wanglab/gogpt-training-data huggingface dataset:
Protein: DnaJ-like protein 1 (Peroxisome assembly protein 22) (P40564)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for peroxisomal protein import which maintains the function of peroxisomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9679141}.
Interaction partners:
- Auxilin-like clathrin uncoating factor SWA2
- Zuotin
- Diphthamide biosynthesis protein 4
- ER-localized J domain-containing protein 5
- Mitochondrial DnaJ homolog 2
- J domain-containing protein 1
- Mitochondrial import receptor subunit TOM70
- Pre-mRNA-splicing factor CEF1
- Mitochondrial import inner membrane translocase subunit TIM14
- J-type co-chaperone JAC1, mitochondrial
Sequence:
MVVDTEYYDLLGVSTTASSIEIKKAYRKKSIQEHPDKNPNDPTATERFQAISEAYQVLGDDDLRAKYDKYGRKEAIPQGGFEDAAEQFSVIFGGDAFASYIGELMLLKNLQKTEELNAEDEAEKEKENVETMEESPADGKTNGTTNAVDAALGNTNEKDDKNKARTTSGNLTVHDGNKKNEQVGAEAKKKKTKLEQFEEEQEVEKQKRVDQLSKTLIERLSILTESVYDDACKDSFKKKFEEEANLLKMESFGLDILHTIGDVYYEKAEIFLASQNLFGMGGIFHSMKAKGGVFMDTLRTVSAAIDAQNTMKELEKMKEASTNNEPLFDKDGNEQIKPTTEELAQQEQLLMGKVLSAAWHGSKYEITSTLRGVCKKVLEDDSVSKKTLIRRAEAMKLLGEVFKKTFRTKVEQEEAQIFEELVAEATKKKRHT
Protein: General transcription factor IIH subunit 2-like protein (General transcription factor IIH polypeptide 2-like protein) (Q6P1K8)
Organism: Homo sapiens (Human)
Function: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- General transcription factor IIH subunit 3
- General transcription factor IIH subunit 1
- General transcription factor IIH subunit 4
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH helicase subunit XPD
- CDK-activating kinase assembly factor MAT1
- Cyclin-dependent kinase 7
- General transcription factor IIH subunit 5
- Transcription initiation factor IIE subunit beta
Sequence:
MDEEPERTKRWEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGQVRLGMMRHLYVVVDGSRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKHITSLKEAVDMTCHGEPSLYNSLSMAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIKTLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVILDESHYKELLTHHLSPPPASSSSECSLIRMGFPQHTIASLSDQDAKPSFSMAHLDGNTEPGLTLGGYFCPQCRAKYCELPVECKICGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQGELKDQHVYVCAVCQNVFCVDCDVFVHDSLHCCPGCIHKIPAPSGV
Protein: Holliday junction branch migration complex subunit RuvA (P44632)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00031}.
Interaction partners:
- Holliday junction branch migration complex subunit RuvB
- Crossover junction endodeoxyribonuclease RuvC
- Protein RecA
Sequence:
MIGRLQGILLEKQPPEILLNVQGVGYELLLPMTSFYDLPEIGQETTLFTHLVVREDAHLLFGFAQKTDRTLFRELIKTNGVGPKLALAILSAMSVEQFAYAIEREELSKLTKIPGVGKKTAERLLVELKGKFKGVKQSDFFVESTHIPLSPSIESHSESSSDEAISALIALGYKPVEAEKMVKRVAKPELTSEQVIREALKVAL
Protein: ARHGAP21 protein (J3JSM9)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004284}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
MATRRTGLSEGDGDKLKACEVSKNKDGKEQSETVSLSEDETFSWPGPKTVTLKRTSQGFGFTLRHFIVYPPESAIQFSYKDEENGNRGGKQRNRLEPMDTIFVKQVKEGGPAFEAGLCTGDRIIKVNGESVIGKTYSQVIALIQNSDTTLELSVMPKDEDILQVAYSQDAYLKGNEAYSGNARNIPEPPPICYPWLPSAPSAMAQPVEISPPDSSLSKQQTSTPVLTQPGRAYRMEIQVPPSPTDVAKSNTAVCVCNESVRTVIVPSEKVVDLLSNRNNHTGPSHRTEEVRYGVSEQTSLKTVSRTTSPPLSIPTTHLIHQPAGSRSLEPSGILLKSGNYSGHSDGISSSRSQAVEAPSVSVNHYSPNSHQHIDWKNYKTYKEYIDNRRLHIGCRTIQERLDSLRAASQSTTDYNQVVPNRTTLQGRRRSTSHDRVPQSVQIRQRSVSQERLEDSVLMKYCPRSASQGALTSPSVSFSNHRTRSWDYIEGQDETLENVNSGTPIPDSNGEKKQTYKWSGFTEQDDRRGICERPRQQEIHKSFRGSNFTVAPSVVNSDNRRMSGRGVGSVSQFKKIPSIMRKTFEKKPTATGTFGVRLDDCPPAHTNRYIPLIVDICCKLVEERGLEYTGIYRVPGNNAAISSMQEELNKGMADIDIQDDKWRDLNVISSLLKSFFRKLPEPLFTNDKYADFIEANRKEDPLDRLKTLKRLIHDLPEHHYETLKFLSAHLKTVAENSEKNKMEPRNLAIVFGPTLVRTSEDNMTHMVTHMPDQYKIVETLIQHHDWFFTEEGAEEPLTTVQEESTVDSQPVPNIDHLLTNIGRTGVSPGDVSDSATSDSTKSKGSWGSGKDQYSRELLVSSIFAAASRKRKKPKEKAQPSSSEDELDNVFFKKENVEQCHNDTKEESKKESETLGRKQKIIIAKENSTRKDPSTTKDEKISLGKESTPSEEPSPPHNSKHNKSPTLSCRFAILKESPRSLLAQKSSHLEETGSDSGTLLSTSSQASLARFSMKKSTSPETKHSEFLANVSTITSDYSTTSSATYLTSLDSSRLSPEVQSVAESKGDEADDERSELISEGRPVETDSESEFPVFPTALTSERLFRGKLQEVTKSSRRNSEGSELSCTEGSLTSSLDSRRQLFSSHKLIECDTLSRKKSARFKSDSGSLGDAKNEKEAPSLTKVFDVMKKGKSTGSLLTPTRGESEKQEPTWKTKIADRLKLRPRAPADDMFGVGNHKVNAETAKRKSIRRRHTLGGHRDATEISVLNFWKVHEQSGERESELSAVNRLKPKCSAQDLSISDWLARERLRTSTSDLSRGEIGDPQTENPSTREIATTDTPLSLHCNTGSSSSTLASTNRPLLSIPPQSPDQINGESFQNVSKNASSAANAQPHKLSETPGTKAEFHPCL
Protein: Acetyl-CoA decarbonylase/synthase complex subunit beta 1 (ACDS complex subunit beta 1) (EC 2.3.1.169) (ACDS complex acyltransferase 1) (P72021)
Organism: Methanosarcina thermophila
Function: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta complex).
Interaction partners:
Sequence:
MAEFPFEISPMFEGERVRKEGMFVELGGPKSLGLELVRAADMDAIEDDKVTIVGPDLKDMEEGKTYPWAMIFNIGGELVEPDLESVVERRVHDFINYCQGIMHLNQRYDVWMRVSKDTAGKMDSFEPFGKAVMMLFKTELPFIEKMQVTFYTGKEEVEKQMELAKEIFKARDARTKDLHDEDVDVFYGCTLCQSFAPTNVCVVSPDRISLCGAINWFDGRAAAKVDPEGPQFEIAKGDLLDAVTGEYTGVNEIAKKLSSGEFDKIKLHSFFDSPHTSCGCFEVVGFYIPEVDGIGWVDREYQGMAPNGIGFSTMAGQTGGGKQIVGFLGIGVNYFYSPKFIQADGGWNRVVWLPSGLKAKIDEAIPADLKDKIATENDATDIASLKDFLEAKNHPVVATWAAAEEEEEEEEEEEEVAVAAAPMMMPAAGFQMPAMPMMSGGSGGGIKLTFKNAKITIDKLVISEKKEKK
Protein: O-succinylhomoserine sulfhydrylase (OSH sulfhydrylase) (OSHS sulfhydrylase) (EC 2.5.1.-) (P55218)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the formation of L-homocysteine from O-succinyl-L-homoserine (OSHS) and hydrogen sulfide. Cannot use the other activated form of L-homoserine, O-acetyl-L-homoserine, as a substrate.
Interaction partners:
- Cysteine synthase B
- Homoserine O-succinyltransferase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Methionine synthase
- Cysteine synthase
- Cysteine synthase
- L-cysteine desulfhydrase Cds1
- Homocysteine synthase
- Adenosylhomocysteinase
- Amidophosphoribosyltransferase
Sequence:
MTQDWDAGRLDSDLEGAAFDTLAVRAGQRRTPEGEHGEALFTTSSYVFRTAADAAARFAGEVPGNVYSRYTNPTVRTFEERIAALEGAEQAVATASGMSAILALVMSLCSSGDHVLVSRSVFGSTISLFDKYFKRFGIQVDYPPLSDLAAWEAACKPNTKLFFVESPSNPLAELVDIAALAEIAHAKGALLAVDNCFCTPALQQPLKLGADVVIHSATKYIDGQGRGMGGVVAGRGEQMKEVVGFLRTAGPTLSPFNAWLFLKGLETLRIRMQAHSASALALAEWLERQPGIERVYYAGLPSHPQHELARRQQSGFGAVVSFDVKGGRDAAWRFIDATRMVSITTNLGDTKTTIAHPATTSHGRLSPEDRARAGIGDSLIRVAVGLEDLDDLKADMARGLAAL
Protein: Phosphoprotein (Protein P) (P33454)
Organism: Bovine respiratory syncytial virus (strain A51908) (BRS)
Function: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (By similarity). Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (By similarity). Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA (By similarity). Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs (By similarity). Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription (By similarity). Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway.
Subcellular location: Virion {ECO:0000250|UniProtKB:P03421}. Host cytoplasm {ECO:0000269|PubMed:32878896}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000269|PubMed:32878896}.
Interaction partners:
Sequence:
MEKFAPEFHGEDANTKATKFLESLKGKFTSSKDSRKKDSIISVNSIDIELPKESPITSTNHNINQPSEINDTIAANQVHIRKPLVSFKEELPSSENPFTKLYKETIETFDNNEEESSYSYDEINDQTNDNITARLDRIDEKLSEIIGMLHTLVVASAGPTAARDGIRDAMVGLREEMIEKIRSEALMTNDRLEAMARLRDEESEKMTKDTSDEVKLTPTSEKLNMVLEDESSDNDLSLEDF
Protein: Nuclear factor 1 (F7F711)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPNSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSTSPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQPNSSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLTMTDTKPITTSTEAYTASGTSQANRYVGLSPRDPSFLHQQQVGT
Protein: Probable 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC 5.3.3.5) (Cholestenol Delta-isomerase) (Delta(8)-Delta(7) sterol isomerase) (D8-D7 sterol isomerase) (O48962)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Delta
- Delta
- Cycloartenol-C-24-methyltransferase
- Delta
- 24-methylenesterol C-methyltransferase 2
- Methylsterol monooxygenase 2-2
- Methylsterol monooxygenase 2-1
- Putative Delta
- 24-methylenesterol C-methyltransferase 3
- 7-dehydrocholesterol reductase
Sequence:
MEELAHPYVPRDLNLPGYVPISMSMSSIVSIYLGSSLLVVSLVWLLFGRKKAKLDKLLMCWWTFTGLTHVILEGYFVFSPEFFKDNTSAYLAEVWKEYSKGDSRYVGRDSAVVSVEGITAVIVGPASLLAIYAIAKEKSYSYVLQLAISVCQLYGCLVYFITAILEGDNFATNSFYYYSYYIGANCWWVLIPSLISFRCWKKICAAAAIANNNVETKTKKKTR
Protein: Schlafen family member 11 (EC 3.1.-.-) (Q7Z7L1)
Organism: Homo sapiens (Human)
Function: Inhibitor of DNA replication that promotes cell death in response to DNA damage. Acts as a guardian of the genome by killing cells with defective replication. Persistently blocks stressed replication forks by opening chromatin across replication initiation sites at stressed replication forks, possibly leading to unwind DNA ahead of the MCM helicase and block fork progression, ultimately leading to cell death. Acts independently of ATR. Also acts as an interferon (IFN)-induced antiviral protein which acts as an inhibitor of retrovirus protein synthesis. Specifically abrogates the production of retroviruses such as human immunodeficiency virus 1 (HIV-1) by acting as a specific inhibitor of the synthesis of retroviruses encoded proteins in a codon-usage-dependent manner. Binds to tRNAs and exploits the unique viral codon bias towards A/T nucleotides. The exact inhibition mechanism is unclear: may either sequester tRNAs, prevent their maturation via post-transcriptional processing or may accelerate their deacylation. Does not inhibit reverse transcription, integration or production and nuclear export of viral RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:22927417, ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}. Chromosome {ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}. Note=Recruited to stressed replication forks carrying extended RPA filaments (PubMed:29395061). Recruited to DNA damage sites via interaction with RPA1 (PubMed:26658330, PubMed:29395061). {ECO:0000269|PubMed:26658330, ECO:0000269|PubMed:29395061}.
Interaction partners:
Sequence:
MEANQCPLVVEPSYPDLVINVGEVTLGEENRKKLQKIQRDQEKERVMRAACALLNSGGGVIRMAKKVEHPVEMGLDLEQSLRELIQSSDLQAFFETKQQGRCFYIFVKSWSSGPFPEDRSVKPRLCSLSSSLYRRSETSVRSMDSREAFCFLKTKRKPKILEEGPFHKIHKGVYQELPNSDPADPNSDPADLIFQKDYLEYGEILPFPESQLVEFKQFSTKHFQEYVKRTIPEYVPAFANTGGGYLFIGVDDKSREVLGCAKENVDPDSLRRKIEQAIYKLPCVHFCQPQRPITFTLKIVNVLKRGELYGYACMIRVNPFCCAVFSEAPNSWIVEDKYVCSLTTEKWVGMMTDTDPDLLQLSEDFECQLSLSSGPPLSRPVYSKKGLEHKKELQQLLFSVPPGYLRYTPESLWRDLISEHRGLEELINKQMQPFFRGILIFSRSWAVDLNLQEKPGVICDALLIAQNSTPILYTILREQDAEGQDYCTRTAFTLKQKLVNMGGYTGKVCVRAKVLCLSPESSAEALEAAVSPMDYPASYSLAGTQHMEALLQSLVIVLLGFRSLLSDQLGCEVLNLLTAQQYEIFSRSLRKNRELFVHGLPGSGKTIMAMKIMEKIRNVFHCEAHRILYVCENQPLRNFISDRNICRAETRKTFLRENFEHIQHIVIDEAQNFRTEDGDWYGKAKSITRRAKGGPGILWIFLDYFQTSHLDCSGLPPLSDQYPREELTRIVRNADPIAKYLQKEMQVIRSNPSFNIPTGCLEVFPEAEWSQGVQGTLRIKKYLTVEQIMTCVADTCRRFFDRGYSPKDVAVLVSTAKEVEHYKYELLKAMRKKRVVQLSDACDMLGDHIVLDSVRRFSGLERSIVFGIHPRTADPAILPNVLICLASRAKQHLYIFPWGGH
Protein: Kelch repeat and BTB domain-containing protein 2 (G3X9X1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSTQEERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAAALQMIIAYAYTGNLAVNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRVKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSRSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNEWKMAANIPAKRYSDPCVRAVVISNSLCVFMRETHLNERAKYVTYQYDLELDRWSLRQHISERVLWDLGRDFRCTVGKLYPSCLEESPWKPPTYLFSPDGTEEFELDGEMVALPPV
Protein: Protein HEG homolog 1 (Q9ULI3)
Organism: Homo sapiens (Human)
Function: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Krev interaction trapped protein 1
- Ras-related protein Rap-1b
- Cerebral cavernous malformations 2 protein
- Programmed cell death protein 10
Sequence:
MASPRASRWPPPLLLLLLPLLLLPPAAPGTRDPPPSPARRALSLAPLAGAGLELQLERRPEREPPPTPPRERRGPATPGPSYRAPEPGAATQRGPSGRAPRGGSADAAWKHWPESNTEAHVENITFYQNQEDFSTVSSKEGVMVQTSGKSHAASDAPENLTLLAETADARGRSGSSSRTNFTILPVGYSLEIATALTSQSGNLASESLHLPSSSSEFDERIAAFQTKSGTASEMGTERAMGLSEEWTVHSQEATTSAWSPSFLPALEMGELTTPSRKRNSSGPDLSWLHFYRTAASSPLLDLSSSSESTEKLNNSTGLQSSSVSQTKTMHVATVFTDGGPRTLRSLTVSLGPVSKTEGFPKDSRIATTSSSVLLSPSAVESRRNSRVTGNPGDEEFIEPSTENEFGLTSLRWQNDSPTFGEHQLASSSEVQNGSPMSQTETVSRSVAPMRGGEITAHWLLTNSTTSADVTGSSASYPEGVNASVLTQFSDSTVQSGGSHTALGDRSYSESSSTSSSESLNSSAPRGERSIAGISYGQVRGTAIEQRTSSDHTDHTYLSSTFTKGERALLSITDNSSSSDIVESSTSYIKISNSSHSEYSSFFHAQTERSNISSYDGEYAQPSTESPVLHTSNLPSYTPTINMPNTSVVLDTDAEFVSDSSSSSSSSSSSSSSGPPLPLPSVSQSHHLFSSILPSTRASVHLLKSTSDASTPWSSSPSPLPVSLTTSTSAPLSVSQTTLPQSSSTPVLPRARETPVTSFQTSTMTSFMTMLHSSQTADLKSQSTPHQEKVITESKSPSLVSLPTESTKAVTTNSPLPPSLTESSTEQTLPATSTNLAQMSPTFTTTILKTSQPLMTTPGTLSSTASLVTGPIAVQTTAGKQLSLTHPEILVPQISTEGGISTERNRVIVDATTGLIPLTSVPTSAKEMTTKLGVTAEYSPASRSLGTSPSPQTTVVSTAEDLAPKSATFAVQSSTQSPTTVSSSASVNSCAVNPCLHNGECVADNTSRGYHCRCPPSWQGDDCSVDVNECLSNPCPSTAMCNNTQGSFICKCPVGYQLEKGICNLVRTFVTEFKLKRTFLNTTVEKHSDLQEVENEITKTLNMCFSALPSYIRSTVHASRESNAVVISLQTTFSLASNVTLFDLADRMQKCVNSCKSSAEVCQLLGSQRRIFRAGSLCKRKSPECDKDTSICTDLDGVALCQCKSGYFQFNKMDHSCRACEDGYRLENETCMSCPFGLGGLNCGNPYQLITVVIAAAGGGLLLILGIALIVTCCRKNKNDISKLIFKSGDFQMSPYAEYPKNPRSQEWGREAIEMHENGSTKNLLQMTDVYYSPTSVRNPELERNGLYPAYTGLPGSRHSCIFPGQYNPSFISDESRRRDYF
Protein: Universal stress protein UP12 (Universal stress protein G) (P39177)
Organism: Escherichia coli (strain K12)
Function: Has intrinsic autoadenylation and autophosphorylation activities, probably on Ser or Thr residues.
Interaction partners:
- Universal stress protein E
- Universal stress protein D
- Universal stress protein C
- Universal stress protein A
- Universal stress protein B
Sequence:
MYKTIIMPVDVFEMELSDKAVRHAEFLAQDDGVIHLLHVLPGSASLSLHRFAADVRRFEEHLQHEAQERLQTMVSHFTIDPSRIKQHVRFGSVRDEVNELAEELGADVVVIGSRNPSISTHLLGSNASSVIRHANLPVLVVR
Protein: Low-density lipoprotein receptor class A domain-containing protein 3 (A2AR95)
Organism: Mus musculus (Mouse)
Function: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production. May regulate ITCH and NEDD4 E3 ligase activity and degradation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21795536}; Single-pass type I membrane protein {ECO:0000269|PubMed:21795536}.
Interaction partners:
Sequence:
MWLLGPLCLLLSSTAESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECPKAKSKCGPTFFPCASGIHCIIGRFRCNGFEDCPDGSDEENCTANPLLCSTARYHCRNGLCIDKSFICDGQNNCQDNSDEESCESSLEPGSGQVFVTSENQLVYYPSITYAIIGSSVIFVLVVALLALVLHHQRKRNNLMTLPVHRLQHPVLLSRLVVLDHPHHCNVTYNVNNGVQYVATQAEQNASEVGSPPSYSEALLDQRPAWYDLPPPPYSSDTESLNQADLPPYRSRSGSAYSASSQAASSLLSVEASSHNPEQPGSPEGSAEPRDSVPSQGTEEV
Protein: Major prion protein (PrP) (CD antigen CD230) (P49927)
Organism: Sus scrofa (Pig)
Function: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000250|UniProtKB:P04156}.
Interaction partners:
- Neural cell adhesion molecule 1
- Tyrosine-protein kinase Fyn
- Stress induced phosphoprotein 1.
