wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasome maturation protein (Proteassemblin) (Protein UMP1 homolog) (mUMP1) (Q9CQT5)
Organism: Mus musculus (Mouse)
Function: Molecular chaperone essential for the assembly of standard proteasomes and immunoproteasomes. Degraded after completion of proteasome maturation (By similarity). Mediates the association of 20S preproteasome with the endoplasmic reticulum (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Microsome membrane {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-2
- Proteasome subunit beta type-3
- Proteasome assembly chaperone 2
- Proteasome subunit beta type-6
Sequence:
MNARGLGSELKDSIPVAELSASGPFESHDLLRKGFSCVKNELLPSHPLELSEKNFQLNQDKMNFSTLRNIQGLFAPLKLQMEFKAVQQVHRLPFLPSSNLSLDILRGNDETIGFEDILNDPSQSELMGEPHVMVEHKLGLL
Protein: Large ribosomal subunit protein eL28 (Probable 60S ribosomal protein L28e) (O14069)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS3
Sequence:
MSVSNDLIWQVIRDNNRFLVKRPEFGGIQFNREPVNVSGKNAQRFSGLCNDKAVGVQANSPRGVVLITKTNPKNAQKPAKLFRKDVIANASSRKTYKSIAGRIGRTGYRDDLVKVSVARASAILSSQRPKKTVA
Protein: AT4G00310 protein (AT4g00310/A_IG005I10_17) (A_IG005I10.17 protein) (F5I10.17 protein) (Membrane lipoprotein) (O23071)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Inactive receptor-like serine/threonine-protein kinase At2g40270
- Ribosome 60S biogenesis amino-terminal protein
- Tetratricopeptide repeat
- U4/U6 small nuclear ribonucleoprotein PRP4-like protein
- Beta-amylase 7
- Proteasome subunit beta type-6
- ATP-dependent zinc metalloprotease FTSH 12, chloroplastic
- Nuclear pore complex protein NUP160
Sequence:
MRIRKNTKLSSVLLSTAGCGGERPDTYVCHLNQSPWDVIPVSSSGDCELTNLVDSSWFLPLSSSSSSSSPPLIHKFIGEEDSFNGNVSLGDCNDTAQRFNSSVSSNQSLVSVEKLNLNAAEEDKYAISPEVEDPMDQSDDYDKKSEALEPNSPVKTSGDDEKVVVTIPTAPKRGRPRGSGKKVSAPALKNPYEFYYYSGFGPRWGRKRGGSDDEKMVINDSKKSRSSASSSSDEDGHKTAAFGGGSVSFDEFDFVDEDYDVMEQDQGSDHGRKKKNEKMIMMKKTMKKGRKPVKERSLKSLM
Protein: Angiopoietin-2 (ANG-2) (O15123)
Organism: Homo sapiens (Human)
Function: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Involved in the regulation of lymphangiogenesis.
Subcellular location: Secreted {ECO:0000269|PubMed:32908006}.
Interaction partners:
- Angiopoietin-1 receptor
- Tyrosine-protein kinase receptor Tie-1
- High affinity nerve growth factor receptor
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 3
- Angiopoietin-4
- Angiopoietin-1
- Immunoglobulin heavy variable 3-43D
- von Willebrand factor
Sequence:
MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGGGWTIIQRREDGSVDFQRTWKEYKVGFGNPSGEYWLGNEFVSQLTNQQRYVLKIHLKDWEGNEAYSLYEHFYLSSEELNYRIHLKGLTGTAGKISSISQPGNDFSTKDGDNDKCICKCSQMLTGGWWFDACGPSNLNGMYYPQRQNTNKFNGIKWYYWKGSGYSLKATTMMIRPADF
Protein: Helix-loop-helix DNA-binding domain containing protein, expressed (Os12g0597800 protein) (Q2QMN2)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Phytochrome B
- Phytochrome A
Sequence:
MMSFPYSSGDLGEATTAAAAAVDMITLDQMFRDYDASTGDDLFELVWESCGGGEIDSGAGEVQPAGVPCCRRLLPGSSPEPTSEDEMAAWLSTIVTGSGGGGGDDVAAGGDHQDPAVKKPDGEPLTEKMDKKLPTRTEERRRVKHKARRNPGYAETHGLTEKRRRSRINEKFKMLQRLVPGCDKCSQSSTLDRTIHYMKSLQQQLQAMYPTMVRPAAVYPVVQPPPAFAAGGPPAASQGGLHRHRRLMVVVSVHHRCRCFRLGRQ
Protein: Ribonuclease P protein subunit p20 (RNaseP protein p20) (Q2MGL3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP complex, which cleaves pre-rRNA sequences (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:O75817}. Cytoplasm {ECO:0000250|UniProtKB:O75817}. Cytoplasmic granule {ECO:0000250|UniProtKB:O75817}.
