wanglab/gogpt-training-data huggingface dataset:
Protein: Protein RAD61 (Radiation sensitivity protein 61) (Q99359)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in resistance to ionizing radiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Sister chromatid cohesion protein PDS5
- Structural maintenance of chromosomes protein 3
- N-acetyltransferase ECO1
- Cohesin subunit SCC3
- Sister chromatid cohesion protein 1
- Structural maintenance of chromosomes protein 1
- Meiotic recombination protein REC8
- ATP-dependent DNA helicase CHL1
- Chromosome transmission fidelity protein 18
- MAU2 chromatid cohesion factor homolog
Sequence:
MRAYGKRGPVLRTPFRSNKGLPSSSDVEFSDDDVNSVIPDVSSTISSSIADHPIEGLLDEPRKAQDSSSSFDGANEKPSSQLDSKRNDQNVKIITSSDTSMAFMKDEKLSAFNFLDGSKASKRKRRRTYQKHDANITSSIEPDVQDEDSITMHNEFESIRKIYNDINEFILKLPRADDDILNKMLENEMKMDDSIENNSIRTSKDKKYGKFRTILINKNKENEIMGEEVDQKANTLSLNNADNSNAEKEGLTSTNHYNELKNMGDTIKYQDDIEFLLSNSKSNDNTTVPINEYFKKLLNLSLMIINDEEFFQYAKRYFKKEIIKLSFAQFRSDFPELILLQGYLLHKVSESQSDFPPSFDNFSIELSKDDGKIRTKKNKHIKKLSHLNFEDFLRKTQFKTGLYYSLSLWEMHGNLSLDIIKRISILASNKDLFSRHVKTFIPLLEKLITASEFCHMYIEQPEMFDSLISNLNNQFKDMLDDDSLIKILILLTNMEVHNYTLWKEADMIFQSSMNTILESIHPLTDAKVDNILLHLGLCLNICSRENSRLKLDGKLWYDMKTIFVKMIRDGSDTENRLVQGLFYLNFSFLIKQRKENSNLDPGELNLLLVELEAFKSETSQFNEGISNKIEIALNYLKSIYTSERITI
Protein: DNA damage-inducible transcript 3 protein (C/EBP zeta) (C/EBP-homologous protein) (C/EBP-homologous protein 10) (CCAAT/enhancer-binding protein homologous protein) (F1Q964)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cyclic AMP-dependent transcription factor ATF-4
- X-box-binding protein 1
- Cyclic AMP-dependent transcription factor ATF-4
- Activating transcription factor 6
- Apoptosis regulator Bcl-2
- Apoptosis regulator Bcl-2
- Nuclear factor
- Mitogen-activated protein kinase 12
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 14B
Sequence:
MTAEWLYPPGVGPLCGAELEAWYEDLQDILGSDTGGAKLTRAPPSSEKEPEFLDVLESCSLTWLTEGQVWGDGVQRVTEDPPVHQSPPRQEERTTENTSSGDLLPPEFFELLSEGGVGDTMVNGGAGYHLHAPPSPAASEEEELPTVPDTSSCSSASRSPSLNCSPPASPPVSSSRKRKRGGALCSASPGKKSRREREQENERKVQELTDQNERLKAEIERLGEEVQRTRRALIERLVNTRR
Protein: ATP-grasp domain-containing protein (Q57ZC5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Peptidase C51 domain-containing protein
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Sequence:
MYRIAIRRFGVASVLRCPLADVLIPKTPTVAVWSCVTVHTLRWKSSNTTIILPSRGAASSVSSKSGGTSSCLTVGGAVPPAAVGTSAHPGGNGINPGTKSAALLSASGTSNGGGASGKSSGMTTAVEIGQGSNRGRSARKGKEDVIGLKKVKASSSKSVVNRSGASTTNTATAMSTGSSSANGSHCTKSATGMVVSQTLGRRRASVKKQLRVCVLNSSYEGTNSVTAEMDNYHCSPAHRVRKDKNRYSFTEVAVRKDDAYRQVRELVTSNNFDVFFNLCDGGKDEKRAGIDVLEALEEHNAAFTGTDSRSFEPSKIDMKVLVAGAGVNTPNFVLLDKTEGLAKKCRHLRFPVIVKHLSGYASVGINKDNRCDTLDELKVKVGTFLKEFNHALVEEFIRGREGTVLACADSGSPHGVKVFRPLMFNFLQNEDDFAYFDKKWSMECNDEACSFLPHNDPAYPRIIDMARNAFQHIMNGVGYGRVDFRIDPKGDVYFLEINPNCGMWYSEKDGGDFADLMVVGDKSWDHDRFVDNAVNRAVREQKARRPWYFISHDSRGNFSSKASRTVRPGKALFSDAAHTVPVIAQAVYKLGEEDPVVGCVILRGDRLHQAVAIRHSCEPNMHFLQGRTLTLVSKRTINSGEELTVDYATLCDERMPPFACSCGTRNCRSVIFPSPPTPRVLEGRGVRQMLREKKEAWNKQKADREAERMLKKRSSSGRNGGQSSQHAGAHSTASNSSASSGSSAPGGSGSSVNANNHSGSDSSTKGHGGKK
