wanglab/gogpt-training-data huggingface dataset:
Protein: Meiotically up-regulated gene 31 protein (Q9US56)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nucleoporin pom152
- Nucleoporin nup60
- Nucleus export protein brr6
- Nuclear envelope protein ndc1
- mRNA export factor gle1
- Protein transport protein sec13
- Uncharacterized WD repeat-containing protein C4F10.18
- Nucleoporin seh1
- Nuclear bridge Ish domain protein les1
Sequence:
MASTFSQSVFARSLYEDSAENKVDSSKNTEANFPITLPKVLPTDPKASSLHKPQEQQPNIIPSKEEDKKPVINSMKLPSIPAPGTDNINESHIPRGYWKHPAVDKIAKRLHDQAPSDRTWSRMVSNLFAFISIQFLNRYLPNTTAVKVVSWILQALLLFNLLESVWQFVRPQPTFDDLQLTPLQRKLMGLPEGGSTSGKHLTPPRYRPNFSPSRKAENVKSPVRSTTWA
Protein: G domain-containing protein (Q387K3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small ribosomal subunit protein mS29
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S13, putative
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- ATP-dependent DEAD/H RNA helicase
- Cytidine deaminase, putative
- GTP-binding protein, putative
- rRNA adenine N
Sequence:
MLSRTFSRLNTVYSRRRWEQRIVSVLSEQKNANVDAVAQRFTRIYKERRFTPVEEAFPLRDTARWVGLNDESNSGSHINQQSTLQQPPDAHKLRAVIVGTQNSGKTSLLNALSLSHIGAVSNRSGVTREWTRGVATVHNTQLVLLDTPGIVICNGEKDRRRHAAPVARTWDAFTVTDLVMLTLPAGLGFVEPEQKTVAREVVHRASLRKMPVVLVITMMDRVQTPRHRELYFAMRTDLESLCLPIACVSETSVKGGNGLVELKDLLCRYASPGDWEFFRNETTDATPVDRVMELLRQCFFEVLPHEIPHQMRHRIIGWTKKDSGTVEVITEVFFDRPAYMFTFYAKLEAICYRAQRIVERELKGRYRFVFQAFITPGGMSCK
Protein: Putative protein disulfide-isomerase C1F5.02 (EC 5.3.4.1) (Q10057)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- ERO1-like protein 2
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase C17H9.14c
- Uncharacterized protein C3D6.13c
- Thioredoxin domain-containing protein C13F5.05
- Thioredoxin domain-containing protein C959.05c
- Calnexin homolog
- Tubulin beta chain
- ERO1-like protein 1
- Heat shock protein 70 homolog lhs1
Sequence:
MKISNLLAAFLAFSGGFFCASAEVPKVNKEGLNELITADKVLMVKFYAPWCGHCKALAPEYESAADELEKDGISLVEVDCTEEGDLCSEYSIRGYPTLNVFKNGKQISQYSGPRKHDALVKYMRKQLLPTVKPISKDTLENFVEKADDLAVVAFFKDQKLNDTYTEVAEVMKDDFVFAASDDKELAKSLGSNFPGIVAFTKDAAQDSDKLVYTGDWDPASIADFIGVSSIPLLDELNQMTFGKYQQSGLPLGIIFYNSTESRDELYDVFQPLAKKYQDTLRFAFLDAVRYGAVAKQMNVESDWPAFVIANLKSMLKYPFPTTELTAKAMTKFVGDFVDGKLQPKIKSQPIPESQEDLVVLVADNFDDIVMDETKDVLVEFYAPWCGHCKNLAPTYEKLAEEYSDDSNVVVAKIDATENDISVSISGFPTIMFFKANDKVNPVRYEGDRTLEDLSAFIDKHASFEPIKKEKESVPAPDLEDQVAVEDEMADEL
Protein: Small ribosomal subunit protein eS26z (40S ribosomal protein S26-2) (Q8LPJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS19z
- Small ribosomal subunit protein uS17y
- Small ribosomal subunit protein eS17z
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein uS5z
- Small ribosomal subunit protein eS8z
- Small ribosomal subunit protein eS10z
Sequence:
MTFKRRNGGRNKHNRGHVNPIRCSNCGKCCPKDKAIKRFIVRNIVEQAAIRDVQEASVYEGYTLPKLYAKTQYCVSCAIHSHVVRVRSRTNRRVRTPPPRFARRKEDTPKPGQPGQAPRPAGPGAAAAAAPRV
Protein: Probable phosphatidylglycerophosphate synthase (PGP synthase) (PGPS) (EC 2.7.8.5) (CDP-diacylglycerol--glycerol-3-phosphate phosphatidyltransferase) (P9WPG3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably catalyzes the synthesis of phosphatidylglycerophosphate by transferring a phosphatidyl group from CDP-diacylglycerol to glycerol 3-phosphate.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol phosphate synthase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidate cytidylyltransferase
- Putative cardiolipin synthase
- Probable CDP-diacylglycerol pyrophosphatase
- CinA-like protein
- UPF0749 protein Rv1823
- UPF0749 protein Rv1825
- Uncharacterized protein Rv1829
- Amino-acid acetyltransferase
Sequence:
MSRSTRYSVAVSAQPETGQIAGRARIANLANILTLLRLVMVPVFLLALFYGGGHHSAARVVAWAIFATACITDRFDGLLARNYGMATEFGAFVDPIADKTLIGSALIGLSMLGDLPWWVTVLILTRELGVTVLRLAVIRRGVIPASWGGKLKTFVQAVAIGLFVLPLSGPLHVAAVVVMAAAILLTVITGVDYVARALRDIGGIRQTAS
Protein: Acetylcholine receptor subunit gamma (P13536)
Organism: Bos taurus (Bovine)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Secreted LY6/PLAUR domain containing 1
- 43 kDa receptor-associated protein of the synapse
- Myogenin
- receptor protein-tyrosine kinase
- Acetylcholine receptor subunit alpha
- MYH3 protein
Sequence:
MCGGQRPLFLLPLLAVCLGAKGRNQEERLLGDLMQGYNPHLRPAEHDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYGGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCVYWLPPAIFRSSCPVSVTFFPFDWQNCSLIFQSQTYSTNEINLQLSQEDGQTIEWIFIDPEAFTENGEWAIRHRPAKMLLDEAAPAEEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIYFLPAKAGGQKCTVAINVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLLVVTILIVVNAVVVLNVSLRSPHTHSMARGVRKVFLRLLPQLLRMHVRPLAPVAVQDAHPRLQNGSSSGWPITAGEEVALCLPRSELLFRQRQRNGLVRAALEKLEKGPESGQSPEWCGSLKQAAPAIQACVEACNLIARARHQQTHFDSGNKEWFLVGRVLDRVCFLAMLSLFVCGTAGIFLMAHYNRVPALPFPGDPRSYLPSSD
Protein: Bestrophin homolog (A0A0B4KGQ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU363126}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363126}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTITYTGEVATCRGFGCFLKLLLRWRGSIYKLVWLDLLAFLTIYYAINMVYRFGLNPAQKETFEAIVQYCDSYRELIPLSFVLGFYVSIVMTRWWNQYTSIPWPDPIAVFVSSNVHGQDERGRMMRRTIMRYVCLCLTMVLANVSPRVKKRFPGLNNLVEAGLLNDNEKTIIETMNKAFPRPSKHWLPIVWAASIITRARKEGRIRDDFAVKTIIDELNKFRGQCGLLISYDTISVPLVYTQVVTLAVYSYFLTCCMGQQWTDGKVVGNTTYLNKVDLYFPVFTTLQFFFYMGWLKVAESLINPFGEDDDDFEVNWMVDRNLQVSYLIVDEMHHDHPELLKDQYWDEVFPNELPYTIAAERFRENHPEPSTAKIEVPKNAAMPSTMSSVRIDEMADDASGIHFSAGNGKMRLDSSPSLVSVSGTLSRVNTVASALKRFLSRDDSRPGSATPSQDQPYKFPASASSASLSGAVVGSATSAGKPAGSLRITQQVIEEVDEQATITSMRANDPRPNVMDIFAQTSSGAGTSGPLQPPPAHSEPVDIPSRPPSYNRAQSQYEPNLFPPGGVDALLSTSAPAGGSPLLLSNAATAPSSPVGESSKSLYDPQKGASRETERPDAPQVFRWFVTPVESMDLRSSTDLLGDAAVQPEDEGDDFDKLKAEREKEKLMRQQKNLARTISTAPGMEATAVPMVPMVPVNVAVQQAQLQPVASSADLLAGGDQFSNSTMKSEDAINGS
Protein: Uncharacterized protein YBR071W (P38243)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized protein YBL012C
- Uncharacterized protein YBL044W
- Putative uncharacterized protein YBL083C
- Putative uncharacterized protein YBR300C
- Uncharacterized protein YBR144C
- UPF0045 protein ECM15
- F-box protein COS111
Sequence:
MLRRSKNSSTNTNADTKKRQSMHLGSKSSLISLTSEFGHGHSKTKQKKEEGTAPSQFLSPTNKRSTSSQSKLKRSSLLLDETLLKDYHSAMRHMQTNAAKEEKLRMAPSPTQSTRSESDASLSSTKSSISSIFSQDNDYSIHDLLYEDIEEMDKTDAFKINNTIAIDDSKALFVFCSNDSSSRTASIETLHESNLDNLDMGSSRRTSLDFF
