wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-inducible double-stranded RNA-dependent protein kinase activator A (PKR-associated protein X) (PKR-associating protein X) (Protein activator of the interferon-induced protein kinase) (Protein kinase, interferon-inducible double-stranded RNA-dependent activator) (O75569)
Organism: Homo sapiens (Human)
Function: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity).
Subcellular location: Cytoplasm, perinuclear region. Cytoplasm.
Interaction partners:
- Endoribonuclease Dicer
- RISC-loading complex subunit TARBP2
- Interferon-induced, double-stranded RNA-activated protein kinase
- Protein argonaute-2
- Ribonuclease 3
- Protein argonaute-1
- Microprocessor complex subunit DGCR8
- Protein argonaute-4
- Double-stranded RNA-binding protein Staufen homolog 1
- Protein argonaute-3
Sequence:
MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTDYIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
Protein: Actin alpha cardiac muscle 1a (Actin, alpha cardiac muscle) (Actin, alpha, cardiac muscle 1a) (Q6IQR3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Myosin heavy chain 7
- Troponin T type 2a
- Tropomyosin alpha-1 chain
- Myosin, heavy chain 6, cardiac muscle, alpha
- Tropomyosin 3
- Dynactin subunit 2
- Actin-related protein 10
- Cardiac myosin light chain-1.
- Tropomyosin 2
- Dynactin 4.
Sequence:
MCDDDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETAYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Replication protein 1a [Includes: ATP-dependent helicase (EC 3.6.4.-); Methyltransferase (EC 2.1.1.-)] (P03588)
Organism: Brome mosaic virus (BMV)
Function: Involved in the virus replication. Contains a helicase domain and a methyltransferase domain. The methyltransferase domain is probably involved in viral RNA capping. Involved in the formation of ER membrane spherular invaginations in which RNA replication complexes form.
Subcellular location: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:19325881}; Peripheral membrane protein {ECO:0000269|PubMed:19325881}.
Interaction partners:
Sequence:
MSSSIDLLKLIAEKGADSQSAQDIVDNQVAQQLSAQIEYAKRSKKINVRNKLSIEEADAFRDRYGGAFDLNLTQQYHAPHSLAGALRVAEHYDCLDSFPPEDPVIDFGGSWWHHFSRRDKRVHSCCPVLGVRDAARHEERMCRMRKILQESDDFDEVPNFCLNRAQDCDVQADWAICIHGGYDMGFQGLCDAMHSHGVRVLRGTVMFDGAMLFDREGFLPLLKCHWQRDGSGADEVIKFDFENESTLSYIHGWQDLGSFFTESVHCIDGTTYLLEREMLKCNIMTYKIIATNLRCPRETLRHCVWFEDISKYVGVSIPEDWSLNRWKCVRVAKTTVREVEEIAFRCFKESKEWTENMKAVASILSAKSSTVIINGQAIMAGERLDIEDYHLVAFALTLNLYQKYEKLTALRDGMEWKGWCHHFKTRFWWGGDSSRAKVGWLRTLASRFPLLRLDSYADSFKFLTRLSNVEEFEQDSVPISRLRTFWTEEDLFDRLEHEVQTAKTKRSKKKAKVPPAAEIPQEEFHDAPESSSPESVSDDVKPVTDVVPDAEVSVEVPTDPRGISRHGAMKEFVRYCKRLHNNSESNLRHLWDISGGRGSEIANKSIFETYHRIDDMVNVHLANGNWLYPKKYDYTVGYNEHGLGPKHADETYIVDKTCACSNLRDIAEASAKVSVPTCDISMVDGVAGCGKTTAIKDAFRMGEDLIVTANRKSAEDVRMALFPDTYNSKVALDVVRTADSAIMHGVPSCHRLLVDEAGLLHYGQLLVVAALSKCSQVLAFGDTEQISFKSRDAGFKLLHGNLQYDRRDVVHKTYRCPQDVIAAVNLLKRKCGNRDTKYQSWTSESKVSRSLTKRRITSGLQVTIDPNRTYLTMTQADKAALQTRAKDFPVSKDWIDGHIKTVHEAQGISVDNVTLVRLKSTKCDLFKHEEYCLVALTRHKKSFEYCFNGELAGDLIFNCVK
