wanglab/gogpt-training-data huggingface dataset:
Protein: TEL2-interacting protein 1 (P36097)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ASTRA complex involved in chromatin remodeling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000305|PubMed:14562095}.
Interaction partners:
- RuvB-like protein 2
- Telomere length regulation protein TEL2
- RuvB-like protein 1
- TEL2-interacting protein 2
- ASTRA-associated protein 1
- Serine/threonine-protein kinase TOR1
- Serine/threonine-protein kinase TOR2
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- ATP-dependent molecular chaperone HSC82
- ATP-dependent molecular chaperone HSP82
Sequence:
MNSDTNAFKDIRISCVELSRIAFLPTESFDPNSLTLLACLKKVEEKLSAYEDDSLSPKFADYVFVPIASLLKQPALGESQTEYVLLIIFHLLRTCWSSNGKFSEQLGQQLFPLITFLVSSDKDNQKLITRSDEFKYAGCLVLHQFFKSVRSQRYHKEFFSNSKPNLLPALGHSVTILLKILEQSPQNNELQFKALASLEVLFQDIISDGEMLSFILPGNVSVFAKILTKPGRQIHYKVCVRTLEVLAKLLVLVYDDFSLDIKVNKLTDIRELSDTKLKHEINQSFMFNGPIVLLRTDGKTHRDTSWLTATSGQINIALEAFIPKLLKRNNESIDEALATFVSILLTRCENSLNNCEKVLVSTLVHLERDPMSKLPSHLVKLKEVVNEDLHKLSDIIRFENADRLSSLSFAITILEKNNERDTMINEVVRCLFESLNESIEPPSLINHKERIIEQSSQLTTTVNFENLESTNALIALPRLSEDMSLKLKKFTYHMGSLLLERHILNDVVTELISEQVDSPRTQKIVALWLSTNFIKAMEKQPKEEEVYLQFESDANYSSSMVEEVCLIVLEFCNELSQDISMEIEGKGIKKSDEFAVCTVLFSIETICAVMREEFQPELIDYIYTVVDALASPSEAIRYVSQSCALRIADTLYHGSIPNMILSNVDYLVESISSRLNSGMTERVSQILMVICQLAGYETIENFKDVIETIFKLLDYYHGYSDLCLQFFQLFKIIILEMKKKYINDDEMILKIANQHISQSTFSPWGMTDFQQVLNILDKETQVKDDITDENDVDFLKDDNEPSNFQEYFDSKLREPDSDDDEEEREEEVEGSSKEYTDQWTSPIPSDSYKILLQILGYGERLLTHPSKRLRVQILIVMRLIFPLLSTQHNLLIREVASTWDSIIQCVLCSDYSIVQPACSCVEQMIKYSGDFVAKRFIELWQKLCQDSFILKELRIDPTVHNHEKKSISKHVKFPPVTENALVSMVHMVLEGVKITEYLISEAVLEQIIYCCIQVVPVEKISSMSLIVGDIVWKIRNIN
Protein: Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) (C-Jun-binding protein) (JBP) (Casein kinase 2-interacting protein 1) (CK2-interacting protein 1) (CKIP-1) (Osteoclast maturation-associated gene 120 protein) (Q53GL0)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170, ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15254037, ECO:0000269|PubMed:16325375}; Peripheral membrane protein {ECO:0000305|PubMed:14729969}. Nucleus {ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170, ECO:0000269|PubMed:15706351}. Cytoplasm {ECO:0000269|PubMed:15706351}. Note=Predominantly localized to the plasma membrane through the binding to phosphatidylinositol 3-phosphate (PubMed:14729969). In C2C12 cells, with the absence of growth factor, it is found in the nucleus (PubMed:14729969). It rapidly translocates to the plasma membrane after insulin stimulation (PubMed:14729969). In response to TNF, it translocates from the plasma membrane to the cytoplasm and then to the nucleus accompanied by cleavage by caspase-3 (PubMed:15706351). However, the subcellular location is highly dependent of the cell type, and this explains why it is found exclusively at the plasma membrane, in some type of cells (Probable). {ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15706351, ECO:0000305}.
Interaction partners:
- Casein kinase II subunit alpha'
- E3 ubiquitin-protein ligase SMURF1
- Casein kinase II subunit beta
- Vacuolar protein sorting-associated protein 45
Sequence:
MMKKNNSAKRGPQDGNQQPAPPEKVGWVRKFCGKGIFREIWKNRYVVLKGDQLYISEKEVKDEKNIQEVFDLSDYEKCEELRKSKSRSKKNHSKFTLAHSKQPGNTAPNLIFLAVSPEEKESWINALNSAITRAKNRILDEVTVEEDSYLAHPTRDRAKIQHSRRPPTRGHLMAVASTSTSDGMLTLDLIQEEDPSPEEPTSCAESFRVDLDKSVAQLAGSRRRADSDRIQPSADRASSLSRPWEKTDKGATYTPQAPKKLTPTEKGRCASLEEILSQRDAASARTLQLRAEEPPTPALPNPGQLSRIQDLVARKLEETQELLAEVQGLGDGKRKAKDPPRSPPDSESEQLLLETERLLGEASSNWSQAKRVLQEVRELRDLYRQMDLQTPDSHLRQTTPHSQYRKSLM
Protein: Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (P-52) (Q03346)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable). Preferentially, cleaves after an arginine at position P2. Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:O75439}.
Interaction partners:
- Mitochondrial-processing peptidase subunit alpha
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Ubiquinol-cytochrome c reductase, complex III subunit X.
Sequence:
MAAAAVSRTLLPVAGRRLWGFTRRLPLRAAAAQPLYFGGDRLRSTQAAPQVVLNVPETQVTCLENGLRVASENSGISTCTVGLWIDAGSRYENEKNNGTAHFLEHMAFKGTKKRSQLDLELEIENMGAHLNAYTSREQTVYYAKAFSKDLPRAVEILADIIQNSTLGEAEIERERGVILREMQEVETNLQEVVFDYLHATAYQNTALGRTILGPTENIKSISRKDLVDYITTHYKGPRIVLAAAGGVCHNELLELAKFHFGDSLCAHKGDVPALPPCKFTGSEIRVRDDKMPLAHLAVAIEAVGWTHPDTICLMVANTLIGNWDRSFGGGMNLSSKLAQLTCHGNLCHSFQSFNTSYTDTGLWGLYMVCEQATVADMLHAVQKEWMRLCTAVSESEVARAKNLLKTNMLLQLDGSTPICEDIGRQMLCYNRRIPIPELEARIDAVDAEMVREVCTKYIYGKSPAIAALGPIERLPDFNQICSNMRWTRD
Protein: Transcription cofactor vestigial-like protein 2 (Vgl-2) (Protein VITO1) (Q8N8G2)
Organism: Homo sapiens (Human)
Function: May act as a specific coactivator for the mammalian TEFs. May play a role in the development of skeletal muscles.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcriptional enhancer factor TEF-1
- WW domain-containing transcription regulator protein 1
- Myoblast determination protein 1
- Nuclear receptor coactivator 2
Sequence:
MSCLDVMYQVYGPPQPYFAAAYTPYHQKLAYYSKMQEAQECNASPSSSGSGSSSFSSQTPASIKEEEGSPEKERPPEAEYINSRCVLFTYFQGDISSVVDEHFSRALSQPSSYSPSCTSSKAPRSSGPWRDCSFPMSQRSFPASFWNSAYQAPVPPPLGSPLATAHSELPFAAADPYSPAALHGHLHQGATEPWHHAHPHHAHPHHPYALGGALGAQAAPYPRPAAVHEVYAPHFDPRYGPLLMPAASGRPARLATAPAPAPGSPPCELSGKGEPAGAAWAGPGGPFASPSGDVAQGLGLSVDSARRYSLCGASLLS
Protein: MEC-5 (G5EFQ9)
Organism: Caenorhabditis elegans
Interaction partners:
- Kunitz/Bovine pancreatic trypsin inhibitor domain protein
- Papilin
- Degenerin mec-10
- Degenerin mec-4
- Mechanosensory protein 2
- Mechanosensory abnormality protein 6
- Tubulin alpha-3 chain
- Tubulin beta-1 chain
- AMP-binding domain-containing protein
Sequence:
MRLLILLLLTISSIYCALDTAAVIAIQTEINKHSADIEMILDHVKNLNARVSDLGRPGPPGTNGSPGFPGSKGEKGDRSEDGMSGRDGMQGIPGVKGDMGPLGPTGMKGDKGSMGFPGQKGEGGNSGIPGLKGDTGIPGKVGEPGSTGQPGSKGEKGMEGLPGTNGLPGAPGWPGSKGEDGLPGRPGSPGFPGKKGDVGNGGVPGVPGMIGERGLPGAPGAQGMMGPIGPPGQLGLPGPKGDLGSAGLPGSKGEMGKDGIPGLPGWIVNDKGYCILALGNCPPAFTQIGAYQAHVDNYRFGDYSLVKSSGIGGNEEQFALKVHACCR
Protein: Peptidyl-prolyl cis-trans isomerase 1 (PPIase 1) (EC 5.2.1.8) (Cyclophilin-1) (Rotamase 1) (P52009)
Organism: Caenorhabditis elegans
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Interaction partners:
- Nsp1_C domain-containing protein
- CHK kinase-like domain-containing protein
- CYclophyliN
Sequence:
MKFLLRASSLAGQSLRFASQRPKVFFDVSIGEEPAGRVTMELFNDVVPKTAENFRALCTGEKGVGEQGVALHFKGSKFHRIIPEFMIQGGDFTRHNGTGGESIYGNKFKDENFDLKHTGPGCLSMANAGPNTNGSQFFICTVDTPWLDGGHVVFGQVTDGMSVVKKIEKMGSRSGAPAKTVTIADCGELKSE
Protein: Probable elongation factor 1-gamma 1 (EF-1-gamma 1) (eEF-1B gamma 1) (O04487)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably plays a role in anchoring the complex to other cellular components.
Interaction partners:
- Elongation factor 1-delta 2
- Elongation factor 1-beta 2
- Elongation factor 1-beta 1
- Elongation factor 1-delta 1
- Methionine--tRNA ligase, cytoplasmic
- Glutathione S-transferase Z1
- Large ribosomal subunit protein uL10y
- Glutathione S-transferase TCHQD
- Elongation factor 2
- Putative transcription elongation factor SPT5 homolog 2
Sequence:
MALVLHTYKGNKSAEKALIAAEYVGVQIDVPSDFQMGVTNKTPAFLKMNPIGKVPVLETPEGSVFESNAIARYVSRLNGDNSLNGSSLIEYAQIEQWIDFSSLEIYASILRWFGPRMGFMPYSAPAEEGAISTLKRALDALNTHLTSNTYLVGHSITLADIITVCNLNLGFATVMTKKFTSEFPHVERYFWTVVNQPNFTKVLGDVKQTEAVPPIASKKAAQPAKPKEEPKKKEAPVAEAPKLAEEEEAPKPKAKNPLDLLPPSPMVLDDWKRLYSNTKSNFREVAIKGFWDMYDPEGYSLWFCDYKYNDENMVSFVTLNKVGGFLQRMDLARKYSFGKMLICGSEGPFKVKGLWLFRGPEIPKFIMDEVYDMELYEWTKVDISDEAQKERVSQMIEDAEPFEGEALLDAKCFK
Protein: OPA3-like protein (Q9P7W0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Transmembrane GTPase fzo1
- Myosin-1
- Pre-mRNA-splicing factor cwf19
Sequence:
MSSLALKIGSLLVRTLSKPIANTIKAQAKEHKAFRKACIEFAQWMHRAEFRITGINRAKSGGANVRLRPLNDAKAVDAGATFLSETFIFTVAGGAILFETWRARRKEKNRRDEVAEAILGLQHEIVRINEIMEKQFVLQKKKNELQSSTEEIDSTEKDFDELHKVILKVERELHTLRQNTPSQNEQAEATPSKEIPRETVSEKADHPPSSNTKSVSTG
Protein: Nectin-4 (Ig superfamily receptor LNIR) (Nectin cell adhesion molecule 4) (Poliovirus receptor-related protein 4) [Cleaved into: Processed poliovirus receptor-related protein 4] (Q96NY8)
Organism: Homo sapiens (Human)
Function: Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, adherens junction {ECO:0000269|PubMed:11544254}. Note=Colocalizes with AFDN at cadherin-based adherens junctions (PubMed:11544254).; SUBCELLULAR LOCATION: [Processed poliovirus receptor-related protein 4]: Secreted {ECO:0000269|PubMed:15784625}. Note=The secreted form is found in breast tumor patients (PubMed:15784625).
Interaction partners:
- Afadin
- Myosin-binding protein H
- Nectin-1
- Nectin-2
- Nectin-3
- Partitioning defective 3 homolog
- Signaling lymphocytic activation molecule
- Membrane cofactor protein
Sequence:
MPLSLGAEMWGPEAWLLLLLLLASFTGRCPAGELETSDVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARVDAGEGAQELALLHSKYGLHVSPAYEGRVEQPPPPRNPLDGSVLLRNAVQADEGEYECRVSTFPAGSFQARLRLRVLVPPLPSLNPGPALEEGQGLTLAASCTAEGSPAPSVTWDTEVKGTTSSRSFKHSRSAAVTSEFHLVPSRSMNGQPLTCVVSHPGLLQDQRITHILHVSFLAEASVRGLEDQNLWHIGREGAMLKCLSEGQPPPSYNWTRLDGPLPSGVRVDGDTLGFPPLTTEHSGIYVCHVSNEFSSRDSQVTVDVLDPQEDSGKQVDLVSASVVVVGVIAALLFCLLVVVVVLMSRYHRRKAQQMTQKYEEELTLTRENSIRRLHSHHTDPRSQPEESVGLRAEGHPDSLKDNSSCSVMSEEPEGRSYSTLTTVREIETQTELLSPGSGRAEEEEDQDEGIKQAMNHFVQENGTLRAKPTGNGIYINGRGHLV
Protein: Cornifelin (Q9BYD5)
Organism: Homo sapiens (Human)
Function: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
Subcellular location: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope. {ECO:0000250}.
Interaction partners:
- Involucrin
- Loricrin
- Keratinocyte differentiation-associated protein
- Late cornified envelope protein 3D
Sequence:
MSYPVTSQPQCATTSCYQTQLSDWHTGLTDCCNDMPVCLCGTFAPLCLACRISDDFGECCCAPYLPGGLHSIRTGMRERYHIQGSVGHDWAALTFCLPCALCQMARELKIRE
Protein: Vacuolar protein-sorting-associated protein 36 (ESCRT-II complex subunit VPS36) (Q9VU87)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex (By similarity). ESCRT-II interacts, through the Vps36 subunit, with bicoid mRNA. This interaction is required for the anterior localization of bicoid mRNA in the developing egg. Plays a role in promoting mitochondrial autophagy (mitophagy).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17268469}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein sorting 20, isoform A
- Vacuolar-sorting protein SNF8
- Vacuolar protein-sorting-associated protein 25
- Tumor suppressor protein 101
- Charged multivesicular body protein 4
- RH72336p
- GH14561p
- LD45836p
- EG:115C2.5 protein
Sequence:
MNRFAYVEARLSPNESFVSRDNRVKIYDGDQKTDFEDGEVVLTTHRLFWGRPGEIARAAVTLCLPLSYVISVSEETTASNFFGRKTRIIMHLHPPTSDKGPGPLDTSRATHIKLSGKNGLSVEFHSALRETLNARVWEILLTSEIIINGVASSPTLEPANDRLARIQKRTGIGGIERHLEAKAKATDENIALAFQDLSVLMAMAKDMVGVSKTISSKIRKQKGEISDDETVRFKSYLMSLGIDDPVTRDNFTSNSAYFSSLARQICEMLLDPIEEQGGMMSLADVYCRVNRARGLELLSPEDLLHACEQLSGPIRLRSFPSGARVLQLESHDDALIAVDTLEKVEAAESLAVEELAKQLGISLLLAKERLLVAERLGKVCRDESVEGLRFYPNLLLGRD
Protein: Ras-responsive element-binding protein 1 (RREB-1) (RAS-responsive zinc finger transcription factor RREB) (Q3UH06)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds specifically to the RAS-responsive elements (RRE) of gene promoters. Represses the angiotensinogen gene (By similarity). Negatively regulates the transcriptional activity of AR (By similarity). Potentiates the transcriptional activity of NEUROD1 (By similarity). Binds specifically to the allelic variant of the CDKN2A promoter present in Balb/c mice, which leads to a down-regulation of CDKN2A expression in this strain, and, as a consequence, to an elevated susceptibility to pristane-induced tumors. Promotes brown adipocyte differentiation. May be involved in Ras/Raf-mediated cell differentiation by enhancing calcitonin expression (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250}.
Interaction partners:
- Lysine-specific histone demethylase 1A
Sequence:
MTSNSPIGLEGSDLSSINTMMSAVMSVASVTENGGSPQGIKSPMKPPGPNRIGRRNQETKEEKSSYNCPLCEKICTTQHQLTMHIRQHNTDTGGADHACSICGKSLSSASSLDRHMLVHSGERPYKCTVCGQSFTTNGNMHRHMKIHEKDTNSTTAAAPPSPLKRRRLSSKRKLSHDAESEDPGPAKKMVEDGQSGDLDKMSDEIFHCPVCFKEFVCKYELETHMETHSDNPLRCDICCVTFRTHRGLLRHNALVHKQLPRDAMGRPFIQNNPSIPAGFHDLGFTDFSCRKFPRISQAWCETNLRRCISEQHRFVCDTCDKAFPMLSSLILHRQSHIPADQGREKLQTKTLAAESLEQKAFLALLGLQHTKDVKPAPAEELLPDDNQAIQLQTLKYQLPQEPGCPTVLSVSPLDAASLGGSLTVLPATKENMKHLSLQPFQKGFIIQPDSSIVVKPISGESAIELADIQQILKMAASAPPQISLPPLSKAPATPLQAIFKHMPPLKPKPLVTPRTVVAASTPPPLINAQQASPGCISPSLPPQSLKFLKGSVEAVSNVHLLQSKSGIQPSTTTQLFLQQAGVELPGQPEMKTQLEQESIIEALLPLNMEAKIKQEITEGDLKAIMTGPSGKKTPAMRKVLYPCRFCNQVFAFSGVLRAHVRSHLGISPYQCNICDYIAADKAALIRHIRTHSGERPYICKICHYPFTVKANCERHLRKKHLKATRKDIEKNIEYVSSPTAELVDAFCAPETVCRLCGEDLKHYRALRIHMRTHCSRGLGGCHKGRKPFECKECNAPFVAKRNCIHHILKQHLHVPEKDIESYVLATNSGLGPADTPTDAASRGEEGSCVTFAECKPLATFLEPQNGFLHSSPTQPLPSHISVKLEPASSFAMDFNEPLDFSQKGLALVQVKQENVSSLLTSSSSSALYDCSMEPIDLSIPKSVKKGDKDTVVPSDAKKPEPEAGQAEPLSPRPPPCPTLSVTVEPKGSLETPTGTVVAVTTAAKLEPHTQPLQGSVQLAVPIYSPALVSNTPLLGNSAALLNNPALLRPLRPKPPLLLPKPSMTEELPPLASIAQIISSVSSAPTLLKTKVADPGPSITSSNTVATDSPGSSIPKAAATPTDTTSSKESSEPPPAASSPEEALPTEQGPAATSSSRKRGRKRGLRNRPLPNSSAVDLDSSGEFASIEKMLATTDTNKFSPFLQTAEDDTQEEVAGAPADQHGPADEEQGSPAEDRLLRAKRNSYANCLQKINCPHCPRVFPWASSLQRHMLTHTDSQSDTDTLTTPGEVLDLTAQAKEQPPAEGASEISPASQDLAIKEAKAAAAPSEEEEEKETEENPEPEEECRVEESTGAADAPEEDTASNQSLDLDFATKLMDFKLAESEAGSVDSQGPAQQEPKHACDTCGKNFKFLGTLSRHKKAHSCQEPKEEEAAAPSLENEGVGRAVEGPSPSPEPEEKPAESLAIDPTPGTREASVAKQNEETEGPTDGEGTAEKRGDGDKRPKTDSPKSMASKADKRKKVCSVCNKRFWSLQDLTRHMRSHTGERPYKCQTCERTFTLKHSLVRHQRIHQKARHSKHHGKDSDKDERAEEDSEDESTHSATNPASENEAESAPSTSNHVAVTRSRKESLSTSGKECSPEERAAAEQAAEPSAPKEQASPGETDPQSPAAIVQDLLELCGKRPAPILAATDGASQLLGME
Protein: Scm polycomb group protein like 2 (B1AVB2)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAEPATAEGTSGLGQQVTKQGHPSTGEMEPATGVQLAGSGELVAEPGPSSTEARENTEEANTMGQTANEDHFDWDKYLKETGSISAPSEYFRQSKTPPTNEFKIGMKLEARDPRNIDSVCVASVIGITGARLRLRLDGSDNKNDFWRLVDSSDIQPVGTCEQGGDLLQPPLGYTLNTSSWPMFLLRVLTGSELAPAVFFKEEPPRPLQNNFIVGMKIEAVDRKNPFMICPATIGAVCGDQLHITFDGWSGAFDYWCDYDSRDIFPVGWCRLTGDVLQPPGKIVEKRPRRKRRTRLWRLRTALLGNEEEAPEAAEEPGTSVLTFGDENRTLKDCRGEAAEEPGTSAFTFGDENRTLKDCQGGWKKPKGRGFIKPGKDETRPGKHDQGAPAGKKPRGRGFTQPLEDEARPGRDVQVAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKRKGKTVTTPWTEDPRLFADQGDAPAEKKPKGKRVTKSRKDQAQFLADEEAMPALFSALSVSSTERTPPSSSEQPKSSTSGKTKSTSRGAQTSRKSPRKTSVVQPVPKTSKKAGKSKSTGNTSSPKKGITIKIVLPKKKGGKSGKKEKSIPVISSTSSASLSTLMKSSSSNKTSAGPSKIVMSTVCVYINKHGDCGPFLDPQKVQQLPNHFGPGPVNVILQRTVQACVNCAFQAKDVFLFLKTDNRGGEMITAFFDGKVHTVQLPPVNSASFALRFLENFCQSLQCDNFLSSQPFRREAQVPTPDTGTDQSKPENGEPKEKRSLKRLSLHPHRSAPVSSKVPRKSGQASKGN
Protein: Proliferating cell nuclear antigen 1 (PfPCNA1) (P61074)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Auxiliary protein of DNA polymerase delta and is involved in the control of DNA replication by increasing the polymerase processibility during elongation of the leading strand (By similarity). Involved in DNA damage response.
Subcellular location: Nucleus {ECO:0000269|PubMed:18554328, ECO:0000269|PubMed:19633266, ECO:0000269|PubMed:26251451}. Chromosome {ECO:0000269|PubMed:26251451}. Cytoplasm {ECO:0000269|PubMed:26251451}. Note=During early-to mid replicating trophozoite stages, colocalizes with ORC1 and ORC5 to distinct nuclear foci which probably are DNA replication origin sites (PubMed:18554328, PubMed:19633266, PubMed:26251451). Dissociates from ORC1 and ORC5 during the late schizont stage (PubMed:18554328, PubMed:19633266). {ECO:0000269|PubMed:18554328, ECO:0000269|PubMed:19633266, ECO:0000269|PubMed:26251451}.
Interaction partners:
- DNA ligase
- Replication factor C subunit 2, putative
- Replication factor C subunit 5, putative
- DNA polymerase
- Replication factor C subunit 4, putative
- Replication factor C subunit 1
- DNA polymerase delta small subunit, putative
- Replication factor C subunit 3, putative
- DNA repair protein REV1, putative
- DNA mismatch repair protein
Sequence:
MLEAKLNNASILKKLFECIKDLVNDANVDADESGLKLQALDGNHVSLVSLHLLDSGFSHYRCDRERVLGVNIASLNKVFKLCGANESVVISSKDDEDNLNFVFENNKEDKVTNFSLKLMSIELDSLNIPDCEEGFDAEVELSSKELTNIFRNLSEFSDTVFIEIDSNCIKFTTKGIVGDAEVALKPRDSTSEDDIGVTIKSKKKIKQSFAIKYLNLFSKSNILADVVVLGLSDSRPIEFKYEIKDTSPDSDTLKIGFVKFFLAPKMDDDMDNKD
Protein: Serralysin (EC 3.4.24.40) (Extracellular metalloproteinase) (Zinc proteinase) (P23694)
Organism: Serratia marcescens
Function: Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death.
Subcellular location: Secreted.
Interaction partners:
- Alkaline proteinase inhibitor
- Type I secretion outer membrane protein LipD.
- Extracellular metalloprotease
- Hemolysin
- Heme acquisition ABC transporter,ATP-binding/permease protein.
- Type I secretion membrane fusion protein LipC.
- Type I secretion system ATPase LipB.
- Heme acquisition ABC transporter,substrate-binding protein.
- Hemolysin transporter protein ShlB
Sequence:
MQSTKKAIEITESSLAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYNDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANPSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEANSSDFIHFVDHFSGTAGEALLSYNASSNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV
Protein: UV radiation resistance-associated gene protein (UV-resistance associated gene) (Q9VK07)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a cell growth regulator. Also has a crucial role in controlling organ rotation by regulating membrane-localized Notch receptor endocytosis and subsequent degradation. Regulation of organ rotation is not by induction of autophagy.
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- non-specific serine/threonine protein kinase
- Rubicon, isoform A
- Beclin-1-like protein
- Autophagy-related 14
- Autophagy protein 5
- Autophagy protein 12-like
- BG1
- Ubiquitin-like-conjugating enzyme ATG3
- Cysteine protease
Sequence:
MNLRPRCRKWLPLATQQLRLRNLNRIQGFNIESWPHEKSLELDDPDDVLLYYTLHTDKASEAFYTSEKLPQRHQQQKWAEICTDDEAWRKTNAQCVCVKVWKHYSAERRDGQPPEVEQRHKDVFGRSQLTPSRLPRPPELLFSWGVYFSGLIPLSPLTLSQCGRNCLVFQLNGEQFASPSMISEQALQSQLHLHYQKYAEEEKLEEPQDEGINSPAVSRSSSPVLRMSTMRYAQLKCQRQEIRRSNNLEKLLTLQRLQRLHQQKRRQMAEVCREIARLSVHCVTRNELRLKPRTTSLSGDYSAHQYHSMGRALSVLLAEQQQIAPLTLYNAQQLTRRIEALSSQQRLLKAERETFRQRNERTRQLLKEMREQREAQQWELHSQRHRLEKERLELRTLAPQHLEQRDQKRQIERQVERRMSTLVLELQEIYNIQNVGGRQFSICGIAFPHMEQYTSESRQAANAQLLDNVSPLAVSAALGYVAHLVQMLAIIMDRPLRNRILYEPSKARIVDDIKELTYTTREFPLYTRSILPSQQTKYAIYLLRQNVSQLCFDITGQCDLRNTFGNLLELFSTLRYIERTQRDEVDERDGTAVGAGCGEARLANGLTAPHLSQSHSSVDMNHVPLPTGVNAVKDALLQQLLPPGVSEALAIEGYASTQRICRSVGSYSDGEDEFRPRLEHNYSNSDSNITLQTERS
Protein: Homeobox even-skipped homolog protein 2 (EVX-2) (P49749)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus.
Interaction partners:
- Endoplasmic reticulum junction formation protein lunapark
Sequence:
MMERIRKEMILMERGLHSPTAGKRFSSLSDSAGGAVLEALENSQHPARLSPRLPSAPLHGALGDLPAKGKFEIDTLFNLQHPSSESTVSSEIASATESRKKPSHYSEAAAEADMSSDVEVGCSALRSPSGLGAAPLKENNAKGYTESGSVAGTTTSASGSGLGSLHGGGGGGNSGAAALGGSGSGSGADQVRRYRTAFTREQIARLEKEFYRENYVSRPRRCELAAALNLPETTIKVWFQNRRMKDKRQRLAMSWPHPADPSFYTYMMTHAAATGSLPYPFHSHVPLHYYPHVGVTAAAAAAAASGAAAAASSPFATSIRPLDTFRALSHPYSRPELLCSFRHPGLYQAPAAAAGLNSAASAAAAAAAAAAAASSAAAAGAPPSGSSAPCSCLSCHSSQSAAAAAAAAAAALGSRGGGGSGGGGGGGAGTAGGSDFGCSAAAPRSESGFLPYSAAVLSKTAVSPPDQRDEAPLTR
Protein: 17-beta-hydroxysteroid dehydrogenase type 2 (17-beta-HSD 2) (20 alpha-hydroxysteroid dehydrogenase) (20-alpha-HSD) (E2DH) (Estradiol 17-beta-dehydrogenase 2) (EC 1.1.1.62) (Microsomal 17-beta-hydroxysteroid dehydrogenase) (Short chain dehydrogenase/reductase family 9C member 2) (Testosterone 17-beta-dehydrogenase) (EC 1.1.1.239) (P37059)
Organism: Homo sapiens (Human)
Function: Catalyzes the NAD-dependent oxidation of the highly active 17beta-hydroxysteroids, such as estradiol (E2), testosterone (T), and dihydrotestosterone (DHT), to their less active forms and thus regulates the biological potency of these steroids. Oxidizes estradiol to estrone, testosterone to androstenedione, and dihydrotestosterone to 5alpha-androstan-3,17-dione. Also has 20-alpha-HSD activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10385431}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- 17-beta-hydroxysteroid dehydrogenase type 1
- 17-beta-hydroxysteroid dehydrogenase type 3
- Dehydrogenase/reductase SDR family member 11
- Aldo-keto reductase family 1 member C3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Aromatase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Cytochrome P450 1A1
Sequence:
MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLILFSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPGAEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELLLMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVTMFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYILAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYDYFAKRHFGQDKPMPRALRMPNYKKKAT