Protein: E3 ubiquitin-protein ligase MSL2 (EC 2.3.2.27) (Male-specific lethal 2-like 1) (MSL2-like 1) (Male-specific lethal-2 homolog) (MSL-2) (Male-specific lethal-2 homolog 1) (RING finger protein 184) (Q9HCI7)
Organism: Homo sapiens (Human)
Function: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure. Acts as an E3 ubiquitin ligase that promotes monoubiquitination of histone H2B at 'Lys-35' (H2BK34Ub), but not that of H2A. This activity is greatly enhanced by heterodimerization with MSL1. H2B ubiquitination in turn stimulates histone H3 methylation at 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) and leads to gene activation, including that of HOXA9 and MEIS1.
Subcellular location: Nucleus {ECO:0000269|PubMed:16227571}. Chromosome {ECO:0000269|PubMed:21726816}. Note=Associates with both promoters and enhancers of target genes, maintaining promoter-enhancer contacts. {ECO:0000250|UniProtKB:Q69ZF8}.
Interaction partners:
- MSL complex subunit 3
- Male-specific lethal 1 homolog
- Histone acetyltransferase KAT8
- Histone acetyltransferase KAT5
- Mortality factor 4-like protein 1
- Enhancer of polycomb homolog 1
- Actin, cytoplasmic 1
- Transformation/transcription domain-associated protein
- MBT domain-containing protein 1
- E1A-binding protein p400
Sequence:
MNPVNATALYISASRLVLNYDPGDPKAFTEINRLLPYFRQSLSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYITQTTLARDIIEAVDCSSDILALLNDGSLFCEETEKPSDSSFTLCLTHSPLPSTSEPTTDPQASLSPMSESTLSIAIGSSVINGLPTYNGLSIDRFGINIPSPEHSNTIDVCNTVDIKTEDLSDSLPPVCDTVATDLCSTGIDICSFSEDIKPGDSLLLSVEEVLRSLETVSNTEVCCPNLQPNLEATVSNGPFLQLSSQSLSHNVFMSTSPALHGLSCTAATPKIAKLNRKRSRSESDSEKVQPLPISTIIRGPTLGASAPVTVKRESKISLQPIATVPNGGTTPKISKTVLLSTKSMKKSHEHGSKKSHSKTKPGILKKDKAVKEKIPSHHFMPGSPTKTVYKKPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKKLEAFAVPEKALEQTRLTLGINVTSIAVRNASTSTSVINVTGSPVTTFLAASTHDDKSLDEAIDMRFDC
Protein: Ribosomal protein L7/L12 C-terminal domain-containing protein (G8BJN1)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- KOW domain-containing protein
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS9m
- KOW domain-containing protein
- Ribosomal protein S16
- Large ribosomal subunit protein bL32m
- Ribosomal protein L17
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL18 C-terminal eukaryotes domain-containing protein
Sequence:
MSITRQTITRALRASPFKRSPSFITSIRFNTTTAAESPSSPVVDPKITQIVDQISTLTLLETSQLVNELKTRLNISDIALPVAGGAAGGVGGGAQQASPAEEEEAKQPVEEKTMFAIKLESFDAKSKPKVIKEVKGLLGLSLVESKKFVESAPKVLKENVAKEDAEKIKATLEGLGAKVVLE
Protein: Piperine synthase (Piperidine N-piperoyltransferase) (Piperoyl-CoA:piperidine piperoyl transferase) (EC 2.3.1.145) (BAHD-type acyl transferase 2) (PipBAHD2) (P0DO56)
Organism: Piper nigrum (Black pepper)
Function: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects. Mediates mainly the conversion of piperidine and piperoyl-CoA to piperine. Can also use pyrrolidine and isobutylamine as acceptors and 3,4-methylenedioxycinnamoyl-CoA as an alternative CoA-donor with a lower efficiency.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:35634755}. Note=Localized at residual cytoplasmic structures in special cells of the fruit perisperm. {ECO:0000269|PubMed:35634755}.
Interaction partners:
Sequence:
MAPSSQLEFNVVRKQPELLPPAEPTPFEWKELSDIDDQDGLRLHISGFFIYPPSTMSNVGRDNVARDIRLGLSKAMVFYYPLAGRIREGPNRKLSVECTGEGIMYCEADADVRLEQFGDIGALSMPFPFMDKVMFETVDDGILGTPLMYFQSTRFICGGIVIAGCYNHAIADGLGFYMFMAAAAQLARGAASPTPLPVWQRERLLSRVPPRVTFIHHEYIHDTPKTETANPLDNEPWPLHSIFFTRVDVAALRAQLPGHLRKSATSFEIISACLWRCRTAALRFAPDELSRLIIAVNARTKFGPPLPQGYYGNSIMLPMVVSEAGKLVLSGLGYAVELVIEAKGKVTEEYVKSVADYLVLNGRPHYVVTNTYLVSDLRQLVEMSKFDWGWGKPAYVGPADVGENAISFLATLKNGEEEGVVVPIRLPESAVGRFKSEVSKMVSFGCLEDVKPNRDGYLSRM
Protein: Bone morphogenetic protein 15 (Q8WMY6)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVLLSIIRTLLLWGLVLFMEHRVQMTQVGQPSVALLPEACTLPLIRELLEEAPGKQQRKPQVLGHPLRYMLELYQRSADARGHPRENRTIGATMVRLVRPLVNGARPLRGPWHIQTLDFPLRPNRVAYQLVRATVVYRHQLHLAPFHLSCHVEPWIQKSTTSHFPSSGRGSLKPSLLPQAWTEMDVTQHVGQKLWNHKGRRVLRLRFMCQQQNGSEILEFRGRGISSLDTAFLLLYFNDTRSVQKAKLLPRGLEEFMARDPSLLLRKARQAGSIASEVLGPSREHDGPESNQCSLHPFQVSFHQLGWDHWIIAPHFYTPNYCKGVCPRVLHYGLNSPNHAIIQNLVNELVDQSVPQPSCVPYKYVPISILLIEANGSILYKEYEDMIAQPCTCR
Protein: Melatonin receptor type 1B (Mel-1B-R) (Mel1b receptor) (P49287)
Organism: Rattus norvegicus (Rat)
Function: High affinity receptor for melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibits adenylate cyclase activity.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Melatonin-related receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MPDNSSIANCCAASGLAARPSWPGSAEAEPPETPRAPWVAPMLSTVVIVTTAVDFVGNLLVILSVLRNRKLRNAGNLFVVNLALADLVVALYPYPLILVAILHDGWVLGEIHCKASAFVMGLSVIGSVFNITAIAINRYWCICHSATYHRACSQWHAPLYISLIWLLTLVALVPNFFVGSLEYDPRIYSCTFIQTASTQYTMAVVAIHFLLPIAVVSFCYLRIWILVLQARRKAKAERKLRLRPSDLRSFLTMFAVFVVFAICWAPLNCIGLAVAINPEAMALQIPEGLFVTSYFLAYFNSCLNAIVYGLLNQNFRREYKRILSALWSTGRCFHDASKCHLTEDLQGPVPPAAMATIPVQEGAL
Protein: Diphthine methyl ester synthase (EC 2.1.1.314) (Diphthamide biosynthesis methyltransferase) (Q9H2P9)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
Interaction partners:
- 2-
- 2-
- Elongation factor 2
- Diphthine--ammonia ligase
- Diphthine methyltransferase
- Diphthamide biosynthesis protein 3
- DnaJ homolog subfamily C member 24
- RNA 3'-terminal phosphate cyclase
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
Sequence:
MLYLIGLGLGDAKDITVKGLEVVRRCSRVYLEAYTSVLTVGKEALEEFYGRKLVVADREEVEQEADNILKDADISDVAFLVVGDPFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPESFFDKVKKNRQNGMHTLCLLDIKVKEQSLENLIKGRKIYEPPRYMSVNQAAQQLLEIVQNQRIRGEEPAVTEETLCVGLARVGADDQKIAAGTLRQMCTVDLGEPLHSLIITGGSIHPMEMEMLSLFSIPENSSESQSINGL
Protein: Forkhead box protein E3 (Q9QY14)
Organism: Mus musculus (Mouse)
Function: Transcription factor that controls lens epithelial cell growth through regulation of proliferation, apoptosis and cell cycle. During lens development, controls the ratio of the lens fiber cells to the cells of the anterior lens epithelium by regulating the rate of proliferation and differentiation. Controls lens vesicle closure and subsequent separation of the lens vesicle from ectoderm. Is required for morphogenesis and differentiation of the anterior segment of the eye. Controls the expression of DNAJB1 in a pathway that is crucial for the development of the anterior segment of the eye (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:17064680}.
Interaction partners:
- Pituitary homeobox 3
- Alpha-crystallin A chain
- Paired box protein Pax-6
Sequence:
MDAQVAFSGFPALPSLTPSGPQLPTLAGAEPGREPEEVVGGGDAEPTAVPGPGKRRRRPLQRGKPPYSYIALIAMALAHAPGRRLTLAAIYRFITERFAFYRDSPRKWQNSIRHNLTLNDCFVKVPREPGNPGKGNYWTLDPAAADMFDNGSFLRRRKRFKRAELPAPPPPPPPFPYAPFPPPPAPASAPPARLFRLDSLLGLQPEPPGPVAPEPPCCAAPDAAFPPCAAAASPPLYSPASERLGLPAPLPAQPLLALAGSAGALGPLGAGEAYLRQPGFAPGLERYL
Protein: Pre-mRNA-splicing factor SYF2 (Q4QRB2)
Organism: Rattus norvegicus (Rat)
Function: Involved in pre-mRNA splicing as component of the spliceosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95926}.
Interaction partners:
- Pre-mRNA-splicing factor SYF1
- Cell division cycle 40.
- SNW domain-containing protein 1
- 116 kDa U5 small nuclear ribonucleoprotein component
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pleiotropic regulator 1
- Protein BUD31 homolog
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor RBM22
Sequence:
MAAVTEVVVPADGAEARPLAAEELAAQKREQRLRKFRELHLKRNEARKLNHQEVVEEDKRLKLPANWEAKKARLEWELQEEEKKKECAARGEDYEKVKLLEISAEDAERWERRKKKKNPDLGFSDYAAAQLRQYHRLTKQIKPDMESYERQREKHGEDFFPTSNSLLHGTHVPSSEEIDRMVLDLEKQIEKRDKYSRRRPYNDDADIDYINERNAKFNKKAERFYGKYTAEIKQNLERGTAV
Protein: Serine-aspartate repeat-containing protein D (O86488)
Organism: Staphylococcus aureus (strain Newman)
Function: Cell surface-associated calcium-binding protein which plays an important role in adhesion and pathogenesis. Mediates interactions with components of the extracellular matrix such as host DSG1 to promote bacterial adhesion to host cells. Contributes to the resistance to killing by innate immune components such as neutrophils present in blood and thus attenuates bacterial clearance (By similarity).
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}. Note=Anchored to the cell wall by sortase A. {ECO:0000305|PubMed:11830639}.