Protein: Ubiquitin-conjugating enzyme E2 19 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 19) (Ubiquitin carrier protein 19) (Q9LJZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Part of the anaphase-promoting complex (APC). May have a key function during cell cycle and be involved in cyclin B1 degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12427990, ECO:0000269|PubMed:34405771}. Nucleus {ECO:0000269|PubMed:12427990, ECO:0000269|PubMed:34405771}.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 11 RING-H2 finger protein
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 7
Sequence:
MATVNGYTGNTPAATTPAATGSKQSAPPTKTVDSHSVLKRLQSELMGLMMGADPGISAFPEEDNIFCWKGTITGSKDTVFEGTEYRLSLTFSNDYPFKSPKVKFETCCFHPNVDLYGNICLDILQDKWSSAYDVRTILLSIQSLLGEPNISSPLNNQAAQLWSNQEEYRKMVEKLYKPLNA
Protein: Translocation protein SEC63 homolog (DnaJ homolog subfamily C member 23) (Q9UGP8)
Organism: Homo sapiens (Human)
Function: Mediates cotranslational and post-translational transport of certain precursor polypeptides across endoplasmic reticulum (ER). Proposed to play an auxiliary role in recognition of precursors with short and apolar signal peptides. May cooperate with SEC62 and HSPA5/BiP to facilitate targeting of small presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen. Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plasma membrane of the primary cilia (By similarity).
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Protein transport protein Sec61 subunit alpha isoform 1
- Translocation protein SEC62
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit gamma
- Glucosidase 2 subunit beta
- Protein transport protein Sec61 subunit alpha isoform 2
- Endoplasmic reticulum chaperone BiP
- Hypoxia up-regulated protein 1
- Serine/threonine-protein kinase OSR1
- STE20/SPS1-related proline-alanine-rich protein kinase
Sequence:
MAGQQFQYDDSGNTFFYFLTSFVGLIVIPATYYLWPRDQNAEQIRLKNIRKVYGRCMWYRLRLLKPQPNIIPTVKKIVLLAGWALFLFLAYKVSKTDREYQEYNPYEVLNLDPGATVAEIKKQYRLLSLKYHPDKGGDEVMFMRIAKAYAALTDEESRKNWEEFGNPDGPQATSFGIALPAWIVDQKNSILVLLVYGLAFMVILPVVVGSWWYRSIRYSGDQILIRTTQIYTYFVYKTRNMDMKRLIMVLAGASEFDPQYNKDATSRPTDNILIPQLIREIGSINLKKNEPPLTCPYSLKARVLLLSHLARMKIPETLEEDQQFMLKKCPALLQEMVNVICQLIVMARNREEREFRAPTLASLENCMKLSQMAVQGLQQFKSPLLQLPHIEEDNLRRVSNHKKYKIKTIQDLVSLKESDRHTLLHFLEDEKYEEVMAVLGSFPYVTMDIKSQVLDDEDSNNITVGSLVTVLVKLTRQTMAEVFEKEQSICAAEEQPAEDGQGETNKNRTKGGWQQKSKGPKKTAKSKKKKPLKKKPTPVLLPQSKQQKQKQANGVVGNEAAVKEDEEEVSDKGSDSEEEETNRDSQSEKDDGSDRDSDREQDEKQNKDDEAEWQELQQSIQRKERALLETKSKITHPVYSLYFPEEKQEWWWLYIADRKEQTLISMPYHVCTLKDTEEVELKFPAPGKPGNYQYTVFLRSDSYMGLDQIKPLKLEVHEAKPVPENHPQWDTAIEGDEDQEDSEGFEDSFEEEEEEEEDDD
Protein: C2H2 and C2HC zinc fingers superfamily protein (F4K1A8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MPSGKYYCDYCEKEFQDTQVARKRHLQSKPHLRAKALWYSSSSSDLVNPQVSNFATKGLCNRFITSNFCPFGDSCRYFHPNNNTGSTGFTNNTQLRVDMLNQQHIQGSTLNRDFVSGRPGTGWFDLPPSLKPPPEQGYPQLPFIDWG
Protein: p95-APP2 (Q9DE64)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSKRLRSSEVCADCSAQDPCWASINRGILICDECCSVHRSLGRHISQVRHLKHTPWPPTLLQMVETLYNNGANSIWEHSLLDPASVMSGRRKANPQDKVHPNKAEFIRAKYQMLAFVHRLPCREDDSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGNTPLHVAAKAGQTLQAELLAVYGADPGTQDSNGKTPVDYARQGGHHELAERLIEIQYELTDRLAFYLCGRKPDHKNGQHFVIPQMADSSLDLSELAKAAKKKLQSLSNHLFEELAMDVYDEVDRRETDAVWLATQNHSTLVTETTVVPFLPVNPEYSSTRNQGRQKLARFNAHEFATLVIDILSDAKRRQQGNPLSGSKENVELILKSISNQHSSESQDNDQPDYDSVASDEDTDLETNAAKSTRQKSLDSDLSDGPVTAQEYMQVKNALVASEVKIQQLMKVNINLSDELRIMQKKLQTLQSENTNLRRQATTNIYQVQTGSEYTDPTNNSSLKRRPSARGSRPMSMYETGSGQKPYLPMGEVTYPEESITRLQPFPPHIGRSAFVTSSSSLPSFPSTLSWSRDESTRRASKLEKQSSVPESDYDNTTASLELEETGSGRKGRQRSVIWQGEGSIPEDTDTAPSSSLPSTEDVIRKTEQITKNIQELLRAAQENKHDSYIPCSERIHVAVTEMAALFPKKPKSELVRTSLRLLTSSAYRLQSECKKTLPVETCPTTDIQLVTQQVIQCAYDIAKAAKQLVTITTKENNN
Protein: Protein E6 (P36799)
Organism: Human papillomavirus 3
Function: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase and modulates its activity. Sequesters tumor suppressor TP53 in the host cytoplasm and modulates its activity by interacting with host EP300 that results in the reduction of TP53 acetylation and activation. In turn, apoptosis induced by DNA damage is inhibited. E6 protects also host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MAVAMSMDANCPKNIFLLCRNTGIGFDDLRLHCIFCTKQLTTTELQAFALRELNVVWRRGAPYGACARCLLVEGIARRLKYWEYSYYVSGVEEETKQSIDTQQIRCYMCHKPLVKEEKDRHRNEKRRLHKISGHWRGSCQYCWSRCTVRIPR
Protein: Exocyst complex component 7 (Exocyst complex component Exo70) (Q9UPT5)
Organism: Homo sapiens (Human)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion (By similarity). It is required for neuron survival and plays an essential role in cortical development (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35250}. Cell membrane {ECO:0000250|UniProtKB:O35250}; Peripheral membrane protein {ECO:0000305}. Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Note=Translocates, as a preformed complex with EXOC3/SEC6 and EXOC4/SEC8, to the plasma membrane in response to insulin through the activation of ARHQ (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (PubMed:16213214). {ECO:0000250|UniProtKB:O35250, ECO:0000269|PubMed:16213214}.
Interaction partners:
- Rho-related GTP-binding protein RhoQ
- Exocyst complex component 4
- Exocyst complex component 1
- Exocyst complex component 2
- Exocyst complex component 6
- Exocyst complex component 8
- Exocyst complex component 5
- Exocyst complex component 3
- Exocyst complex component 6B
- Cell division control protein 42 homolog
Sequence:
MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTKNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKEALESEFRSLMTRHSKVVSPVLILDLISGDDDLEAQEDVTLEHLPESVLQDVIRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFHKSSSSSGVPYSPAIPNKRKDTPTKKPVKRPGTIRKAQNLLKQYSQHGLDGKKGGSNLIPLEGLLPCTPRGGLPGPWINAACVCAADISPGHEHDFRVKHLSEALNDKHGPLAGRDDMLDVETDAYIHCVSAFVKLAQSEYQLLADIIPEHHQKKTFDSLIQDALDGLMLEGENIVSAARKAIVRHDFSTVLTVFPILRHLKQTKPEFDQVLQGTAASTKNKLPGLITSMETIGAKALEDFADNIKNDPDKEYNMPKDGTVHELTSNAILFLQQLLDFQETAGAMLASQETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYILKSLEKSELIQLVAVTQKTAERSYREHIEQQIQTYQRSWLKVTDYIAEKNLPVFQPGVKLRDKERQIIKERFKGFNDGLEELCKIQKAWAIPDTEQRDRIRQAQKTIVKETYGAFLQKFGSVPFTKNPEKYIKYGVEQVGDMIDRLFDTSA
Protein: Anon1A3 (Q9U4R4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GVENLPSVAEAKQNHVDEVKPISEEPGNSSEEVPKAEEPLKSSGETSENGAATETAAAPKEPASVIDVDEDETLVENIPSANKEKALDDEKEPEQKSEEHAAAVLESKEQNEPAKEPTPEPMEVDGSSKGSSDTAQVDTPAIENVSAAPETEAAAKTTESSNDVVEVATEGKETVLEVPAAEPKEAESTVESAEELTETSTVVVTEPKEAASSEEEPSKVVDSAEPKEAESNTDESATPVPIDVSTAPASNDVSKPLEIDTTLVKTADSPAKEPQEICEVKKAEINVNGEPKIVNSSAEVGENAAPKVCN
Protein: Stage III sporulation protein AH (P49785)
Organism: Bacillus subtilis (strain 168)
Function: Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localizes to the engulfing septal membranes during spore formation. {ECO:0000269|PubMed:15574594, ECO:0000269|PubMed:15752199, ECO:0000269|PubMed:18812514}.
Interaction partners:
- Stage II sporulation protein Q
- Stage III sporulation protein AG
- Stage III sporulation protein AE
- Stage III sporulation protein AF
- Stage III sporulation protein AA
- Stage II sporulation protein P
- Stage II sporulation protein M
- Stage II sporulation protein D
- Stage III sporulation protein AC
- Stage III sporulation protein AB
Sequence:
MLKKQTVWLLTMLSLVVVLSVYYIMSPESKNAVQMQSEKSASDSGEVATEKAPAKQDTKEKSGTETEKGKEDGTKGTKDSSADKETSAEASEKGTVVTETADDDLFTTYRLDLEDARSKEREELNAIVSSDDATAKEKSEAYDKMTALSEVEGTEKQLETLIKTQGYEDALVNAEGDKINITVKSDKHSKSKATAIIDLVAKEIKTMKDVAVTFEPSK
Protein: C2H2-type domain-containing protein (Q57WB0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Gar1/Naf1 RNA binding region
- RRM domain-containing protein
- Nucleoside diphosphate kinase-like domain-containing protein
Sequence:
MRNIWVSVPNGHGHGQGAAVPATDNSSISADSSPPCTKRMRRYIAPTSVDLQRCRKEEPIPMPMPAPSPSTMLSAKQWPQHMLQGRVHVAATCGQPTVTVGSKLIPPFSTATVRVGGPTFRAGVTVSAPLQPVPFQGHQSQEPRGKHLCVRMYLPQSDPPLQSWCDVHPNPLIGLPGRVTNAPPMEREPPKYFCDPCQKGYNTQEQYDRHMKTHIWCSFPGCKFTCLRSREWKMEAHIETLHNRPDAPNLSDVGAYLAQRRGRFPTQDSVKAKMEELFYKASRGVVLPDDRRRWLRQHGILVGKRPRTGESYIVTSASRNAKKVVCSESEDVKANEGRADTSDAPETQRVCEEGCSGASDSSQCDGNRLRNKEDPSVSVGRGGECESADCTGSAIEHRQHKQKDHSRPRRIIPCGPNGSLSNAQKVQLIRERYREAKTVPRFYVCSCCGEKGQHWVTDCPKRSDQVFERRIVWGEERRDPPKPKLRDDNIVPAMTSCSEGNAVVDETAAGPSSGDVGVTSDVAEPWVEDVGPPPELPARRACNEEDSRVPNNAAEGRGGATHKCGVKEERRQRAQRRDHRRVPPPPPTLFERLTEDRNSVEHGLLLQAIRFFVKSNFFEPR
Protein: Myocyte enhancer factor 2cb (B5A8L9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESKDKYREINDDIDLHMISRQRICAVPSSTYDMTIPVNNQIYPGNHNLLPLAHHGLQRNSMSPGVTHRPPSAGGLMGTDLSTGAGTSAGKDGIPTYYRNGYGNHRNSPGLLVSSGGMNKSMQAKSPPPVNLGMNSRKPDLRVLIPPGAKNNMPSINQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTSYGTEYSLSSADLSSISGFNSANTLHLGSMSGWQQHQIQNMQHSALSQLGNCSSSHLCQGSNLSLPSTQSLHIKSEPVSPPRDRSSSTTPGGYGQLPSHQQHQGPTSQGRQDSGRSPADSLSSCGSSHEGSDRDEHRPDFHSPLGLGRPGLDDQDSPSIKRVRLSEGWAT
Protein: ATP-sulfurylase 3, chloroplastic (EC 2.7.7.4) (O23324)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast stroma {ECO:0000250}.
