wanglab/gogpt-training-data huggingface dataset:
Protein: Syntaxin-1B (Syntaxin-1B1) (Syntaxin-1B2) (P61266)
Organism: Homo sapiens (Human)
Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity).
Subcellular location: [Isoform 1]: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:18691641}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18691641}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18691641}. Note=Colocalizes with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma-tubulin in the pericentrosomal region of the mitotic spindle in dividing cells.
Interaction partners:
- Syntaxin-binding protein 1
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 2
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 1
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 4
- Vesicle-associated membrane protein 8
- Alpha-soluble NSF attachment protein
- Beta-soluble NSF attachment protein
Sequence:
MKDRTQELRSAKDSDDEEEVVHVDRDHFMDEFFEQVEEIRGCIEKLSEDVEQVKKQHSAILAAPNPDEKTKQELEDLTADIKKTANKVRSKLKAIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMTEYNATQSKYRDRCKDRIQRQLEITGRTTTNEELEDMLESGKLAIFTDDIKMDSQMTKQALNEIETRHNEIIKLETSIRELHDMFVDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVVLGVVLASSIGGTLGL
Protein: ATP-dependent zinc metallopeptidase, putative (EC 3.4.24.-) (Q57Y25)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Prohibitin
- Prohibitin
Sequence:
MRRYLLASLPMAHRPRYPSHTGLVISMSHVSFEPKQQSKLQVLTAYSVARDSSPQFGRSSPFNHLRQLVTAFGTSMAVKQLSRGKILSAKPSDGGNNTAGEQNGRDKKEEESPIFPNSSSEDDNTEELIVARSVLFVLVMLGTSYVLYKLSQPLGKQTGWASLLKNAEIVKSIKLYHNYAQVYLSEGKVYLGLVDDQHTQEKLEKLNKAYNDAVTTRIKEPRPQGNGETVTTKSEGIEVSLQGTPLGEQALVVLGVFAWVVPFVFFPVFVMVLSNSIGKSLALTLEAGKKTHKSKEMVFRVELSSSTRFKHIAGLKEAKKEVTEVVDFLRHPERYTSLGAKVPTGALLLGPPGTGKTLLAKAVAGESGVGFIPVCGSDFVELYVGMGALRVRQLFEVAKKQRCIVYIDEIDAIGLKRTGAGIGEKQEQEHTLNELLTQLDGFSSSRRGDVMILASSNVSQEQLDPALVRPGRFDRIIHVDMPVISERIDIFKVHLSALTLVKESNKGAKGAEVEQQTEEASTESSESKKSDAKANAKSDDEGKMESGTVPSSENKSPTADEAKGFNSCEVSTANATTSSLVVSKLQEEMEAEQELLEQEKLTGDPSYDFRTLLANKSERERALINSYAERMSSLCPGFTGADIANVCNEAAILAARENNSNVDITHLERSIDRVLAGIEHRSRVLSPFERQVVAHHEAGHAVAGWFLNRADPLMKVSIVPRGGSALGYAQYLPNENNVRTAAEIRDSISVTLGGRVAEKIFFNHLSTGASDDLNKVARMAYMFVSSFAPRPVYPAPGTAGTRIVKPFGPKVSNHIDVEAKKLVDEIYEQTYSLLLSKKEEMETLAKHLLENEVLTFDDVVRYLGTRKARETDRKKGV
Protein: Polyprenal reductase 2 (EC 1.3.1.94) (Q9SI62)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism. Involved in the regulation of plant growth and reproductive processes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26628744}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichol kinase EVAN
- Polyprenal reductase 1
- NAD
- Alpha/beta-Hydrolases superfamily protein
- At3g49420
- Alpha/beta-Hydrolases superfamily protein
- Small ribosomal subunit protein eS17w
- Dehydrodolichyl diphosphate synthase 4
- Ribosomal protein S24/S35
- At4g13500
Sequence:
MVELEIVWLVRGAWITVWIVSILPLVIASIPTSKLNSFRELVLSFAGRGKILHPSSQKFTIPQKCFAHFYVIGVVWTTLLLAATWMYACKMAPLSSEEFQLSDIASRLAGGSDVFSVHKSNMTPVEHRFKVWRAVFLLLLMEIHVLRRLIESFYVFKYSPSARMHILGYFAGLFFYVTAPLSLCSNIAPEVAGFVGNQVAEFIANGKSHTSAPEFNLLSSISPLMKLGSLQWIGGAIFLWGWIHQRRCHAILGSLRENPSQAKEYIIPYGDWFGMVSSPHFLAEIVLYAGLLIASGGTDITIWLLFGFVAANLTYAAGETHRWYLRKFENYPANRHAIFPYVY
Protein: RNA-binding motif protein 14a (RNA-binding protein 14a) (Zgc:110682) (Q503D7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tmem50a protein
- EWS RNA-binding protein 1b.