Protein: FYVE-type domain-containing protein (Q57UC6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDHIDLAEEREMGNGDPIMVLNVSVPYSANSSDRKSNVSSPLLSKCASKQTSGVMWLTKPTLDPSCIRLCPLRRWVPDTQVSTCMAHGCNVAFSMFNRRHHCRVCGRVFCSACCSETVNALVQSALEVQSNPIEACGGVDKTSLPSGRVSGTDIANGEDNISQQQQQGQVQFMNPTTVAAYRVCFACHYEVQLVVSRRDRNGEVRRKCRGELKMLQWSLLVRVLSYLTMEELLGVSLVSSDFYFMSRDNVIWYRYNMTRCLREEELQRMLSTTLGSRNSTRRQRLPQKQLGELTFGTDFDSITSAGAAKPTISLNARYNFTQFLDFTRRREATRCKGLSCFSVGMRDLLSSPIKIALIGPCGVGKTSLMREWGRQRRPGDNSARFAVTPPTVTFNQFDKTVFLTGGLTARAQLRVFDISGHPRFRELTRFVCASCHAVVICYDPQRKSSLMEAKAIIADVETKLGVQPVIVCGLIPPADAGRGGSAVEVSAEEATEISSRERGSLLCAWHEGKILFEHVVQCLLDCIALGTSAISFTAPVSPLGVPVDSEEFSVNRSTAQELLRITMCPSAIDVLLD
Protein: Glycine cleavage system H protein, mitochondrial (Lipoic acid-containing protein) (P23434)
Organism: Homo sapiens (Human)
Function: The glycine cleavage system catalyzes the degradation of glycine. The H protein (GCSH) shuttles the methylamine group of glycine from the P protein (GLDC) to the T protein (GCST).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:36190515}.
Interaction partners:
- Aminomethyltransferase, mitochondrial
- Glycine dehydrogenase
- Dihydrolipoyl dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Lipoyl amidotransferase LIPT1, mitochondrial
- Myosin-binding protein H
- Alanine--glyoxylate aminotransferase
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- P protein
Sequence:
MALRVVRSVRALLCTLRAVPSPAAPCPPRPWQLGVGAVRTLRTGPALLSVRKFTEKHEWVTTENGIGTVGISNFAQEALGDVVYCSLPEVGTKLNKQDEFGALESVKAASELYSPLSGEVTEINEALAENPGLVNKSCYEDGWLIKMTLSNPSELDELMSEEAYEKYIKSIEE
Protein: Large ribosomal subunit protein uL3 (60S ribosomal protein L3) (B5MCW2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MTHIVREVDRPGSKVNKKEVVEAVTIVETPPMVVVGIVGYVETPRGLRTFKTVFAEHISDECKRRFYKNWHKSKKKAFTKYCKKWQDEDGKKQLEKDFSSMKKYCQVIRVIAHTQMRLLPLRQKKAHLMEIQVNGGTVAEKLDWARERLEQQVPVNQVFGQDEMIDVIGVTKGKGYKGVTSRWHTKKLPRKTHRGLRKVACIGAWHPARVAFSVARAGQKGYHHRTEINKKIYKIGQGYLIKDGKLIKNNASTDYDLSDKSINPLGGFVHYG
Protein: Leptin (Obesity factor) (Q8MJ10)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
LDFIPGLHPLLSLSKMDQTLVIYRQILTSLPSRNVVQISNDLENLRDLLHLLAASKSCPLPQVRALESLESLGVVLEASLYSTEVV
Protein: Speriolin-like protein (Spermatogenesis and centriole-associated protein 1-like protein) (Q9D9W0)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H0A9}.
