wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar morphogenesis protein 6 (Vacuolar protein sorting-associated protein 39) (Q07468)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vacuolar assembly. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion.
Subcellular location: Vacuole membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 8
- Syntaxin VAM3
- Vacuolar protein sorting-associated protein 16
- Vacuolar protein sorting-associated protein 33
- Ypt/Rab-type GTPase YPT7
- Vacuolar v-SNARE NYV1
- Vacuolar protein sorting-associated protein 3
- Vacuolar morphogenesis protein 7
- Vacuolar protein sorting-associated protein 41
- E3 ubiquitin-protein ligase PEP5
Sequence:
MLRAQKLHSLKSSDITAILPTEQSQKLVLAKKNGDVEVYSRDGNTLKLFQVYPDLLQNAKNDPLPPVIENFYFANELSTIFAQCKETLILLSTTNLHEYDRIIDRRGINHCWLFERSHKNKEEKNTYLIYSTINTAKMRVLIWEGRTYKNMMEASLSYRKETIRSIYPGETGITLATDLGIYHWPYNKPSLIRIEKTVKNKFPKDMISALTELKEQAEKVIEKKPKKNSHFDAQSFSSMDRMSRKSSMSSLWYRTIRNERGNKIRYTFELDGNDATPMIIDGATKKIFKVELMHNNEEPFLIATDHATFSESNSEFDHMQYLSSNLLMLYNSSTIKFVDYENGFTFLQQKIPEGIKWVKNLSGTYFLVWTSNDEVQLFSYHVDDGSEDDDQESICGDINDPDFYQLWRKVLFYKFFIDSPHSKELCVSDNPEESLDICAMKLRDLTVMWCLRIFDKFQNYMVQLERSRNSRMIRSKCEEMIIKSIFDLFIKFWAPPQLVILKVFPSAISSLVLEITGQEHHCLLKEAEEVKETYDIPPHLLNRWCLPYLTDTRRHLQNLLSKENDDESRITWCYRDREIKQSFDFFLISNHDDVDLNTMLTLIDTVLFKCYLYYNPPMVGPFIRVENHCDSHVIVTELKIRHMFKDLIDFYYKRGNHEEALKFLTDLVDELENDNTDQKQRQKIDHGVKILVIYYLKKLSNPQLDVIFTYTDWLLNRHNDSIKEILSSIFFYDSQACSSRDHLKVYGYIKKFDKLLAIQYLEFAISTFRLEGNKLHTVLIKLYLENLDIPSTRIKLKSLLETTSVYEPRTILKLLNDAIESGSDQLPTNQLNFVKYLKIFPLSKLENHKEAVHILLDEIDDYKAATSYCNDVYQSDSTKGEELLLYLYSKLVSIYDSNRNSKLILNFLQDHGSKLNSAEIYKNLPQDISLYDIGRVVSQLLKKHTSKMDETRLEKALLQVELVATTYKLNERMSSYGVLSDSHKCPICKKVISNFGTDSISWFTREGRNIITHYNCGKVLQERFNAKNEKSSRIKQKTLGEVINELNNK
Protein: Upstream stimulatory factor 1 (B1AQP1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKGQQKTAETEEGTVQIQEGAVATGEDPTSVAIASIQSAATFPDPNVKYVFRTENGGQVMYRVIQVSEGQLDGQTEGTGAISGYPATQSMTQAVIQGAFTSDDAVDTEGTAAETHYTYFPSTAVGDGAGGQFFVMMSPQEVLQGGSQRSIAPRTHPYSPKSEAPRTTRDEKRRAQHNEVERRRRDKINNWIVQLSKIIPDCSMESTKSGQSKGGILSKACDYIQELRQSNHRLSEELQGLDQLQLDNDVLRQQVEDLKNKNLLLRAQLRHHGLEVVIKNDSN
Protein: Cell division control protein 6 (P09119)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a crucial role in forming the pre-replicative complexes. Interacts with the origin recognition complex (ORC) and MCM2-7 helicase complex leading to the linking of those complexes and loading of the replicative helicase MCM2-7 onto the pre-replicative complexes. Required for the initiation of DNA replication and then actively participates in the suppression of nuclear division.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Cyclin-dependent kinase 1
- Origin recognition complex subunit 3
- DNA replication licensing factor MCM3
- Minichromosome maintenance protein 5
- Minichromosome maintenance protein 10
- Origin recognition complex subunit 6
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM4
- Cell division control protein 45
- Origin recognition complex subunit 4
Sequence:
MSAIPITPTKRIRRNLFDDAPATPPRPLKRKKLQFTDVTPESSPEKLQFGSQSIFLRTKALLQKSSELVNLNSSDGALPARTAEYEQVMNFLAKAISEHRSDSLYITGPPGTGKTAQLDMIIRQKFQSLPLSLSTPRSKDVLRHTNPNLQNLSWFELPDGRLESVAVTSINCISLGEPSSIFQKIFDSFQDLNGPTLQIKNMQHLQKFLEPYHKKTTFVVVLDEMDRLLHANTSETQSVRTILELFLLAKLPTVSFVLIGMANSLDMKDRFLSRLNLDRGLLPQTIVFQPYTAEQMYEIVIQKMSSLPTIIFQPMAIKFAAKKCAGNTGDLRKLFDVLRGSIEIYELEKRFLLSPTRGSLNSAQVPLTPTTSPVKKSYPEPQGKIGLNYIAKVFSKFVNNNSTRTRIAKLNIQQKLILCTIIQSLKLNSDATIDESFDHYIKAITKTDTLAPLQRNEFLEICTILETCGLVSIKKTKCKGKTKRFVDKIDVDLDMREFYDEMTKISILKPFLH
Protein: Os05g0597000 protein (Q5KQG3)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MSHIAVERNRRRQMNDHLKVLRSLTPAFYIKRGDQASIIGGAIDFIKELQTLLQSLEAQKKRRQQPQAHLISPASISASGGGSPSPTPSPRSLITSCSPTAAAGSSAGSSSSISPKDENKQQLQLVAELAACCNSPMADVEARISGANVLLRTLSRRAPPVRIIALLESLHLEVLHLNITTMDDTVLYSFVLKIGLDCHLSVDDLAMEVHQSFMPPPAAHPDNHLHS
Protein: Agamous-like MADS-box protein AGL5 (Protein SHATTERPROOF 2) (P29385)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor. Interacts genetically with TT16/AGL32 in a partially antagonistic manner during flower development. Is essential for the coordination of cell divisions in ovule, seed coat development and endosperm formation.
Subcellular location: Nucleus.
Interaction partners:
- Developmental protein SEPALLATA 3
- B3 domain-containing protein At5g18000
- BEL1-like homeodomain protein 9
- Homeobox protein BEL1 homolog
- F-box protein 7
- Zinc finger protein JAGGED
- Large ribosomal subunit protein uL14my
- Floral homeotic protein APETALA 2
- Protein SPOROCYTELESS
- Protein CRABS CLAW
Sequence:
MEGGASNEVAESSKKIGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALVIFSTRGRLYEYANNSVRGTIERYKKACSDAVNPPTITEANTQYYQQEASKLRRQIRDIQNLNRHILGESLGSLNFKELKNLESRLEKGISRVRSKKHEMLVAEIEYMQKREIELQNDNMYLRSKITERTGLQQQESSVIHQGTVYESGVTSSHQSGQYNRNYIAVNLLEPNQNSSNQDQPPLQLV
Protein: F-box domain-containing protein (P91305)
Organism: Caenorhabditis elegans
Interaction partners:
- Skp1-related protein
- DDB1- and CUL4-associated factor 11 homolog
Sequence:
MALEEIMDFEEEEAGWKHLPREIRRNILTRLPFPDKQNMMLVSWENSQICSTLPNKLHELGITELPSTAKTILIMKWKNEIGRVVSRMVEFRGTSLRQTECPDHTAEAMRAFLRIWRFSKIKSIVIEIPCFEGLSSIWEEGMAEVKTNIAVRSFNIRTNDYRLVTKALTAPKNKGQDISLLANDHGGMETAVFDIDKFKYARSVILWSLVSNIQDHQLYSLSAHNIRLHSEFITSNCIAKMIQEWKEGRRSLERLHITSPIIDLDTIVRQVLGVCWKNMTDICSIIWREVDEEGYSYAVRGPTYDIPAAIGIIPNQDGVPTFIFRIIRMTHEMSRIVYERCSVQCPNMVSSEDLARQQQRV
Protein: Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48) (Q9UTM7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Histone acetyltransferase type B subunit 2