Sequence:
MDDSSAVKLFVGNLDLETTQDDLIALFAPFGEVVHITVLRQFAFVHLQGEGAADSAIRDLNGREYRGRSLVVEESKGRPLNSTKVFVGNLCASCSVEDLYDLFSPYGKVLDCDKVKTKPSSLTGYAFVYMEHKEDAEQAIEGLHGTTFMGRPLAVELSKVQQSTNKVPCASCGAHGHFAGECPINRPPMEHHQSQAAVLAAAAAAAAGLPLQVQQSVHNSFYNTASSDPTFAALKDLTTSRVDGKPVSSMVYGALASQVYSSVADQVIGSTSQTAEGYPTEAEAPPGVAYGTEPDPHTLFEAARARFFEQGQQVLAEQQAVTKSDRDRSPIRRTAPLLPDPSPQQFSQARPKRRALLPTPPGGPELPPVKNGDPIARCYAEYYQQYQQYQQYQQYQQYHQYHQYQYNYPPPPPPPPAPMPMMPPGPMDVQQMMAPGTSIPPRVYEPTPTHKEPLLRRPDYPHQHTSESPYR
Protein: Pyridoxal 4-dehydrogenase (tPLDH) (EC 1.1.1.107) (Q988B7)
Organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099))
Function: Involved in the degradation of pyridoxine or pyridoxamine (free, phosphate-unbound, forms of vitamin B6). Oxidizes pyridoxal to 4-pyridoxolactone, but does not have activity toward pyridoxal 5'-phosphate, pyridoxine, pyridoxamine, pyridoxamine 5'-phosphate, 4-phthalaldehyde, 2-nitrobenzaldehyde, pyridine, formaldehyde, 2-carboxybenzaldehyde or sugars.
Interaction partners:
Sequence:
MTERLAGKTALVTGAAQGIGKAIAARLAADGATVIVSDINAEGAKAAAASIGKKARAIAADISDPGSVKALFAEIQALTGGIDILVNNASIVPFVAWDDVDLDHWRKIIDVNLTGTFIVTRAGTDQMRAAGKAGRVISIASNTFFAGTPNMAAYVAAKGGVIGFTRALATELGKYNITANAVTPGLIESDGVKASPHNEAFGFVEMLQAMKGKGQPEHIADVVSFLASDDARWITGQTLNVDAGMVRH
Protein: Diphthamide biosynthesis protein 3 (CSL-type zinc finger-containing protein 2) (DelGEF-interacting protein 1) (DelGIP1) (Q8K0W9)
Organism: Mus musculus (Mouse)
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase. Acts as an electron donor to reduce the Fe-S cluster in DPH1-DPH2 keeping the [4Fe-4S] clusters in the active and reduced state. Restores iron to DPH1-DPH2 iron-sulfur clusters which have degraded from [4Fe-4S] to [3Fe-4S] by donating an iron atom to reform [4Fe-4S] clusters, in a manner dependent on the presence of elongation factor 2 and SAM. Associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96FX2}. Nucleus {ECO:0000250|UniProtKB:Q96FX2}.
Interaction partners:
- 2-
- Secretion-regulating guanine nucleotide exchange factor
- 2-
- Elongation factor 2
- Diphthine methyl ester synthase
- DnaJ homolog subfamily C member 24
- Diphthine methyltransferase
- Diphthine--ammonia ligase
- Elongator complex protein 3
- Elongator complex protein 1
Sequence:
MAVFHDEVEIEDFQYDEDSETYFYPCPCGDNFAITKEDLENGEDVATCPSCSLIIKVIYDKDQFMCGETVPAPSTNKELVKC
Protein: ADP-ribosylation factor-like protein 2 (Q2TA37)
Organism: Bos taurus (Bovine)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle.
