wanglab/gogpt-training-data huggingface dataset:
Protein: Cytoplasmic envelopment protein 3 (Q83153)
Organism: Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus)
Subcellular location: Virion tegument {ECO:0000256|HAMAP-Rule:MF_04041}. Virion membrane {ECO:0000256|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04041}. Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04041}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04041}. Host Golgi apparatus membrane {ECO:0000256|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000256|HAMAP-Rule:MF_04041}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_04041}. Note=Virion membrane-associated tegument protein. Associates with host membrane lipids rafts. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000256|HAMAP-Rule:MF_04041}.
Interaction partners:
Sequence:
MGAECCKQLCRSLHPYAADSLKDSSGRRVDLGTEFSVLTDTSDDEDQVGAGERDDFVQKQLTTPLLSDKNSAIPLTVVTPIQLGANKGGGKRTSSLKSAKNGAGVKKKVRAL
Protein: Beta-galactoside alpha-2,6-sialyltransferase 1 (Alpha 2,6-ST 1) (EC 2.4.3.1) (B-cell antigen CD75) (CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1) (ST6Gal I) (ST6GalI) (Sialyltransferase 1) (P15907)
Organism: Homo sapiens (Human)
Function: Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein {ECO:0000305}. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Interaction partners:
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
- Beta-galactoside alpha-2,6-sialyltransferase 2
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
- Alpha-
Sequence:
MIHTNLKKKFSCCVLVFLLFAVICVWKEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDSQSVSSSSTQDPHRGRQTLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRTKAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTEKRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNPPSSGMLGIIIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFFDSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC
Protein: Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (PDHE1-A) (EC 1.2.4.1) (Q54C70)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase complex subunit homolog DDB_G0271564
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Pyruvate kinase
- Glucose-6-phosphate isomerase
- NADP-dependent malic enzyme
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MLSNFLKVNSKALGHIRTFASKSGEIKHNFKKADTYLCDGPSDSTVTNKDELISFFTEMSRFRRLETVCDGLYKKKLIRGFCHLYTGQEAVCAGLESAITKDDHIITAYRDHTYMLSRGATPEEIFAELLMKETGCSKGKGGSMHMFTKNFYGGNGIVGAQCPLGAGIAFAQKYNKTGNVCLAMYGDGAANQGQLFEAFNMASLWKLPVIFICENNKYGMGTSQKRSTAGHDFYTRGHYVAGLKVDGMDVFAVKEAGKYAAEWCRAGNGPIILEMDTYRYVGHSMSDPGITYRTREEVNHVRQTRDPIENIRQIILDNKIATEDQLAAIEETVRDEMEKASEKAIAAPLPQARELFTNVYLQEVPVRGVEFVNSFKP
Protein: Rrp15p protein (F4K087)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Peter Pan-like protein
- At4g01560
- AT5g04600/T32M21_200
- AT5g20600/F7C8_190
- Protein MAK16 homolog
- Ribosome production factor 2 homolog
- Transducin/WD40 repeat-like superfamily protein