Interaction partners:
Sequence:
MAEGSELMSRLMSENADLKKQVRLLKENQMLKRLLSESCQESCGRGSRDLLYPKVPTYPEACSPGNGGPDFGRFAGVPDTPSQLPTSSLEDLLCSHAPLSSEDEASPGCATTSQMPFKSFLSPSELHSRIADRKLSPLLSPLQDSLADKTLLEPREISRPKKVCFSESNLPTGDRSRRTYYLNEIQSFSGAEKDGRIVGEIAFQLDRRILAYVFPGVTRLYGFTVSNIPEKIKQTSIKSLDGSVDEKKLRELTHRYLTLTARLEKLGYSREVHPVFSEFLINTYGILKQRPDLRANPLHSSPAALRKLVIDIVPPKFLGDSLLLLNCLCELSKEDSKPLFAW
Protein: Coatomer subunit zeta-1 (Zeta-1-coat protein) (Zeta-1 COP) (P35604)
Organism: Bos taurus (Bovine)
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. 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). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (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 gamma-1
- Coatomer subunit beta'
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit epsilon
- ADP-ribosylation factor 1
- ADP-ribosylation factor 3
- Coatomer subunit gamma-2
- ER lumen protein-retaining receptor
Sequence:
MEALILEPSLYTVKAILILDNDGDRLFAKYYDDTYPSVKEQKAFEKNIFNKTHRTDSEIALLEGLTVVYKSSIDLYFYVIGSSYENELMLMTVLNCLFDSLSQMLRKNVEKRALLENMEGLFLAVDEIVDGGVILESDPQQVVHRVALRGEDVPLTEQTVSQVLQSAKEQIKWSLLR
Protein: DNA polymerase (EC 2.7.7.7) (A6NMQ1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAPVHGDDCEIGASALSDSGSFVSSRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDFTGVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDADEKGKDGKARNKDKRNVKKLAVTKPNNIKSMFIACAGKKTADKAVDLSKDGLLGDILQDLNTETPQITPPPVMILKKKRSIGASPNPFSVHTATAVPSGKIASPVSRKEPPLTPVPLKRAEFAGDDVQVESTEEEQESGAMEFEDGDFDEPMEVEEVDLEPMAAKAWDKESEPAEEVKQEADSGKGTVSYLGSFLPDVSCWDIDQEGDSSFSVQEVQVDSSHLPLVKGADEEQVFHFYWLDAYEDQYNQPGVVFLFGKVWIESAETHVSCCVMVKNIERTLYFLPREMKIDLNTGKETGTPISMKDVYEEFDEKIATKYKIMKFKSKPVEKNYAFEIPDVPEKSEYLEVKYSAEMPQLPQDLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKSPQLLNQPVSWCKVEAMALKPDLVNVIKDVSPPPLVVMAFSMKTMQNAKNHQNEIIAMAALVHHSFALDKAAPKPPFQSHFCVVSKPKDCIFPYAFKEVIEKKNVKVEVAATERTLLGFFLAKVHKIDPDIIVGHNIYGFELEVLLQRINVCKAPHWSKIGRLKRSNMPKLGGRSGFGERNATCGRMICDVEISAKELIRCKSYHLSELVQQILKTERVVIPMENIQNMYSESSQLLYLLEHTWKDAKFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKAAYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVASEAQKVTEDGEQEQIPELPDPSLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLILQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKEMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDGVFKSLLLLKKKKYAALVVEPTSDGNYVTKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDKKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTASQRAYAPEQLQKQDNLTIDTQYYLAQQIHPVVARICEPIDGIDAVLIATWLGLDPTQFRVHHYHKDEENDALLGGPAQLTDEEKYRDCERFKCPCPTCGTENIYDNVFDGSGTDMEPSLYRCSNIDCKASPLTFTVQLSNKLIMDIRRFIKKYYDGWLICEEPTCRNRTRHLPLQFSRTGPLCPACMKATLQPEYSDKSLYTQLCFYRYIFDAECALEKLTTDHEKDKLKKQFFTPKVLQDYRKLKNTAEQFLSRSGYSEVNLSKLFAGCAVKS
Protein: Ribosomal RNA large subunit methyltransferase K/L [Includes: 23S rRNA m2G2445 methyltransferase (EC 2.1.1.173) (rRNA (guanine-N(2)-)-methyltransferase RlmL); 23S rRNA m7G2069 methyltransferase (EC 2.1.1.264) (rRNA (guanine-N(7)-)-methyltransferase RlmK)] (P75864)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- ATP-binding protein Uup
- Ribosomal RNA small subunit methyltransferase C
- Ribosomal RNA large subunit methyltransferase M
- Ribosomal RNA large subunit methyltransferase G
- Ribosomal RNA small subunit methyltransferase D
- Dual-specificity RNA methyltransferase RlmN
- 23S rRNA
- tRNA1
- Ribosomal large subunit pseudouridine synthase B
- Ribosomal RNA large subunit methyltransferase H-methyltransferase)
Sequence:
MNSLFASTARGLEELLKTELENLGAVECQVVQGGVHFKGDTRLVYQSLMWSRLASRIMLPLGECKVYSDLDLYLGVQAINWTEMFNPGATFAVHFSGLNDTIRNSQYGAMKVKDAIVDAFTRKNLPRPNVDRDAPDIRVNVWLHKETASIALDLSGDGLHLRGYRDRAGIAPIKETLAAAIVMRSGWQPGTPLLDPMCGSGTLLIEAAMLATDRAPGLHRGRWGFSGWAQHDEAIWQEVKAEAQTRARKGLAEYSSHFYGSDSDARVIQRARTNARLAGIGELITFEVKDVAQLTNPLPKGPYGTVLSNPPYGERLDSEPALIALHSLLGRIMKNQFGGWNLSLFSASPDLLSCLQLRADKQYKAKNGPLDCVQKNYHVAESTPDSKPAMVAEDYTNRLRKNLKKFEKWARQEGIECYRLYDADLPEYNVAVDRYADWVVVQEYAPPKTIDAHKARQRLFDIIAATISVLGIAPNKLVLKTRERQKGKNQYQKLGEKGEFLEVTEYNAHLWVNLTDYLDTGLFLDHRIARRMLGQMSKGKDFLNLFSYTGSATVHAGLGGARSTTTVDMSRTYLEWAERNLRLNGLTGRAHRLIQADCLAWLREANEQFDLIFIDPPTFSNSKRMEDAFDVQRDHLALMKDLKRLLRAGGTIMFSNNKRGFRMDLDGLAKLGLKAQEITQKTLSQDFARNRQIHNCWLITAA
Protein: Dermaseptin-O1 (DRS-O1) (Dermaseptin-01) (DS 01) (P83637)
Organism: Pithecopus oreades (Orange-legged leaf frog) (Phyllomedusa oreades)
Function: Has antibacterial activity against the Gram-positive bacteria S.aureus (MIC=5.7 uM), S.dysgalactiae (MIC=5.7 uM), Nocardia sp (MIC=22.9 uM) and S.uberis (MIC=5.7 uM), and the Gram-negative bacteria P.aeruginosa, E.coli and A.calcoaceticus. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=0.37 uM), C.guilliermondii (MIC=22.9 uM), C.albicans (MIC=5.7 uM) and C.albicans ATCC 1023 (MIC=5.7 uM). Lacks hemolytic activity against human and murine erythrocytes. Does not cause morphological changes in murine liver, spleen and kidney. Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes.
Subcellular location: Secreted {ECO:0000269|PubMed:12379643}.
Interaction partners:
Sequence:
GLWSTIKQKGKEAAIAAAKAAGQAALGAL
Protein: Myosin phosphatase Rho-interacting protein (Rho-interacting protein 3) (RIP3) (p116Rip) (Q9ERE6)
Organism: Rattus norvegicus (Rat)
Function: Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with F-actin. {ECO:0000250}.
Interaction partners:
- Transforming protein RhoA
- Protein phosphatase 1 regulatory subunit 12A
Sequence:
MSAAKENPCRKFQANIFNKSKCQNCFKPRESHLLNDEDLTQAKPIYGGWLLLAPDGTDFDNPVHRSRKWQRRFFILYEHGLLRYALDEMPTTLPQGTINMNQCTDVVDGEARTGQKFSLCILTPDKEHFIRAETKEIISGWLEMLMVYPRTNKQNQKKKRKVEPPTPQEPGPAKMAVTSSSGGSSGSSSSSSSSSIPSAEKVPTTKSTLWQEEMRAKDQPDGTSLSPVQSPSQSQPPAACTPRETGLDSKEDENILSGDRVDGGRKVRVESGYFSLEKAKQDLRAEEQLPPLLSPPSPSTPHSRRSQVIEKFEALDIEKAEHMETNMLILTTPSSDTRQGRSERRAIPRKRDFASETPTAPLSDACPLSPHRRAKSLDRRSTESSMTPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEINLSTCYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVLPTSAPDVTSSLPEGKNKSTSFDTCLRPSEKQEAEPGEPDPEQKKSRARERRREGRSKTFDWAEFRPIQQALAQERASTVGSSDSGDPGCLEAEPGELERERARRREERRKRFGMLDTNDGPGMEDTALRMDIDRSPGLLGTPDLKTQNVHVEIEQRWHQVETTPLREEKQVPIAPLHLSLEDRSERLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSINSDIEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTREGGGESTGLPLTQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPEGTTVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSVIEQVSWDN
Protein: Histone deacetylase complex subunit SAP18 (18 kDa Sin3-associated polypeptide) (2HOR0202) (Cell growth-inhibiting gene 38 protein) (Sin3-associated polypeptide p18) (O00422)
Organism: Homo sapiens (Human)
Function: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function.
Subcellular location: Nucleus {ECO:0000269|PubMed:16314458}. Cytoplasm {ECO:0000269|PubMed:16314458}. Nucleus speckle {ECO:0000269|PubMed:20966198}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (PubMed:20966198). {ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:20966198}.
Interaction partners:
- Apoptotic chromatin condensation inducer in the nucleus
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- Histone deacetylase complex subunit SAP30
- RNA-binding protein with serine-rich domain 1
- Sin3 histone deacetylase corepressor complex component SDS3
- Histone deacetylase 1
- Pinin
- Histone deacetylase 2
- Paired amphipathic helix protein Sin3a
Sequence:
MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFTDVKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPPSGRMRPY
Protein: PH domain-containing protein (H1UBJ0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLLIVKQRGANYVCKDYIMCSNLMLNEWICPEEPLSFQVLSFDNPRAQYVFMASSMEQKRTWMQELKRMMLDHYSVEIPEKTKQLMLSIDNTRIVPFGRPEFAEVSMKNHKKVPKYLEKRRKSVDAKEESNRRRSLSASRLLGGSKTSISEPIKEEQKCTCHMNGGIYNGANPTTSKSIVHITEPNSAAVMSSRSRYQQARNRRLPPRHNQESRSTSSRRMGEEEIDRTFDQLYEELVSFGDSTKPTVTSNRSQRLRSEAPQSTVTTITVAATPATATLSIAECANTRLRSKSLTRLDEYEAEPISLKPSIERRYSKVDQLKKRSRKYQVNQEPEAADVLRPSVGRFSLTDHEIIIHGEEPYKRSSGRQRTPLTAQQTAELDDYFPSSNSMNSAPQTCSSSATPSLMSIIRQYENA
Protein: AP-3 complex subunit delta-1 (AP-3 complex subunit delta) (Adaptor-related protein complex 3 subunit delta-1) (Delta-adaptin) (O14617)
Organism: Homo sapiens (Human)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. Involved in process of CD8+ T-cell and NK cell degranulation. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit sigma-1
- AP-3 complex subunit mu-1
- AP-3 complex subunit beta-1
- AP-3 complex subunit sigma-2
- AP-3 complex subunit mu-2
- AP-3 complex subunit beta-2
- AP-4 complex subunit beta-1
- AP-4 complex subunit mu-1
- Arpin
- AP-1 complex subunit mu-1
Sequence:
MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRIGYLAASQSFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAVLISLSSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQYITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSALLDSAHLLASSTQRNGICEVLYAAAWICGEFSEHLQEPHHTLEAMLRPRVTTLPGHIQAVYVQNVVKLYASILQQKEQAGEAEGAQAVTQLMVDRLPQFVQSADLEVQERASCILQLVKHIQKLQAKDVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPLSDSESEDERPRAVFHEEEQRRPKHRPSEADEEELARRREARKQEQANNPFYIKSSPSPQKRYQDTPGVEHIPVVQIDLSVPLKVPGLPMSDQYVKLEEERRHRQKLEKDKRRKKRKEKEKKGKRRHSSLPTESDEDIAPAQQVDIVTEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPIQKHRNTETSKSPEKDVPMVEKKSKKPKKKEKKHKEKERDKEKKKEKEKKKSPKPKKKKHRKEKEERTKGKKKSKKQPPGSEEAAGEPVQNGAPEEEQLPPESSYSLLAENSYVKMTCDIRGSLQEDSQVTVAIVLENRSSSILKGMELSVLDSLNARMARPQGSSVHDGVPVPFQLPPGVSNEAQYVFTIQSIVMAQKLKGTLSFIAKNDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMSSIKVDGIRMSFQNLLAKICFHHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGENSVSVDGKCSDSTLLSNLLEEMKATLAKC
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.179) (Q72CS9)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Oxidoreductase, short chain dehydrogenase/reductase family
- Enoyl-[acyl-carrier-protein] reductase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Oxidoreductase, short chain dehydrogenase/reductase family
- Acyl carrier protein
- Acetyl-coenzyme A carboxylase carboxyl transferase subunits beta/alpha
- Beta-ketoacyl synthase, putative
Sequence:
MTGKRVVVTGLAALTPLGNDIETSWDNLVAGKSGIGPITRFDATEYASRIAGEVKDFDPEKFMPAKQARRMDRFVQFAVATGKMLVEHSGLVIDESNADRVGVLLGVGLGGLETIEVFHTKLMEAGPNKVSPFMIPMLISNMAPGQVSIFTGARGPNVVMTSACASATHAIGYAFSEIKLGRIDAAITGGVESTITPMGVSGFTALKALSTAHNDSPEKASRPFDKERDGFVLGEGSGMLMLESLDSALARGATIYAEVVGFGASGDAYHMTAPHESGDGMALAMRNAVREAGIPVEAVDHINAHATSTHLNDLCETRAIKQVFGQHAYNIAITANKSMTGHLLGAAGGLESVFTVLTLHRGIIPGTINHETPDPECDLNYMTEGSKEMQAHYALCNSFGFGGTNASLLFKRYED
Protein: Peptidase zinc-dependent (Q2IDH1)
Organism: Anaeromyxobacter dehalogenans (strain 2CP-C)
Interaction partners:
- Transcriptional regulator, CarD family
- Glycosyltransferase RgtA/B/C/D-like domain-containing protein
- DUF4179 domain-containing protein
Sequence:
MIRVVTLDPVDPTDMAALIRTLYQAFGLGTEFAGEKPVPAEAEGKDGRLDAITLLREVEPVRTFADDKVLYIAGAPLSLPPGPLGEPPCWGFADYGKERAVITTAKLPARGVTEASIETYRRRLAREAIHAIGHLWDLHHCVDARCAMHPSWSPSLAANPDSDLCTFCREKSERKIRLAKT
Protein: BTB/POZ and MATH domain-containing protein 1 (Protein BTB-POZ AND MATH DOMAIN 1) (AtBPM1) (Q8L765)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:19843165}.
Interaction partners:
- Cullin-3A
- Cullin-3B
- L-type lectin-domain containing receptor kinase I.7
- Homeobox-leucine zipper protein ATHB-6
- Transcription factor MYB56
- UDP-glycosyltransferase 74E1
Sequence:
MGTTRVCSEVSSGSSKSLSQSLTVSTSTTETVNGFHEFKICGYSLAKGVGVGKYVASDTFMVGGYSWAIYFYPDGKSPEDNSSYVSLFIALASEGADVRALFELTLVDQSGNGKHKVHSHFGRALDSGPYTLKYRGSMWGYKRFFRRSSLESSDYLKENSLLVRCRVGVVKSVTEGPRYYNIPVPVSNLGQQLGNLLESGKGCDVVFQVDGETFNAHKLVLATRSPVFNAQLFGPLGDRNTKCITIEDMEAPIFKVLLHFIYWDELPDMQELIGTDSTLASTLVAQHLLAAADRYALERLKAICESKLCEGVAINTVATTLALAEQHHCLQLKAVCLKFVALPENLKAVMQTDGFDYLKESCPSLLTELLQYVARLSEHSVIVSGHRKEIFADGCDASGRRVKPRLH
Protein: Cytochrome b559 subunit beta (PSII reaction center subunit VI) (P09191)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:34937700}.
Interaction partners:
- Photosystem II D2 protein
- Photosystem II reaction center protein X
- Photosystem II protein D1 2
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein K
- Photosystem II CP47 reaction center protein
- Photosystem II extrinsic protein O
- Photosystem II reaction center protein Y
- Photosystem II reaction center protein J
- Photosystem II extrinsic protein V
Sequence:
MATQNPNQPVTYPIFTVRWLAVHTLAVPSVFFVGAIAAMQFIQR