- Caveolin-1
- Neural cell adhesion molecule 2
- Caveolin-3
- Amyloid-beta precursor protein
- Endoplasmic reticulum chaperone BiP
- Glycogen synthase kinase 3 beta
- Casein kinase II subunit alpha
Sequence:
MVKSHIGGWILVLFVAAWSDIGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGGSHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMYRYPNQVYYRPVDQYSNQNSFVHDCVNITVKQHTVTTTTKGENFTETDVKMIERVVEQMCITQYQKEYEAYAQRGASVILFSSPPVILLISFLLFLIVG
Protein: Ras-related protein RABA4b (AtRABA4b) (Ras-related protein GB3) (AtGB3) (Ras-related protein Rab11G) (AtRab11G) (Q9SMQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulator of membrane trafficking. May be required for secretion of cell wall components in cells.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:21134079}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:21134079}; Lipid-anchor {ECO:0000305|PubMed:21134079}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta 1
- Phosphatidylinositol 4-kinase beta 2
- Phosphoinositide phosphatase SAC7
- ADP-ribosylation factor GTPase-activating protein AGD1
- V-type proton ATPase subunit a1
- Kinesin-like protein KIN-14E
- Tlg2p-like protein a
- Syntaxin-61
- Vesicle transport v-SNARE 12
- Probable protein S-acyltransferase 22
Sequence:
MAGGGGYGGASGKVDYVFKVVLIGDSAVGKSQLLARFARDEFSMDSKATIGVEFQTRTLSIEQKSIKAQIWDTAGQERYRAVTSAYYRGAVGAMLVYDMTKRETFEHIPRWLEELRAHADKNIVIILIGNKSDLEDQRAVPTEDAKEFAEKEGLFFLETSALNATNVENSFNTLMTQIYNTVNKKNLASEGDSNNPGSLAGKKILIPGSGQEIPAKTSTCCTSS
Protein: Matrix protein (Q91F56)
Organism: human metapneumovirus
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004501}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004501}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004501}. Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host nucleus {ECO:0000256|ARBA:ARBA00004147}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MESYLVDTYQGIPYTAAVQVDLIEKDLLPASLTIWFPLFQANTPPAVLLDQLKTLTITTLYAASQNGPILKVNASAQGAAMSVLPKKFEVNATVALDEYSKLEFDKLTVCEVKTVYLTTMKPYGMVSKFVSSAKSVGKKTHDLIALCDFMDLEKNTPVTIPAFIKSVSIKESESATVEAAISSEADQALTQAKIAPYAGLIMIMTMNNPKGIFKKLGAGTQVIVELGAYVQAESISKICKTWSHQGTRYVLKSR
Protein: Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180) (Unsaturated glucuronyl hydrolase) (SagUGL) (Q8E372)
Organism: Streptococcus agalactiae serotype III (strain NEM316)
Function: Catalyzes the hydrolysis of unsaturated hyaluronate and chondroitin disaccharides. Also degrades unsaturated heparin disaccharides. Releases 4-deoxy-4,5-didehydro D-glucuronic acid or 4-deoxy-4,5-didehydro L-iduronic acid from chondroitin disaccharides, hyaluronan disaccharides and heparin disaccharides and cleaves both glycosidic (1->3) and (1->4) bonds. Prefers sulfated glycosaminoglycans compared to unsulfated glycosaminoglycans. Probably required for mammalian cells invasion through the degradation of extracellular sulfated glycosaminoglycans such as chondroitin and hyaluronan.
Interaction partners:
Sequence:
MMKIKPVKVESIENPKRFLNSRLLTKIEVEEAIEKALKQLYINIDYFGEEYPTPATFNNIYKVMDNTEWTNGFWTGCLWLAYEYNQDKKLKNIAHKNVLSFLNRINNRIALDHHDLGFLYTPSCTAEYRINGDVKALEATIKAADKLMERYQEKGGFIQAWGELGYKEHYRLIIDCLLNIQLLFFAYEQTGDEKYRQVAVNHFYASANNVVRDDSSAFHTFYFDPETGEPLKGVTRQGYSDESSWARGQAWGIYGIPLSYRKMKDYQQIILFKGMTNYFLNRLPEDKVSYWDLIFTDGSGQPRDTSATATAVCGIHEMLKYLPEVDPDKETYKYAMHTMLRSLIEQYSNNELIAGRPLLLHGVYSWHSGKGVDEGNIWGDYYYLEALIRFYKDWELYW
Protein: Cysteine and glycine-rich protein 2 (Cysteine-rich protein 2) (CRP2) (Q05158)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Function: Interacts with zyxin. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression. Totally down-regulated in transformed cells.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MPNWGGGNKCGACGRTVYHAEEVQCDGRSFHRCCFLCMVCRKNLDSTTVAIHDAEVYCKSCYGKKYGPKGYGYGQGAGTLNMDRGERLGIKPESSPSPHRPTTNPNTSKFAQKFGGAEKCSRCGDSVYAAEKVIGAGKPWHKNCFRCAKCGKSLESTTLTEKEGEIYCKGCYAKNFGPKGFGYGQGAGALVHAQ