- Ribosome biogenesis protein BRX1 homolog 2
- Ribosome biogenesis protein BRX1 homolog 1
- Probable rRNA-processing protein EBP2 homolog
Sequence:
MSTGEEGHMAMADRGSRKRRVGVKKGTKAARNKKQKSKPSTSDRFKVTMKNQKLFQKRARDYNSDDDEEEDDESKKQPEVTIREKIFSDANMGPNYEEIGEEDNDENSDGEDHGEIESGITKFATDGCNAFKIAFKAIMKKTKGDDTLGPVLSAHKHLIGEKLAEDEAEKKAKGQARKAKHLIAEKGHVKPGSYLDSHEKILIGVATKGVVKLFNAVNKAQHAQKGLNPSRSKDAKVLKKRRKEAFLSELGKTKTDTKPFDARRNKLVFCLDLAPIESHEKNHLMSESKLVFCLELASIEKGSPSAHKSEDEAPVWAPLRDNYMLANPKLKDWDKKQETSEGDDFAGLSGDESYED
Protein: Large ribosomal subunit protein uL4m (Q385G8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Peptidyl-prolyl cis-trans isomerase
- 50S ribosomal protein L13, putative
- Tetratricopeptide repeat
- Large ribosomal subunit protein bL21m
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- 50S ribosomal protein L14, putative
- Uncharacterized protein
Sequence:
MKERIIAPVFNLKNEVIYTRELDPFIFGMYPEVEELSKNLTYWMVRCQNFASKWDYETREIWRKAKKNWPNTGMGMPRVGNRKNHLYTWGGRTKPSKPWNMLMPTMDVKTWSKSNRMMLTLKMLQGRLQVVDRLTLEEPTQECYLELCRNMSWDVRHTGGGVLFMDGGSRITPSSEFDRAFFFGSFFNGRNKIVRPTVLCDEQYDYNKTAAKQRMKGPKGAKNPIPINRFNAYDAMKHDRLVITEGALMQLEDELYEHKLQILPPHIRNQLPEYGYLDSEALGDCVPSLKTIQMEAAARTEEAESDMYKSFIDNPYNPWKDNMDASYAVDGADGTVQKFVDGKKVSWSMLS
Protein: Protein kinase C-like (EC 2.7.11.13) (P87253)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Interaction partners:
- non-specific serine/threonine protein kinase
- Rho-type GTPase
- Uncharacterized protein
- M-phase inducer phosphatase
- P-loop containing nucleoside triphosphate hydrolase protein
- Rho-type GTPase
- Uncharacterized protein
- Small GTPase RAC
- RHO family GTPase Rho2
- Rho guanyl nucleotide exchange factor
Sequence:
MNDEDKVHDISKKIEREKALINAAQAMRQQTNNEQVRSKLDTQMREGRRNLEFFEEKLRELQMRRLGHGVDNMSLGASPMSGSHRQSVDDFEGYGAPSPPPKEDVRGHSSHQSQGSGPLMPASAPYPGGPPDSNVPRARPNYTRLDLIKFDTPHLGPRIQLMLSQIQFKLNVEEQYLKGIEKMVQLYQMEGDKKSKLDAAAKRVESKQKIVLLKQALKRYEELHIDIDVDGPDDDSINLPALRKPLSGTLSIRILAVKDVDHAPLGRFARSPETFIAVKAEDIVVARTKPSRNDKWEAEFHTFPVDKTNEIEFTVYDKPAEHPVPIAMLWVRISDIVEELRRKKIEAEMTSAGWVSADRVGSRAPPPQFPMGAQSPQFAAPPTSPGSQEQNTMIPPQAPPPSQVVSQPVDGWFNLEPYGQIHLSFNFIKGARPQGMDRLGRKGAVRQRKEEVHEMYGHKFVQKQFYNIMRCALCGDFLKYSAGMQCEDCKYTCHTKCYTSVVTKCISKSNAETDPDEEKINHRIPHRFIPFSNLTANWCCHCGYMLPIGSKKNSRKCSECALTAHAQCVHLVPDFCGMSMAVANQILEGMRTQKKTHKDKASSMSERTLRPGSKTSISSGSIAQASTYSGSTAYTSIASPEATEAAKLMYSQTTPRPGGPDRTSTSSTTASAAAAAAMAPKHSSQPSQAGSIPDFGGSPGYGRPDSRDDEYSAQQQQGYGSPQQRKYNPADYANIDAYSSPQARPQQQQQQQQQTPQQVSPMYQQNPQTPISKPQPVAPSYDNQVVPSASGVPVPTKKPLPSATDPGTGMRIGLDHFNFLAVLGKGNFGKVMLAETKKSRKLYAIKVLKKEFIIENDEVESIRSEKRVFLIANRERHPFLTNLHACFQTETRVYFVMEYISGGDLMLHIQRGMFGTKRAQFYAAEVCLALKYFHENGVIYRDLKLDNILLTLDGHIKIADYGLCKEDMWYGSTTSTFCGTPEFMAPEILLDKKYGRAVDWWAFGVLIYQMLLQQSPFRGEDEDEIYDAILADEPLYPIHMPRDSVSILQKLLTREPDQRLGSGPTDAQEIMSQPFFRNINWDDIYHKRVQPPFLPQIKSATDTSNFDSEFTSVTPVLTPVQSVLSQAMQEEFRGFSYTADFE
Protein: Ribonuclease VapC28 (RNase VapC28) (EC 3.1.-.-) (Toxin VapC28) (P9WF81)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB28.
Interaction partners:
- Antitoxin VapB30
- Antitoxin VapB28
- Ribonuclease VapC32
- Ribonuclease VapC15
- Uncharacterized protein
- Ribonuclease VapC26
- Ribonuclease VapC29
- Ribonuclease VapC25
- Ribonuclease VapC33
- Putative antitoxin VapB34
Sequence:
MIVDTSAIIAILRDEDDAAAYADALANADVRRLSAASYLECGIVLDSQRDPVISRALDELIEEAEFVVEPVTERQARLARAAYADFGRGSGHPAGLNFGDCLSYALAIDRREPLLWKGNDFGHTGVQRALDRR
Protein: Angiopoietin-related protein 4 (425O18-1) (Angiopoietin-like protein 4) (Fasting-induced adipose factor) (Hepatic fibrinogen/angiopoietin-related protein) (HFARP) (Secreted protein Bk89) [Cleaved into: ANGPTL4 N-terminal chain; ANGPTL4 C-terminal chain] (Q9Z1P8)
Organism: Mus musculus (Mouse)
Function: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism. May also play a role in regulating glucose homeostasis and insulin sensitivity. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (By similarity). Depending on context, may modulate tumor-related angiogenesis (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:14583458, ECO:0000269|PubMed:15837923}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9BY76}. Note=The unprocessed form interacts with the extracellular matrix. This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4. {ECO:0000250|UniProtKB:Q9BY76}.
Interaction partners:
- Lipoprotein lipase
- Angiopoietin-like protein 8
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Angiopoietin-related protein 3
- Claudin-5
- Cadherin-5
- Peroxisome proliferator-activated receptor gamma
- Integrin beta-1
- [Pyruvate dehydrogenase
- Platelet glycoprotein 4
Sequence:
MRCAPTAGAALVLCAATAGLLSAQGRPAQPEPPRFASWDEMNLLAHGLLQLGHGLREHVERTRGQLGALERRMAACGNACQGPKGKDAPFKDSEDRVPEGQTPETLQSLQTQLKAQNSKIQQLFQKVAQQQRYLSKQNLRIQNLQSQIDLLAPTHLDNGVDKTSRGKRLPKMTQLIGLTPNATHLHRPPRDCQELFQEGERHSGLFQIQPLGSPPFLVNCEMTSDGGWTVIQRRLNGSVDFNQSWEAYKDGFGDPQGEFWLGLEKMHSITGNRGSQLAVQLQDWDGNAKLLQFPIHLGGEDTAYSLQLTEPTANELGATNVSPNGLSLPFSTWDQDHDLRGDLNCAKSLSGGWWFGTCSHSNLNGQYFHSIPRQRQERKKGIFWKTWKGRYYPLQATTLLIQPMEATAAS
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FX54)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Adhesin AWP2
- Candida glabrata strain CBS138 chromosome C complete sequence
Sequence:
MKLSKSLVAVYALIGVNAIDPTTTLAPTDFRVNMIELQAYLADIKGHMMQYLSFQGAHPDQPYPSQMIGAVMFGNTSPLSEIAPETITMMITGVPWYSERLIGAIASRLADEGIATAWPTSSSSTKTTTTMSTSNSSPTSISSSDSTASSDSTFSSSVSSSSSTSVTSSTSASSSTSVTSSTSASSSTSASSSTSASSSTSASSSTSASSSTSASSSTSASSSTSASSSSLYVSALSSVSASSSPSSHTSSVVASNSSSFPTLMSTVSSTESVTSHQEASLSSSVTISSSSVALTSKQTSSQNSAFANKTVSIPSPSTSIFTDTVGKTITKVITYCSETDNQGNVGTRTSSYTIDASNANLDATGSLVVSRETTTKSRRQDASEAITGKSHSLTSSVSVVELHSSAVISQYAGSAANLSCLSRIGALATLLALLLLS
Protein: Pentatricopeptide repeat-containing protein At1g71460, chloroplastic (Q9C9I3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Trimethylguanosine synthase
- Aspartate-glutamate racemase family
- Glyoxylase I 4
- At4g01860
- Membrane lipoprotein
- Organic cation/carnitine transporter 6
- Zinc finger protein CONSTANS-LIKE 8
- Putative ALA-interacting subunit 4
Sequence:
MEVVSSLGIRDLPASLSVTTSLNHRPHRSDKDGAPAKSPIRPSRTRRPSTSPAKKPKPFRERDAFPSSLPLHSKNPYIIHRDIQIFARQNNLEVALTILDYLEQRGIPVNATTFSALLEACVRRKSLLHGKQVHVHIRINGLESNEFLRTKLVHMYTACGSVKDAQKVFDESTSSNVYSWNALLRGTVISGKKRYQDVLSTFTEMRELGVDLNVYSLSNVFKSFAGASALRQGLKTHALAIKNGLFNSVFLKTSLVDMYFKCGKVGLARRVFDEIVERDIVVWGAMIAGLAHNKRQWEALGLFRTMISEEKIYPNSVILTTILPVLGDVKALKLGKEVHAHVLKSKNYVEQPFVHSGLIDLYCKCGDMASGRRVFYGSKQRNAISWTALMSGYAANGRFDQALRSIVWMQQEGFRPDVVTIATVLPVCAELRAIKQGKEIHCYALKNLFLPNVSLVTSLMVMYSKCGVPEYPIRLFDRLEQRNVKAWTAMIDCYVENCDLRAGIEVFRLMLLSKHRPDSVTMGRVLTVCSDLKALKLGKELHGHILKKEFESIPFVSARIIKMYGKCGDLRSANFSFDAVAVKGSLTWTAIIEAYGCNELFRDAINCFEQMVSRGFTPNTFTFTAVLSICSQAGFVDEAYRFFNLMLRMYNLQPSEEHYSLVIELLNRCGRVEEAQRLAVMSSSSSLQT
Protein: Actin patches distal protein 1 (P38281)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for normal localization of actin patches. Involved in tolerance to sodium ions and hydrogen peroxide.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Uncharacterized protein YDR102C
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MAFLNIFKQKRGDEASQLSAKGREEISQSIKICKSDDAANEHSCSGDCKTEIEEGEQAFAKLKIEHETPLLNSSKTPKIHFVVPTSQIDWQHDACLEDPKSVQYKISQWCDKNSAKFSNVGTGKTLNCAVSSLPKDIMDIDVMRGTKNNVLILPYFIWLNDLRSDDVEATLDGLVPDLLDENISREKLLETRPNVAVARERAFVFICSHTTRDKRCGITAPYLKKVFDSKLQEHGLYRDNSDYRAEGVKIAFVNHVGGHKFAANVQIYLRNPNTLIWLGRVTPTIVPSIVEHLIVPEEPTLPFPEKVRCIKKYQSW
Protein: Phospholipase A1-IIdelta (EC 3.1.1.-) (Q9SJI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine (PC) at the sn-1 position. High activity toward PC, medium activity toward monogalactosyldiacylglycerol (MGDG) and low activity toward triacylglycerol (TAG). Confers sensitivity to UV-B radiation probably by deesterifying membrane phospholipids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15181214}.