- Histone H4
- NASP-related protein sim3
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- Origin recognition complex subunit 4
- Origin recognition complex subunit 2
- Origin recognition complex subunit 6
- Histone chaperone cia1
- Histone H3.1/H3.2
Sequence:
MSAVDEWVHNANECIEIVQVNEKHEKDCQYHPSNTYAIFGDAEVIYGYKDLNVTITYECPLMVPKLEISYSERLAPDSGVEPTDIEGTLNTYLKDRSIKVEGNSFDVHSANSIHNYSFNGKTFKILQATVLEASEIMQHLQIFSLFFIEGGSFIDLNDPRWMVYLLYETTEDDYCLRGYCTVYKYYKWDKLIHDGIRARISQFVILPPFQHQGHGSQLYNAIVSTFLKNPKILDFTVEDASEAFDSLRDHCDYKRLLSMGIFSEPDFHPSLSRQWINSKIAETKLTQRQFSRCCELAFTTKLKKLSLLERKSVRLGIKERIFRQNLDVLLQLDKSERIEKIHNAYENQFDEYKQIVKKLPKLKEDSPRKRQKLAQSSS
Protein: Nucleoside diphosphate phosphatase ENTPD5 (EC 3.6.1.6) (CD39 antigen-like 4) (ER-UDPase) (Ectonucleoside triphosphate diphosphohydrolase 5) (NTPDase 5) (Guanosine-diphosphatase ENTPD5) (GDPase ENTPD5) (Inosine diphosphate phosphatase ENTPD5) (Nucleoside diphosphatase) (Uridine-diphosphatase ENTPD5) (UDPase ENTPD5) (O75356)
Organism: Homo sapiens (Human)
Function: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP. In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000269|PubMed:10400613, ECO:0000269|PubMed:15698960}.
Interaction partners:
- Ectonucleoside triphosphate diphosphohydrolase 3
- Ectonucleoside triphosphate diphosphohydrolase 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleoside triphosphate diphosphohydrolase 4
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleoside triphosphate diphosphohydrolase 8
- Adenylosuccinate synthetase isozyme 1
- Soluble calcium-activated nucleotidase 1
- Inosine triphosphate pyrophosphatase
- AMP deaminase 3
Sequence:
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGFEPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAREVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHLLQSLGISH
Protein: C-type lectin domain family 1 member A (C-type lectin-like receptor 1) (CLEC-1) (Q8NC01)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- C-type lectin domain family 4 member E
- Lithostathine-1-beta
Sequence:
MQAKYSSTRDMLDDDGDTTMSLHSQGSATTRHPEPRRTEHRAPSSTWRPVALTLLTLCLVLLIGLAALGLLFFQYYQLSNTGQDTISQMEERLGNTSQELQSLQVQNIKLAGSLQHVAEKLCRELYNKAGAHRCSPCTEQWKWHGDNCYQFYKDSKSWEDCKYFCLSENSTMLKINKQEDLEFAASQSYSEFFYSYWTGLLRPDSGKAWLWMDGTPFTSELFHIIIDVTSPRSRDCVAILNGMIFSKDCKELKRCVCERRAGMVKPESLHVPPETLGEGD
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (P69596)
Organism: Avian infectious bronchitis virus (strain Beaudette) (IBV)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04097}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04097}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04097}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04097}.
Interaction partners:
Sequence:
MASGKAAGKTDAPAPVIKLGGPKPPKVGSSGNASWFQAIKAKKLNTPPPKFEGSGVPDNENIKPSQQHGYWRRQARFKPGKGGRKPVPDAWYFYYTGTGPAADLNWGDTQDGIVWVAAKGADTKSRSNQGTRDPDKFDQYPLRFSDGGPDGNFRWDFIPLNRGRSGRSTAASSAAASRAPSREGSRGRRSDSGDDLIARAAKIIQDQQKKGSRITKAKADEMAHRRYCKRTIPPNYRVDQVFGPRTKGKEGNFGDDKMNEEGIKDGRVTAMLNLVPSSHACLFGSRVTPKLQLDGLHLRFEFTTVVPCDDPQFDNYVKICDQCVDGVGTRPKDDEPKPKSRSSSRPATRGNSPAPRQQRPKKEKKLKKQDDEADKALTSDEERNNAQLEFYDEPKVINWGDAALGENEL
Protein: Alpha-2A adrenergic receptor (Alpha-2A adrenoreceptor) (Alpha-2A adrenoceptor) (Alpha-2AAR) (P18871)
Organism: Sus scrofa (Pig)
Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- G protein subunit alpha 13
- G protein subunit alpha 12
- G protein subunit beta 2
Sequence:
MFRQEQPLAEGSFAPMGSLQPEAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLFTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIVTVWVISAVISFPPLISIEKKAGGGGQQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAAAALPGGAERRPNGLGPERGVGRVGAEAEPLPVQLNGAPGEPAPAGPRDADGLDLEESSSSEHAERPPGPRRSERGPRAKSKARASQVKPGDSLPRRGPGAPGPGAPATGAGEERGGVAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPPTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV
Protein: Leucine-rich repeat-containing protein 3 (Q9BY71)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Caspase-1
- Apoptosis-associated speck-like protein containing a CARD
Sequence:
MGTVRPPRPSLLLVSTRESCLFLLFCLHLGAACPQPCRCPDHAGAVAVFCSLRGLQEVPEDIPANTVLLKLDANKISHLPDGAFQHLHRLRELDLSHNAIEAIGSATFAGLAGGLRLLDLSYNRIQRIPKDALGKLSAKIRLSHNPLHCECALQEALWELKLDPDSVDEIACHTSVQEEFVGKPLVQALDAGASLCSVPHRTTDVAMLVTMFGWFAMVIAYVVYYVRHNQEDARRHLEYLKSLPSAPASKDPIGPGP
Protein: Coiled-coil domain-containing protein 141 (Coiled-coil protein associated with myosin II and DISC1) (D3ZEY0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:E9Q8Q6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:E9Q8Q6}. Note=Co-localized with DISC1 at/around the centrosome. Localizes to the centrosome, at least in part, in a DISC1-dependent manner. Accumulates and oscillates at the dilation in cortical neurons during migration. CAMDI protein level is stabilized at the G1 phase and destabilized at the G2 /M phase. {ECO:0000250|UniProtKB:E9Q8Q6}.