Interaction partners:
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit p29
- GH06023p
- FI09323p
- FI18256p1
- Ribonuclease P/MRP subunit p21, isoform A
- Ribonuclease P/MRP subunit p14 a
- GEO10372p1
- GEO12594p1
- tRNA
Sequence:
MMGSNYPEHGTKPRSAKYHKQQNHRVVRKQPPRPAVSDRHNIYITSKTDFKAQQRRCEELINSGAHEIFLHCMGFSVTRGLNIALRLVQNSDGALSYAINTSTVQLVDELHPLCDAEDITFRQRNNSALHIKILNNSLFDIAVPQPSQSQTQAQSLGQFRGKAKARQ
Protein: RNA-binding protein 38 (CLL-associated antigen KW-5) (HSRNASEB) (RNA-binding motif protein 38) (RNA-binding region-containing protein 1) (ssDNA-binding protein SEB4) (Q9H0Z9)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that specifically bind the 3'-UTR of CDKN1A transcripts, leading to maintain the stability of CDKN1A transcripts, thereby acting as a mediator of the p53/TP53 family to regulate CDKN1A. CDKN1A is a cyclin-dependent kinase inhibitor transcriptionally regulated by the p53/TP53 family to induce cell cycle arrest. Isoform 1, but not isoform 2, has the ability to induce cell cycle arrest in G1 and maintain the stability of CDKN1A transcripts induced by p53/TP53. Also acts as a mRNA splicing factor. Specifically regulates the expression of FGFR2-IIIb, an epithelial cell-specific isoform of FGFR2. Plays a role in myogenic differentiation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17050675}. Nucleus {ECO:0000269|PubMed:17050675}.
Interaction partners:
- ELAV-like protein 1
- RNA binding protein fox-1 homolog 2
- Eukaryotic translation initiation factor 4E
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MLLQPAPCAPSAGFPRPLAAPGAMHGSQKDTTFTKIFVGGLPYHTTDASLRKYFEGFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRSLQTGFAIGVQQLHPTLIQRTYGLTPHYIYPPAIVQPSVVIPAAPVPSLSSPYIEYTPASPAYAQYPPATYDQYPYAASPATAASFVGYSYPAAVPQALSAAAPAGTTFVQYQAPQLQPDRMQ
Protein: Galactose-3-O-sulfotransferase 3 (Gal3ST-3) (EC 2.8.2.-) (Beta-galactose-3-O-sulfotransferase 3) (Gal3ST3) (Gal-beta-1, 3-GalNAc 3'-sulfotransferase 3) (Q96A11)
Organism: Homo sapiens (Human)
Function: Transfers a sulfate to position 3 of non-reducing beta-galactosyl residues in N-glycans and core2-branched O-glycans. Has high activity towards Gal-beta-1,4-GlcNAc, Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc and lower activity towards Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
Sequence:
MPPILQRLQQATKMMSRRKILLLVLGCSTVSLLIHQGAQLSWYPKLFPLSCPPLRNSPPRPKHMTVAFLKTHKTAGTTVQNILFRFAERHNLTVALPHPSCEHQFCYPRNFSAHFVHPATRPPHVLASHLRFDRAELERLMPPSTVYVTILREPAAMFESLFSYYNQYCPAFRRVPNASLEAFLRAPEAYYRAGEHFAMFAHNTLAYDLGGDNERSPRDDAAYLAGLIRQVEEVFSLVMIAEYFDESLVLLRRLLAWDLDDVLYAKLNARAASSRLAAIPAALARAARTWNALDAGLYDHFNATFWRHVARAGRACVEREARELREARQRLLRRCFGDEPLLRPAAQIRTKQLQPWQPSRKVDIMGYDLPGGGAGPATEACLKLAMPEVQYSNYLLRKQKRRGGARARPEPVLDNPPPRPIRVLPRGPQGP
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A0A8I6A6D9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRRLLEPCWWILFLKITSSVLHYVVCFPALTEGYVGTLQESRQGSSVQIRRRKASGDPYWAYSGAYGPEHWVTSSVSCGGSHQSPIDILDHHARVGEEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGAGLPGRFKAEKVEFHWGHSNGSAGSEHSVNGRRFPVEMQIFFYNPDDFDSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDHVKSVEYLRNNFRPQQALNDRVVSKSAVRDAWNHDLADFLDNPLGTEASKVCSSPPIHMKVQPLNQTALQVSWSQPETIYHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKATISHISPDSLYLFRVQAVCRNDMRSDFSQTMLFQANTTRIFQGTRIVKTGVPTASPASSADMAPISSGSSTWTSSGIPFSFVSMATGMGPSSSGSQATVASVVTSTLLAGLGFGGGGISSFPSTVWPTRLPTASAASKQAGRPVLATTEALASPGPDGDSAPTKDGEGAEEGEKEEKSESEDGEREQEEEEKDSEKKEKSEATHTAAESDQTAPAPTPSSPHRTAQEGGHQTIPGHRQDHSAPVTDQPGHVDPGLDTLVDTATQVPPTATEEHYSGSDPKRPEMPSKKPISRGDRFSEDSKFITVNPAEKNTSGMISRPSPGRMEWIIPLIVVSALTFVCLVLLIAVLVYWRKCFQTAHFYVEDSSSPRVVPNESIPIIPIPDDMEAIPVKQFGKHIGELYSNSQHGFSGDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIIMITNLVEKGRRKCDQYWPTENTEEYGNIIVTLKSTEVHACYTVRRFSVRNTKVKKGQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPDMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAILGKETEVSSSQLHSYVNSILIPGVGGKTRLEKQFKLITQCNAKYVECFSAQKECNKEKNRNSSVVPAERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALARDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFVYKAMLSLVSTKENGNGPMTGDKNGAVLTAEESDPAESMESLV
Protein: Sigma-like sequence protein 1, mitochondrial (Protein SLS1) (P42900)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in aerobic respiration where it is required for assembly of respiratory chain enzyme complexes III and IV. Also has a role in mitochondrial gene expression. May be part of a mitochondrial membrane-associated RNA-shuttling system, delivering NAM1-associated transcripts to the translation machinery.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:8917313}.
Interaction partners:
- Ribonuclease MRP protein subunit RMP1
- Mitochondrial translation factor 2
Sequence:
MWKFNKKLARLTYRLYSSSGPSSPLHGKKKLPQNLKFVVLNPTQSGLVKNDQKQPRHRPSKKRSHKETGDNNLDFGSKLLVFEKQNSLDSALNSIRLKKPTSASLPSLEYNALLQSLTSSYNRYQLREFISTHQPDSSSHLTHWKKSKLSQYIIEKIWNCQPISTPTTPTGIKSTSLTFQFDSPREIFLLLITQNGKILTNFNKLGLTFIISIQDNELTVKGSPSLLKYAEISLNKIWSNITHENVRMYSLMPSKDVINLIQKETHTFFEYLPDLQMYKISALSTKKISMAKVFLLNAVASNPNTTQHHHTIASPALKTELYPFNNTLENLDWLNKSQDWARLQSVVPKNCTDLMTPTENATPELTDAQVSQFESSLSKNIPSLSPSDSISQSLSITLGHSLQSASFSSIFQPLIHKSFISKLLNLPMYKESSSSAVPVPVPLDQHLITNAHQSFIQLNFTPVPPTSGSSSSPFLQIWFEIDEFDNIVTTSMRPLLKLQENSVILRTPQCQTDYKITSDYIQDLLPDFDQTNPDAWLSEQKGLQEFLLKSHWKLNKYQNLMKKINISLPDNLIQQYQLTDVLTHRVLNLRFPTNTAQDDKYIIQYSDISRGFLNNGSYRQLDFINVNPSETSLKTFINDVLSF
Protein: Protocatechuate 3,4-dioxygenase alpha chain (EC 1.13.11.3) (3,4-PCD) (P20371)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Interaction partners:
- Protocatechuate 3,4-dioxygenase beta chain
- 3-carboxy-cis,cis-muconate cycloisomerase
- p-hydroxybenzoate hydroxylase
- 4-carboxymuconolactone decarboxylase
- Catabolic 3-dehydroquinate dehydratase
- 3-oxoadipate enol-lactonase 1
Sequence:
MNGWNFQELKETPSQTGGPYVHIGLLPKQANIEVFEHNLDNNLVQDNTQGQRIRLEGQVFDGLGLPLRDVLIEIWQADTNGVYPSQADTQGKQVDPNFLGWGRTGADFGTGFWSFNTIKPGAVPGRKGSTQAPHISLIIFARGINIGLHTRVYFDDEAEANAKDPVLNSIEWATRRQTLVAKREERDGEVVYRFDIRIQGENETVFFDI
Protein: Dual specificity protein phosphatase, putative (Q57XT6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEREATKRERGKKGKKNERGETPPGSSSDHWDGRNTASLHPTTEPTGRASRSSGGTRFEPRARVHSLPPDSHLVSSVPLHVPPITTTTTGGRAKVALQRQKQQEEEEEFSKTMPLPLTTTFNWDEELTDEHEDLWPPLAVQKDSLATGAQKITMSAAAGDERQSNANSRAPDHRSNPTQRERAAGLLTTLPATCKTTSYVRPFVGSVRIEGEEESRDSQLVAGLTSTRTTSAFTPRSPLARAPLGTNERTFRSNISCTGGALRCEALGGLEGRVCNTRGGVPRSTAKFDDIVTPPLSVGKDEARSFSIGRCSDILRGGARICPGVDTSEDTEGNRTPEAVSQSPTVDVSQPLVREYSYFEEQSVSINRGLGEGRDFSPSLPCQGMVEEGPGVDTMAARAEGGEEVGSNSRWQRIRDRLSAANANPLLITLPQSPSFSPVTAASPEASANNETDRHSAPRGPSTTLSAVSCRLDLSRHPSSTAMSALTGPMDKSWRAESDTIGGRGSRTPQQISPCKRKKGMDSGEKRKVLRKDNDHPPQNGSVISRPAVLTGFNAAEVVSGLFIGSYADSKRPEVLAERGISLVINVATECAVTPEMLNNPCNVHYMKFHMKDNSDEDVARYLVSFAQLIHTQLHRRQFELTRTETTPPFCKHPTNGNTNCCHSSQCAAGSTGSNATKVATNGAVGTRKFGKGAEQGMVGDGNIGAATCHGVTNAGDGCGGSNKPVASSTHNSNSVLPPMFQSWGAGGILVHCREGVSRSATIVLGYLILYGEFLSSNGCWGRISDEVATLIKEAENHSAPAVRDGSCAPVCCGSALPPSTHPSSPNGAMIRAGNCSFSPRRGVNTTTPAAVTSGSGSPSTAVGASSFAVCGNDASNNIPMSATPGTSSNNNGGAEVPNVGKNDCDVIADCACCCCVARRSVEEGSKTAGSYQWAFEMLRKKRNISPNIGFVLALQALAGECASPH
Protein: P antigen family member 2 (PAGE-2) (G antigen family C 2) (Prostate-associated gene 2 protein) (Q7Z2X7)
Organism: Homo sapiens (Human)
Interaction partners:
- P antigen family member 1
Sequence:
MSELLRARSQSSERGNDQESSQPVGSVIVQEPTEEKRQEEEPPTDNQGIAPSGEIENQAVPAFQGPDMEAFQQELALLKIEDEPGDGPDVREGIMPTFDLTKVLEAGDAQP
Protein: Probable ethanolamine kinase (EC 2.7.1.82) (Protein EMBRYO DEFECTIVE 1187) (O81024)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis (By similarity).
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Regulatory-associated protein of TOR 1
- Regulatory-associated protein of TOR 2
- Phosphoethanolamine N-methyltransferase 1
- Non-functional target of rapamycin complex subunit LST8-2
- Target of rapamycin complex subunit LST8-1
- Phosphoethanolamine N-methyltransferase 2
- Phosphoethanolamine N-methyltransferase 3
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Choline/ethanolaminephosphotransferase 1
Sequence:
MGAAKNIWALANAEDAANDAEQIPYSSFVVDTSLPLPLMIPRIIELCKDLFKNWGELDDSLFSVERVSGGITNLLLKVSVKEDTNKEVSVTVRLYGPNTEYVINREREILAIKYLSAAGFGAKLLGGFGNGMVQSFINARTLEPSDMREPKIAAQIARELGKFHKVDIPGSKEPQLWVDILKFYEKASTLTFEEPDKQKLFETISFEELHKEIIELREFTGLLNAPVVFAHNDLLSGNFMLNDEEEKLYLIDFEYGSYNYRGFDIGNHFNEYAGYDCDYSLYPSKEEQYHFIKHYLQPDKPDEVSIAEVESVFVETDAYKLASHLYWAIWAIIQARMSPIEFEYLGYFFLRYNEYKKQKPLTFSLVTSHLSASL
Protein: Disco-interacting protein 2 homolog A (DIP2 homolog A) (EC 6.2.1.1) (Q14689)
Organism: Homo sapiens (Human)
Function: Catalyzes the de novo synthesis of acetyl-CoA in vitro (By similarity). Promotes acetylation of CTTN, possibly by providing the acetyl donor, ensuring correct dendritic spine morphology and synaptic transmission (By similarity). Binds to follistatin-related protein FSTL1 and may act as a cell surface receptor for FSTL1, contributing to AKT activation and subsequent FSTL1-induced survival and function of endothelial cells and cardiac myocytes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20054002}; Peripheral membrane protein {ECO:0000305}. Mitochondrion {ECO:0000250|UniProtKB:Q8BWT5}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q8BWT5}.
Interaction partners:
- Follistatin-related protein 1
- Hydroxysteroid dehydrogenase-like protein 2
- Beta-alanine-activating enzyme
Sequence:
MADRGCPLEAAPLPAEVRESLAELELELSEGDITQKGYEKKRAKLLARYIPLIQGIDPSLQAENRIPGPSQTTAAAPKQQKSRPTASRDERFRSDVHTEAVQAALAKYKERKMPMPSKRRSVLVHSSVETYTPPDTSSASEDEGSLRRPGRLTSTPLQSHSSVEPWLDRVIQGSSTSSSASSTSSHPGGRPTTAPSAAATPGAAATTALAGLEAHTHIDLHSAPPDVTTGLVEHSYFERPQVASVRSVPRGCSGSMLETADGVPVNSRVSSKIQQLLNTLKRPKRPPLKEFFVDDFEELLEVQQPDPNQPKPEGSETSVLRGEPLTAGVPRPPSLLATLQRWGTTQPKSPCLTALDTTGKAVYTLTYGKLWSRSLKLAYTLLNKLTSKNEPLLKPGDRVALVFPNSDPVMFMVAFYGCLLAELVPVPIEVPLTRKDAGSQQVGFLLGSCGVFLALTTDACQKGLPKAQTGEVAAFKGWPPLSWLVIDGKHLAKPPKDWHPLAQDTGTGTAYIEYKTSKEGSTVGVTVSHASLLAQCRALTQACGYSEAETLTNVLDFKRDAGLWHGVLTSVMNRMHVVSVPYALMKANPLSWIQKVCFYKARAALVKSRDMHWSLLAQRGQRDVSLSSLRMLIVADGANPWSISSCDAFLNVFQSRGLRPEVICPCASSPEALTVAIRRPPDLGGPPPRKAVLSMNGLSYGVIRVDTEEKLSVLTVQDVGQVMPGANVCVVKLEGTPYLCKTDEVGEICVSSSATGTAYYGLLGITKNVFEAVPVTTGGAPIFDRPFTRTGLLGFIGPDNLVFIVGKLDGLMVTGVRRHNADDVVATALAVEPMKFVYRGRIAVFSVTVLHDDRIVLVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKAPLGGIHISETKQRFLEGTLHPCNVLMCPHTCVTNLPKPRQKQPEVGPASMIVGNLVAGKRIAQASGRELAHLEDSDQARKFLFLADVLQWRAHTTPDHPLFLLLNAKGTVTSTATCVQLHKRAERVAAALMEKGRLSVGDHVALVYPPGVDLIAAFYGCLYCGCVPVTVRPPHPQNLGTTLPTVKMIVEVSKSACVLTTQAVTRLLRSKEAAAAVDIRTWPTILDTDDIPKKKIASVFRPPSPDVLAYLDFSVSTTGILAGVKMSHAATSALCRSIKLQCELYPSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLVPPLELESNVSLWLSAVSQYKARVTFCSYSVMEMCTKGLGAQTGVLRMKGVNLSCVRTCMVVAEERPRIALTQSFSKLFKDLGLPARAVSTTFGCRVNVAICLQGTAGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVKVIIAHTETKGPLGDSHLGEIWVSSPHNATGYYTVYGEEALHADHFSARLSFGDTQTIWARTGYLGFLRRTELTDASGGRHDALYVVGSLDETLELRGMRYHPIDIETSVIRAHRSIAECAVFTWTNLLVVVVELDGLEQDALDLVALVTNVVLEEHYLVVGVVVIVDPGVIPINSRGEKQRMHLRDGFLADQLDPIYVAYNM
Protein: LD21275p (Q95T24)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFASVGADGSVRMFDLRHLEHSTIIYEDPAHTALLRLAWNKQDPNYLATVAMDSCEVIILDVRVPCTPVARLSNHRACVNGIAWAPHSSCHICTAGDDHQALIWDIQQMPRAIEDPILAYTAAEGEVNQIQWGATQPDWIAICYNKACEILRV
Protein: Histone deacetylase HDT1 (HD-tuins protein 1) (Histone deacetylase 2a) (AtHD2A) (Q9FVE6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Required for histone H3 'Lys-9' deacetylation. Involved in rRNA gene silencing in nucleolar dominance. Seems to be implicated in the regulation of genes involved in seeds development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14505352, ECO:0000269|PubMed:14992728, ECO:0000269|PubMed:15144374}.
Interaction partners:
- Histone deacetylase 6
- Histone deacetylase 19
- Histone deacetylase 2
- Histone deacetylase 8
- Histone deacetylase 9
- Histone deacetylase 7
- NAD-dependent protein deacetylase SRT1
- NAD-dependent protein deacylase SRT2
- Histone deacetylase 17
- Histone deacetylase 18
Sequence:
MEFWGIEVKSGKPVTVTPEEGILIHVSQASLGECKNKKGEFVPLHVKVGNQNLVLGTLSTENIPQLFCDLVFDKEFELSHTWGKGSVYFVGYKTPNIEPQGYSEEEEEEEEEVPAGNAAKAVAKPKAKPAEVKPAVDDEEDESDSDGMDEDDSDGEDSEEEEPTPKKPASSKKRANETTPKAPVSAKKAKVAVTPQKTDEKKKGGKAANQSPKSASQVSCGSCKKTFNSGNALESHNKAKHAAAK
Protein: Erythrocyte binding antigen-175 (Q8IBE8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Nucleoporin NUP221, putative
- Merozoite surface protein 1
- Apical membrane antigen 1
Sequence:
MKCNISIYFFASFFVLYFAKARNEYDIKENEKFLDVYKEKFNELDKKKYGNVQKTDKKIFTFIENKLDILNNSKFNKRWKSYGTPDNIDKNMSLINKHNNEEMFNNNYQSFLSTSSLIKQNKYVPINAVRVSRILSFLDSRINNGRNTSSNNEVLSNCREKRKGMKWDCKKKNDRSNYVCIPDRRIQLCIVNLSIIKTYTKETMKDHFIEASKKESQLLLKKNDNKYNSKFCNDLKNSFLDYGHLAMGNDMDFGGYSTKAENKIQEVFKGAHGEISEHKIKNFRKKWWNEFREKLWEAMLSEHKNNINNCKNIPQEELQITQWIKEWHGEFLLERDNRSKLPKSKCKNNTLYEACEKECIDPCMKYRDWIIRSKFEWHTLSKEYETQKVPKENAENYLIKISENKNDAKVSLLLNNCDAEYSKYCDCKHTTTLVKSVLNGNDNTIKEKREHIDLDDFSKFGCDKNSVDTNTKVWECKKPYKLSTKDVCVPPRRQELCLGNIDRIYDKNLLMIKEHILAIAIYESRILKRKYKNKDDKEVCKIINKTFADIRDIIGGTDYWNDLSNRKLVGKINTNSNYVHRNKQNDKLFRDEWWKVIKKDVWNVISWVFKDKTVCKEDDIENIPQFFRWFSEWGDDYCQDKTKMIETLKVECKEKPCEDDNCKRKCNSYKEWISKKKEEYNKQAKQYQEYQKGNNYKMYSEFKSIKPEVYLKKYSEKCSNLNFEDEFKEELHSDYKNKCTMCPEVKDVPISIIRNNEQTSQEAVPEESTEIAHRTETRTDERKNQEPANKDLKNPQQSVGENGTKDLLQEDLGGSRSEDEVTQEFGVNHGIPKGEDQTLGKSDAIPNIGEPETGISTTEESRHEEGHNKQALSTSVDEPELSDTLQLHEDTKENDKLPLESSTITSPTESGSSDTEETPSISEGPKGNEQKKRDDDSLSKISVSPENSRPETDAKDTSNLLKLKGDVDISMPKAVIGSSPNDNINVTEQGDNISGVNSKPLSDDVRPDKNHEEVKEHTSNSDNVQQSGGIVNMNVEKELKDTLENPSSSLDEGKAHEELSEPNLSSDQDMSNTPGPLDNTSEETTERISNNEYKVNEREGERTLTKEYEDIVLKSHMNRESDDGELYDENSDLSTVNDESEDAEAKMKGNDTSEMSHNSSQHIESDQQKNDMKTVGDLGTTHVQNEISVPVTGEIDEKLRESKESKIHKAEEERLSHTDIHKINPEDRNSNTLHLKDIRNEENERHLTNQNINISQERDLQKHGFHTMNNLHGDGVSERSQINHSHHGNRQDRGGNSGNVLNMRSNNNNFNNIPSRYNLYDKKLDLDLYENRNDSTTKELIKKLAEINKCENEISVKYCDHMIHEEIPLKTCTKEKTRNLCCAVSDYCMSYFTYDSEEYYNCTKREFDDPSYTCFRKEAFSSMPYYAGAGVLFIILVILGASQAKYQSSEGVMNENNENNFLFEVTDNLDKLSNMFNQQVQETNINDFSEYHEDINDINFKK
Protein: Protein SERAC1 (Serine active site-containing protein 1) (Q96JX3)
Organism: Homo sapiens (Human)
Function: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:22683713}. Mitochondrion {ECO:0000269|PubMed:22683713}. Note=Localizes at the endoplasmic reticulum and at the endoplasmic reticulum-mitochondria interface.
Interaction partners:
Sequence:
MSLAAYCVICCRRIGTSTSPPKSGTHWRDIRNIIKFTGSLILGGSLFLTYEVLALKKAVTLDTQVVEREKMKSYIYVHTVSLDKGENHGIAWQARKELHKAVRKVLATSAKILRNPFADPFSTVDIEDHECAVWLLLRKSKSDDKTTRLEAVREMSETHHWHDYQYRIIAQACDPKTLIGLARSEESDLRFFLLPPPLPSLKEDSSTEEELRQLLASLPQTELDECIQYFTSLALSESSQSLAAQKGGLWCFGGNGLPYAESFGEVPSATVEMFCLEAIVKHSEISTHCDKIEANGGLQLLQRLYRLHKDCPKVQRNIMRVIGNMALNEHLHSSIVRSGWVSIMAEAMKSPHIMESSHAARILANLDRETVQEKYQDGVYVLHPQYRTSQPIKADVLFIHGLMGAAFKTWRQQDSEQAVIEKPMEDEDRYTTCWPKTWLAKDCPALRIISVEYDTSLSDWRARCPMERKSIAFRSNELLRKLRAAGVGDRPVVWISHSMGGLLVKKMLLEASTKPEMSTVINNTRGIIFYSVPHHGSRLAEYSVNIRYLLFPSLEVKELSKDSPALKTLQDDFLEFAKDKNFQVLNFVETLPTYIGSMIKLHVVPVESADLGIGDLIPVDVNHLNICKPKKKDAFLYQRTLQFIREALAKDLEN
Protein: Lectin-related NK cell receptor LY49L3 (Q9JIQ0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSEQEVTFSAVRFHKSSGLQNRVRLEETGKPQKAGLRVPWQLIVIALGILISLRLVIVSVLVTNIFQNSQQNHELQETLNCHDKCSTTTQSDINLKDELLSSTSIECRPGNDLLESLHKEQNRWYSETKTFSDSSQHTGVHKRPISKAEGKGRGFEKYWFCYGIKCYYFVMDRKTWSGCKQTCQISSLSLLKIDNEDELKFLKLLVPSDSCWIGLSYDNKKKDWAWINNGPSKLALNTMKYNIRDGGCMLLSKTRLDNDNCDKSFICICGKRLDKFPH
Protein: Penton protein P31 (GpC) (Protein C) (P27384)
Organism: Enterobacteria phage PRD1 (Bacteriophage PRD1)
Function: In association with P2 and trimeric P5, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity.
Subcellular location: Virion.
Interaction partners:
Sequence:
MNVNNPNQMTVTPVYNGCDSGEGPQSVRGYFDAVAGENVKYDLTYLADTQGFTGVQCIYIDNAENDGAFEIDVEETGQRIKCPAGKQGYFPLLVPGRAKFVARHLGSGKKSVPLFFLNFTIAQGVW
Protein: Type 3 secretion system stator protein (Q9Z780)
Organism: Chlamydia pneumoniae (Chlamydophila pneumoniae)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Type 3 secretion system ATPase
- Flagellar motor switch Domain/YscQ family
- Pathogenicity-related ORF2
- Secretion protein
- Flagellum-specific ATP synthase
- Type III secretion inner membrane protein SctT
- Type III secretion inner membrane protein SctS
- Type III secretion inner membrane protein SctU
- Flagellar M-Ring Protein
- Flagellar Secretion Protein
Sequence:
MKFFSLIFKDDDVSPNKKVLSPEAFSAFLDAKELLEKTKADSEAYVAETEQKCAQIRQEAKDQGFKEGSESWSKQIAFLEEETKNLRIRVREALVPLAIASVRKIIGKELELHPETIVSIISQALKELTQNKHIIISVNPKDLPLVEKSRPELKNIVEYADSLILTAKPDVTPGGCIIETEAGIINAQLDVQLDALEKAFSTILKAKNPVDEPSETSSSTDSSSLSNDQDKKE
Protein: Ethylene-responsive transcription factor ERF014 (Q9LPE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- MLO-like protein 3
- Transcription factor bHLH87
- Ethylene-responsive transcription factor ERF116
Sequence:
MVKTLQKTPKRMSSPSSSSSSSSSTSSSSIRMKKYKGVRMRSWGSWVSEIRAPNQKTRIWLGSYSTAEAAARAYDAALLCLKGSSANNLNFPEISTSLYHIINNGDNNNDMSPKSIQRVAAAAAAANTDPSSSSVSTSSPLLSSPSEDLYDVVSMSQYDQQVSLSESSSWYNCFDGDDQFMFINGVSAPYLTTSLSDDFFEEGDIRLWNFC