wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquilin-2 (Chap1) (DSK2 homolog) (Protein linking IAP with cytoskeleton 2) (PLIC-2) (Ubiquitin-like product Chap1/Dsk2) (Q9QZM0)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS), autophagy and the endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome. Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion. Negatively regulates the endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically reducing the rate at which receptor-arrestin complexes concentrate in clathrin-coated pits (CCPs) (By similarity). Links CD47 to vimentin-containing intermediate filaments of the cytoskeleton.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10549293}. Nucleus {ECO:0000269|PubMed:10549293}. Membrane {ECO:0000269|PubMed:10549293}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9UHD9}. Note=Colocalizes with a subset of proteasomes, namely those that are cytoskeleton associated or free in the cytosol. Associated with fibers in mitotic cells. {ECO:0000250|UniProtKB:Q9UHD9}.
Interaction partners:
- Desumoylating isopeptidase 1
- RNA-binding protein FUS
- TAR DNA-binding protein 43
- Transitional endoplasmic reticulum ATPase
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Ubiquitin conjugation factor E4 B
- Proteasomal ubiquitin receptor ADRM1
- Guanine nucleotide exchange factor C9orf72 homolog
- Epidermal growth factor receptor substrate 15
Sequence:
MAENGESSGPPRPSRGPAAAPGAASPPAEPKIIKVTVKTPKEKEEFAVPENSTVQQFKEAISKRFKSQTDQLVLIFAGKILKDQDTLMQHGIHDGLTVHLVIKSQNRPQGQATTQPSTTAGTSTTTTTTTTAAAPAATTSSAPRSSSTPTTTNSSSFGLGSLSSLSNLGLNSPNFTELQNQMQQQLLASPEMMIQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHLLNNPDIMRQTLEIARNPAMMQEMMRNQDLALSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFATVGSSSTSGEGTQPSRTENRDPLPNPWAPPPTTQTAATTTTTTTTSSGSGSGSSSSSTTAGNTMAAANYVASIFSTPGMQSLLQQITENPQLIQNMLSAPYMRSMMQSLSQNPDMAAQMMLSSPLFTSNPQLQEQMRPQLPNFLQQMQNPETIAAMSNPRAMQALMQIQQGLQTLATEAPGLIPSFAPGVGMGVLGTAITPVGPVTPIGPIGPIVPFTPIGPIGPIGPTGPASSPGSTGTGIPPATTVSSSAPTETISPTSESGPNQQFIQQMVQALTGGSPPQPPNPEVRFQQQLEQLNAMGFLNREANLQALIATGGDINAAIERLLGSQPS
Protein: Metallothionein-2 (MT-2) (Metallothionein-2A) (Metallothionein-II) (MT-II) (P02795)
Organism: Homo sapiens (Human)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Interaction partners:
- Metallothionein-1X
- Metallothionein
- Protein EOLA1
- Metallothionein-1H
- Metallothionein-1G
- Metallothionein-1F
- Quinone oxidoreductase-like protein 1
- Metal-response element-binding transcription factor 2
- Apolipoprotein D
- Cystatin-B
Sequence:
MDPNCSCAAGDSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA
Protein: Transcription factor (Q9C6K4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable transcription factor At3g04930
- Transcription factor STKL1
- B3 domain-containing protein At5g60142
- Sequence-specific DNA binding transcription factor
- Trihelix transcription factor ASIL2
- GLABROUS1 enhancer-binding protein
- Protein YIP
- Protein YIP
- Protein YIP
- Protein LOL2
Sequence:
MEGNCSQGRFDSQVSSMRDLRPNAINQNQKQHHPNSRQDSGFNNTMDTRHNNVDRGKKSMSEDDELCLLSSDGQNKSKENSPWQRVKWMDKMVKLMITALSYIGEDSGSDKKFAVLQKKGKWRSVSKVMDERGYHVSPQQCEDKFNDLNKRYKKLNEMLGRGTSCEVVENPSLLDKIDYLNEKEKDEVRRIMSSKHLFYEEMCSYHNGNRLHLPHDPAVQRSLHLITLGSRDDHDNDEHGKHQNEDLDDDDDYEEDHDGALSDRPLKRLRQSQSHEDVGHPNKGYDVPCLPRSQADVNRGISLDSRKAAGLQRQQIESKSLELEGRKLQIQAEMMELERQQFKWEVFSKRREQKLAKMRMENERMKLENERMSLELKRIELGAKL
Protein: Dolichol kinase (EC 2.7.1.108) (P20048)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the synthesis of the sugar donor Dol-P-Man which is required in the synthesis of N-linked and O-linked oligosaccharides and for that of GPI anchors. It is required for spore germination. Has an essential role in cellular metabolism.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2657387}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase
- Dolichyldiphosphatase
- Polyprenal reductase
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Dehydrodolichyl diphosphate synthase complex subunit RER2
- Phosphomannomutase
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Lipid phosphate phosphatase 1
- Dehydrodolichyl diphosphate synthase complex subunit SRT1-farnesyl diphosphate specific))
Sequence:
MVAIIPHASFTTIKLTQKTEGSQMPTEEICKINMRTRKFDVGGNSRDFECFYSNFVQTVILLGTFFYCVERLQPWSIVTADISYKQIFVNVFVVCLIMVGLIFTKYWQHGYKSLPKFDTIYSLYLPFMVSLLFDTSSTVINTILILSVLNSYRWRTQLVVIILQLCLIFFNFEAGDRLKNIISIVINSLLSLILKYIGQLKSLDNIDSNLFSILLTNILYVSEAGTVHFRILKGIILALTTIISINYVLKKVMHFKPFMLSISFAIGLPLFANTFIHLEDGENPLLWLVKYILESTIRQKILFAWSSILILSIPSILIEKDSLSLNTSRKLWHFIIFLLIIPSFQMDSNFVKIALSGTIPVFLSIEYIRFQNLPPLGSAIELQLRRFADDRDHSGPLIISYLYLLFGISTPLLMNNSPMGLIGLGIGDSLASIIGKRYGRIRWKGTQKTLEGTLAFIVTSFIVCLVLLRFDKAAIFNHLTTLQLLTLCTLSGVLEGNSVLNDNILIPAFMMICEKLITL
Protein: Calpain-like protein, putative calpain-like cysteine peptidase, Clan CA, family C2 (Q4GZ06)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGLFLSKQGEGQLLAEPTMQSTIQVPLFNGLLYRLVDEADGTIGFFNNSKDYEFHVTYLFSANSLIEPLDKATAAQQDDGILCEVTIYPLETQRFVKGEITGYESKIDALLLSDDYFRLNEDRNPERYFRHTGPFKATSF
Protein: Floral homeotic protein DEFICIENS (P23706)
Organism: Antirrhinum majus (Garden snapdragon)
Function: Transcription factor involved in the genetic control of flower development. Acts in conjunction with GLOBOSA (glo).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MARGKIQIKRIENQTNRQVTYSKRRNGLFKKAHELSVLCDAKVSIIMISSTQKLHEYISPTTATKQLFDQYQKAVGVDLWSSHYEKMQEHLKKLNEVNRNLRREIRQRMGESLNDLGYEQIVNLIEDMDNSLKLIRERKYKVISNQIDTSKKKVRNVEEIHRNLVLEFDARREDPHFGLVDNEGDYNSVLGFPNGGPRIIALRLPTNHHPTLHSGGGSDLTTFALLE
Protein: Signal peptidase complex subunit 2 (Microsomal signal peptidase 25 kDa subunit) (SPase 25 kDa subunit) (Q9XWW1)
Organism: Caenorhabditis elegans
Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q28250}.
Interaction partners:
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
- Signal peptidase complex catalytic subunit SEC11
- Golgi resident protein GCP60
- Translocon-associated protein subunit delta
- Mitochondrial inner membrane protease subunit 2
- Peptidase S26 domain-containing protein
- Signal recognition particle subunit SRP68
- Eukaryotic translation initiation factor 5A-2
- J domain-containing protein
Sequence:
MTDEPVKVVNKWDGPTVKNALDEVVKKILNDKVGWTESHNLMNLRLLISFIGVAFSAFACGYDYYEPFPKSKIVLAVCSVSYFICMGILQMYQWYVEKDCIYEATEVDGKQSRKWAWSSEIKAHDDKYTLSAEFKKEGRSGQGKITKSIGAYIDNDGEIIVPLVKKEVDDLYNRLIRSEQ
Protein: Cytochrome P450 (EC 1.14.14.1) (D4A820)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368053}. Microsome membrane {ECO:0000256|RuleBase:RU368053}.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 2E1
- Epoxide hydrolase 1
- Cytochrome P450 2F2
- Cytochrome P450 3A18
- Cytochrome P450 3A1
- Cytochrome P450 3A9
- Cytochrome P450 4A12
- Cytochrome P450 4A10
Sequence:
MEAASTWALLLALLLLLLALTLPRTPARGQLPPGPTPLPLLGNLLQLRPGALYSGFLRLSKKYGPVFTVHLGPWRRVVVLVGHDAIREALGGQAEEFSGRGTLATLDKTFDGHGVFFANGERWKQLRKFTLLALRDLGMGKREGEELIQEEVQNLVKAFQRTEGRPFNPSMLLAQATSNVVCSLIFGIRLPYEDKEFQAVIQAASGTLLGISSPWGQAYEMFSWLLQPLPGPHTQLQHHLGTLAAFTIQQVQRHQGRSHTSGPARDVVDAFLQKMAQEKEDPGTEFTEKNLLMTVTYLLFAGTMTIGATIRYALLLLLKYPQVQKRVREELIQELGPSRTPSLSDRVRLPYTDAVLHEAQRLLALVPMGMPHTVTKTTSFRGYTLPKGTEVFPLIGSVLHDPAVFRNPEEFHPSRFLDDDGRIRKHEAFLPYSLGKRVCLGEGLARAELWLFFTSILQAFSLDTPCPPGDLSLKPAVRGLFNIPPDFQLQVWPTGDQSR
Protein: Scarecrow, isoform F (A8Y527)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MANPYAMGTLYHSPGVQTYCGPTDNLSLAGHYTDMRNSASWYGSTANDPRFAISRLMSSSASGTMSHMGNMSGLAACSVSDSKPLQFPLAQRRKRRVLFTQAQVYELERRFKQQRYLSAPEREHLASLIHLTPTQVKIWFQNHRYKCKRQAKEKAMAEQNQHNQPASSPRRVAVPVLVKDGKPCSGNNSSSQSQQHGTNSTSAGNNTGSANNGNANSGIVSVTANVSGGLNLITGDAPNSHSPDTSSSLLASYGTVGGSNVAMLQQPCNNTLMSNSLAMAYRNQNNFISNGHQQQCGGYLPLQGRAW
Protein: Nascent polypeptide-associated complex subunit alpha (NAC-alpha) (Alpha-NAC) (Q6FJD5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. EGD2 may also be involved in transcription regulation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic, may also transiently localize to the nucleus. {ECO:0000250}.
Interaction partners:
- Nascent polypeptide-associated complex subunit beta
- YL17
- 60S ribosomal protein L13
- 60S ribosomal protein L8
- Candida glabrata strain CBS138 chromosome K complete sequence
- 60S ribosomal protein L20
- Candida glabrata strain CBS138 chromosome M complete sequence
- L2
- Candida glabrata strain CBS138 chromosome M complete sequence
- Large ribosomal subunit protein uL23
Sequence:
MAEIPEGANVTILNRNEKKARELISKLGLKKVPGIIRVTFRKKDNQIFAIEKPEVFRSVGGNYVVFGEAKVDNFTQRLAAAQQQAQSQTATKTPEDIQADMQAAAVANENKTEGDAAEEDVDAGDLSNDDIDLVVQQTNATKGQAIKALKEHNGDIVNAIMSLSK
Protein: OSJNBa0042L16.11 protein (Q7XT88)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MASLAMLVNLSPRAHLMKLIMSSWIFWQTDKATIVEATINYIKNLQDKIHKMEMLKVEREHAIALATAATATAAASADTALQAPPPSEEENEEHDSVVAAATREMALADMVHAWEQQQEAAATGGSHGGHAVPPPPPAASLQTWTGPNMTASLTGDDGFITLSLPHQGGQKNLVAGAVSVLERHHIDVVTATVSASEQGDNLISLHCHLSPGSSSSQNLTPLDKFKLAMSELMLWVISV
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (Q86BK8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004438}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004438}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004438}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004387}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004387}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004387}.
Interaction partners:
- Rab GDP dissociation inhibitor
- Rab proteins geranylgeranyltransferase component A
- non-specific serine/threonine protein kinase
- Kinesin-like protein Klp98A
Sequence:
MSKVRSVVNKLHERIDYFIEKCPNMTAAPYNYNYIFKYIIIGDMGVGKSCLLHQFTEKKFMANCPHTIGVEFGTRIIEVDDKKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDTRNLTNPSTVIFLIGNKSDLESTREVTYEEAKEFADENGLMFLEASAMTGQNVEEAFLETARKIYQNIQEGRLDLNASESGVQHRPSQPSRTSLSSEATGAKDQCSC
Protein: Two-component response regulator, ParR (Q9I2U3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- histidine kinase
- Sensor protein kinase PmrB
- Two-component sensor PhoQ
- Sensor protein
- histidine kinase
- histidine kinase
- histidine kinase
- Sensor protein
- histidine kinase
- histidine kinase
Sequence:
MDCPTLSKVLLVEDDQKLARLIASFLSQHGFEVRQVHRGDAAFAAFLDFKPQVVVLDLMLPGQNGLQVCREIRRVANLPILILTAQEDDLDHILGLESGADDYVIKPIEPPVLLARLRALMRRHAPLPASPESLTFGKLNIDRRRREAELEGLGIELTTMEFELLWLLASQAGEILSRDEILNQIRGIGFDGLNRSVDVCISKLRNKLKDNPREPVRIKTVWGKGYLFNPLGWEL
Protein: Lysine-rich arabinogalactan protein 17 (Lys-rich AGP 17) (O22194)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- 5'-3' exoribonuclease 2
- 5'-3' exoribonuclease 3
- Non-classical arabinogalactan protein 30
- 5'-3' exoribonuclease 4
- Hydroxyproline-rich glycoprotein family protein
- Probable UDP-arabinopyranose mutase 5
- Arabinogalactan protein 20
- Fasciclin-like arabinogalactan protein 17
- Arabinogalactan protein 16
- Isovalerate--CoA ligase AAE2
Sequence:
MTRNILLTVTLICIVFITVGGQSPATAPIHSPSTSPHKPKPTSPAISPAAPTPESTEAPAKTPVEAPVEAPPSPTPASTPQISPPAPSPEADTPSAPEIAPSADVPAPALTKHKKKTKKHKTAPAPGPASELLSPPAPPGEAPGPGPSDAFSPAADDQSGAQRISVVIQMVGAAAIAWSLLVLAF
Protein: Forkhead box O3 (D3ZBQ1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
- Cyclin-dependent kinase 2
- RAC-alpha serine/threonine-protein kinase
- NAD-dependent protein deacetylase sirtuin-1
- Catenin beta-1
- Mothers against decapentaplegic homolog 2
- Hypoxia-inducible factor 1-alpha
- Focal adhesion kinase 1
- Transcription factor E2F1
- NAD-dependent protein deacetylase
- RAC-beta serine/threonine-protein kinase
Sequence:
MAEAPASPVPLSPLEVELDPEFEPQSRPRSCTWPLQRPELQASPAKPSGETAADSMIPEEDDDEDDEDSGGRGSSAMVIGGGVSSALGSGLLLEDSARLLSPGGQDLGTGPASSAGALSGGTQTQLQPQQPLPPPQPGAAGGSGQPRKCSSRRNAWGNLSYADLITRAIESSPDKRLTLSQIYEWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFMRVQNEGTGKSSWWIINPDGGKSGKAPRRRAVSMDNSNKYTKSRGRAAKKKAALQAAPESADDSPSQLSKWPGSPTSRSSDELDAWTDFRSRTNSNASTVSGRLSPILASTELDDVQDDDGPLSPMLYSSSASLSPSVSKPCTVELPRLTDMAGTMNLNDGLAENLMDDLLDNIALPPSQASPPGGLMQRSSSFPYTAKSSGLGSPTSSFNSTVFGPASLNSLRQSPMQTIQENRPATFSSVSHYGNQTLQDLLTSDSLSHSDVMMTQSDPLMSQASTAVSAQNARRNVMLRNDPMMSFAAQPTQGSLVNQNLLHHQHQTQGALGGSRALSNSVSNMGLSDSSSLGSAKHQQQSPVSQSMQTLSDSLSGSSLYSASANLPVMGHDKFPSDLDLDMFNGSLECDMESIIRSELMDADGLDFNFDSLISTQNVVGLNVGNFTGAKQASSQSWVPG
Protein: Adenylosuccinate synthetase, chloroplastic (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase) (Q96529)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Inosine-5'-monophosphate dehydrogenase 1
- AICARFT/IMPCHase bienzyme family protein
- Inosine-5'-monophosphate dehydrogenase 2
- AMP deaminase
- Hypoxanthine phosphoribosyltransferase
- Argininosuccinate synthase, chloroplastic
- Inosine triphosphate pyrophosphatase
- Asparagine synthetase 1
Sequence:
MSLSSLTLDSNPRFAVGGPYHRRYPPLHHPRSFVSCSAKRPAVSASLSVAADSAATESLGRIGSLSQVSGVLGCQWGDEGKGKLVDILAQHFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILNEDTTCVIGNGVVVHLPGLFKEIDGLESNGVSCKGRILVSDRAHLLFDFHQEVDGLRESELAKSFIGTTKRGIGPAYSSKVIRNGIRVGDLRHMDTLPQKLDLLLSDAAARFQGFKYTPEMLREEVEAYKRYADRLEPYITDTVHFINDSISQKKKVLVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGIAPSVVGDLIGVVKAYTTRVGSGPFPTENLGTGGDLLRLAGQEFGTTTGRPRRCGWLDIVALKFSCQINGFASLNLTKLDVLSDLNEIQLGVAYKRSDGTPVKSFPGDLRLLEELHVEYEVLPGWKSDISSVRNYSDLPKAAQQYVERIEELVGVPIHYIGIGPGRDALIYK
Protein: Pectinesterase/pectinesterase inhibitor 3 (Protein OVERLY ZINC SENSITIVE 2) [Cleaved into: Pectinesterase 3 of 42 kDa; Pectinesterase 3 of 38 kDa] [Includes: Pectinesterase inhibitor 3 (Pectin methylesterase inhibitor 3); Pectinesterase 3 (PE 3) (EC 3.1.1.11) (Pectin methylesterase 27) (AtPME27) (Pectin methylesterase 3) (AtPME3)] (O49006)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:15593128}. Secreted, cell wall {ECO:0000269|PubMed:26183897}. Note=Present in hypocotyl cell walls. {ECO:0000269|PubMed:26183897}.
Interaction partners:
- Probable pectate lyase 13
- Probable pectate lyase 20
- Pectin lyase-like superfamily protein
- Pectinesterase inhibitor 1
- Pectinesterase inhibitor 2
- Probable pectate lyase 8
- Protein kinase superfamily protein
- Pectate lyase
- Pectin lyase-like superfamily protein
- Pectate lyase
Sequence:
MAPSMKEIFSKDNFKKNKKLVLLSAAVALLFVAAVAGISAGASKANEKRTLSPSSHAVLRSSCSSTRYPELCISAVVTAGGVELTSQKDVIEASVNLTITAVEHNYFTVKKLIKKRKGLTPREKTALHDCLETIDETLDELHETVEDLHLYPTKKTLREHAGDLKTLISSAITNQETCLDGFSHDDADKQVRKALLKGQIHVEHMCSNALAMIKNMTDTDIANFEQKAKITSNNRKLKEENQETTVAVDIAGAGELDSEGWPTWLSAGDRRLLQGSGVKADATVAADGSGTFKTVAAAVAAAPENSNKRYVIHIKAGVYRENVEVAKKKKNIMFMGDGRTRTIITGSRNVVDGSTTFHSATVAAVGERFLARDITFQNTAGPSKHQAVALRVGSDFSAFYNCDMLAYQDTLYVHSNRQFFVKCLIAGTVDFIFGNAAVVLQDCDIHARRPNSGQKNMVTAQGRTDPNQNTGIVIQKCRIGATSDLQSVKGSFPTYLGRPWKEYSQTVIMQSAISDVIRPEGWSEWTGTFALNTLTYREYSNTGAGAGTANRVKWRGFKVITAAAEAQKYTAGQFIGGGGWLSSTGFPFSLGL
Protein: Expansin-A5 (AtEXPA5) (Alpha-expansin-5) (At-EXP5) (AtEx5) (Ath-ExpAlpha-1.4) (Q38864)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Subcellular location: Secreted, cell wall. Membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MGVLVISLLVVHLLAFSVCVQGGYRRGGHHPGGHMGPWINAHATFYGGGDASGTMGGACGYGNLYSQGYGLETAALSTALFDQGLSCGACFELMCVNDPQWCIKGRSIVVTATNFCPPGGACDPPNHHFDLSQPIYEKIALYKSGIIPVMYRRVRCKRSGGIRFTINGHSYFNLVLVTNVGGAGDVHSVSMKGSRTKWQLMSRNWGQNWQSNSYLNGQSLSFVVTTSDRRSVVSFNVAPPTWSFGQTYTGGQFRY
Protein: Cilia- and flagella-associated protein 58 (B2RW38)
Organism: Mus musculus (Mouse)
Function: Has an essential role in the assembly and organization of the sperm flagellar axoneme. Required for the elongation of the primary cilium and sperm flagellar midpiece via modulation of the Notch signaling pathway.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:A8HUA1}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:32791035}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:31904090}. Note=Localized to the entire flagellum and predominantly concentrated in the midpiece. Co-localizes with ODFP2 at the centrosome. {ECO:0000269|PubMed:31904090, ECO:0000269|PubMed:32791035}.
Interaction partners:
- Cilia- and flagella-associated protein 43
- Tetratricopeptide repeat protein 29
- Cilia- and flagella-associated protein 61
Sequence:
MTEDKAEKVMPEETAFEEIEKDFQEVLSELSGDKSLEKFRTEYEKLHSIMKKSYENEKRLMAKCRELNAEIVVNSAKVATALKLSQDDQTTIASLKKEIEKAWKMVDSAYDKEQKAKETILALKEEIVNLTKLVEQGSGLSMDQDSNIRDLLKFKEEVTKERDQLLSEVVKLRENLAQTIEKQQAAEHAKEEAEMAISQFQQEIQHRQNEASRESRKKEKLEKELRQIQTDMDGRQAEIKAMQQYMHKSKEELQRLEQQLKEQKILNERAAKEVEQFQMRNAKLQQENDQHTLTCEQLSQENQQKALELKAKEDEIHQMRLDLGKLNKIREQIHKKLHQLDDQKAEVEQQKDTLKNQILGLEREVESSKKQAELDKKAMEELLRERDILNKNMLKAVSATQKQVDLVKLHEQAKKNLEEEIQNYKDEAQKQRKIIFQLEKERDRYINEASDLTQRVLANMEDIKVREIQIFDYRKKIAESETKLKQQQNLYEAVRSDRNLYSKNLVEAQDEITEMKRKLKIMTHQVDQLKEEISAKEAALVKLHLEQQRIEKEKETLKAELQKLRQQALETKHFIEKQEVEERKLLRIIAEADGERVRQKKELDQVISERDILGSQLVRRNDELALLYEKIKIQQSVLNKGETQYNQRVEDMRILKLEIKKLRREKGILARSVANVEELRQELYHMQREFLKERTRCRALEEELENPMNVHRWRKLEASDPSTFELIQKIHTLQKRLISKTEEVVEKELLLQEKEKLYVELKHILARQPGPEAAEQLQIYRHTLREKTKQLKVLSSELNMYESQSQEYKYEIERLGNELMSLKKKYLAQKRKELVLKNKDRMSMNNIFSETKKSVPRFTGGGFPLHQATKVKF
Protein: Transcription termination factor MTEF18, mitochondrial (Mitochondrial transcription termination factor 18) (Protein SUPPRESSOR OF HOT1-4 1) (Q9M219)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription termination factor involved in the regulation of mitochondrial-encoded gene expression. Essential for normal plant growth and development.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21464319, ECO:0000269|PubMed:22942382}.
Interaction partners:
- Transcription termination factor MTEF1, chloroplastic
- Transcription termination factor MTERF5, chloroplastic
- Transcription termination factor MTERF9, chloroplastic
- Transcription termination factor MTERF4, chloroplastic
- Transcription termination factor MTERF15, mitochondrial
- Transcription termination factor MTERF6, chloroplastic/mitochondrial
- Transcription termination factor MTERF8, chloroplastic
- Transcription termination factor MTERF2, chloroplastic
- Chaperone protein ClpB1
- Holliday junction resolvase MOC1, chloroplastic
Sequence:
MFMVRLKFASISHNFSTVAAKHRRVPSKYKSLAIGKAQQAITDYLHTTRSLSYTHAEQIASNASVSIRNLILKLDFSVPTFSKSLRKHLSYHPINEFEFFFESIGIDYSEVSEFLPEKKFFFSEDRTVLDAAFALSGFGFPWNKLGKLYKEERLVFVQRPGEIESRLLKFKDIGFSTVAVIGTCLAIPRTLCGGGELGSEIRCLFVKLKRLFDEFDSHHLFEENVDSWLAVSRKIRIFYDLGCENEEMWELMCRNKSLFLEYSEEALMNKAGYFCRFGVSKEDAALLILRNPAIMNFDLEKPVISVTGMLKHFGLRQDEVDAVAQKYPYVFGRNQLKNLPYVLRAIDLHERIFDILKNGNHHLLASYTLMDPDEDLEREYQEGLEELQNSRTKRHNIQKLDFLHEIGFGENGITMKVLQHVHGTAVELHDRFQILLNSGIIFSKICMLIRSAPKILNQKPHSIQDKLRFLCGEMGDSLDYLEVFPAYLCFDLENRISPRFRFHKWLVEKGFSEKSYSIASIVATSEKAFIARLYGIHPAIPKHWFERFSSRKTRDTVS
Protein: Transcriptional regulator protein Pur-beta (Purine-rich element-binding protein B) (Q68A21)
Organism: Rattus norvegicus (Rat)
Function: Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts (By similarity). Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35295}.
Interaction partners:
Sequence:
MADGDSGSERGGGGPGSFQPAPRGGGGPGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGGGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGEDDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGDESEGEEVDED
Protein: Zinc finger protein RTS2 (P40962)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- U2 snRNP component IST3
- U2 snRNP component HSH155
- Pre-mRNA-splicing factor RSE1
- Pre-mRNA-splicing factor PRP9
- Pre-mRNA-splicing factor PRP11
- Pre-mRNA-splicing factor CWC26
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-splicing helicase BRR2
- Histidine protein methyltransferase 1
- Pre-mRNA-processing factor 17
Sequence:
MADYDSAKYWSKQGARRGLQKTRYYCQICQRQCKDANGFQSHNKSPSHLRKISQVTAEDARRYNIQFEKGFLQLLKQRHGEKWIDANKVYNEYVQDRDHVHMNATMHRSLTQFVRYLGRAGKVDVDMDIDDTSENVEGPLLIRIHPSSLSSPSEDGMLRSQQEEQEVIAAELLKRQLNRAKRQTEKVYQPEMKSEISGDSTLKRVQVTFHGNGRVNKKKKKVPPRKDGIKFR