Subcellular location: Nucleus {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm. Mitochondrion. Note=The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. {ECO:0000250}.
Interaction partners:
- Tubulin-specific chaperone D
- ADP-ribosylation factor-like protein 2-binding protein
- Protein unc-119 homolog A
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- ADP-ribosylation factor-like protein 2-binding protein
- ELMO domain-containing protein 2
- Tubulin-folding cofactor B
- Tubulin-specific chaperone E
- X-linked retinitis pigmentosa GTPase regulator
Sequence:
MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQNLLVEERLAGATLLIFANKQDLPGALSSNAIREALELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFMAD
Protein: V-type proton ATPase subunit F (Q6DRK0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- V-type proton ATPase subunit G
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit D
- Vacuolar proton pump subunit B
- ATPase H+-transporting V1 subunit E1b.
- H
- V-type proton ATPase proteolipid subunit
- ATPase H+-transporting V1 subunit E1a
Sequence:
MPGRGKLIAVIGDEDTCTGFLLGGIGELNKNRKPNFLVVEKETSVTEIEETFKSFLARNDIGIILINQFIAEMIRHAIDAHMQSIPAVLEIPSKEHPYDASKDSILRRAKGMFSAEDFR
Protein: ENAH, actin regulator (A0A0G2K6I4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Vasodilator-stimulated phosphoprotein
- Ena/VASP-like protein
- Zyxin
Sequence:
MDVEFVSYSIPKLRSSQSLRISEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQEAGPTLPRQNSQLPAQVQNGPSQEEMEIQRRQLQEQQRQKELERERMERERLERERLERERLERERLEQEQLERQRQEREHVERLERERLERLERERQDRERERERLEQLEREQVEWERERRMSNAAAPASVETPLNPELGDSSASEPGLQAASQPAETPAPQGHVLGPPAPPPPPPLPSGPAYASALPPPPGPPPPPPLPSAGPPPPPPPPPPLPNQVPPPPPPPPAPPLPASGIFSGSMSEDNRPLTGLAAAIAGAKLRKVSRVEDGSFPSGGNTVSVNLASSKTDSGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDRSEDAEPVTSKAASTSTPEPTRKPWERTNTMNGSKSPVISRPKSTPSSQPSANGVQTEGLDYDRLKQDILDEMRKELAKLKEELIDAIRQELSKSNTA
Protein: NAD(+) kinase (EC 2.7.1.23) (F7EXV6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- NAD kinase 2, mitochondrial
- Glutamine-dependent NAD
- Nicotinamide-nucleotide adenylyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- NAD-dependent protein deacetylase sirtuin-1
- NAD-dependent protein deacetylase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Sirtuin 6 6
Sequence:
MEMEQEKMNLSKELNPDSASYNCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKIRDASLLQPFKELCIYLMEENNMIVYVEKKVLEDPAIVGDENFGPVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFNFENFQSQVNQVIEGNAAVILRSRLKVRVVKEPRDKKTAIHNGLSENGLDTEGGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMVHPNVPAIMVTPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVCDPVSDWFESLAQCLHWNVRKKQAHFPEDEEDQDEEDS
Protein: Cullin-2 (CUL-2) (Q13617)
Organism: Homo sapiens (Human)
Function: Core component of multiple cullin-RING-based ECS (ElonginB/C-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination of target proteins. CUL2 may serve as a rigid scaffold in the complex and may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the ECS complex depends on the substrate recognition component. ECS(VHL) mediates the ubiquitination of hypoxia-inducible factor (HIF). A number of ECS complexes (containing either KLHDC2, KLHDC3, KLHDC10, APPBP2, FEM1A, FEM1B or FEM1C as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. ECS complexes and ARIH1 collaborate in tandem to mediate ubiquitination of target proteins. ECS(LRR1) ubiquitinates MCM7 and promotes CMG replisome disassembly by VCP and chromatin extraction during S-phase (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9D4H8}.
Interaction partners:
- COMM domain-containing protein 1
- Ubiquitin-like protein NEDD8
- E3 ubiquitin-protein ligase RBX1
- Elongin-C
- Hypoxia-inducible factor 1-alpha
- von Hippel-Lindau disease tumor suppressor
- Elongin-B
- RING-box protein 2
- Leucine-rich repeat protein 1
- Protein zer-1 homolog
Sequence:
MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA
Protein: 2-phosphosulfolactate phosphatase (EC 3.1.3.71) (Q58540)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Hydrolyzes both enantiomers of 2-phosphosulfolactate. Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids with pseudosymmetric centers of inversion. Specifically hydrolyzes (S)-phospholactate and (S)-phosphoglycerate.
Interaction partners:
- Phosphosulfolactate synthase
- L-sulfolactate dehydrogenase
- Ribonuclease P protein component 3
- Probable sulfurtransferase
- Uncharacterized protein MJ0206
Sequence:
MITLCNRFTEYKCGNVAIVVDVLRASTTITTLLSFIDEVYITTSTSKKENAIYIGERKGRKIEGFDFGNSPTEILANKDIIKERYENGEKVILTTTNGTRVLKSLDAEHIFIGAIVNAKYVAKAVEDFEDVSLVPCHRENNFAIDDFIGCGVIAKYLNGEFDEFIKAALELTKHDWMSLILNSSSAENLKNLGYEKDVTFAILENSIDAVGIYKKDKSKVVRFK
Protein: TPR-repeat-containing chaperone protein DNAJ, putative (Q38BB1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEPDDGVASWMELREEGNKAFKSEAYANAVKLYSEAIKLNSKEAALFSNRSAAYIKMKEYQKAVLDAEAAIANDKTFVKGYSRLHNALCHLGRFREATQKLKEALVVLEACGASPEDKKQIQELHRTAEEGQRGFEAGQRLLEERNFLAAERELVKAAQLFPDCAIVGIMLGESQASLYPERVIRSLTALSSAHADDTYYLYVRALASYYSGQSGLNNAQSILRHTIELDPDNRKATELLKKIRAVESQKTEGNAAFKEKRFTAAVNCYKAAIEVDPSNIRMTAVLRGNQAAAKMELKEYSSALLDCDFAIKNGAESAKLYARRSRIHEALENYDDALRDIQRAAEMDPSYNGEAQQMKISAKRAKRKDYYKILGLPQGESDDSSIKRAYKKGCLQWHPDKWAHATEEEKAHAEKMFKEVGEAFSILSDPQKKRLYDSGQLDDASSPGGTSDFPARQADIFQMMNMMFQGGCGEGGMPSGFSFTVDPRSRRQKQTFHYR
Protein: Light-harvesting complex-like protein 3 isotype 1, chloroplastic (LHC-like protein 3 isoform 1) (Q9SYX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Light-harvesting-like protein required for biosynthesis of phytylated chlorophylls and alpha-tocopherol in green seedlings. Functions by anchoring geranylgeranyl reductase (GGR) in the thylakoid membrane, leading to the stabilization of GGR activity. Binds chlrophyll a in the thylakoid membrane (By similarity). Plays a role in the regulation of chlorophyll biosynthesis under light stress and under standard growth conditions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24275650, ECO:0000269|PubMed:25808681, ECO:0000269|PubMed:26320415}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with subcomplexes of LHC antenna of photosystem II. {ECO:0000269|PubMed:25808681}.
Interaction partners:
- Light-harvesting complex-like protein 3 isotype 2, chloroplastic
- Photosystem II 22 kDa protein, chloroplastic
- Chlorophyll a-b binding protein CP26, chloroplastic
- Protein CURVATURE THYLAKOID 1B, chloroplastic
- PsbP-like protein 1, chloroplastic
- ATP synthase gamma chain 1, chloroplastic
- Chlorophyll a-b binding protein 2.2, chloroplastic
- Chlorophyll a-b binding protein 3, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Chlorophyll a-b binding protein 2.1, chloroplastic
Sequence:
MALFSPPISSSSLQNPNFIPKFSFSLLSSNRFSLLSVTRASSDSGSTSPTAAVSVEAPEPVEVIVKEPPQSTPAVKKEETATAKNVAVEGEEMKTTESVVKFQDARWINGTWDLKQFEKDGKTDWDSVIVAEAKRRKWLEENPETTSNDEPVLFDTSIIPWWAWIKRYHLPEAELLNGRAAMIGFFMAYFVDSLTGVGLVDQMGNFFCKTLLFVAVAGVLFIRKNEDVDKLKNLFDETTLYDKQWQAAWKNDDDESLGSKKK
Protein: Periplakin (190 kDa paraneoplastic pemphigus antigen) (195 kDa cornified envelope precursor protein) (O60437)
Organism: Homo sapiens (Human)
Function: Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling.
Subcellular location: Cell junction, desmosome {ECO:0000269|PubMed:9412476}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9412476}. Cell membrane {ECO:0000250|UniProtKB:Q9R269}. Cytoplasm {ECO:0000250|UniProtKB:Q9R269}.
Interaction partners:
- Envoplakin
- Kazrin
- Periaxin
- Neuroblast differentiation-associated protein AHNAK
- Ezrin
- Desmoplakin
- Butyrophilin subfamily 3 member A1
- Desmoglein-1
- Desmoglein-3
- Butyrophilin subfamily 1 member A1
Sequence:
MNSLFRKRNKGKYSPTVQTRSISNKELSELIEQLQKNADQVEKNIVDTEAKMQSDLARLQEGRQPEHRDVTLQKVLDSEKLLYVLEADAAIAKHMKHPQGDMIAEDIRQLKERVTNLRGKHKQIYRLAVKEVDPQVNWAALVEEKLDKLNNQSFGTDLPLVDHQVEEHNIFHNEVKAIGPHLAKDGDKEQNSELRAKYQKLLAASQARQQHLSSLQDYMQRCTNELYWLDQQAKGRMQYDWSDRNLDYPSRRRQYENFINRNLEAKEERINKLHSEGDQLLAAEHPGRNSIEAHMEAVHADWKEYLNLLICEESHLKYMEDYHQFHEDVKDAQELLRKVDSDLNQKYGPDFKDRYQIELLLRELDDQEKVLDKYEDVVQGLQKRGQQVVPLKYRRETPLKPIPVEALCDFEGEQGLISRGYSYTLQKNNGESWELMDSAGNKLIAPAVCFVIPPTDPEALALADSLGSQYRSVRQKAAGSKRTLQQRYEVLKTENPGDASDLQGRQLLAGLDKVASDLDRQEKAITGILRPPLEQGRAVQDSAERAKDLKNITNELLRIEPEKTRSTAEGEAFIQALPGSGTTPLLRTRVEDTNRKYEHLLQLLDLAQEKVDVANRLEKSLQQSWELLATHENHLNQDDTVPESSRVLDSKGQELAAMACELQAQKSLLGEVEQNLQAAKQCSSTLASRFQEHCPDLERQEAEVHKLGQRFNNLRQQVERRAQSLQSAKAAYEHFHRGHDHVLQFLVSIPSYEPQETDSLSQMETKLKNQKNLLDEIASREQEVQKICANSQQYQQAVKDYELEAEKLRSLLDLENGRRSHVSKRARLQSPATKVKEEEAALAAKFTEVYAINRQRLQNLEFALNLLRQQPEVEVTHETLQRNRPDSGVEEAWKIRKELDEETERRRQLENEVKSTQEEIWTLRNQGPQESVVRKEVLKKVPDPVLEESFQQLQRTLAEEQHKNQLLQEELEALQLQLRALEQETRDGGQEYVVKEVLRIEPDRAQADEVLQLREELEALRRQKGAREAEVLLLQQRVAALAEEKSRAQEKVTEKEVVKLQNDPQLEAEYQQLQEDHQRQDQLREKQEEELSFLQDKLKRLEKERAMAEGKITVKEVLKVEKDAATEREVSDLTRQYEDEAAKARASQREKTELLRKIWALEEENAKVVVQEKVREIVRPDPKAESEVANLRLELVEQERKYRGAEEQLRSYQSELEALRRRGPQVEVKEVTKEVIKYKTDPEMEKELQRLREEIVDKTRLIERCDLEIYQLKKEIQALKDTKPQVQTKEVVQEILQFQEDPQTKEEVASLRAKLSEEQKKQVDLERERASQEEQIARKEEELSRVKERVVQQEVVRYEEEPGLRAEASAFAESIDVELRQIDKLRAELRRLQRRRTELERQLEELERERQARREAEREVQRLQQRLAALEQEEAEAREKVTHTQKVVLQQDPQQAREHALLRLQLEEEQHRRQLLEGELETLRRKLAALEKAEVKEKVVLSESVQVEKGDTEQEIQRLKSSLEEESRSKRELDVEVSRLEARLSELEFHNSKSSKELDFLREENHKLQLERQNLQLETRRLQSEINMAATETRDLRNMTVADSGTNHDSRLWSLERELDDLKRLSKDKDLEIDELQKRLGSVAVKREQRENHLRRSIVVIHPDTGRELSPEEAHRAGLIDWNMFVKLRSQECDWEEISVKGPNGESSVIHDRKSGKKFSIEEALQSGRLTPAQYDRYVNKDMSIQELAVLVSGQK
Protein: Phytosulfokine receptor 1 (AtPSKR1) (EC 2.7.11.1) (EC 4.6.1.2) (Guanylate cyclase) (Phytosulfokine LRR receptor kinase 1) (Protein serine-threonine kinase) (Q9ZVR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phytosulfokine receptor with both a serine/threonine-protein kinase activity and a guanylate cyclase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis, somatic embryogenesis, cellular proliferation and plant growth. Involved in plant immunity, with antagonistic effects on bacterial and fungal resistances. Not involved in PSY perception. CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26071421}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- ATPase 1, plasma membrane-type
- Somatic embryogenesis receptor kinase 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- ATPase 2, plasma membrane-type
- Protein-tyrosine sulfotransferase
- Precursor of elicitor peptide 1
- Phytosulfokines 1
- Cyclic nucleotide-gated ion channel 17
- Phytosulfokines 3
- Putative phytosulfokines 4
Sequence:
MRVHRFCVIVIFLTELLCFFYSSESQTTSRCHPHDLEALRDFIAHLEPKPDGWINSSSSTDCCNWTGITCNSNNTGRVIRLELGNKKLSGKLSESLGKLDEIRVLNLSRNFIKDSIPLSIFNLKNLQTLDLSSNDLSGGIPTSINLPALQSFDLSSNKFNGSLPSHICHNSTQIRVVKLAVNYFAGNFTSGFGKCVLLEHLCLGMNDLTGNIPEDLFHLKRLNLLGIQENRLSGSLSREIRNLSSLVRLDVSWNLFSGEIPDVFDELPQLKFFLGQTNGFIGGIPKSLANSPSLNLLNLRNNSLSGRLMLNCTAMIALNSLDLGTNRFNGRLPENLPDCKRLKNVNLARNTFHGQVPESFKNFESLSYFSLSNSSLANISSALGILQHCKNLTTLVLTLNFHGEALPDDSSLHFEKLKVLVVANCRLTGSMPRWLSSSNELQLLDLSWNRLTGAIPSWIGDFKALFYLDLSNNSFTGEIPKSLTKLESLTSRNISVNEPSPDFPFFMKRNESARALQYNQIFGFPPTIELGHNNLSGPIWEEFGNLKKLHVFDLKWNALSGSIPSSLSGMTSLEALDLSNNRLSGSIPVSLQQLSFLSKFSVAYNNLSGVIPSGGQFQTFPNSSFESNHLCGEHRFPCSEGTESALIKRSRRSRGGDIGMAIGIAFGSVFLLTLLSLIVLRARRRSGEVDPEIEESESMNRKELGEIGSKLVVLFQSNDKELSYDDLLDSTNSFDQANIIGCGGFGMVYKATLPDGKKVAIKKLSGDCGQIEREFEAEVETLSRAQHPNLVLLRGFCFYKNDRLLIYSYMENGSLDYWLHERNDGPALLKWKTRLRIAQGAAKGLLYLHEGCDPHILHRDIKSSNILLDENFNSHLADFGLARLMSPYETHVSTDLVGTLGYIPPEYGQASVATYKGDVYSFGVVLLELLTDKRPVDMCKPKGCRDLISWVVKMKHESRASEVFDPLIYSKENDKEMFRVLEIACLCLSENPKQRPTTQQLVSWLDDV
Protein: Uncharacterized protein (Q5A4Z1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Cta3p
Sequence:
MSSHIFKDIQDKENELKTSGIRRKGIISNENAGPLLSKDSNSRQVQQPQQTQQQQQQSKFTNKRIPLGGKNHNSNKLLLNRSQSSLNTKPTTQGITNVKPPSLPKSNSSLGFSVVSDQPTEQQKQLPQPFVVHNEQVLPVKRKLLQDTKDELSQNSKRVKLEKKESNANTFTDSLTKPTQNVLAHVDDLQTTISSKTDQLNSSNLTHNDINRNNVDPVKRNSRLKAIDDLVESHWQDPIETIPETVGAENNNGEQLEELDIKFFSTPNESFDIGDLDENHLANNEQKLSLELDFEDESNVGEIPIIEGIDEEIGLTSDDLDNLLG
Protein: FHF complex subunit HOOK interacting protein 2A (FHIP2A) (Q5W0V3)
Organism: Homo sapiens (Human)
Function: Required for proper functioning of the nervous system.
Interaction partners:
- Protein Hook homolog 3
- Protein Hook homolog 1
Sequence:
MFSKFTSILQHAVEALAPSLPLQEDFVYHWKAITHYYIETSDDKAPVTDTNIPSHLEQMLDILVQEENERESGETGPCMEYLLHHKILETLYTLGKADCPPGMKQQVLVFYTKLLGRIRQPLLPHINVHRPVQKLIRLCGEVLATPTENEEIQFLCIVCAKLKQDPYLVNFFLENKMKSLASKGVPNVISEDTLKGQDSLSTDTGQSRQPEELSGATGMEQTELEDEPPHQMDHLSTSLDNLSVTSLPEASVVCPNQDYNLVNSLLNLTRSPDGRIAVKACEGLMLLVSLPEPAAAKCLTQSTCLCELLTDRLASLYKALPQSVDPLDIETVEAINWGLDSYSHKEDASAFPGKRALISFLSWFDYCDQLIKEAQKTAAVALAKAVHERFFIGVMEPQLMQTSEMGILTSTALLHRIVRQVTSDVLLQEMVFFILGEQREPETLAEISRHPLRHRLIEHCDHISDEISIMTLRMFEHLLQKPNEHILYNLVLRNLEERNYTEYKPLCPEDKDVVENGLIAGAVDLEEDPLFTDISPENTLPNQEWLSSSPPATPDHPKNDGKTEVHKIVNSFLCLVPDDAKSSYHVEGTGYDTYLRDAHRQFRDYCAICLRWEWPGSPKALEKCNLEAAFFEGHFLKVLFDRMGRILDQPYDVNLQVTSVLSRLSLFPHPHIHEYLLDPYVNLAPGCRSLFSVIVRVVGDLMLRIQRIQDFTPKLLLVRKRLLGLEPEGPIIDHITLLEGVIVLEEFCKELAAIAFVKYHASSTP
Protein: UDP-N-acetylglucosamine kinase (EC 2.7.1.176) (UDP-N-acetylglucosamine kinase) (O53701)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ParD-like antitoxin of type II toxin-antitoxin system
- Conserved protein
- VWFA domain-containing protein
- protein adenylyltransferase
- Ribonuclease VapC51
Sequence:
MKRLDLVAGPNGAGKSTFVALTLAPLLPGIVFVNADEIAKQRWPDDPTSHAYQAAQVAADTRARLIDLGRPFIAETVFSHPSKLELIRTARTAGYTVVLHVLVIPEGLAVERVRHRVAAGGHDVPETKIRERHRRLAELVAQAITLADGATVYDNSRLAGPRIVAQFSGGGIIGRACWPSWTPPPLMSRWSNRPETA