Interaction partners:
- Adenylyl-sulfate kinase 1, chloroplastic
- Adenylyl-sulfate kinase 2, chloroplastic
- Adenylyl-sulfate kinase 3
- Adenylyl-sulfate kinase 4, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- Bifunctional adenosine 5'-phosphosulfate phosphorylase/adenylylsulfatase HINT4
- FAD synthase
- ATP sulfurylase 1, chloroplastic
Sequence:
MASMSTVFPKPTSFISQPLTKSHKSDSVTTSISFPSNSKTRSLRTISVRAGLIEPDGGKLVDLVVPEPRRREKKHEAADLPRVRLTAIDLQWMHVLSEGWASPLRGFMRESEFLQTLHFNLLNLDDGSVVNMSVPIVLAIDDQQKALIGESKRVSLVDSDDNPIAILNDIEIYKHPKEERIARTWGTTAPGLPYVEEAITNAGDWLIGGDLEVLEPVKYNDGLDRFRLSPFELRKELEKRGADAVFAFQLRNPVHNGHALLMTDTRRRLLEMGYKNPILLLHPLGGFTKADDVPLSWRMKQHEKVLEDGVLDPETTVVSIFPSPMLYAGPTEVQWHAKARINAGANFYIVGRDPAGMGHPVEKRDLYDADHGKKVLSMAPGLERLNILPFRVAAYDKTQGKMAFFDPSRAQDFLFISGTKMRALAKNRENPPDGFMCPGGWKVLVDYYDSLTLTGNTKLPEKIPV
Protein: DnaJ homolog subfamily C member 5 (Cysteine string protein) (CSP) (Cysteine-string protein isoform alpha) (P60904)
Organism: Mus musculus (Mouse)
Function: Acts as a co-chaperone for the SNARE protein SNAP-25. Involved in the calcium-mediated control of a late stage of exocytosis. Acts as a general chaperone in regulated exocytosis (By similarity). May have an important role in presynaptic function (By similarity). May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29455}. Membrane {ECO:0000269|PubMed:17034881}; Lipid-anchor {ECO:0000269|PubMed:17034881}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:Q29455}. Melanosome {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane {ECO:0000250|UniProtKB:Q9H3Z4}. Note=The association with membranes is regulated by palmitoylation (By similarity). Colocalizes with insulin granules, when overexpressed in an islet cell line (PubMed:17034881). {ECO:0000250|UniProtKB:Q29455, ECO:0000269|PubMed:17034881}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Vesicle-associated membrane protein 2
- Synaptotagmin-1
- Ras-related protein Rab-3A
- Vesicular inhibitory amino acid transporter
- Synaptosomal-associated protein 25
- Synapsin-1
- Synaptophysin
- Heat shock 70 kDa protein 1B
- Otoferlin
Sequence:
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVVCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
Protein: Beta-3 adrenergic receptor (Beta-3 adrenoreceptor) (Beta-3 adrenoceptor) (P26255)
Organism: Rattus norvegicus (Rat)
Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Beta-2 adrenergic receptor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Mitochondrial brown fat uncoupling protein 1
- Guanine nucleotide-binding protein G
- Beta-1 adrenergic receptor
- Neuroendocrine secretory protein 55
- Hormone-sensitive lipase
- Guanine nucleotide-binding protein G
- 30 kDa adipocyte complement-related protein
Sequence:
MAPWPHKNGSLAFWSDAPTLDPSAANTSGLPGVPWAAALAGALLALATVGGNLLVITAIARTPRLQTITNVFVTSLATADLVVGLLVMPPGATLALTGHWPLGATGCELWTSVDVLCVTASIETLCALAVDRYLAVTNPLRYGTLVTKRRARAAVVLVWIVSATVSFAPIMSQWWRVGADAEAQECHSNPRCCSFASNMPYALLSSSVSFYLPLLVMLFVYARVFVVAKRQRRLLRRELGRFPPEESPRSPSRSPSPATVGTPTASDGVPSCGRRPARLLPLGEHRALRTLGLIMGIFSLCWLPFFLANVLRALVGPSLVPSGVFIALNWLGYANSAFNPLIYCRSPDFRDAFRRLLCSYGGRGPEEPRVVTFPASPVASRQNSPLNRFDGYEGERPFPT
Protein: Threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) (P0A8M3)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate-limiting step is amino acid activation in the presence of tRNA. The 2'-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2'-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isosteric amino acid valine. Also activates L-serine, but does not detectably transfer it to tRNA(Thr). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain, in a post-transfer reaction probably via water-mediated hydrolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
Interaction partners:
- Translation initiation factor IF-3
- Cysteine--tRNA ligase
- Serine--tRNA ligase
- Valine--tRNA ligase
- Alanine--tRNA ligase
- Large ribosomal subunit protein bL20
- Methionine--tRNA ligase
- Histidine--tRNA ligase
- Leucine--tRNA ligase
- Asparagine--tRNA ligase
Sequence:
MPVITLPDGSQRHYDHAVSPMDVALDIGPGLAKACIAGRVNGELVDACDLIENDAQLSIITAKDEEGLEIIRHSCAHLLGHAIKQLWPHTKMAIGPVIDNGFYYDVDLDRTLTQEDVEALEKRMHELAEKNYDVIKKKVSWHEARETFANRGESYKVSILDENIAHDDKPGLYFHEEYVDMCRGPHVPNMRFCHHFKLMKTAGAYWRGDSNNKMLQRIYGTAWADKKALNAYLQRLEEAAKRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQEVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTEEQIRDEVNGCIRLVYDMYSTFGFEKIVVKLSTRPEKRIGSDEMWDRAEADLAVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPSRLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQVVIMNITDSQSEYVNELTQKLSNAGIRVKADLRNEKIGFKIREHTLRRVPYMLVCGDKEVESGKVAVRTRRGKDLGSMDVNEVIEKLQQEIRSRSLKQLEE
Protein: Rifin (Q8I4P3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MMLNYTNILLFYLSLNILSSSSEVYNQRNHFITYTPKRSTRLLCECELYTSIFDNDPEMKSLIEHFNKQTQQRFHEYDERMKTTRQKCREQCDKEIQKIILKDKLEKELAEKFVTLQTDIQSDAIPTCICEKSLADKVEKTCLKCGGVLGGGVTPAWGFLSGIVYTGWKAAALAAATKEAIAEGAAKGAAAGTKAGIKAVMDVLYSDFGLSIEGVQKMGLVLSATNYKDVPMITKALYSKFQVSSCLRGGPVPGVPPVRPTDGTFCSAMLEKILAQENVVKQNSLEGSIKSVVNQIVTEAKSAAVSETAKVTASETETLKATNIAAVNATYASSQTAIIASIIAIVVIILIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Putative QA-SNARE protein (Q4QDK9)
Organism: Leishmania major
Interaction partners:
- Putative Sec1/Munc18 related protein
- Putative Qc-SNARE protein
- Qa-SNARE protein
- Soluble NSF attachment protein, SNAP family protein
- Putative SNAP protein
- Putative SNAP protein
- Putative SNARE protein
- Putative QA-SNARE protein
- Putative R-SNARE protein
- Putative Qc-SNARE protein
Sequence:
MPLENGEVLSRCIQQVAKACSDAQSSMKELGTGRDAIARGRLRRTRLLVQQCNSRVEEVLSDAEPSLESLRQQYAQQKAVFELINVEATRRERQTFQQKDPASMREGDLDALESQVTFCEARPLNMSEFHTEEAIQREKLQSAREIESDVMDLKMAYQEFHSLAHQQQESLDRVTNNVTESRSLIERGHDQIQGATRRQRSFRKIGCISGAVVIVIMVIVMIVVMVLTR
Protein: Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5) (P03147)
Organism: Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979) (HBV-D)
Function: Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04076}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04076}.
Interaction partners:
Sequence:
MDIDPYKEFGATVELLSFLPSDFFPSVRDLLDTAAALYRDALESPEHCSPHHTALRQAILCWGDLMTLATWVGTNLEDPASRDLVVSYVNTNVGLKFRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC