wanglab/gogpt-training-data huggingface dataset:
Protein: Chromatin assembly factor 1 p55 subunit (CAF-1 p55 subunit) (CAF-1) (Nucleosome-remodeling factor 55 kDa subunit) (NURF-55) (Q24572)
Organism: Drosophila melanogaster (Fruit fly)
Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.
Subcellular location: Nucleus {ECO:0000269|PubMed:8887645, ECO:0000269|PubMed:9419341}.
Interaction partners:
- Metastasis-associated protein MTA3
- Chromatin-remodeling complex ATPase chain Iswi
- Histone-lysine N-methyltransferase E
- Polycomb protein Su
- Polycomb protein esc
- Polycomb protein esc
- Histone deacetylase HDAC1
- Chromatin assembly factor 1, p105 subunit
- LD06557p
- Inorganic pyrophosphatase
Sequence:
MVDRSDNAAESFDDAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQWLPDVTKQDGKDYSVHRLILGTHTSDEQNHLLIASVQLPSEDAQFDGSHYDNEKGEFGGFGSVCGKIEIEIKINHEGEVNRARYMPQNACVIATKTPSSDVLVFDYTKHPSKPEPSGECQPDLRLRGHQKEGYGLSWNPNLNGYLLSASDDHTICLWDINATPKEHRVIDAKNIFTGHTAVVEDVAWHLLHESLFGSVADDQKLMIWDTRNNNTSKPSHTVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHSFESHKDEIFQVQWSPHNETILASSGTDRRLHVWDLSKIGEEQSTEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWIICSVSEDNIMQVWQMAENVYNDEEPEIPASELETNTA
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (D3ZV15)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Growth factor receptor-bound protein 2
- Adapter molecule crk
- Crk-like protein
- Receptor protein-tyrosine kinase
- SH3 domain-containing kinase-binding protein 1
- Protein sprouty homolog 2
- Proto-oncogene tyrosine-protein kinase Src
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Hepatocyte growth factor receptor
- Proto-oncogene vav
Sequence:
MAGNVKKSSGAGGSGSGGSGAGGLIGLMKDAFQPHHHHHHHLSPHPPCTVDKKMVEKCWKLMDKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKTIVPWKSFRQALHEVHPISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWSSLLRNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYIFRLSCTRLGQWAIGYVTADGNILQTIPHNKPLFQALIDGFREGFYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDSLFMMKELAGAKVERPSSPFSMAPQASLPPVPPRLDLLQQRAPVPASTSVLGTASKASSSSLHKDKPLPIPPTLRDLPPPPPPDRPYSVGTETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLSRPIPKVPVATPNPGDPWNGRELTNRHSLPFSLPSQMEPRADVPRLGSTFSLDTSTTMNSSPVAGPESEHPKIKPSSSANAIYSLAARPLPVPKLPPGEQGDSEEDTEYMTPTSRPVGVQKPEPKRPAETAQSSRACDCDQQIDSCTYEAMYNIQSQALSVAENSACGEGNLATAHTSTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGEPTNFNEGSQVPERPPKPFPRRINSERKASSYQQGGGAMANPAAAAPSPQLSKPRLSASLRSPTDLAAGQVSQSSDHLAL
Protein: Glutamate 5-kinase (EC 2.7.2.11) (Gamma-glutamyl kinase) (GK) (P0A7B5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}.
Interaction partners:
- Gamma-glutamyl phosphate reductase
- Pyrroline-5-carboxylate reductase
- Bifunctional protein PutA
- Amino-acid acetyltransferase
- Acetylglutamate kinase
- N-acetyl-gamma-glutamyl-phosphate reductase
Sequence:
MSDSQTLVVKLGTSVLTGGSRRLNRAHIVELVRQCAQLHAAGHRIVIVTSGAIAAGREHLGYPELPATIASKQLLAAVGQSRLIQLWEQLFSIYGIHVGQMLLTRADMEDRERFLNARDTLRALLDNNIVPVINENDAVATAEIKVGDNDNLSALAAILAGADKLLLLTDQKGLYTADPRSNPQAELIKDVYGIDDALRAIAGDSVSGLGTGGMSTKLQAADVACRAGIDTIIAAGSKPGVIGDVMEGISVGTLFHAQATPLENRKRWIFGAPPAGEITVDEGATAAILERGSSLLPKGIKSVTGNFSRGEVIRICNLEGRDIAHGVSRYNSDALRRIAGHHSQEIDAILGYEYGPVAVHRDDMITR
Protein: Slr1p (A0A1D8PIP0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Nuclear cap-binding protein complex subunit 1
- Nuclear cap-binding protein subunit 2
- Mtr10p
- Protein-arginine omega-N methyltransferase
- RRM domain-containing protein
- mRNA-binding protein
- Poly
- U1 small nuclear ribonucleoprotein component SNU71
- RRM domain-containing protein
- RRM domain-containing protein
Sequence:
MPKNTLYVTGFSRESKAADLAPDFEKYGELVRLDIPPPRSDDGEKYAFVEYKDAESCERALELDGKTLPYSIKDGLVVQVARSDPYRVRQQFSGPRGGYRDGGYGGRGGYRDGGYGGRGGYRDGGYGGRGGYGGGRGGGYGGYRDGGRGGYRDGGRGGYGGYRDGGRGGGYGGYRDGGRGGGYRDGGYRDGGYRDGGRGGYGGGRGGYDRDREEGRGGYDREEDRGGYERDEGREPRVEERRYSRSPSRSPPRRDRSRSPERY
Protein: Desumoylating isopeptidase 1 (DeSI-1) (EC 3.4.-.-) (PPPDE peptidase domain-containing protein 2) (Palmitoyl protein thioesterase DESI1) (EC 3.1.2.22) (Polyubiquitinated substrate transporter) (POST) (S-depalmitoylase DESI1) (Q6ICB0)
Organism: Homo sapiens (Human)
Function: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity (By similarity). Desumoylates ZBTB46 (By similarity). Collaborates with UBQLN4 in the export of ubiquitinated proteins from the nucleus to the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29666234}. Nucleus {ECO:0000269|PubMed:29666234}. Note=Shuttles between the nucleus and the cytoplasm; exported from the nucleus in a XPO1/CRM1-dependent manner via its nuclear export signal motifs. {ECO:0000269|PubMed:29666234}.
Interaction partners:
- Ubiquilin-4
- Ubiquilin-1
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 8
- 26S proteasome regulatory subunit 6B
- 26S proteasome regulatory subunit 6A
- Proteasome subunit alpha type-2
- Bax inhibitor 1
- Proteasome subunit alpha type-7
- 26S proteasome regulatory subunit 7
Sequence:
MEPPNLYPVKLYVYDLSKGLARRLSPIMLGKQLEGIWHTSIVVHKDEFFFGSGGISSCPPGGTLLGPPDSVVDVGSTEVTEEIFLEYLSSLGESLFRGEAYNLFEHNCNTFSNEVAQFLTGRKIPSYITDLPSEVLSTPFGQALRPLLDSIQIQPPGGSSVGRPNGQS
Protein: Myeloid leukemia-associated SET translocation protein (SET nuclear proto-oncogene b) (Q6TGU0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSASAAKVSRKEQNSNHDGADETSEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKAGKDLTKRTGQTPNKAGKKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDEEEGEGEEEDDEEEEEGLEDIDEEGDEDDGEEDEEEDEGEDGEDDGEDD
Protein: Uncharacterized protein (Q385L2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- SAC3/GANP/THP3 conserved domain-containing protein
Sequence:
MMPVFGPPPSPVVMGPAPPPATHPPRNPIYNSVFGAFLSEQQKQAVSPLPSPNRMPFSNFTLGGPENSGTKAEVTGSEISKPVFAAPSATPTLWLQTDTDVGMPAGIDRALPAVRMGTTNTSFPPVFTTQRPQTAGASGGGFLLGADSGPTPAKTGAGSPEADMNASTRMVSPKPSIFTSPPFLKGKPLMPQITQKHTGGDASSTSILGANRPSVFSSKRNFSSMEVSGRSPTLKPVVAGAGSVFADAKRVRGETLECGKGVDAAWSAYGPQQNGGGTFSAAAVRSPAPTGTSVSLFNRSSQMQKQHGGGNTAKIMKVVRVFSSFMINVMNADEAQREVVEEFIEEAFFGTVESHDVDNFPAALRQLQSAWIALKGSQSQLKGERWVVLFALGSHLNVVTRTIQKEEEVNGNEEKEGTKVLGGAVRHDIWNVLSDSCTHANLLCEICLQLFSNQRDNHVPYCILPIVLRRARSVFELACNNGVSTVQSNMRSVLLKLHRYVRVAPPKRQLSTVVEKQRAVAFAALLSEMMLYGSAPPESSAFVEAFHQHCMDAVKIRCALYRHCADNLLQEPLTDSIIVQAMELLARAFVIVDDEAIENKRMLFVKLTACALALGRVPVADFQQAFVATGLEDLIVAVRSCNIRLFNVAMRNNSELYVRCGIHNVLQFVSKRISLLMVVKYYSTCFSDRIQVQDMIDYYQLPYNVSEGCNVWLLPLLVEKRINGVIESGVLILSNANPFDDYSKDAIRAFVE
Protein: Acyl-coenzyme A thioesterase 8 (Acyl-CoA thioesterase 8) (EC 3.1.2.1) (EC 3.1.2.11) (EC 3.1.2.2) (EC 3.1.2.3) (EC 3.1.2.5) (Choloyl-coenzyme A thioesterase) (EC 3.1.2.27) (Peroxisomal acyl-coenzyme A thioester hydrolase 1) (PTE-1) (Peroxisomal long-chain acyl-CoA thioesterase 1) (Q8VHK0)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains. Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (By similarity).
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:11785945}. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:11785945}.
Interaction partners:
- Bile acid-CoA:amino acid N-acyltransferase
- Long-chain fatty acid transport protein 5
- Acyl-coenzyme A amino acid N-acyltransferase 1
- Acyl-coenzyme A amino acid N-acyltransferase 2
- Acyl-CoA thioesterase 5
- Acyl-coenzyme A thioesterase 13
- AN1-type zinc finger protein 2B
- Acyl-CoA thioesterase 9
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-CoA thioesterase 5
Sequence:
MSKPEDLGDANGDADRGDLSGDLRSVLVTSVLNLEPLDEDLYRGRHYWVPTSQRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKVPVLYHVERTRTGASFSVRAVKAVQHGKAIFICQASFQQMQPSPLQHQFSMPTVPPPEELLDHEALIDQYLRDPNLHEKYRVGLNRIAAREVPIEIKLVNPPALNQLQTLEPKQMFWVRARGYIGEGDIKMHCCVAAYISDYAFLGTALLPHQSKYKVNFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRRDGVLAVTCAQEGVIRSKPRVSESKL
Protein: Kinesin 1 cargo adaptor alternative variant a (Kinesin Cargo Adaptor) (G5EBU5)
Organism: Caenorhabditis elegans
Interaction partners:
- Kinesin heavy chain
- Kinesin light chain
- Kinesin light chain
- RING-type domain-containing protein
- Kinesin motor domain-containing protein
- MEiotic SPindle
- RING-type domain-containing protein
- Kinesin-like protein klp-19
- Osmotic avoidance abnormal protein 3
Sequence:
MVRQDAGVMIGEDALSYCSGQSTSDSSFRTMKSTSLSSSWHSMASPHTSDVQGVSFFRPFSWFVWRQTEKDLKKKQDKETVDEIMKCFRNNDVDGMEKFVEKKTRESVSSMKNDEFWWDDDEISYWKHRTTPAQDELPEDHKYTPHPSKGFKLPPRVLKAVRFELDNTPEDRQPRPFTPLYTSTPKNPAINEDGSDDEYSLVPLRYCDSNTVAVPAAVFNNTSSILLDNAVIMTTLNKSREETNEILCKSLNRDFYQLAYVDSEDAEQDHGKPEQSTQNPLCNTYVVHSSEEMSSEPSSSTINLDQANVSDDARSAILGLDRVENAIQRALANQNGPEQGLARQLRERIQSIKKSIDEICSECPNGPEIDTDRVSRESDHDVSADFEDSDWQPHLESDVGSFDECML
Protein: Autophagy-related 8a, isoform A (LD05816p) (Q9W2S2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Cysteine protease
- Ubiquitin-like-conjugating enzyme ATG3
- Cysteine protease
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related 1, isoform B
- Autophagy protein 12-like
- Autophagy protein 5
- BNIP3, isoform A
- Protein ref
- Autophagy-related protein 13 homolog
Sequence:
MKFQYKEEHAFEKRRAEGDKIRRKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRPEDALFFFVNNVIPPTSATMGSLYQEHHEEDYFLYIAYSDENVYGMAKIN
Protein: Cathelicidin-like antimicrobial protein, isoform A (RE49550p) (Q8MRA9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
Sequence:
MALTITKFRTSRGMVVAVQPTVVLSPKIPDSQDNEKKPFSKSEPGNATVRVNAGGIVLNKIPAIIRPSMKRAATTKMTGATAAGATTTTSSTGAVGYPVLKTPKYVVQTSPSGSSGHQLQMLARKDTQSLGVAINSLPPNTIIKATTRPSQTAPLTPNSAAVTPSTPSSSRNSTQSTPTVVPDARVSSAVRQAVFIKRELPQPQRSMRNMTLGLVEQAPLLHLGVAPQHLSLLKRHICRNANVTHLDCCLTLRKLKQNEHFALLAEHFELSESDVEDTFKRTLIKLARYLRPLIRWPDARHHNERFKHTPLNYRANLLHVRSLIECVETDVPIDLGLGSGSYKFILCINTNGIISYVSSAFPGSCDDLQLFEASRFRDVIPNYLTLCAEPGKAVRRARRSGFGDPHDSADEDEAAAEPKRSLTKFEAQRLSGQLASQQSLSVVDGALTSKRAPAIQLPTFNAQEPACRAQMRDMIDYLREFRMLDNSAIKQKSLLGYLDEMIVVAAGLCNLKRQELES
Protein: Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase (EC 2.4.1.256) (Alpha-1,2-glucosyltransferase ALG10-A) (Alpha-2-glucosyltransferase ALG10-B) (Asparagine-linked glycosylation protein 10 homolog B) (Potassium channel regulator 1) (Q5I7T1)
Organism: Homo sapiens (Human)
Function: Putative alpha-1,2-glucosyltransferase, which adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity). When coupled to KCNH2 may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by mediating glycosylation of KCNH2. Has a role in maintenance of cochlear outer hair cell function (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20950623}; Multi-pass membrane protein {ECO:0000255}. Note=Also detected at the plasma membrane. {ECO:0000250|UniProtKB:O88788}.
Interaction partners:
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dol-P-Man:Man
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Sequence:
MAQLEGYCFSAALSCTFLVSCLLFSAFSRALREPYMDEIFHLPQAQRYCEGHFSLSQWDPMITTLPGLYLVSVGVVKPAIWIFAWSEHVVCSIGMLRFVNLLFSVGNFYLLYLLFHKVQPRNKAASSIQRVLSTLTLAVFPTLYFFNFLYYTEAGSMFFTLFAYLMCLYGNHKTSAFLGFCGFMFRQTNIIWAVFCAGNVIAQKLTEAWKTELQKKEDRLPPIKGPFAEFRKILQFLLAYSMSFKNLSMLFCLTWPYILLGFLFCAFVVVNGGIVIGDRSSHEACLHFPQLFYFFSFTLFFSFPHLLSPSKIKTFLSLVWKHGILFLVVTLVSVFLVWKFTYAHKYLLADNRHYTFYVWKRVFQRYAILKYLLVPAYIFAGWSIADSLKSKPIFWNLMFFICLFIVIVPQKLLEFRYFILPYVIYRLNITLPPTSRLVCELSCYAIVNFITFYIFLNKTFQWPNSQDIQRFMW
Protein: LisH domain-containing protein ARMC9 (Q9D2I5)
Organism: Mus musculus (Mouse)
Function: Involved in ciliogenesis (By similarity). It is required for appropriate acetylation and polyglutamylation of ciliary microtubules, and regulation of cilium length (By similarity). Acts as a positive regulator of hedgehog (Hh) signaling. May participate in the trafficking and/or retention of GLI2 and GLI3 proteins at the ciliary tip.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q7Z3E5}. Cell projection, cilium {ECO:0000269|PubMed:29459677}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q7Z3E5}. Note=Localized to the proximal region in cilia. Stimulation of Hh signaling leads to redistribution of ARMC9 toward the ciliary tip within 6 hours, follow by a gradual return to its original proximal location (PubMed:29459677). Localizes to the daughter centriole of the primary cilium in RPE1 cells (By similarity). {ECO:0000250|UniProtKB:Q7Z3E5, ECO:0000269|PubMed:29459677}.
Interaction partners:
Sequence:
MGDILAHESELLGLVKEYLDFAEFEDTLKTFSKECKVKGKPLCKNVGGPLKKDSKSLVIQRDLVAAFDSGDQKAFFDLWEGHIPSSVRDTDSLAQKLEFYLHIHFAIYLLKYCRGRPDKQELDKRISYFKTYLETKGAALSQTTEFLPFYALPFVPNPMVHPSFKELFQDSWTPELKLKLEKFLALTFKANNTPKLLTIYKENGPNSKELLQQLHQQLVEAERRAMTYLKRYNKIQADYHNLIGVTAELVDSLEATVSGKMITPEYLQSVCVRLFSNQMRQSLAHSVDFTRPGTASTMLRASLAPEKLKDVPLLPSLDYEKLKKDLIWGSDRLKAFLLQALRWRLTTSHPGEQRETVLQAYISNDLLDCHSHNQRSVLQLLHSKSEAVRQYMARLINALASLAEGRLYLAQNTKVLRMLEGRLKEEDKDVITRENVLGALQKFSLRRPLQTAMIRDGLIFWLIDLLKDPDCLSDYTLEYSVALLMNLCLRSAGKNMCAKVAGLMLKVLSDLLGHENHEIQPYVNGALYSILSIPSIREEARAMGMEDILRCFIKEGNAEMIRQIEFIIKQLNSEDLLDGVLESDDDEDEDDEEDHDIMEADLDKDELIQPQLGELSGEKLLTTEYLGIMTNTGKARRKGPASVQWSGDEPLRRPVTPGGHRTGCPVLGDHLISPQNAQQARNGCLRAMPVAHPDDYKEGKPGVTGCGTSSSFMDHKPREWSPAGHQKSRLVPTAALGWPREMTQDPSSGHITREFVPAFTCKPQVPSTPETVEQNPLKAKALSLAPQFSSSGPQQASRPASTASSTRGLHSSQSIRK
Protein: Uncharacterized vacuolar protein YLR297W (Q05899)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative vacuolar protein sorting-associated protein TDA6
- Uncharacterized protein YER053C-A
- SVF1-like protein YDR222W
- Interacting with cytoskeleton protein 1
- Zinc finger protein STP4
Sequence:
MVEGDFVDEQSNIALLSSKSMCGDHHSVKNSIGDEIFKLLTKILNSDEKASGDVHTLVSGTPDLSNFNLDNEPLENILAVFIISFIIVVVGVLLLGLIGMIFISLRSGSSNDKKLQSNDEEKQALAEKA
Protein: Rac-like GTP-binding protein 6 (GTPase protein RacB) (OsRac6) (Q6ZHA3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with the membrane when activated.
Interaction partners:
- Expressed protein
- Os10g0372500 protein
- Os05g0392050 protein
- Os05g0392000 protein
- Dol-P-Glc:Glc
- Uncharacterized protein Os04g0629400
- Protein LOL5
- Os02g0719000 protein
- Os06g0318300 protein
- Os01g0913600 protein
Sequence:
MSASRFIKCVTVGDGAVGKTCMLISYTSNTFPTDYVPTVFDNFSANVVVDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLISKASYENVSKKWIPELKHYAPGVPIILVGTKLDLRDDKQFFVDHPGAVPITTAQGEELRKQIGAPYYIECSSKTQLNVKGVFDAAIKVVLQPPKAKKKKKAQRGACSIL
Protein: ATP-citrate synthase beta chain protein 2 (ATP-citrate synthase B-2) (EC 2.3.3.8) (ATP-citrate lyase B-2) (Citrate cleavage enzyme B-2) (Q9FGX1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. n contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12376641}.
Interaction partners:
- ATP-citrate synthase alpha chain protein 1
- ATP-citrate synthase alpha chain protein 2
- ATP-citrate synthase alpha chain protein 3
- Citrate synthase 2, peroxisomal
- Citrate synthase 4, mitochondrial
- Citrate synthase 3, peroxisomal
- Citrate synthase 5, mitochondrial
- Citrate synthase 1, peroxisomal
- Aconitate hydratase 2, mitochondrial
- Aconitate hydratase 1
Sequence:
MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHAAIEAACAAHPTADVFINFASFRSAAASSMAALKQPTIKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTIDNIIQCKLYRPGSVGFVSKSGGMSNEMYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEGKVNKPVVAWVSGTCARLFKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKETFEKLVEEGKVSPIKEVIPPQIPEDLNSAIKSGKVRAPTHIISTISDDRGEEPCYAGVPMSSIIEQGYGVGDVISLLWFKRSLPRYCTKFIEICIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDACDRNLTPYEFVEGMKKKGIRVPGIGHRIKSRDNRDKRVELLQKFARSNFPSVKYMEYAVTVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDEIVQIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK
Protein: Disease resistance protein CHS1 (EC 3.2.2.6) (Protein CHILLING SENSITIVE 1) (F4I902)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Confers resistance to low temperatures by limiting chloroplast damage and cell death, thus maintaining growth homeostasis. Regulates steryl-esters and sterols accumulation. Limits leaf necrosis associated with virulent bacterial infection (e.g. Pseudomonas syringae pv. tomato DC3000).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23617639, ECO:0000269|PubMed:23651299}. Nucleus {ECO:0000269|PubMed:23651299}.
Interaction partners:
- U-box domain-containing protein 44
- Exocyst complex component EXO70B1
- Probable disease resistance protein At5g04720
- Protein LSD1
- Probable disease resistance protein At4g33300
- Naringenin,2-oxoglutarate 3-dioxygenase
- Chalcone--flavanone isomerase 1
- Dihydroflavonol 4-reductase
- Leucine-rich repeat
Sequence:
MSTSYSFLLAGRELDVFLSFSGKIALDVDFGYDLSRNGIKAFKSESWKESSFKPIDLRTLEALTESKVAVVMTSDEEVSSVGFLEELIVIIEFQEKRSLTVIPVFLTKHPLDVEKVSQIFPERAKIWRTAIAKLDNIAAQYSFSRNLAVMHGTHRIKQIADDIRLMFLSSASSDFKGLAGMDRHMKALYALLALESDEKVRTIGIWGSSGVGKTTLARYTYAEISVKFQAHVFLENVENMKEMLLPSENFEGEDLRSVNHEMNEMAEAKQKHRKVLLIADGVNNIEQGKWIAENANWFAPGSRVILITQEKSLLVQSGVNHVYEVGSLRYDEALQLFSRFAFKQPYPSPDFERLSVRAVQLAGFLPVTIRLFGSFLTGRDKEEWEATLLKLNAKQGKDIKEVWKIMEALEDKDIVEASQR
Protein: ATP-grasp domain-containing protein (Synapsin) (G5EGI2)
Organism: Caenorhabditis elegans
Subcellular location: Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MKDAKVLLVIDSHHVDWSKYFRNHTEYAIRVEQGDIDELDVMCTEKNCTVELNTPGKDVRTFTPSAVFLGAGATRCAQLKTITRAFIAAHIPFLNSHTSAVAFLDRNNLKKQLKKITLSDGASIPMLPIVHYPHFHKFHQSQSSTYPMVVSVNEGFQGIGKIKVNNHEELCDVEGMLQIMSKGDTEVEVQPFVDAKYDLHIQKIGHEYKTFIRRGICKHWKSNVGSSVLEQISTCERHKKYLKAITDHVGPMHICSIDILVSKEGREFVHDVNDVIAYFGESAEDDRRAASLLLRALVAPRITSPIAAEPPATSPTTSAVTNGHGNHGPAPAVPTRRLPPHPSSSSAAPPRGHMSDKVESRHKDHYDPPPQIPRTGSRESVSYVDDTMGQLKRTFAGFFGE
Protein: Cytochrome P450 81F3 (EC 1.14.-.-) (Q0WTF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in indole glucosinolate biosynthesis. Catalyzes hydroxylation reactions of the glucosinolate indole ring. Converts indol-3-yl-methylglucosinolate (I3M) to 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and/or 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) intermediates. These hydroxy intermediates are converted to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) and 1-methoxy-indol-3-yl-methylglucosinolate (1MO-I3M) by indole glucosinolate methyltransferase 1 and 2 (IGMT1 and IGMT2).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Indole glucosinolate O-methyltransferase 1
- Indole glucosinolate O-methyltransferase 2
- Flavin-containing monooxygenase FMO GS-OX5
- Flavin-containing monooxygenase FMO GS-OX2
- Cytosolic sulfotransferase 16
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Probable 2-oxoacid dependent dioxygenase
- Cytosolic sulfotransferase 18
- Transcription factor MYB28
- Transcription factor MYB29
Sequence:
MFYYVIVLPLALFLLAYKLFFTSKTKRFNLPPSPPYSLPILGHHNLLKPPVHRLFHRLSKTHGPIFSLQFGSRRAVVISSSSLATQCFTGQNDIILSNRPCFLTAKYVAYNYTTVGTAPYGDHWRNLRRICSLEILSSNRLTNFLHIRKDEIHRMLTRLSRDVNKEIELEPLLSDLTFNNIVRMVTGKRYYGDEVHNEEEANVFKKLVADINDCSGARHPGDYLPFMKMFGGSFEKKVKALAEAMDEILQRLLEECKRDKDGNTMVNHLLSLQQNEPEYYTDVTIKGLMLGMMIAGTDTSAVTLEWAMSSLLNHPEALEKAKLEIDEKIGQERLIDEPDIANLPYLQNIVSETFRLYPAAPLLVPRSPTEDIKVGGYDVPRGTMVMVNAWAIHRDPELWNEPEKFKPERFNGGEGGGRGEDVHKLMPFGNGRRSCPGAGLGQKIVTLALGSLIQCFDWQKVNGEAIDMTETPGMAMRKKIPLSALCQSRPIMSKLQAHLKG
Protein: F-actin-capping protein subunit alpha-3 (CapZ alpha-3) (CP-alpha-3) (Germ cell-specific protein 3) (Q96KX2)
Organism: Homo sapiens (Human)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the morphogenesis of spermatid (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A0PFK5}.
Interaction partners:
- F-actin-capping protein subunit beta
- Tropomodulin-4
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit alpha-2
- Myotrophin
Sequence:
MTLSVLSRKDKERVIRRLLLQAPPGEFVNAFDDLCLLIRDEKLMHHQGECAGHQHCQKYSVPLCIDGNPVLLSHHNVMGDYRFFDHQSKLSFKYDLLQNQLKDIQSHGIIQNEAEYLRVVLLCALKLYVNDHYPKGNCNMLRKTVKSKEYLIACIEDHNYETGECWNGLWKSKWIFQVNPFLTQVTGRIFVQAHFFRCVNLHIEISKDLKESLEIVNQAQLALSFARLVEEQENKFQAAVLEELQELSNEALRKILRRDLPVTRTLIDWHRILSDLNLVMYPKLGYVIYSRSVLCNWII