Interaction partners:
Sequence:
MSCKESPHVGVSTTTVSSVAVQAGDSKIVIAVVKCGKWVRLQLAEAQPNLLEIGSSQDETRKLLHDHELLLAKLKALEDRVWGLLQEADRTAEANKEQSEVYDAMAQTLGEAWATLVSMLERRRELLGLTSEFFQSALEFAIKIDQAEDFLQNPHEFESAEALQSLLLLHDRHAKELLERSLVLLNKSQQLTDFIEKFKCDGSPVNSELIQGAQSSCLKIDSLLELLQDRRRQLDKHLQQQRQELSQVLQLCLWDQQESQVSCWFQKTIRDLQEQSLGSSLSDNKELIRKHEDLTIKAKEWDLAMEKLKSQALGILLSKDLTEKEHLQLSNQKLNRLQEEFGRLMVDRKAWLTMAHDFFTSANEAFDVLGKVEDYLKLLKSEGLSLPALAAKHEELHREIKDSTAAALQKGRTLISQVDSCRAQVTGIHETMGRIQKRVDRLSQQCTAHQEFALKKQQLATSVDDYLRKVEMSVQEMRLVLATTLDVGSSPSESEKILNKYLELDIQAKETAHALEAAAKITTEKNELELNEVALLPFKVKRLEEELSTLSRSVSYRSQVLQTYIAFRKSSEEVEEQLQSLKEFYLTESPWEDEDDAVVTCQSNSAERKWQLFLKKSFLTQDLSLEFLNLISMAKENEILNVKKEMHIVENVMEKQTNGREELSRLRMAWHLKAMEGKPVKERWETFKEKLKKTTHNVKLLHEVLMPVSALDLGGNLQSMSDLRRRWIAMQPQLQQLHEDVQQIMKEWEVLSGQGVPLKEKAEQLKDLIHLHQRQRERIQEYEEILYKTVQFHQVKEELTHLIKPRELELLAQPMELEGSKEVLMQLGRSQGRRAHVDHLHRLALSLGVDIISSVQRPNCSNISAKSLQQQLEALELDSRDWSAKAKEYEQVLACSLEYCTTREEINELKESFKDIKKKFNNLKFNYSKKNEKSRNLKTLQYQIQQVETYADKIQALRKKMEKVNKKISDSVLSYPSNKANTLVEAMEDLKKHVDDFDKVVTDYKMNLDLTEHLQEVIEECNFWYEDASATVVRVGKYSMECQTREAVDILHRQFQKFVTPSVPQQEERIQEVVSLAQRLYGLEEGQKYAEKIVTRHKEILESITELCGSLVELKEKLMQGDVPKVNSNLEDFHGNSIDLLKEPGRDEQTTFSEERSEGQAQGADVSAINGTREDGLPVGLRQSFDKEDSAQGLTLPEDTLSGEDSECISSDDISLPPLPVTPESPLAPSDMEVEEPASSSALALHISGYRMRTGTGGLGKAPESVLPPPTAFTDGYHNKKDTFTSHFERPYPQFKAEPLLTSRGSGEMSTKLHVNVKCPARMPREVHDKALPPSSQAQEISLGTQEKVHADSNVTKTQDRLHAALDVSPGLSSQSDTSRSHQRQVGPQGDRKNSSAEKSVVSLAGQAPHFSRLLSNVTVTEGSPVTLEVEVTGFPEPTLTWFKKGQKLCADGHLQVLHKDTKHSVFIPKVCEADAGLYVAQAQNSSGTLSSKAILHVTGNHGPPITRINWIVLCIIYVSVSVIYWLLTQ
Protein: Chromatin modification-related protein png2 (ING1 homolog 2) (O74736)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the clr6 histone deacetylase complex I' responsible for 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. Has a role in silencing of mating type genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone deacetylase clr6
- Transcriptional regulatory protein sds3
- Transcriptional regulatory protein rxt2
- Putative histone deacetylase complex subunit cti6
- RbAp48-related WD40 repeat-containing protein prw1
- Chromatin modification-related protein eaf3
- Paired amphipathic helix protein pst2
- Paired amphipathic helix protein pst1
- Paired amphipathic helix protein pst3
- Uncharacterized protein C2F7.07c
Sequence:
MGTSGIEIFAALNDFTDAIVSVPESVCGKFTSLKEIDAQVRDIRQNVIQEIGVVLKNEKNDELSGEERCERLQKTLKEILPYSDSKICLATDAMNNIKSCIDRLDAGFEYVELEIPQQLRLGYPDDRALMNYHSTVTPQTSERRRETRRHQNNQHSQQYSSQERSSSYNNFEDASSPQSSYHTPTKRRKNAVPRKSSSPPLSSTKHAPQSTERRPVRRSESRLKQTNGEPLVKHDTLDSSDISREGEQLYCYCQQVSYGQMIGCDNENCKREWFHLPCVGLVEPPKGIWYCKECEELAKSSESRQ
Protein: H/ACA ribonucleoprotein complex subunit 1 (Nucleolar protein family A member 1) (snoRNP protein GAR1) (Q9CY66)
Organism: Mus musculus (Mouse)
Function: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Note=Also localized to Cajal bodies (coiled bodies). {ECO:0000250}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit DKC1
- H/ACA ribonucleoprotein complex subunit 2
- H/ACA ribonucleoprotein complex subunit 3
- Telomerase Cajal body protein 1
- Nucleolar protein 58
- Nucleolar protein 56
- rRNA 2'-O-methyltransferase fibrillarin
- Telomerase reverse transcriptase
- RNA 2'-O-methyltransferase FBLL1
- NHP2-like protein 1
Sequence:
MSFRGGGRGGFNRGGGGGGFNRGGGSNNHFRGGGGGGGGSFRGGGGGGGGSFRGGGRGGFGRGGGRGGFNKFQDQGPPERVVLLGEFMHPCEDDIVCKCTTEENKVPYFNAPVYLENKEQVGKVDEIFGQLRDFYFSVKLSENMKASSFKKLQKFYIDPYKLLPLQRFLPRPPGEKGPPRGGGGGGRGGRGGGRGGGGRGGGRGGGFRGGRGGGGGFRGGRGGGGFRGRGH
Protein: NAD(P)H-quinone oxidoreductase subunit K, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit K) (NADH-plastoquinone oxidoreductase subunit K) (P0C341)
Organism: Oryza sativa (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01356}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01356}.
Interaction partners:
Sequence:
MSLIEFPLLDQTSSNSVISTTLKDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDALTKLRKKISREIVEDRTLSQKKNRCFTTSHKLYVRRSTNTGTYEQELLYQSPSTLDISSETFFKSKSPVSSYKLVN
Protein: 2',3'-cyclic nucleotide 3' phosphodiesterase (K7ERZ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSSGAKDKPELQFPFLQDEDTVATLLECKTLFILRGLPGSGKSTLARVIVDKYRDGTKMVSADAYKITPGARGAFSEEYKRLDEDLAAYCRRRDIRILVLDDTNHERERLEQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADD
Protein: DPY30 domain-containing protein 2 (Q96IM9)
Organism: Homo sapiens (Human)
Interaction partners:
- Nucleoside diphosphate kinase homolog 5
- DPY30 domain-containing protein 1
- Protein dpy-30 homolog
Sequence:
METNYLKRCFGNCLAQALAEVAKVRPSDPIEYLAHWLYHYRKTAKAKEENREKKIHLQEEYDSSLKEMEMTEMLKQEEYQIQQNCEKCHKELTSETVSTKKTIFMQEDTNPLEKEALKQEFLPGTSSLIPGMPQQVPPSESAGQIDQNFKMPQEINYKEAFQHEVAHEMPPGSKSPF
Protein: Protein EDS1 (Enhanced disease susceptibility 1) (Q9SU72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of basal resistance and of effector-triggered immunity specifically mediated by TIR-NB-LRR (TNL) resistance proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR resistance protein interactions constitutes the first step in resistance activation. Acts redundantly with salicylic acid to regulate resistance gene-mediated signaling. Triggers early plant defenses and hypersensitive response independently of PAD4, and then recruits PAD4 to potentiate plant defenses through the accumulation of salicylic acid. Nuclear localization is essential for basal and TNL-conditioned immunity and for reprogramming defense gene expression, while cytoplasmic EDS1 is required to induce a complete immune response. Heterodimerization with PAD4 and/or SGA101 is necessary for TNL-mediated effector-triggered immunity. Contributes to nonhost resistance against E.amylovora. Loss of EDS1-PAD4 interaction compromises basal but not TNL-triggered resistance. Necessary for systemic acquired resistance (SAR) signal generation and perception. Has no direct lipase activity. Putative lipase activity is dispensable for immune functions.
Subcellular location: Nucleus {ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:22158819}. Cytoplasm {ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:22158818, ECO:0000269|PubMed:22158819}. Microsome {ECO:0000269|PubMed:22158819}. Note=Found in both the nucleus and diffuse in the cytosol when associated with PAD4, in the nucleus and in punctate spots in the cytoplasm when interacting with SRFR1, SNC1 or RPS4, only in the nucleus when associated with SAG101 and in the cytosol when it dimerizes. Found in the nucleus when interacting with VICTR and PAD4. Interacts with AvrRps4 and HopA1 effectors in microsomes. {ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:22158819, ECO:0000269|PubMed:23275581}.
Interaction partners:
- Senescence-associated carboxylesterase 101
- Lipase-like PAD4
- Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1
- Toll/interleukin-1 receptor-like protein
- Isochorismate synthase 1, chloroplastic
- Protein EDS1B
- Regulatory protein NPR1
- Disease resistance protein RRS1
- Alpha/beta-Hydrolases superfamily protein
- Pathogenesis-related protein 5
Sequence:
MAFEALTGINGDLITRSWSASKQAYLTERYHKEEAGAVVIFAFQPSFSEKDFFDPDNKSSFGEIKLNRVQFPCMRKIGKGDVATVNEAFLKNLEAIIDPRTSFQASVEMAVRSRKQIVFTGHSSGGATAILATVWYLEKYFIRNPNVYLEPRCVTFGAPLVGDSIFSHALGREKWSRFFVNFVSRFDIVPRIMLARKASVEETLPHVLAQLDPRKSSVQESEQRITEFYTRVMRDTSTVANQAVCELTGSAEAFLETLSSFLELSPYRPAGTFVFSTEKRLVAVNNSDAILQMLFYTSQASDEQEWSLIPFRSIRDHHSYEELVQSMGKKLFNHLDGENSIESTLNDLGVSTRGRQYVQAALEEEKKRVENQKKIIQVIEQERFLKKLAWIEDEYKPKCQAHKNGYYDSFKVSNEENDFKANVKRAELAGVFDEVLGLMKKCQLPDEFEGDIDWIKLATRYRRLVEPLDIANYHRHLKNEDTGPYMKRGRPTRYIYAQRGYEHYILKPNGMIAEDVFWNKVNGLNLGLQLEEIQETLKNSGSECGSCFWAEVEELKGKPYEEVEVRVKTLEGMLGEWITDGEVDDKEIFLEGSTFRKWWITLPKNHKSHSPLRDYMMDEITDT
Protein: Mannosyltransferase APTG1 (EC 2.4.1.-) (Glycosyltransferase 22) (Protein ABNORMAL POLLEN TUBE GUIDANCE 1) (Q94A15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Required for the pollen tube micropylar guidance and embryo development by regulating GPI-anchor mediated protein localization (e.g. COBL10 and A36).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24963069}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- GPI mannosyltransferase 1
- Phosphatidylinositol-glycan biosynthesis class X-like protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- GPI mannosyltransferase 2
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- GPI ethanolamine phosphate transferase 3
- At1g16040
- GPI ethanolamine phosphate transferase 1
- Dolichol-phosphate mannosyltransferase subunit 1
- GPI transamidase subunit PIG-U
Sequence:
MDIRKRKNAGGDGDGGADGASVNVGDEPDSFGGRIGSPRRIFLFCLAFRVVNALLIQTYFNPDEHWQSLEVAHRTIFGYGYMTWEWKRGIRSYLHPMLFAFLYKLLQVTGLDTPYIMIKAPRLMQSIFSAIGDLYLYKLSDALYGGNVATWSLFCQMANWFIFFCLNRTFSNCLETVLTIMGLYYWPCIRDSSIDYPVNRKWGLVIAALACAIRPTSAVIWLYVGMLELFLTPNKVKFIILEVIPIGSLVLGFTCLLDRLMYGSWVIVPLNFLKFNFLSSGGDYYGTHPWHWYFTQGFLVMLFTFTPFSIAGIIKSKNQKLSALILWVLAIYSILGHKEFRFVLPVLPIALIFSGYAFAQMEVSGSSSSSSVTKKKQVPRQNHTKWSPKLRLSVYFLLATNIPMALYMSLFHQRGTEDAMNYLSDEAYKGRVKSILFLMPCHSTPYYSTLHRNIPMQFLDCTPSAEKGELDESDQFLVNPLGFASELARNWSEPPSHIVLFASEETKLRDFMIQHSFKEVRRFFHAHFKVDRDLQSSVVVYVVNHAFP