Interaction partners:
Sequence:
MLNRENKTAITRKGMVSNRLNKFSIRKYTVGTASILVGTTLIFGLGNQEAKAAESTNKELNEATTSASDNQSSDKVDMQQLNQEDNTKNDNQKEMVSSQGNETTSNGNKLIEKESVQSTTGNKVEVSTAKSDEQASPKSTNEDLNTKQTISNQEALQPDLQENKSVVNVQPTNEENKKVDAKTESTTLNVKSDAIKSNDETLVDNNSNSNNENNADIILPKSTAPKRLNTRMRIAAVQPSSTEAKNVNDLITSNTTLTVVDADKNNKIVPAQDYLSLKSQITVDDKVKSGDYFTIKYSDTVQVYGLNPEDIKNIGDIKDPNNGETIATAKHDTANNLITYTFTDYVDRFNSVQMGINYSIYMDADTIPVSKNDVEFNVTIGNTTTKTTANIQYPDYVVNEKNSIGSAFTETVSHVGNKENPGYYKQTIYVNPSENSLTNAKLKVQAYHSSYPNNIGQINKDVTDIKIYQVPKGYTLNKGYDVNTKELTDVTNQYLQKITYGDNNSAVIDFGNADSAYVVMVNTKFQYTNSESPTLVQMATLSSTGNKSVSTGNALGFTNNQSGGAGQEVYKIGNYVWEDTNKNGVQELGEKGVGNVTVTVFDNNTNTKVGEAVTKEDGSYLIPNLPNGDYRVEFSNLPKGYEVTPSKQGNNEELDSNGLSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQDEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLTTTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDGKYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVWEDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSGNDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYCFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMSTTKDHHNKAKALPETGNENSGSNNATLFGGLFAALGSLLLFGRRKKQNK
Protein: Probable proteasome subunit beta type-2 (EC 3.4.25.1) (Q09841)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (Potential).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit alpha type-5
- Probable proteasome subunit beta type-3
- Probable proteasome subunit alpha type-3
- Probable proteasome subunit beta type-7
- Probable proteasome subunit beta type-4
- Probable proteasome subunit beta type-1
- Probable proteasome subunit alpha type-6
- Probable proteasome subunit alpha type-1
- Probable proteasome subunit alpha type-7
- Probable proteasome subunit beta type-5
Sequence:
MMGINERKGFDFEYYQRNLLLQEKGFPTPKATSTGTTIVGVIAKDCIVLGADTRATAGPIIADKNCKKLHLISPNIWCAGAGTAADTEFVTSMISSNIELHSLYTNRKPRVVTALTMLKQHLFRYQGHIGAYLVLGGYDCKGPHLFTIAAHGSSDKLPYVALGSGSLAAISVLETKYQPDLERHEAMELVKEAIEAGIFNDLGSGSNCDLVVIDEEKATPYRGYSKPNERATKQSKYTYDRGTTAVLKEDIYKFVTVQDLDEMQVDV
Protein: dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) (A0QSK6)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction (By similarity). Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage.
Interaction partners:
- Glucose-1-phosphate thymidylyltransferase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase
- dTDP-4-dehydrorhamnose reductase
- NAD dependent epimerase/dehydratase family protein
- NAD-dependent epimerase/dehydratase
- UDP-galactopyranose mutase
- Decaprenyl-phosphate N-acetylglucosaminephosphotransferase
- Membrane protein
Sequence:
MRLLVTGGAGFIGANFVHLALREARTSSITVLDALTYAGSRESLAPVADRIRLVQGDITDAALVGDLVAESDAVVHFAAETHVDNALADPEPFLHSNVVGTYTILEAVRRHNVRLHHVSTDEVYGDLELDNPARFNETTPYNPSSPYSSTKAAADLLVRAWVRSYGVRATISNCSNNYGPYQHVEKFIPRQITNVLTGRRPKLYGAGANVRDWIHVDDHNSAVWRILTDGTIGRTYLIGAECERNNLTVMRTILKLMGRDPDDFDHVTDRAGHDLRYAIDPSTLQDELGWAPKHTDFEAGLTDTIDWYRANESWWRPLKDTVEAKYQERGQ
Protein: Heat shock protein beta-8 (HspB8) (Alpha-crystallin C chain) (E2-induced gene 1 protein) (Heat shock protein family B member 8) (Protein kinase H11) (Small stress protein-like protein HSP22) (Q9UJY1)
Organism: Homo sapiens (Human)
Function: Displays temperature-dependent chaperone activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}. Note=Translocates to nuclear foci during heat shock.
Interaction partners:
- BAG family molecular chaperone regulator 3
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- E3 ubiquitin-protein ligase CHIP
- Heat shock protein beta-2
- Heat shock protein HSP 90-beta
- Heat shock protein beta-1
- DnaJ homolog subfamily B member 1
- Heat shock protein beta-7
- Heat shock protein beta-3
Sequence:
MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT