wanglab/gogpt-training-data huggingface dataset:
Protein: AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) (F1MH24)
Organism: Bos taurus (Bovine)
Function: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Preferentially, may phosphorylate substrates on threonine residues. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11877461}; Peripheral membrane protein {ECO:0000269|PubMed:11877461}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:P0C1X8}. Presynapse {ECO:0000250|UniProtKB:P0C1X8}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:P0C1X8}.
Interaction partners:
- AP-2 complex subunit mu
- Numb-like protein
- Protein numb homolog
- AP-1 complex subunit beta-1
- RALBP1 associated Eps domain containing 1
- Epidermal growth factor receptor substrate 15
Sequence:
MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINSVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKVITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPTKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKTQPPPSQPLPQSQPKQPQAPPTSQQPPSAPAQALPTQAQATPQHQQQLFLKQQQQQQTAPPAQQPAGTFYQQPQQQAQAPQFQAVHPAAQQPVIAQFPVVSQGSSQQQLIQNFYQQQQQQQQLATALHQQQLLTQQAALQQKTTAAAAPQPQAQPAAAASPAPAQEPAQIQAPVRQQPKVQTTPPPTIQGQKLGSLTPPSSPKAQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRASQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKYPEKLGGSAESLIPGFQPTQGDAFAASSFSAGTAEKRKGGQTMDSSLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLIDCSLLSNPTTDLLEEFAPIAISAPAHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL
Protein: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4 (EC 2.4.1.149) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4) (BGnT-4) (Beta-1,3-Gn-T4) (Beta-1,3-N-acetylglucosaminyltransferase 4) (Beta3Gn-T4) (Q9C0J1)
Organism: Homo sapiens (Human)
Function: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,4-galactosyltransferase 2
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 4
- Beta-1,4-galactosyltransferase 1
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Galactoside alpha-
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT6
Sequence:
MLPPQPSAAHQGRGGRSGLLPKGPAMLCRLCWLVSYSLAVLLLGCLLFLRKAAKPAGDPTAHQPFWAPPTPRHSRCPPNHTVSSASLSLPSRHRLFLTYRHCRNFSILLEPSGCSKDTFLLLAIKSQPGHVERRAAIRSTWGRVGGWARGRQLKLVFLLGVAGSAPPAQLLAYESREFDDILQWDFTEDFFNLTLKELHLQRWVVAACPQAHFMLKGDDDVFVHVPNVLEFLDGWDPAQDLLVGDVIRQALPNRNTKVKYFIPPSMYRATHYPPYAGGGGYVMSRATVRRLQAIMEDAELFPIDDVFVGMCLRRLGLSPMHHAGFKTFGIRRPLDPLDPCLYRGLLLVHRLSPLEMWTMWALVTDEGLKCAAGPIPQR
Protein: Hyaluronan synthase 1 (EC 2.4.1.212) (Hyaluronate synthase 1) (Hyaluronic acid synthase 1) (HA synthase 1) (HuHAS1) (Q92839)
Organism: Homo sapiens (Human)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction. Also able to catalyze the synthesis of chito-oligosaccharide depending on the substrate (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-glucose 6-dehydrogenase
- CD44 antigen
- Hyaluronidase-1
Sequence:
MRQQDAPKPTPAACRCSGLARRVLTIAFALLILGLMTWAYAAGVPLASDRYGLLAFGLYGAFLSAHLVAQSLFAYLEHRRVAAAARGPLDAATARSVALTISAYQEDPAYLRQCLASARALLYPRARLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAAAGAVGAGAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCLRMVLLSLYAPLYMCGLLPAKFLALVTMNQSGWGTSGRRKLAANYVPLLPLALWALLLLGGLVRSVAHEARADWSGPSRAAEAYHLAAGAGAYVGYWVAMLTLYWVGVRRLCRRRTGGYRVQV
Protein: Voltage-dependent L-type calcium channel subunit beta-2 (CAB2) (Calcium channel voltage-dependent subunit beta 2) (Q8VGC3)
Organism: Rattus norvegicus (Rat)
Function: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:12042350}; Peripheral membrane protein {ECO:0000269|PubMed:12042350}; Cytoplasmic side {ECO:0000269|PubMed:12042350}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent calcium channel subunit alpha-2/delta-2
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent L-type calcium channel subunit alpha
Sequence:
MVQSDTSKSPPIAAVAQESQMELLESAAPAGALGAQSYGKGARRKNRFKGSDDSTSSDTTSNSFVRQGSADSYTSRPSDSDVSLEEDREAVRREAERQAQAQLEKAKTKPVAFAVRTNVRYSAAQEDDVPVPGMAISFEAKDFLHVKEKFNNDWWIGRLVKEGCEIGFIPSPVKLENMRLQHEQRAKQGKFYSSKSGGNSSSSLGDIVPSSRKSTPPSSAIDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKKTEHTPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFEGRISITRVTADISLAKRSVLNNPSKHAIIERSNTRSSLAEVQSEIERIFELARTLQLVVLDADTINHPAQLSKTSLAPIIVYVKISSPKVLQRLIKSRGKSQAKHLNVQMVAADKLAQCPPQESFDVILDENQLEDACEHLADYLEAYWKATHPPSSNLPNPLLSRTLATSTLPLSPTLASNSQGSQGDQRTDRSAPRSASQAEEEPCLEPVKKSQHRSSSATHQNHRSGTGRGLSRQETFDSETQESRDSAYVEPKEDYSHEHVDRYVPHREHNHREESHSSNGHRHREPRHRTRDMGRDQDHNECSKQRSRHKSKDRYCDKEGEVISKRRSEAGEWNRDVYIRQ
Protein: Co-chaperone protein p23-1 (Atp23-1) (p23 co-chaperone) (Q8L7U4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a co-chaperone for HSP90. Controls root development through the modulation of auxin distribution in the root meristem.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26163704}. Nucleus {ECO:0000269|PubMed:26163704}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP40
- Protein SGT1 homolog B
- Heat shock protein 90-1
- Endoplasmin homolog
- Protein SGT1 homolog A
- Co-chaperone protein p23-2
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
- Heat shock protein 90-6, mitochondrial
- Heat shock protein 90-5, chloroplastic
- Heat shock protein 90-4
Sequence:
MSRHPEVKWAETTEKIFLTVVLADTKDTKVNLDPEGVFDFSAKVGPENHVYELKLELADKVNVEESKINIGERSIFCIIEKAEPERWNKLLRVKKPPHYVKVDWDKWVDEDDEGSAGAADMDMAGMEGMGGMGGMGGMGGMGGMGGMGGMGGMEGMDFSKLMGGMGGMGGMGGLEGLGGMGGMGGMGGMGGMGGMEEFEDSDDEEETAKSGDKKDDAVKEEGLATEKAPAAEETTSVKEDK
Protein: Importin-11 (Imp11) (Ran-binding protein 11) (RanBP11) (Q9UI26)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBE2E3, and of RPL12 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11032817}. Nucleus {ECO:0000269|PubMed:11032817}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 E3
- Importin-5
- Large ribosomal subunit protein uL11
- Importin subunit beta-1
- Leucine-rich repeat-containing protein 70
- Large ribosomal subunit protein uL23
- Importin-13
- Transportin-3
- Importin-4
- Ubiquitin-conjugating enzyme E2 E1
Sequence:
MDLNSASTVVLQVLTQATSQDTAVLKPAEEQLKQWETQPGFYSVLLNIFTNHTLDINVRWLAVLYFKHGIDRYWRRVAPHALSEEEKTTLRAGLITNFNEPINQIATQIAVLIAKVARLDCPRQWPELIPTLIESVKVQDDLRQHRALLTFYHVTKTLASKRLAADRKLFYDLASGIYNFACSLWNHHTDTFLQEVSSGNEAAILSSLERTLLSLKVLRKLTVNGFVEPHKNMEVMGFLHGIFERLKQFLECSRSIGTDNVCRDRLEKTIILFTKVLLDFLDQHPFSFTPLIQRSLEFSVSYVFTEVGEGVTFERFIVQCMNLIKMIVKNYAYKPSKNFEDSSPETLEAHKIKMAFFTYPTLTEICRRLVSHYFLLTEEELTMWEEDPEGFTVEETGGDSWKYSLRPCTEVLFIDIFHEYNQTLTPVLLEMMQTLQGPTNVEDMNALLIKDAVYNAVGLAAYELFDSVDFDQWFKNQLLPELQVIHNRYKPLRRRVIWLIGQWISVKFKSDLRPMLYEAICNLLQDQDLVVRIETATTLKLTVDDFEFRTDQFLPYLETMFTLLFQLLQQVTECDTKMHVLHVLSCVIERVNMQIRPYVGCLVQYLPLLWKQSEEHNMLRCAILTTLIHLVQGLGADSKNLYPFLLPVIQLSTDVSQPPHVYLLEDGLELWLVTLENSPCITPELLRIFQNMSPLLELSSENLRTCFKIINGYIFLSSTEFLQTYAVGLCQSFCELLKEITTEGQVQVLKVVENALKVNPILGPQMFQPILPYVFKGIIEGERYPVVMSTYLGVMGRVLLQNTSFFSSLLNEMAHKFNQEMDQLLGNMIEMWVDRMDNITQPERRKLSALALLSLLPSDNSVIQDKFCGIINISVEGLHDVMTEDPETGTYKDCMLMSHLEEPKVTEDEEPPTEQDKRKKMLALKDPVHTVSLQQFIYEKLKAQQEMLGEQGFQSLMETVDTEIVTQLQEFLQGF
Protein: Homeobox protein Hox-C9 (Homeobox protein Hox-3B) (P31274)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-C6
- Homeobox protein Hox-C10
- Homeobox protein Hox-C8
- Pre-B-cell leukemia transcription factor 2
- Pre-B-cell leukemia transcription factor 1
- Pre-B-cell leukemia transcription factor 3
- Homeobox protein Hox-C4
- Transmembrane protein 26
- Pre-B-cell leukemia transcription factor 4
Sequence:
MSATGPISNYYVDSLISHDNEDLLASRFPATGAHPAAARPSGLVPDCSDFPSCSFAPKPAVFSTSWAPVPSQSSVVYHPYGPQPHLGADTRYMRTWLEPLSGAVSFPSFPAGGRHYALKPDAYPGRRADCGPGEGRSYPDYMYGSPGELRDRAPQTLPSPEADALAGSKHKEEKADLDPSNPVANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARVLNLTERQVKIWFQNRRMKMKKMNKEKTDKEQS
Protein: Gap junction protein (Q6AZ42)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU000630}.
Interaction partners:
- Gap junction beta-2 protein
- Gap junction beta-1 protein
- Gap junction alpha-1 protein
- Gap junction gamma-1 protein
- Gap junction gamma-2 protein
- ATP-sensitive inward rectifier potassium channel 10
- Gap junction alpha-5 protein
Sequence:
MDWGTLHTVIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETARKFIRGEKRNEFKDLEDIKRQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTVFMISASVICMLLNVAELCYLLLKLCFRRSKRTQAQRNHPNHALKESKQNEMNELISDSGQNAITSFPS
Protein: Cnh1p (A0A1D8PKY1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAWSQLELEPPHIAYACVGIFSTLFSLVSLFVKERLYIGEATVASIAGLILGPHCLNWFDPVSWGNSDYITLEICRIVLCIQIVAVAVELPKKYMMKHWLSVTIFLLPVMTCGWLIVGLFIWCLIPHFTFNDGLLVSACVTATDPVLAAAVVGKGKFAERVPGHLRNLLSAESGCNDGMAFPFIFLSLNLIIHSGHAGEIVKDWFLLTILWECIFGCLLGTVIGYVLRKLVAFAENQNLIDRESFLAIFVFIAFISAGIGSMLGVDDLLVSFAAGTAFGWNGAFAKKTEESHVSTVIDLLLNLSFFVYFGAIIPWPQFNNADLGLNVWRLVVLAFVIIFLRRIPAVVALKPITPDVKTWREALFCGHFGPIGVGAIFASILARKDLEAHYTTEETPLHHLPNEDFPHYQLLATIWPIVCFIVITSIIVHGSSVAVLTLGKRLNRMAITMSFTTDQEGNGSGGWMQRLQKLDRATTSFSLHRVDTMAPTEKSQPETTGTKVRPTGGAKRKKNHRDDRTPPEAQILQLGGNKTPEPESASDTLAIPNKTSGLSAFGEKPPTKAEKAPVPTVAYQDGDQVIIEDQYGEVMENLKLTTKPVRAPDIGSIHSMESLERHLTQYSTGSGEYTTDEDTHGLQEKLSRSLSRRSYYKKDDPNKRKVYAHRVDDLIVIENEDGDIIRRYKVNKHAPAPRARSGSIMGMVKSMVGIKPPPEISVTDLEHGTQHKIILPEEENTPMSSKTEQKLEDTIANILQENHTQPISEESADEESADEEETEVEKKRRLQALGYLPSSRRDREDEEE
Protein: Histone H2B.1 (Suppressor of Ty protein 12) (P02293)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2A.Z
- Histone H3
- Histone H2A.2
- Histone H4
- Histone H2A.1
- FACT complex subunit SPT16
- Histone H2B.2
- Histone H3-like centromeric protein CSE4
- FACT complex subunit POB3
- Regulatory protein SIR3
Sequence:
MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
Protein: Putative truncated guanine nucleotide exchange factor SDC25 (P0CF34)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Promotes the exchange of Ras-bound GDP by GTP.
Interaction partners:
Sequence:
MPITSSPDLFYLNDCDVVYWYDLTRLVCHYVNLTERDLLANEREKFLTSLDLLTAQITYVYMLFRNLRLVEDSFKKTLKKLIYTLSRFSINANIWFHSTLFEEREAIASQKDPERRSPLLQSILGTFQKFHFLLRLLHFLSNPNELTILPQLTPRFFKDSFNTISWNNPFLRKRLNQHMSHDLPRQMIKAVAGASGIVAENIDEIPASKQGTSCSSETSHHSPSAPFQRRRRGTIFSNVSGSSDESDTIWSKRKKPYPLNEETLSLVRARKKQLDGKLKQMIKSANEYLSNTANFSKMLNFEMNFKTYEEVSGTIPIIDILENLDLTIFLNLRELGDENRVFDEDVAIDDEDEEFLKHSLSSLSYILSDYFNMKQYFHDVVVKFIIVAQHLTLEDPFVFSPMQNDLPTGYYEPMKPSSLNLDNAKDKKNGSQNTDIQEEEDEYEPDPDSLILFHNLINQDSDFNDLKFFNLAHVFKKSCDDYFDVLKLAIEFVNQLILERENLLNYAARMMKNNITELLLRGEEGYGSYDGGETAEKSDTNAVYADSDTKDNDEWRDSQVKLPRYLQREYDSELIWGSNNRIKGGSKHALISYLTDNEKKDLFFDITFLITFRSIFTTTEFLSYLISQYNLDPPEDLCFEEYNEWVTKKLIPVKCRVVEIMTTFFKQYWFLGYDEPDLATLNLDYFAQVAIKENITGSVELLKEVNQKFKHGNIQEATAPMKTLDQQICQDHYSGTLYSTTESILAVDPVLFATQLTILEHEIYCEITIFDCLQKIWKNKYTKSYGASPGLNEFISFANKLTNFISYSVVKEADKSKRAKLLSHFIFIAEYCRKFNNFSSMTAIISALYSSPIYRLEKTWQAVIPQTRDLLQSLNKLMDPKKNFINYRNELKSLHSAPCVPFFGVYLSDLTFTDSGNPDYLVLEHGLKGVHDEKKYINFNKRSRLVDILQEIIYFKKTHYDFTKDRTVIECISNSLENIPHIEKQYQLSLIIEPKPRKKVVPNSNSNNKSQEKSRDDQTDEGKTSTKKDRFPKFQLHKTKKKAPKVSK
Protein: Probable inactive poly [ADP-ribose] polymerase SRO1 (Protein SIMILAR TO RCD ONE 1) (O82289)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable inactive ADP-ribosyltransferase that functions with RCD1 to regulate oxidative stress, hormonal and developmental responses. May regulate some stress-responsive genes. Seems to play a smaller developmental role than R.
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:19548978}. Note=Speckle-like pattern.
Interaction partners:
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 4b
- Poly [ADP-ribose] polymerase 2
- Dehydration-responsive element-binding protein 2A
- Protein ADP-ribosyltransferase PARP3
Sequence:
MEAKIVKVSDSSYKDGLGKKRKHPGNYTPYDSGRSYAKLQWVLSPNSSTQKLEKRRNLDGENKVIVSENHVEKSLVRYFSYYKKTGVPKRVMFHENGEWIDLPDHILCDIRNDLEAKRATIEFNWCGRHFLLDFLHMYRLDLETGVKTQLAWIDIAGKCFFPETFDTLERDGCHHIRGEDPEQHDQREIKLHIEIDVNSGELPRLNLNVVTDESGDNMDDFQAVQRSSNGPNDEASEDSCSRELDDAVEKWDKTETDRFSGVKPAEEELDKDAVKQMFALGAATLGHVESLDVYQFSSEIAKARLSLFQKQADITKKHRGDANIRYAWVPAKKEVLSAVMMHGLGVGGAFIKKSMYGVGVHAANCPYFSARYCDIDDNGVRHMVLCRVIMGNMEPLRGDNTQYFTGGEEYDNGVDDVESPKHYLIWNMNMNTHIYPEFVVSFKLSIPNAEGNILPTTQSRHESSGLTLEGPKGSPSNEPGRVSNGGSGSEKNSSSSRRPRSPIMPFPLLFKAISSKIARKDMDLIIAGYQELREKKVSRKEFYKTLSMIVGDDDLLISTITGLQRSLG
Protein: Atrial natriuretic peptide receptor 1 (EC 4.6.1.2) (Atrial natriuretic peptide receptor type A) (ANP-A) (ANPR-A) (NPR-A) (Guanylate cyclase A) (GC-A) (P18293)
Organism: Mus musculus (Mouse)
Function: Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Natriuretic peptides B
- Natriuretic peptides A
- Atrial natriuretic peptide receptor 2
- Pro-glucagon
- Pro-opiomelanocortin
- VIP peptides
- Pituitary adenylate cyclase-activating polypeptide
- Bis
- Inosine triphosphate pyrophosphatase
- Gastric inhibitory polypeptide
Sequence:
MPGSRRVRPRLRALLLLPPLLLLRSGHASDLTVAVVLPLTNTSYPWSWARVGPAVELALGRVKARPDLLPGWTVRMVLGSSENAAGVCSDTAAPLAAVDLKWEHSPAVFLGPGCVYSAAPVGRFTAHWRVPLLTAGAPALGIGVKDEYALTTRTGPSHVKLGDFVTALHRRLGWEHQALVLYADRLGDDRPCFFIVEGLYMRVRERLNITVNHQEFVEGDPDHYTKLLRTVQRKGRVIYICSSPDAFRNLMLLALDAGLTGEDYVFFHLDVFGQSLQGAQGPVPRKPWERDDGQDRRARQAFQAAKIITYKEPDNPEYLEFLKQLKLLADKKFNFTMEDGLKNIIPASFHDGLLLYVQAVTETLAQGGTVTDGENITQRMWNRSFQGVTGYLKIDRNGDRDTDFSLWDMDPETGAFRVVLNFNGTSQELMAVSEHRLYWPLGYPPPDIPKCGFDNEDPACNQDHFSTLEVLALVGSLSLVSFLIVSFFIYRKMQLEKELVSELWRVRWEDLQPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAIGSHGNLKSSNCVVDGRFVLKITDYGLESFRDPEPEQGHTLFAKKLWTAPELLRMASPPARGSQAGDVYSFGIILQEIALRSGVFYVEGLDLSPKEIIERVTRGEQPPFRPSMDLQSHLEELGQLMQRCWAEDPQERPPFQQIRLALRKFNKENSSNILDNLLSRMEQYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGQLHAREVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALRIHLSSETKAVLEEFDGFELELRGDVEMKGKGKVRTYWLLGERGCSTRG
Protein: T. brucei spp.-specific protein (Q38A12)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRGRNYLTRYYFNTVKLVMDVQSKGMNADCEGAWDVCVCFFFNYCCCLFIYFSEHMCLCCISYFNVSLTTIIYTLVWFLFSSVTLWGTLPHFVTHFFPFHRAIICIYCLLTSIFFSFFFLFVGGDAHQYHGIFHSYVLVPVLNVSLLMFFPPPFSSYFAT
Protein: Expressed protein (Transmembrane protein) (Q8S8K0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKSLHFLAPNSTIINLKQQSYTKTKFQLHRSNRRTLSINCVNSGGDEEKITQPLDGVEIRFKRGSRRKMREEGSGEGGGQSGKKKETVQKPWEEMTLNEKALELYVGEKGLLFWLNKLAYASIYIVIGGWIFFRFVGPAFNLYQLDTPPLDPKNILKG
Protein: 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) (4-hydroxyphenylpyruvic acid oxidase) (4HPPD) (HPD) (HPPDase) (P93836)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10198110}.
Interaction partners:
- Homogentisate 1,2-dioxygenase
- Probable aminotransferase TAT2
- Tyrosine transaminase family protein
- Probable aminotransferase TAT4
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
- Probable aminotransferase TAT3
- Homogentisate solanesyltransferase, chloroplastic
- Aspartate aminotransferase 3, chloroplastic
- Aspartate aminotransferase, cytoplasmic isozyme 2
Sequence:
MGHQNAAVSENQNHDDGAASSPGFKLVGFSKFVRKNPKSDKFKVKRFHHIEFWCGDATNVARRFSWGLGMRFSAKSDLSTGNMVHASYLLTSGDLRFLFTAPYSPSLSAGEIKPTTTASIPSFDHGSCRSFFSSHGLGVRAVAIEVEDAESAFSISVANGAIPSSPPIVLNEAVTIAEVKLYGDVVLRYVSYKAEDTEKSEFLPGFERVEDASSFPLDYGIRRLDHAVGNVPELGPALTYVAGFTGFHQFAEFTADDVGTAESGLNSAVLASNDEMVLLPINEPVHGTKRKSQIQTYLEHNEGAGLQHLALMSEDIFRTLREMRKRSSIGGFDFMPSPPPTYYQNLKKRVGDVLSDDQIKECEELGILVDRDDQGTLLQIFTKPLGDRPTIFIEIIQRVGCMMKDEEGKAYQSGGCGGFGKGNFSELFKSIEEYEKTLEAKQLVG
Protein: DNA repair protein RAD51 homolog 3 (R51H3) (RAD51 homolog C) (RAD51-like protein 2) (Q8R2J9)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O43502}. Cytoplasm {ECO:0000250|UniProtKB:O43502}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O43502}. Mitochondrion {ECO:0000250|UniProtKB:O43502}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA. {ECO:0000250|UniProtKB:O43502}.
Interaction partners:
Sequence:
MQRELVSFPLSPTVRVKLVAAGFQTAEDVLGVKPSELSKEVGISKEEALETLQIVRRESLTDKPRCAGASVAGKKYTALELLEQEHTQGFIITFCSALDNILGGGIPLMKTTEVCGVPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRVVTLANACIQHLHLIAGTHKDEEHQKALEGFTLENILSHIYYFRCHDYTELLAQVYLLPDFLSNHSKVQLVIIDGIALPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDKNQALLVPALGESWGHAATIRLIFHWEQKQRFATLYKSPSQKESTIPFQITPQGFRDAAVTASSSQTEGSSNLRKRSREPEEGC