat-containing protein 5.2-A (Survivin2-A) (xSurvivin2A) (xSvv2/SIX) (xL_Survivin1) (Su1) (Q50L39)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (By similarity). Does not appear to exhibit anti-apoptotic activity. Plays a role in increasing blood vessel size during development.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. {ECO:0000250|UniProtKB:O15392}.
Interaction partners:
Sequence:
MMSISPIVSLRRCDNEPSMPDEWRLYKLASRLRTFSNWPFTEDCACTPERMAEAGFVHCPTDNSPDVVKCFFCLKELEGWQPEDDPMDEHKKHSPSCLFIALKKKAEELTLSEFLKLDLEHTKIKMQKQMNLHIERFQAKANEVRGHLEKLDADETQ
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (A0A0R4IVC8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103}; Matrix side {ECO:0000256|ARBA:ARBA00004443, ECO:0000256|RuleBase:RU368103}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 6C
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 2
- Complex III subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 6A
Sequence:
MISAAVLRGFLGLSRTRAAQTAPLAVRCYSHAKVETDEEFDSRWVTYFSKPDLDAWELRKGMNTLIGYDLVPEPKILDSALRACRRLNDLASAIRILEAVKDKSGPHKEIYPYVIQELKPTLQELGISTPEELGIDKI
Protein: Exportin 1 (Q7Z2C1)
Organism: Trypanosoma brucei brucei
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDILDFSKPVDVQRFDQVVQYLSTGSPQEIVRAQEVLTAFKERPDSFLRVGDLLTKSVNLTTRFFALQVLEDAILHRWNTFTAEQCQEIRNFVVNMIVGECVSFNQIRSRRALLMKMNSALVSIAKREWPVRWPTFIKDVCSSAGPDEPLVENNLNILRMVGEEIFEFSEKTLTTRWLKRKKEALQSDFQAILQLCLSILSTSDEALLKTNLECLEKYLSWVEPASVFNEELLKYLAGLIARKSAVSRCAVRCLTVACSVETDHGSVGDAQAQVMVRVFRTILDNIMNLLPTNHSSVEARIVQFSNMEGSVDAGFVGDLNLLLVAFLKHYTRNIMYDDLLLISANQLIVGMSHINDKELFKSCVDYWWWLGEKMVRSASPTPLHRKLALVLSNVRFTLIKKMARPEEVIIVVEDGEVRRVHMKDVEELQLYKLMRETLVFLTYLDPQDMQAIMTKIVMKLEDLSEWSWHNCNTLSWAVGAISVALTEEQESSLFVVIVRGLLDLCSKLQGKENRAVVASGIMFVVGQYPRFLRAHQPFFRAVVKKVIEFMCDLFPGVQEMAVDTLLKVASQVPDQFVCVKNNGISLAEETAKRWTEITSLLKPQHMHTCFVAAGWMVKGEKPERQPSLLGMFLQDANDSFRIIVERAASKGPAFGEDFSGMGELIHILRVFSSIASSCGTSFVNEMGIIIYDLQGLYRTFFSAQTALVADHGTDAMERQEARYLRLAKREILRIFECFVDNTEECDFVATNCMPSILTTVLEDYRDSLPIVKEAGALALVTACVNKLGTRLAGDCAAILDHTSDTTISMICANAEDFPEFRVNLFKLLHALNTRCFSNFLSYASTKGDVINGMLWVIKHTDFAIMETGLKTLDAFLENVSRSELLQPFYDAFMQQIFVEVLVSAMDSLHAAGFELHCSILIKLFTVSSMFPVDLPKLGRNDIESFLCENLSTIATLTPVLIKQFIAGAYEKYGDPVEFRRSFADFLIEMQVWGAEEENRLQQEEEQRRREEDIPGFAALSVKGPPPTPSFYP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0U1RS40)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MWAGRRRARAVPLPGKRRRRVAHAQCRPQRPLSPQSEGVTGEPWPLRAAVFSGSWGSSCCPLPSRLGSRAPSASPARRGRSRAARSSRLCRLCRRRPRASLPPGSVAMAMTGSTPCSSMSNHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVRMFYSFQDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLTFPPEVPVSEKAKGLILRFCCEWEHRIGAPGVEEIKSNPFFEGVDWEHIRERPAAISIEIKSIDDTSNFDEFPESDILKPTVTTSNHPETDYKSKDWVFINYTYKRFEGLTARGAIPSYMKAAK
Protein: Probable disease resistance protein At5g66910 (Q9FKZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable disease resistance protein.
Interaction partners:
- Powdery mildew resistance protein, RPW8 domain-containing protein
- At5g58530
- Protein disulfide isomerase-like 1-6
- Thioredoxin-like 1-3, chloroplastic
- MLO-like protein 9
Sequence:
MVVVDWLGLGLGSVAGALVSEGLKVLISEAKKVLAFKSVSNELASTMESLLPVIKEIESMQDGMELQDLKDTIDKALLLVEKCSHVEKWNIILKSKYTRKVEEINRKMLKFCQVQLQLLLFRNQLKSMPSMEAILNNYFQNINKKLDRLSGSPAPPLVSKRCSVPKLDNMVLVGLDWPLVELKKKLLDNSVVVVSGPPGCGKTTLVTKLCDDPEIEGEFKKIFYSVVSNTPNFRAIVQNLLQDNGCGAITFDDDSQAETGLRDLLEELTKDGRILLVLDDVWQGSEFLLRKFQIDLPDYKILVTSQFDFTSLWPTYHLVPLKYEYARSLLIQWASPPLHTSPDEYEDLLQKILKRCNGFPLVIEVVGISLKGQALYLWKGQVESWSEGETILGNANPTVRQRLQPSFNVLKPHLKECFMDMGSFLQDQKIRASLIIDIWMELYGRGSSSTNKFMLYLNELASQNLLKLVHLGTNKREDGFYNELLVTQHNILRELAIFQSELEPIMQRKKLNLEIREDNFPDECLNQPINARLLSIYTDDLFSSKWLEMDCPNVEALVLNISSLDYALPSFIAEMKKLKVLTIANHGFYPARLSNFSCLSSLPNLKRIRFEKVSVTLLDIPQLQLGSLKKLSFFMCSFGEVFYDTEDIDVSKALSNLQEIDIDYCYDLDELPYWIPEVVSLKTLSITNCNKLSQLPEAIGNLSRLEVLRMCSCMNLSELPEATERLSNLRSLDISHCLGLRKLPQEIGKLQKLENISMRKCSGCELPDSVRYLENLEVKCDEVTGLLWERLMPEMRNLRVHTEETEHNLKLLLTF
Protein: cAMP-dependent protein kinase type I-alpha regulatory subunit [Cleaved into: cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processed] (P00514)
Organism: Bos taurus (Bovine)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Subcellular location: Cell membrane {ECO:0000250}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Protein kinase cAMP-dependent X-linked catalytic subunit
- A-kinase anchor protein 10, mitochondrial
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase type II-beta regulatory subunit
- Hormone-sensitive lipase
- Protein kinase cAMP-dependent type I regulatory subunit beta
- non-specific serine/threonine protein kinase
- Ribosomal protein S6 kinase beta-2
Sequence:
MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV
Protein: Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 3 (W8DXL4)
Organism: Mus musculus (Mouse)
Function: Plays a role in the synapse formation and synaptic transmission between cone photoreceptor cells and retinal bipolar cells. Required for normal transmission of a light-evoked stimulus from the cone photoreceptor cells to the ON-bipolar cells and ON-ganglion cells in the inner retina. Required in retinal ON-bipolar cells for normal localization of the cation channel TRPM1 at dendrite tips. Seems to play a specific role in synaptic contacts made by ON-bipolar cells with cone photoreceptor pedicles. May also have a role in cone synapse formation. Might facilitate FGFR1 exit from the endoplasmic reticulum to the Golgi (By similarity). Could be a regulator of the FGFRs (By similarity).
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:25997951}. Perikaryon {ECO:0000269|PubMed:25997951}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3SXY7}; Single-pass type I membrane protein {ECO:0000305}. Note=Punctate expression at dendrite tips. {ECO:0000269|PubMed:25997951}.
Interaction partners:
- G-protein coupled receptor 179
- Voltage-dependent L-type calcium channel subunit alpha-1F
- Transient receptor potential cation channel subfamily M member 1
- Calcium-binding protein 4
- Metabotropic glutamate receptor 6
Sequence:
MWLSACLCLVLSFLGGVNGTCPSQCSCEYHGRHDGSGSRLVLCNDLDMNEVPANFPVDTSKLRIEKTVVRRLPAEAFYYLVELQYLWLAYNSVASIETSSFYNLRQLHELRLDGNSLTAFPWVSLLDMPHLRTLDLHNNRIASVPNEAVRYLRNLTCLDLSSNRLTTLPPDFLDSWSHLAVTPSRSPDFPPRRIILGLQDNPWFCDCHISKVIELSKVTDHAVVLLDPLMVCSEPERFQGILFQRVELEKCLKPSVMMSATKITSALGSNVLLRCDAKGHPTPQLTWTRSDGSTVNYTVIQESPGEGIRWSIISLTSISHKDAGDYRCKAKNLAGISEAVVTVTVVGGVTTTLSPDSSERSPGEPPEQHPQPGLGGSTPPSKSWLSPGLTSAPSYPTPSAALYTSTWSPPPSSLPPIFSAASATTSVQTSISGRTARTSHQPPLLHPGGKSNAKIEKNGRKFPPLSASKKEELALLDQAAPMETNVTIKDLRVARETGVSVTLMWNSSSSTQESSVTVLYSKYGEKDLLLVNADDYGKNQATINGLEPGSQYVACVCPKGVGPREDLCITFSTNRVEGRGSQWSLLLVVTSTACVIVVPLICFLLYKVCKLQCTSDPFWEEDLSKETYIQFETLSPRSQSIGELWTRRHRDDGERLLLCSQSSVDSQMNLKSDGCRTEYYG
Protein: Cerebellar degeneration-related protein 2 (Major Yo paraneoplastic antigen) (Paraneoplastic cerebellar degeneration-associated antigen) (Q01850)
Organism: Homo sapiens (Human)
Interaction partners:
- Myc proto-oncogene protein
- Cerebellar degeneration-related protein 2-like
- Serine/threonine-protein kinase BRSK1
- Inter-alpha-trypsin inhibitor heavy chain H4
- Wee1-like protein kinase
- Immunoglobulin heavy variable 4-38-2
- Kinectin
Sequence:
MLAENLVEEFEMKEDEPWYDHQDLQQDLQLAAELGKTLLDRNTELEDSVQQMYTTNQEQLQEIEYLTKQVELLRQMNEQHAKVYEQLDVTARELEETNQKLVADSKASQQKILSLTETIECLQTNIDHLQSQVEELKSSGQGRRSPGKCDQEKPAPSFACLKELYDLRQHFVYDHVFAEKITSLQGQPSPDEEENEHLKKTVTMLQAQLSLERQKRVTMEEEYGLVLKENSELEQQLGATGAYRARALELEAEVAEMRQMLQSEHPFVNGVEKLVPDSLYVPFKEPSQSLLEEMFLTVPESHRKPLKRSSSETILSSLAGSDIVKGHEETCIRRAKAVKQRGISLLHEVDTQYSALKVKYEELLKKCQEEQDSLSHKAVQTSRAAAKDLTGVNAQSEPVASGWELASVNPEPVSSPTTPPEYKALFKEIFSCIKKTKQEIDEQRTKYRSLSSHS
Protein: Nonsense-mediated mRNA decay protein 2 (Up-frameshift suppressor 2) (P38798)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nonsense-mediated decay of mRNAs containing premature stop codons. It interacts, via its C-terminus, with NAM7/UPF1. Could be involved in determining the efficiency of translational termination or reinitiation or factors involved in the initial assembly of an initiation- and termination-competent mRNP.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- ATP-dependent helicase NAM7
- Nonsense-mediated mRNA decay protein 3
- Eukaryotic peptide chain release factor GTP-binding subunit
- 5'-3' exoribonuclease 1
- Putative ATP-dependent RNA helicase ECM32
- RNA-binding protein SGN1
- Eukaryotic peptide chain release factor subunit 1
- Nuclear cap-binding protein complex subunit 1
- m7GpppN-mRNA hydrolase
- ATP-dependent RNA helicase FAL1
Sequence:
MDDGRKKELHDLNTRAWNGEEVFPLKSKKLDSSIKRNTGFIKKLKKGFVKGSESSLLKDLSEASLEKYLSEIIVTVTECLLNVLNKNDDVIAAVEIISGLHQRFNGRFTSPLLGAFLQAFENPSVDIESERDELQRITRVKGNLRVFTELYLVGVFRTLDDIESKDAIPNFLQKKTGRKDPLLFSILREILNYKFKLGFTTTIATAFIKKFAPLFRDDDNSWDDLIYDSKLKGALQSLFKNFIDATFARATELHKKVNKLQREHQKCQIRTGKLRDEYVEEYDKLLPIFIRFKTSAITLGEFFKLEIPELEGASNDDLKETASPMITNQILPPNQRLWENEDTRKFYEILPDISKTVEESQSSKTEKDSNVNSKNINLFFTDLEMADCKDIIDDLSNRYWSSYLDNKATRNRILKFFMETQDWSKLPVYSRFIATNSKYMPEIVSEFINYLDNGFRSQLHSNKINVKNIIFFSEMIKFQLIPSFMIFHKIRTLIMYMQVPNNVEILTVLLEHSGKFLLNKPEYKELMEKMVQLIKDKKNDRQLNMNMKSALENIITLLYPPSVKSLNVTVKTITPEQQFYRILIRSELSSLDFKHIVKLVRKAHWDDVAIQKVLFSLFSKPHKISYQNIPLLTKVLGGLYSYRRDFVIRCIDQVLENIERGLEINDYGQNMHRISNVRYLTEIFNFEMIKSDVLLDTIYHIIRFGHINNQPNPFYLNYSDPPDNYFRIQLVTTILLNINRTPAAFTKKCKLLLRFFEYYTFIKEQPLPKETEFRVSSTFKKYENIFGNTKFERSENLVESASRLESLLKSLNAIKSKDDRVKGSSASIHNGKESAVPIESITEDDEDEDDENDDGVDLLGEDEDAEISTPNTESAPGKHQAKQDESEDEDDEDDDEDDDDDDDDDDDDGEEGDEDDDEDDDDEDDDDEEEEDSDSDLEYGGDLDADRDIEMKRMYEEYERKLKDEEERKAEEELERQFQKMMQESIDARKSEKVVASKIPVISKPVSVQKPLLLKKSEEPSSSKETYEELSKPKKIAFTFLTKSGKKTQSRILQLPTDVKFVSDVLEEEEKLKTERNKIKKIVLKRSFD
Protein: Protein STRUBBELIG-RECEPTOR FAMILY 2 (Leucine-rich repeat receptor kinase-like protein SRF2) (Q9FG24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein DEHYDRATION-INDUCED 19 homolog 5
Sequence:
MKTKQQLRFLATILLTTILFVLAKTDTDPLEVLALQDLYKSLRNPEQLRGWRLEGGDPCGEAWLGISCSGSSIVDLQLRELKLLGSLGNQLQHLHNLKILDVSFNNLEGEIPFGLPPNATHINMAYNNLTQSIPFSLPLMTSLQSLNLSHNSLSGPLGNVFSGLQIKEMDLSFNNLTGDLPSSFGTLMNLTSLYLQNNRLTGSVIYLADLPLADLNIEDNQFSGIIPSHFQSIPHLWIWGNKFHVEPNYKPWKFPLDVRPLIQNDTGYPTTESSAIMNFPRPETQKVKKKKKGIGAGSTFLLVGGLALLGTFFALFAVRMNHRRAQNLAAIHRSNNSIAYSLPVSTGREYPVATEDNPQIKRFQPPPAPQLRHLPSPPVRIDKSARRKSFSATCQYPSFAKLFSAAELQLATNCFSEENLLGEGPLGSVYRAKLPDGQFAVVRNIPMSSLSLHEEEQFTEVLQTASKLRHPNIVTLLGFCIENGEHLLVYEYVGHLSLYNAMHDEVYKPLSWGLRLRIAIGVARALDYLHSSFCPPIAHSDLKATNILLDEELTPRIADCGLASLRPLTSNSVKLRASEIAIQNTGYIAPEHGQPGSSGTKSDTYALGVLLLELLTGRKAFDSSRPRGEQLLVKWASTRLHDRRSLEQMIDGGIAGTFSSRVASQYADIISLCTQAEKEFRPPVSEIVEALTALIQKQNKEASSSVADKTDPFSKSFCSTRTRFISSPTFSYLSS
Protein: Vacuolar protein sorting-associated protein 35 (Vacuolar protein-targeting protein 7) (P34110)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor VPS10. Vacuolar carboxypeptidase Y (CPY) sorting is completely dependent on the presence of functional VPS35. The latter may play a role in the function, modification or packaging of a CPY-specific receptor complex. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The VPS29-VPS26-VPS35 subcomplex may be involved in cargo selection.
Subcellular location: Membrane; Peripheral membrane protein.
Interaction partners:
- Vacuolar protein sorting-associated protein 5
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-3
- Carboxypeptidase Y-deficient protein 8
- Vacuolar protein sorting-associated protein 17
- Vacuolar protein sorting/targeting protein VPS10
- Sorting nexin-4
- Sorting nexin MVP1
- Uncharacterized protein YKR078W
- Ypt/Rab-type GTPase YPT7
Sequence:
MAYADSPENAIAVIKQRTALMNRCLSQHKLMESLQHTSIMLTELRNPNLSPKKYYELYVIIFDSLTNLSTYLIENHPQNHHLADLYELVQYTGNVVPRLYLMITVGTSYLTFNEAPKKEILKDMIEMCRGVQNPIRGLFLRYYLSQRTKELLPEDDPSFNSQFIMNNFIEMNKLWVRLQHQGPLRERETRTRERKELQILVGSQLVRLSQIIDDNFQMYKQDILPTILEQVIQCRDLVSQEYLLDVICQVFADEFHLKTLDTLLQTTLHLNPDVSINKIVLTLVDRLNDYVTRQLEDDPNATSTNAYLDMDVFGTFWDYLTVLNHERPDLSLQQFIPLVESVIVLSLKWYPNNFDNLNKLFELVLQKTKDYGQKNISLESEHLFLVLLSFQNSKLQLTSSTTAPPNSPVTSKKHFIFQLISQCQAYKNILALQSISLQKKVVNEIIDILMDREVEEMADNDSESKLHPPGHSAYLVIEDKLQVQRLLSICEPLIISRSGPPANVASSDTNVDEVFFNRHDEEESWILDPIQEKLAHLIHWIMNTTSRKQTMKNKIQFSLEAQLEILLLIKSSFIKGGINVKYTFPAIITNFWKLMRKCRMIQEYLLKKRPDNKTLLSHYSNLLKQMFKFVSRCINDIFNSCNNSCTDLILKLNLQCAILADQLQLNEISYDFFSQAFTIFEESLSDSKTQLQALIYIAQSLQKTRSLYKEAYYDSLIVRCTLHGSKLLKKQDQCRAVYLCSHLWWATEISNIGEEEGITDNFYRDGKRVLECLQRSLRVADSIMDNEQSCELMVEILNRCLYYFIHGDESETHISIKYINGLIELIKTNLKSLKLEDNSASMITNSISDLHITGENNVKASSNADDGSVITDKESNVAIGSDGTYIQLNTLNGSSTLIRGVVATASGSKLLHQLKYIPIHHFRRTCEYIESQREVDDRFKVIYV
Protein: cGMP-dependent protein kinase 2 (cGK 2) (cGK2) (EC 2.7.11.12) (cGMP-dependent protein kinase II) (cGKII) (Q13237)
Organism: Homo sapiens (Human)
Function: Crucial regulator of intestinal secretion and bone growth. Phosphorylates and activates CFTR on the plasma membrane. Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum. Acts downstream of NMDAR to activate the plasma membrane accumulation of GRIA1/GLUR1 in synapse and increase synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863 (By similarity). Acts as regulator of gene expression and activator of the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid shear stress, mediates ERK activation and subsequent induction of FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the osteoblast anabolic response to mechanical stimulation (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:8636133}; Lipid-anchor {ECO:0000269|PubMed:8636133}.
Interaction partners:
- Guanylate cyclase soluble subunit alpha-2
- Guanylate cyclase soluble subunit beta-1
- Guanylate cyclase soluble subunit alpha-1
- Inositol 1,4,5-triphosphate receptor associated 1
- Vasodilator-stimulated phosphoprotein
- Calcium-activated potassium channel subunit alpha-1
- General transcription factor II-I
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Ras-GEF domain-containing family member 1B
- Potassium channel subfamily U member 1
Sequence:
MGNGSVKPKHSKHPDGHSGNLTTDALRNKVTELERELRRKDAEIQEREYHLKELREQLSKQTVAIAELTEELQNKCIQLNKLQDVVHMQGGSPLQASPDKVPLEVHRKTSGLVSLHSRRGAKAGVSAEPTTRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDMVECMYGRNYQQGSYIIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEQYRNFLRSVSLLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFEELQKYLEGYVANLNRDDEKRHAKRSMSNWKLSKALSLEMIQLKEKVARFSSSSPFQNLEIIATLGVGGFGRVELVKVKNENVAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDAEGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGVDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLKARSLPSPLQRELKGPIDHSYFDKYPPEKGMPPDELSGWDKDF