Interaction partners:
- Dem-like protein
- Nuclear protein
- Putative ribosomal protein uL16-like
- Uveal autoantigen with coiled-coil/ankyrin
- Kunitz trypsin inhibitor 2
- soluble epoxide hydrolase
- DJ-1 protein homolog E
Sequence:
MATTTTSWEELLGSKNWDTILDPLDQSLRELILRCGDFCQATYDAFVNDQNSKYCGASRYGKSSFFDKVMLENASDYEVVNFLYATARVSLPEGLLLQSQSRDSWDRESNWFGYIAVTSDERSKALGRREIYIALRGTSRNYEWVNVLGARPTSADPLLHGPEQDGSGGVVEGTTFDSDSEDEEGCKVMLGWLTIYTSNHPESKFTKLSLRSQLLAKIKELLLKYKDEKPSIVLTGHSLGATEAVLAAYDIAENGSSDDVPVTAIVFGCPQVGNKEFRDEVMSHKNLKILHVRNTIDLLTRYPGGLLGYVDIGINFVIDTKKSPFLSDSRNPGDWHNLQAMLHVVAGWNGKKGEFKLMVKRSIALVNKSCEFLKAECLVPGSWWVEKNKGLIKNEDGEWVLAPVEEEPVPEF
Protein: SWI/SNF chromatin-remodeling complex subunit snf22 (EC 3.6.4.-) (ATP-dependent helicase snf22) (SWI/SNF complex subunit snf22) (O94421)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Helicase. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, ECO:0000269|PubMed:16823372}.
Interaction partners:
- SWI/SNF chromatin-remodeling complex subunit sol1
- SWI/SNF chromatin-remodeling complex subunit snf5
- SWI/SNF and RSC complexes subunit arp42
- SWI/SNF and RSC complexes subunit arp9
- SWI/SNF and RSC complexes subunit ssr3
- SWI/SNF and RSC complexes subunit ssr2
- SWI/SNF and RSC complexes subunit ssr1
- SWI/SNF global transcription activator complex subunit snf59
- SWI/SNF chromatin-remodeling complex subunit snf30
- Transcription initiation factor TFIID subunit 14
Sequence:
MFAVQGNQKFPKGLTKDNIQSLYQQWQVMRNQGATEENNPEFAQISSILRMVQRAHYARMQQMRNQSSEFPDAENTNLRKQQDTLPTTGFNNLPEGKAGMQTLPGRPASNGPTPPNPGNGNVGLNNPSYMNSQASPNIMNAPLQRDTSVPPAPSMVHPHTNTNANSNNLKVYANQLSQQNTSNPTYHNAYDMASMMKNGSRMNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYNGYQNDAASFAHSKLPSSANPNTPFNSTATVDVGAAGSHFPYPQPSNLDAINAKTYFQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPRMSPSPSASALKTQSHVPSAKVPPTSKLNHAQLAMLKSQIVAYNCLNSPNGQVPPAVQQAIFGRVYGASNEVSPSMPFQQNVPQMSSVKKDTPTRDANMRTSKAPYIQNIPNQFQRRAYSATIPVKNESLAKPSVSPMPLQQSTGKTEVAKRAQFPTNVNYSSCVDPRTYVKTPIPFSKFSSSENLSLIPSLLPPSISWDDVFLSSEIAIACSIANRIDFLEKENRPKSVNKKILQQDKSKSMIELRCLRLLEKQRSLRETINSVIPHSDSLAAGNLRLMFRNVKRQTMQEANLVLALAEKQKTEHAMRQKEKLLTHLRSIMLHRKSIVTKVDKQNKAKTQRCKDIINFHAHLEKEEKKRIERSARQRLQALRADDEAAYLQLLDKAKDTRITHLLKQTDQYLENLTRAVRIQQSNIHSGNTSGKGSNSAELEAPISEEDKNLDYFKVAHRIHEEVEQPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVDGEKGKTGIKGLQNTVMQLKKICNHPFIFEDVERAIDPSGTNVDLLWRAAGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLITEKSIEENILSRAQYKLDLDGKVIQAGKFDNKSTPEEREAFLRSLLEHDGDDDHDLTYGELQDDELNELISRTDEELVLFKKLDKERAATDIYGKGKPLERLLTVNELPDFYKVEVDSFAVQSSSELEDQYLERKRRRRNSISYTELTLDELNTVDDPSSTLMPRKRGRPRKKTNSGSSLSTPLSQESSLARSGRKNTPSYKQKALRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVIEDLEKNNSLHAYEEEALNEEQASLVFLENSEAELPLDSGIVSAEDDKVITYEDSSSSYSE
Protein: Peptidyl-prolyl cis-trans isomerase FKBP18, chloroplastic (PPIase FKBP18) (EC 5.2.1.8) (FK506-binding protein 18) (AtFKBP18) (Immunophilin FKBP18) (Rotamase) (Q9LM71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511}.
Interaction partners:
- Thylakoid lumenal 15.0 kDa protein 2
- Peptidyl-prolyl cis-trans isomerase FKBP17-3, chloroplastic
- Heat shock protein 90-6, mitochondrial
- Heat shock 70 kDa protein 15
- Heat shock protein 90-4
- Heat shock protein 90-2
- Peptidyl-prolyl cis-trans isomerase FKBP15-3
- Peptidyl-prolyl cis-trans isomerase FKBP16-3, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP20-1
- Peptidyl-prolyl cis-trans isomerase FKBP43
Sequence:
MASISSLHRWASNQHSRLPRITSISEADQSRPINQVVAFSVPISRRDASIILLSSIPLTSFFVLTPSSSEARERRSRKVIPLEEYSTGPEGLKFYDIEEGKGPVATEGSTAQVHFDCRYRSITAISTRESKLLAGNRSIAQPYEFKVGSTPGKERKREFVDNPNGLFSAQAAPKPPPAMYFITEGMKVGGKRTVIVPPEAGYGQKGMNEIPPGATFELNIELLRVTPPPEEK
Protein: DNA packaging tegument protein UL25 (D3YP88)
Organism: Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1)
Interaction partners:
Sequence:
MDPYCPFDALDVWEHRRFIVADSRNFITPEFPRDFWMSPVFNLPRETAAEQVVVLQAQRTAAAAALENAAMQAAELPVDIERRLRPIERNVHKIAGALEALETAAAAAEEADAARGDEPAGGGDGGAPPSLAVAEMEVQIVRNDPPLRYDTNLPVDLLHMVYAGRGATGSSGVVFGTWYRTIQDRTITDFPLTTRSADFRDGRMSKTFMTALVLSLQSCGRLYVGQRHYSAFECAVLCLYLLYRNTHGAADDSDRAPVTFGDLLGRLPRYLACLAAVIGTEGGRPQYRYRDDKLPKTQFAAGGGRYEHGALASHIVIATLMHHGVLPAAPGDVPRDASTHVNPDGVAHHDDINRAAAAFLSRGHNLFLWEDQTLLRATANTITALGVIQRLLANGNVYADRLNNRLQLGMLIPGAVPSEAIARGASGSDSGAIKSGDNNLEALCANYVLPLYRADPAVELTQLFPGLAALCLDAQAGRPVGSTRRVVDMSSGARQAALVRLTALELINRTRTNPTPVGEVIHAHDALAIQYEQGLGLLAQQARIGLGSNTKRFSAFNVSSDYDMLYFLCLGFIPQYLSAV
Protein: Uncharacterized protein (Q54K15)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MGGSWMFFAAGALMAKSLPVIEGSWRYMGGSSIVFHSMKTFIFGKLVRTIEYPDGEMVSIVIRTNNLNRLKNEIIKQQPALFPGVELDFSDVKYLSRWTPPHFTEPCIKNKDLKMVPDGGVIFWSRFDSIPKRGVTLDIKDKENIKLDQAIQYVSKLGKGGVAEESLKLTEQQENALIDLLLEKDEAILALHRNFSPYPNIFKYHALRYLSHKKGLNFEQPSTKFKNDIELSQPPQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQQQQQQTQQQTKPIQTDSKTSTKPPSITDINATI
Protein: Cytohesin-interacting protein (Cytohesin binder and regulator) (CYBR) (Cytohesin-associated scaffolding protein) (CASP) (Cytohesin-binding protein HE) (Cbp HE) (Pleckstrin homology Sec7 and coiled-coil domains-binding protein) (O60759)
Organism: Homo sapiens (Human)
Function: By its binding to cytohesin-1 (CYTH1), it modifies activation of ARFs by CYTH1 and its precise function may be to sequester CYTH1 in the cytoplasm.
Subcellular location: Cytoplasm. Early endosome. Note=Recruited from the cytosol to endosomes by SNX27.
Interaction partners:
- Cytohesin-1
- Sorting nexin-27
- Cytohesin-3
- CD48 antigen
- Protein EVI2B
- Serpin B3
- Diacylglycerol kinase zeta
- Cytohesin-2
Sequence:
MSLQRLLQHSSNGNLADFCAGPAYSSYSTLTGSLTMDDNRRIQMLADTVATLPRGRKQLALTRSSSLSDFSWSQRKLVTVEKQDNETFGFEIQSYRPQNQNACSSEMFTLICKIQEDSPAHCAGLQAGDVLANINGVSTEGFTYKQVVDLIRSSGNLLTIETLNGTMILKRTELEAKLQVLKQTLKQKWVEYRSLQLQEHRLLHGDAANCPSLENMDLDELSLFGPLPGPGPALVDRNRLSSESSCKSWLSSMTMDSEDGYQTCVSEDSSRGAFSRQTSTDDECFIPKEGDDFLRRSSSRRNRSISNTSSGSMSPLWEGNLSSMFGTLPRKSRKGSVRKQLLKFIPGLHRAVEEEESRF
Protein: Uncharacterized protein slr1565 (P74596)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr1098 protein
- Slr1566 protein
Sequence:
MLQLTPSAAQEIKRLQHSRQLTRHHFRLAVRPGGCAGWLYHLDFVPEITADDLEYESGGVTVLVDSQSAGYLHNLKLDYAEDLMGGGFRFTNPNAAQVCSCSLSFAPNLEKNL
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 (Complex I-B14.5a) (CI-B14.5a) (NADH-ubiquinone oxidoreductase subunit B14.5a) (O95182)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 4
Sequence:
MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL
Protein: Esterase YpfH (EC 3.1.-.-) (P76561)
Organism: Escherichia coli (strain K12)
Function: Displays esterase activity toward palmitoyl-CoA and pNP-butyrate.
Interaction partners:
- 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
- Esterase YqiA
- Esterase YjfP
- Esterase FrsA
- Esterase YbfF
- tRNA
- S-formylglutathione hydrolase YeiG
- Uncharacterized protein YfgD
- Uncharacterized protein YhcF
Sequence:
MKHDHFVVQSPDKPAQQLLLLFHGVGDNPVAMGEIGNWFAPLFPDALVVSVGGAEPSGNPAGRQWFSVQGITEDNRQARVDAIMPTFIETVRYWQKQSGVGANATALIGFSQGAIMVLESIKAEPGLASRVIAFNGRYASLPETASTATTIHLIHGGEDPVIDLAHAVAAQEALISAGGDVTLDIVEDLGHAIDNRSMQFALDHLRYTIPKHYFDEALSGGKPGDDDVIEMM