wanglab/gogpt-training-data huggingface dataset:
Protein: Probable LRR receptor-like serine/threonine-protein kinase At5g10290 (EC 2.7.11.1) (C0LGT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Alpha-hydroxynitrile lyase
- F14O23.23 protein
Sequence:
MRMFSLQKMAMAFTLLFFACLCSFVSPDAQGDALFALRISLRALPNQLSDWNQNQVNPCTWSQVICDDKNFVTSLTLSDMNFSGTLSSRVGILENLKTLTLKGNGITGEIPEDFGNLTSLTSLDLEDNQLTGRIPSTIGNLKKLQFLTLSRNKLNGTIPESLTGLPNLLNLLLDSNSLSGQIPQSLFEIPKYNFTSNNLNCGGRQPHPCVSAVAHSGDSSKPKTGIIAGVVAGVTVVLFGILLFLFCKDRHKGYRRDVFVDVAGEVDRRIAFGQLKRFAWRELQLATDNFSEKNVLGQGGFGKVYKGVLPDNTKVAVKRLTDFESPGGDAAFQREVEMISVAVHRNLLRLIGFCTTQTERLLVYPFMQNLSLAHRLREIKAGDPVLDWETRKRIALGAARGFEYLHEHCNPKIIHRDVKAANVLLDEDFEAVVGDFGLAKLVDVRRTNVTTQVRGTMGHIAPEYLSTGKSSERTDVFGYGIMLLELVTGQRAIDFSRLEEEDDVLLLDHVKKLEREKRLGAIVDKNLDGEYIKEEVEMMIQVALLCTQGSPEDRPVMSEVVRMLEGEGLAERWEEWQNVEVTRRHEFERLQRRFDWGEDSMHNQDAIELSGGR
Protein: Probable galacturonosyltransferase 13 (EC 2.4.1.-) (Q0WV13)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pectin and/or xylans biosynthesis in cell walls (By similarity). Together with GAUT14, required for pollen tube growth, possibly through the regulation of pectin biosynthesis and repartition in the pollen tube wall.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23709340}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Cellulose synthase-like protein D1
- Galacturonosyltransferase
- Cellulose synthase-like protein D4
- Probable pectinesterase 48
- RBR-type E3 ubiquitin transferase
- At3g15420
- Expressed protein
- Alpha/beta hydrolase family protein
- Alkaline ceramidase TOD1
- Pectinesterase PPME1
Sequence:
MQLHISPSMRSITISSSNEFIDLMKIKVAARHISYRTLFHTILILAFLLPFVFILTAVVTLEGVNKCSSFDCFGRRLGPRLLGRIDDSEQRLVRDFYKILNEVSTQEIPDGLKLPESFSQLVSDMKNNHYDAKTFALVFRAMVEKFERDLRESKFAELMNKHFAASSIPKGIHCLSLRLTDEYSSNAHARRQLPSPELLPVLSDNAYHHFVLATDNILAASVVVSSAVQSSSKPEKIVFHVITDKKTYAGMHSWFALNSVAPAIVEVKSVHQFDWLTRENVPVLEAVESHNSIRNYYHGNHIAGANLSETTPRTFASKLQSRSPKYISLLNHLRIYLPELFPNLDKVVFLDDDIVIQKDLSPLWDIDLNGKVNGAVETCRGEDVWVMSKRLRNYFNFSHPLIAKHLDPEECAWAYGMNIFDLRTWRKTNIRETYHSWLKENLKSNLTMWKLGTLPPALIAFKGHVQPIDSSWHMLGLGYQSKTNLENAKKAAVIHYNGQSKPWLEIGFEHLRPFWTKYVNYSNDFIKNCHILE
Protein: Protein roller-3 (Q8I7I5)
Organism: Caenorhabditis elegans
Function: Thought to have a role in developmental establishment of posterior morphology.
Subcellular location: Membrane {ECO:0000255, ECO:0000305}; Single-pass type I membrane protein {ECO:0000255, ECO:0000305}.
Interaction partners:
- Tyrosine protein-kinase src-1
- Apple domain-containing protein
- SAM domain-containing protein
- Protein kinase domain-containing protein
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- GILT-like protein F37H8.5
Sequence:
MLSLHLRSLAILFLLFFLLHDVVKSATVFSSSLKTCQSQCEERNLAYPLDSGEVHWTGLAEYNYSSRISSCRHGCEDVDERESKCDVKCSEEGIVSNACKQGCRAVLVSFLAQAQALLIQVHVNMEVLETSMKLKWEFPETLAEELKEIANADIFWFSQTKPLNGILGWRWTSLPQNSFRNSSLSSEVHVPFEHGEHVEVRLALSYRNQVLVSRTTTYHLPLSKSGTTLEVIGQLQLSDDRVAVCYRTNQPTPKFKLTIMTLNDNTINTEESIARCHLFSNLPRDNCCKASISAIDEHGATTAFVEIKLDFYVNQVEIELVSVASSRLIFSNGTHLLESEIDQYALGDSATVIPFPLPTDDTITAIAGISDTTIAIGSSKGSLWTYQMSANQTDEDQPSSVIQLKTVGEMDTKINQIEIDHIQRTLYAVQHDKGIIRCKLRTMEAEESPNCVLIVNNDALNAPKEITLDSVNGHVYTLNADNKVYRTEMVAFNATGIETVASLQYLQDMSPSNGIFFDVSKFLLYSALQNGSMMTLNPVTDHVHIFKDVGYADIQHFRIKNDLIYWMKKKCGETDADENCIFAENLQRSEEDIPNKFTYSSSLMSFGVLEEILLKPRITAVSTIAMLTSDKTARVSWDESNTLPFQAQGSSWRNFTYFLKVTAPDITDFSPIEIYTSNTEMKIDVTPGNIYNAQVQVCSDDFCSIPTSTSNTALPDLGDVVPFVFTKRQADDIISVDILGNIIPADDSVKIVEKLQYPHVLDNTTKTVYLAGDHSMGIFKKYLDDTAGLPKPFKDGLFVEMMSIMPARSIILIASSYKITSYRLPTTFDFEYFSCEEPLEACSEVMGISSDDTTGMVHFLTQARNGTITLWESDPENRTPRDIASVPSIVPFRRFLILHDKMILVTKNNHIVQTDKKLKVVNVATELERVDHILPLRYATISHKIEFSDEIKFIDGSKTNLQWTLSPPLEAGTVLFKVSIFREKMGGQDPPIITIQSETNFTIPSEVLEAWSSAQRFDVSVQAMTPWATAVLNRTGLTAPVKPPTSPTQLRIFATQQKTVDGPRALISFFWGPPSEWNGTPYQYIVNCTKDDGSWIGGPVTTSQSHYSFAVKSGKVSCQAAAANEPTNIGSFSELITIDSSELKPLVKLFAIDSTNSLISINDLAHEEPRRETRQVAQPVKLEYQAMAFIGEDLYAVRKEGESAQPVLVQIDTNHIDNTVHKVSIGGDVTRIDAMTSDWVGNRLIFVAGTNVYQLSLEPFLSTSLLNPHKLIQLTSATDAKQLAYDPFMNTAYLLTKNGSLFALDMNKNTEANLALTVSCLASQTVTWMMTEFAWNRASSPKIYALTWNGLIYVDLTEDSQCNEVRIDWTKFGDKGLKDISSFAIADKLFAFVTSSEMLIYGKDTVTPITIANPPLKQILAVSQSSQPYPERSCFELPSSKGIVFSIVNEGKTGSFLEVTKSSSSSSCQEVSMPQTQYEIYFTRKNTDKVKHVRSFSDRIHVENGILDKETDYDVTVTWLNRYSPASGVSASKSFRTGFGYPSAPRDPHAIPVTPDTVYLYWNLPETLNAPISEIKYKISQQAAGISVPTSIAVIALSETVSSNISSDTTSCLINPCRVKIANLRPSNEYKFWVTATHISHLDAATILKDDDAVSSEAVARTLDVPGTLRPDNVTGSSLLLRWNGLEPEHRPSSIAVQYRESGGANNEWQFPMNVSFEPDVTTELVPITNLLSATSYDYRFVATYTGTYTIDGKVLAFKEDYLQLPQQARTKAGVPTAPQFVEAKQDEEGWIVTWKEPMSDGGSPITSYAVETRINKTAEWEIAERGLDGWKTWWRPGKSDTTSSTSTSSTEVSEFRIRAANIEGFGAYAYTEDKKEEKEEEPSSVLPYLLLLSIIFLLAAMILVACFWLKSRRRQQQKKREAEDERNCIRLDVVANMNFSSSHQSLPPEYESEMRNLPVVNYSTVTFNDYIDTCAYGIVHSGTAEEVPMSWEKDVRVAIKKLKPNHSFQEKMMFMKEAILLNNLDHPNIVKELGVCITPGQELILLEYMEGGNLLKFLQKSTPNEYQSSELSPRDLLSISVDIARGMNYLERLPHVHKNLSARKCLLAGRPGVTKLEMGMSKELSNGQVNRSDLENMEIVRWMAPEVLKDFQFSSKSDVWAYGVLLYEVFSFGEVPYGDKDNRRIMTDVRNGSVLPIPSYCPSKRIYKVIKQCLTSDSTKRANFATILKIFETFRDDQKCQDDKPIQFNDGTDNTNFSASQDSTSSREPPSPSHRMRDFIDTRDLEPPSPSHLNQSFGGFEHPYEGERPATMWNGSGARNSAKNSIGRSMKKEKLRNPIHSMDDLVARNQRPLSIHSEDTESTDYGASSSMYSPGSSNRISSQVDPPIGRLSSAPGIGIVNDAFESSNPSLNLSRSWAGLSREVNQNPAGAGSSGTLPQHTNSAGHLRLPGVQVGAGGGRVYRNASGGGGPSNRGRISQV
Protein: Lipoxygenase 2.3, chloroplastic (EC 1.13.11.12) (LOX2:Hv:3) (Q8GSM2)
Organism: Hordeum vulgare (Barley)
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. This enzyme exhibits linoleate 13-lipoxygenase activity.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MIHLKQPLVLSAQSSNVASPLFVAGGQQRRASGAGRTCSGRRLSARRISCASTEEAVGVSTSVTTKERALTVTAIVTAQVPTSVYVARGLDDIQDLFGKTLLLELVSSELDPKTGRERERVKGFAHMTLKEGTYEAKMSVPASFGPVGAVLVENEHHREMFIKDIKLITGGDESTAITFDVASWVHSKFDDPEPRAFFTVKSYLPSQTPPGIEALRKKELETLRGDGHSERKFHERVYDYDTYNDLGDPDKNIDHKRPVLGTKEHPYPRRCRTGRPKTLYDPETETRSSPVYVPRDEQFSDVKGRTFSATTLRSGLHAILPAVAPLLNNSHGFSHFPAIDALYSDGIPLPVDGHGGNSFNVINDVIPRVVQMIEDTTEHVLRFEVPEMLERDRFSWFRDEEFARQTLAGLNPICIRRLTEFPIVSKLDPAVYGPAESALSKEILEKMMNGRMTVEEAMEKKRLFLLDYHDVFLPYVHRVRELPDTTLYGSRTVFFLSDEGTLMPLAIELTRPQSPTKPQWKRAFTHGSDATESWLWKLAKAHVLTHDTGYHQLVSHWLRTHACVEPYIIATNRQLSRMHPVYRLLHPHFRYTMEINALAREALINADGIIEEAFLAGKYSIELSSVAYGAAWQFNTEALPEDLINRGLAVRRDDGELELAIKDYPYADDGLLIWGSIKQWASDYVDFYYKSDGDVAGDEELRAWWEEVRTKGHADKKDEPWWPVCDTKENLVQILTIIMWVTSGHHAAVNFGQYHYAGYFPNRPTVVRRNIPVEENRDDEMKKFMARPEEVLLQSLPSQMQAIKVMATLDILSSHSPDEEYMGEYAEPAWLAEPMVKAAFEKFSGRLKEAEGTIDMRNNNPENKNRCGAGIVPYELLKPFSEPGVTGRGIPNSISI
Protein: Actin-related protein 2 (Actin-like protein 14D) (Actin-like protein 2) (P45888)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 3
- RE12101p
- Glia maturation factor
- WHAMM and JMY related, isoform B
Sequence:
MDSKGRNVIVCDNGTGFVKCGYAGSNFPTHIFPSMVGRPMIRAVNKIGDIEVKDLHVDDLMVGDEASQLRSLLEVSYPMENGVVRNWDDMCHVWDYTFGPKKMDIDPTNTKILLTEPPMNPTKNREKMIEVMFEKYGFDSAYIAIQAVLTLYAQGLISGVVIDSGDGVTHICPVYEEFALPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRIMKEKLCYIGYDIEMEQRLALETTVLVESYTLPDGRVIKVGGERFEAPEALFQPHLINVEGPGIAELAFNTIQAADIDIRPELYKHIVLSGGSTMYPGLPSRLEREIKQLYLERVLKNDTEKLAKFKIRIEDPPRRKDMVFIGGAVLAEVTKDRDGFWMSKQEYQEQGLKVLQKLQKISH
Protein: Guanine nucleotide-binding protein subunit beta 1 (Gbeta mimic kelch protein 1) (Q08886)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Beta subunit of a guanine nucleotide-binding protein (G proteins). G proteins are involved as modulators or transducers in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. Involved in the determination of the cAMP level according to nutritional conditions, most probably as a regulator of cAMP phosphodiesterase. Required for the control of pseudohyphal and haploid invasive growth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Inhibitory regulator protein IRA2
- G protein-coupled receptor GPR1
- Heterotrimeric G protein gamma subunit GPG1
- Inhibitory regulator protein IRA1
- Guanine nucleotide-binding protein alpha-2 subunit
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM13
- Mitochondrial import inner membrane translocase subunit TIM8
- Adenylate cyclase
- Guanine nucleotide-binding protein subunit beta 2
Sequence:
MPQASTFGSHSLEAHPLHIQPAVHIKLSKEERSHYREQYDSLKYISNYVSVFDQALSDNIDSRIRKENEALLKKYYESRKPFTFTSFRQGSVISSSDSSTGFTERTKTYCFLNDFVSNCVNEVDPYTLKMTVRNRNTALNMENLDDERKSKDDIYDFEDNTDDECNAKCHGAFHYSSERLEILRSRSTISYFKYYKKLLTVDLRDSDVLKRHNLWMPMITRRFRFLLVSSSKPEDVRLTTPIPTFSESDLDIFKNKTCPLFINGTDCVPRSYDTFSGSSVIASIFSEYKLPSLSYHCSVELNDQLFIVGGLMACHRYDEEAPDLKDFYVDGIKNLPPPLIPELINNPSMIPNPHLYCFSLTSSRLTRPDISGYIPPPLVCTQGCKLTERHIFLYGGFEIKSETQVDDKGRYFIRKRAFLNNTGYILDTVTFNFSKIELVAPPYQFAIYNNFSPRFGHMQASISNSNNNVSNENTTTSAKGRRSISPYRQGNGDHKIDDLVGSPGSTDYLEDDAIPPVTNPRSTDSLSSKHCSTATHICSSVNTILIFGGYSQTGDDKYEAMNDMWKINIPVVSRGKRNYYKFADTVTATKIPIIDDPELWPSRRAFSACCVPDYFTKDVEPIETRLLRNLKNDFSIDLEIRPGNKPSQPLFPNIPHSRKEKKSGRDSMHISNSNNSTSEDTSSKSTRNTTSSPPTSPKHTPPLNPSKKCASIGRTIAFHGGSDGYDVCSDMWWFDFDSETWTKIDLYAKTQEESDGLVPINLCMVGHSMTTVGHKVVLIGGLRQGDVDRIYRDETLPEEVISGVPLGSGVINVVDLNTQCLQGCKLIRNDGDTKESVIMDPHVGTPHQVLAVAGTIELVKGTMTLIGGVVAGREDISSLYLRGAVLQFILPSMNLAN
Protein: GTPase LSG1-2 (AtLSG1-2) (DAR GTPase 7) (Protein YEAST LSG1 ORTHOLOG 2) (Q9SJF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTPase involved in ribosome biogenesis (Probable). Binds to 23S rRNA and associates with 60S pre-ribosomes. Involved in early cotyledon and leaf development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25319368}. Nucleus {ECO:0000269|PubMed:25319368}. Note=The C-terminus is sufficient for the targeting into the nucleus. {ECO:0000269|PubMed:25319368}.
Interaction partners:
- 60S ribosomal export protein NMD3
- Pescadillo homolog
- Probable rRNA-processing protein EBP2 homolog
- Ribosome biogenesis protein BOP1 homolog
- Eukaryotic translation initiation factor 6-2
- Large ribosomal subunit protein uL18y
- Ribosome biogenesis protein BRX1 homolog 2
- ERBB-3 BINDING PROTEIN 1
- RNA-binding NOB1-like protein
- Chlorophyll synthase, chloroplastic
Sequence:
MGKSEKTSLGRSLVKHHNHMIQESKDKGKYYKNLQKKVLESVTEVSDIDAIIEQAEEAERLYTINHSSSTPLSINLDTNSSSSVIAAEEWREQQKIEEALHASSLQVPRRPPWTPEMSVEELDANEKQAFLNWRRMLVSLEENEKLVLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKIMLLVNKADLLPTDVREKWAEYFRLNNILFVFWSAIAATATLEGKVLKEQWRQPDNLQKTDDPDIMIYGRDELLSRLQFEAQEIVKVRNSRAASVSSQSWTGEYQRDQAVVGFVGYPNVGKSSTINALVGQKRTGVTSTPGKTKHFQTLIISDELMLCDCPGLVFPSFSSSRYEMIASGVLPIDRMTEHREAIQVVADKVPRRVIESVYNISLPKPKTYERQSRPPHAAELLKSYCASRGYVASSGLPDETKAARLILKDYIGGKLPHYAMPPGMPQADEPDIEDTQELEDILEGSESDDSAVGDETENEQVPGIDDVLDDLSSFDLANGLKSSKKVTAKKQTASHKQHKKPQRKKDRTWRVQNTEDGDGMPSVKVFQKPANTGPLTMR
Protein: Polygalacturonase QRT3 (AtQRT3) (PG QRT3) (EC 3.2.1.15) (Pectinase QRT3) (Protein QUARTET 3) (O49432)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Polygalacturonase required for degrading the pollen mother cell wall during microspore development.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:14551328}.
Interaction partners:
- Polygalacturonase QRT2
- Pectinesterase QRT1
- Probable glucan endo-1,3-beta-glucosidase A6
- ATA20 protein
- Cytochrome P450 703A2
- Non-specific lipid-transfer protein 12
- Protein RIK
- Tetraketide alpha-pyrone reductase 2
- Polygalacturonase ADPG2
- 3-ketoacyl-CoA synthase 7
Sequence:
MELRKSQVAMPVFLAIMSLMVSQVVFAEKDSGSMSPHDRALAEMQALKASLVRRNLPALVSPPPTPPQAVPGPRVYQVISYGADPTGKLDSTDAILKAMEEAFDGPNHGVLMQGINDLGGARIDLQGGSYLISRPLRFPSAGAGNLLISGGTLRASNDFPVDRYLIELKDESSKLQYIFEYITLRDLLIDCNYRGGAIAVINSLRTSIDNCYITRFGDTNGILVKSGHETYIRNSFLGQHITAGGDRGERSFSGTAINLMGNDNAVTDTVIFSARIGVMVSGQANLLSGVHCYNKATGFGGTGIYLRLPGLTQNRIVNSYLDYTGIVAEDPVQLQISGTFFLGDAFILLKSIAGYIRGVSIVDNMFSGSGHGVQIVQLDQRNTAFDDVGQVVVDRNSVNGMVEKSTVARGSVDGNGTSWTVDFNPVLLFPDLINHVQYTLVASEAGVFPLHALRNVSDNRVVVETNAPVTGTVYVTVNQGV
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (P11977)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00560}. Mitochondrion {ECO:0000250|UniProtKB:P00560}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Enolase
- Triosephosphate isomerase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Fructose-bisphosphate aldolase
- Phosphoglycerate mutase family protein
- Glucose-6-phosphate isomerase
- Probable assembly chaperone of rpl4
- Pyruvate kinase
Sequence:
MSLTSKLSITDVDLKDKRVLIRVDFNVPLDKNDNTTITNPQRIVGALPTIKYAIDNGAKAVILMSHLGRPDGKKNPKYSLKPVVPKLKELLGRDVIFTEDCVGPEVEETVNKASGGQVILLENLRFHAEEEGSSKDADGNKVKADKDAVAQFRKGLTALGDIYINDAFGTAHRAHSSMVGVDLPQKASGFLVKKELEYFAKALEEPQRPFLAILGGSKVSDKIQLIDNLLPKVNSLIITGGMAFTFKKTLENVKIGSSLFDEAGSKIVGNIIEKAKKHNVKVVLPVDYVTADKFAADAKTGYATDEQGIPDGYMGLDVGEKSVESYKQTIAESKTILWNGPPGVFEMEPFAKATKATLDAAVAAVQNGATVIIGGGDTATVAAKYGAEDKISHVSTGGGASLELLEGKELPGVAALSEKSK
Protein: Large ribosomal subunit protein uL11A (60S ribosomal protein L12-A) (L15) (YL23) (P0CX53)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS24A
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5B
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL6A
Sequence:
MPPKFDPNEVKYLYLRAVGGEVGASAALAPKIGPLGLSPKKVGEDIAKATKEFKGIKVTVQLKIQNRQAAASVVPSASSLVITALKEPPRDRKKDKNVKHSGNIQLDEIIEIARQMRDKSFGRTLASVTKEILGTAQSVGCRVDFKNPHDIIEGINAGEIEIPEN
Protein: Uncharacterized protein (A0A1D8PQ33)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- ATPase expression protein 1
- Fgr39p
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MKFVLVSARCRISIIPKLTFPRVPFHKNYSLTPETSLNRRVGKETVNPRLKTLDNFDPEKQPNETSAVYTRFGWFYIPTEFYLDGKIGVEIQNSLDDKGVTLETPKSEIQKLILEWCRQQPYEPKKKIKQRVKRRTPDVILNKFFSNGKNGSVEEEKPEPLVIEQKRKPSDETLARRIERETYRVTPRSIFARYDENTGKYEIKGHVSQNAAFQYYLSKEWDNYKGQFKTKVETRVALGESWKKKTPEEKEALRLEFLEMLQNGQDLASGKIIPLESRLSTAVFNDGFRLRVRSDHTKNLMKIKQSSNEYLKN
Protein: Beta-glucosidase 45 (AtBGLU45) (EC 3.2.1.21) (O80689)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes p-nitrophenyl beta-D-glucoside and natural glucosides such as syringin, coniferin and p-coumaryl alcohol glucoside. May be involved in lignification by hydrolyzing monolignol glucosides.
Interaction partners:
- CRIB domain-containing protein RIC9
- Cysteine-rich PDZ-binding protein
- glucan endo-1,3-beta-D-glucosidase
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
- Beta-glucosidase 46
- Beta-glucosidase 21
- Beta-glucosidase 22
- Beta-glucosidase 19
- Beta-glucosidase 33
- Beta-glucosidase 7
Sequence:
MKNLTSFVIVILLQSLLFHVYGRHQSSSKNILVDSSPFPSDFLFGTASSAYQYEGAFLTDGKSLNNWDVFTHKNPGKILDKNNADRAVDQYNRFLEDIQLMSFLGVNSYRFSISWCRILPRGRFGEINYLGIKYYNIFIDALISRGIKPFVTLNHVDYPQELEDRFQSWLNPEMQKEFGYLADICFKHFGNRVKYWTTLNEPNQQLILGYLTGKFPPSRCSSPYGNCSQGNSETEPFIAAHNMILAHAKAVNIYKTKYQKEQKGSIGIVVQTSWFEPISDSNADKEAAERAQSFYSNWILDPVIYGKYPKEMVDILGPALPQFSSNEVKNLEKSRADFVGINHYTSYFIQDCLTSACNTGHGAFKAEGYALKLDRKGNVTIGELTDVNWQHIDPTGFHKMLNYLKDRYPNMPMFITENGFGDLQKPETTDKELLNDTKRIQYMSGYLEALQAAMRDGANVKGYFVWSLLDNFEWLFGYKVRFGLFHVDLTTLKRSPKQSASWYKNYIEEHVNRRDIVDNY
Protein: DNA helicase B (EC 3.6.4.12) (Q6NVF4)
Organism: Mus musculus (Mouse)
Function: 5'-3' DNA helicase involved in DNA damage response by acting as an inhibitor of DNA end resection. Recruitment to single-stranded DNA (ssDNA) following DNA damage leads to inhibit the nucleases catalyzing resection, such as EXO1, BLM and DNA2, possibly via the 5'-3' ssDNA translocase activity of HELB. As cells approach S phase, DNA end resection is promoted by the nuclear export of HELB following phosphorylation. Acts independently of TP53BP1. Unwinds duplex DNA with 5'-3' polarity. Has single-strand DNA-dependent ATPase and DNA helicase activities. Prefers ATP and dATP as substrates. During S phase, may facilitate cellular recovery from replication stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:26774285}. Cytoplasm {ECO:0000269|PubMed:26774285}. Chromosome {ECO:0000250|UniProtKB:Q8NG08}. Note=Predominantly nuclear. Phosphorylation at Ser-942 by CDK2 during the G1/S transition results in its nuclear export into the cytoplasm as cells approach and progress through S phase. Following DNA damage, recruited to sites of double-strand breaks by the RPA complex. {ECO:0000250|UniProtKB:Q8NG08}.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
- Thymidine phosphorylase
- DNA polymerase alpha subunit B
- Tonsoku-like protein
- DNA primase large subunit
- DNA primase small subunit
- DNA excision repair protein ERCC-5
- DNA polymerase delta catalytic subunit
- DNA polymerase delta subunit 3
- DNA polymerase delta subunit 2
Sequence:
MARQDRLRELLGPLHPYKSDDEEEDCAQEEEGEQEEEFVDAEELCSGGIKAGSLPGRARVSIPDEYTKEKCTVYGRFPLKGPWWRVKVQVLKPQRSRSYQVQGFPAYFLQVDMSPPDQKQICSLFLKECNLASERIQEFLKWVEKVSSFENLHFENLWETLRLFYRETEKKDKKLSTPREQQGEEMRVEKSFAFISAMVALQFPKVMEFLPSLFPRHFKRLISSSSDWVLGCIEDVLGTQPWKLGFRRITYREMKLVRCEASWTAFSQCPSLLQLMTPLQKNALVIYSKLRQTCREDGHTYIEVKDLTSGLSEHMSFEEACQSLAFLKDIDVVIYEKDYVFLSELYEAEQDIASSICELMSRPPWHLKVDVKNVLASIRGAKPNDPGSAEAVEGSKPEEVGSEQGDSVLDAQDGDDHVRSNGEHVANAEINDVPLDQDQVVALETICANAVTVLSGKGGCGKTTIVSRLFKHMEHLEETEVQQACEDFEQDQEASEEWLDCPKQSPAGVDKAVEVLLTAPTGKAAGLLRQRTDLPAYTLCQVNYSFYMWKTKNEVDKPWKFSTVRVLVVDEGSLVSVGIFKSVLQLLCKHSKLSKLIILGDVRQLPSIEPGNMLQDVFETLKSRQCAIELKTNHRTESQLIVDNATRISRRQFPKFDAELNICGNPTLPLSIQDKTFIFVRLPEEDSRSQSSKGEHRSNLYTAVKTLLQGKDFCSFESSKTSQFIAFRRQDCDLINDCCCKHYTGHLIKDHEKKLIFAVGDKICCTRNAYLSDLLPDKDQEAEGKGYGDAPDDDAKIKQDFESSTRLCNGEIFFITRDVTDVTFKRKRLLTINNEAGLEVTVDFSKLMANCQIKHAWARTIHTFQGSEENTVVYVVGKAGRQHWQHVYTAVTRGRSRVYIIAQESELRSATRKRGFPRQTRLKHFLQKKLSGSCAPSTGFASQPSSPRVGGRPDTQPPASHLCRTPDNKATADSARGDERWLSASVNDDVDTDEESAQLRGSKRIGDGFPFDEESPSKFRMVEAPSPQVSSVFQNMRLNTLTPRQLFKPTDNQDTGTAGVADDANDPSNQEMEM
Protein: p44-72 outer membrane protein (Q2GK55)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MSAKNYNNLFLGSIMMSLAVLITCQGAQARDAAKSTFEVEKPQYFYIGLDYSPAFSNIRNFTIQESNGETKAIYPYIRGDKEIILDASRFDWNMPNPRIGFKNSTLVAVGSSIGYAMGSMRLEIEVSHERFKSRGRYIGNEREEESDTIYLLAKELGHSTVTEKTEDLVSALTKVKGEDIVRLANALEKTRPDIGRKICRTRSITGGKNYGKYNRYTSWLKDTNNLTALCGDIGGNSDKHEHHNMIQNSFKDFAREALLGGSTNWPTTTGDKTRGNDNAKALARDLITVLSREEKIAVAGLMVNTIEGGEVVDIGEISSTSVMVNVCYDFLSKEGSIVPYGCMGLGSNFVGIVKGHFTPKPAYRLKAGVSYKLFSGVDIFAAGFYHRVFGSTEYTDIPVEYLIDDVSPYGRTKETAMADFRMSYAGGEFGMRFAF
Protein: Vitamin K-dependent protein C (EC 3.4.21.69) (Anticoagulant protein C) (Autoprothrombin IIA) (Blood coagulation factor XIV) [Cleaved into: Vitamin K-dependent protein C light chain; Vitamin K-dependent protein C heavy chain; Activation peptide] (P04070)
Organism: Homo sapiens (Human)
Function: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function.
Subcellular location: Secreted {ECO:0000269|PubMed:25618265}. Golgi apparatus {ECO:0000269|PubMed:22531345, ECO:0000269|PubMed:25748729}. Endoplasmic reticulum {ECO:0000269|PubMed:22531345, ECO:0000269|PubMed:25748729}.
Interaction partners:
- Endothelial protein C receptor
- Thrombomodulin
- Prothrombin
- Alpha-2-antiplasmin
- Plasma serine protease inhibitor
- Proteinase-activated receptor 1
- Coagulation factor VIII
- Plasminogen activator inhibitor 1
- Coagulation factor V
- Alpha-1-antitrypsin
Sequence:
MWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP
Protein: LDL receptor related protein 5 (F1MAD0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Dickkopf WNT signaling pathway inhibitor 4
- Dickkopf homolog 1
- Dickkopf WNT signaling pathway inhibitor 2
- Protein Wnt
- Sclerostin
- Protein Wnt
- Protein Wnt
- Low-density lipoprotein receptor-related protein
- Frizzled-4
- Protein Wnt
Sequence:
METAPTRAPPPPPQPLLLLLALCCSLVPAAASPLLLFANRRDVRLVDAGGVKLESTIVASGLEDAAAVDFQFSKGAVYWTDVSEEAIKQTYLNQTGAAAQNIVISGLVSPDGLACDWVGKKLYWTDSETNRIEVANLNGTSRKVLFWQDLDQPRAIALDPAHGYMYWTDWGEAPRIERAGMDGSTRKIIVDSDIYWPNGLTIDLEEQKLYWADAKLSFIHRANLDGSFRQKVVEGSLTHPFALTLSGDTLYWTDWQTRSIHACNKWTGEKRKEILSALYSPMDIQVLSQERQPHFHTPCEEGNGGCSHLCLLSPREPFYSCACPTGVQLQDNGKTCKAGAEEVLLLARRTDLRRISLDTPDFTDIVLQVGDIRHAIAIDYDPLEGYVYWTDDEVRAIRRAYLDGSGAQTLVNTEINDPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTSRKILVSEDLDEPRAIVLHPVMGLMYWTDWGENPKIECANLDGRDRHVLVNTSLGWPNGLALDLQEGKLYWGDAKTDKIEVINIDGTKRQTLLEDKLPHIFGFTLLGDFIYWTDWQRRSIERVHKVKASRDVIIDQLPDLMGLKAVNVAKVVGTNPCADGNGGCSHLCFFTPHATKCGCPIGLELLSDMKTCIIPEAFLVFTSRATIHRISLETNNNDVAIPLTGVKEASALDFDVSNNHIYWTDVSLKTISRAFMNGSSVEHVIEFGLDYPEGMAVDWMGKNLYWADTGTNRIEVARLDGQFRQVLVWRDLDNPRSLALDPTKGYIYWTEWGGKPRIVRAFMDGTNCMTLVDKVGRANDLTIDYADQRLYWTDLDTNMIESSNMLGQERMVIADDLPYPFGLTQYSDYIYWTDWNLHSIERADKTSGRNRTLIQGHLDFVMDILVFHSSRQDGLNDCVHSNGQCGQLCLAIPGGHRCGCASHYTLDPSSRNCSPPSTFLLFSQKFAISRMIPDDQLSPDLILPLHGLRNVKAINYDPLDKFIYWVDGRQNIKRAKDDGTQPSMLTSPSQSLSPDRQPHDLSIDIYSRTLFWTCEATNTINVHRLDGDAMGVVLRGDRDRPRAIAVNAERGYMYFTNMQDHAAKIERASLDGTEREVLFTTGLIRPVALVVDNALGKLFWVDADLKRIESCDLSGANRLTLEDANIVQPVGLTVLGRHLYWIDRQQQMIERVEKTTGDKRTRVQGRVTHLTGIHAVEEVSLEEFSAHPCARDNGGCSHICIAKGDGTPRCSCPVHLVLLQNLLTCGEPPTCSPDQFACATGEIDCIPGAWRCDGFPECADQSDEEGCPVCSASQFPCARGQCVDLRLRCDGEADCQDGSDEANCDAVCLPNQFRCASGQCVLIKQQCDSFPDCADGSDELMCEINKPPSDDVPAHSSAIGPVIGIILSLFVMGGVYFVCQRVMCQRYTGASGPFPHEYVGGTPHVPLNFIAPGGSQHGPFPGIPCSKSMMSSVSLVGGAGQRAPL