wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-ribosomal protein eL40B fusion protein [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40B (60S ribosomal protein L40-B) (CEP52)] (P0CH09)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40B]: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLKALASKYNCDKSVCRKCYARLPPRATNCRKRKCGHTNQLRPKKKLK
Protein: Protein NTM1-like 9 (Calmodulin-binding NAC protein) (F4JN35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP). Calmodulin-regulated transcriptional repressor. Binds several synthetic promoters with randomly selected binding sites. Functions synergistically with SNI1 as negative regulator of pathogen-induced PR1 expression and basal resistance to a virulent strain of P.syringae. Binds directly to the promoter of the PR1 gene. Acts as positive regulator of innate immunity. Involved in the effector-triggered immunity (ETI) induction of immunity-related gene expression. Mediates osmotic stress signaling in leaf senescence by up-regulating senescence-associated genes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18443413}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24329768}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:17947243, ECO:0000269|PubMed:18443413}. Note=Localized primarily in plasma membrane or endoplasmic reticulum membrane as dormant form and, upon osmotic stress or pathogen attack, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:18443413, ECO:0000269|PubMed:24329768}.
Interaction partners:
- Protein CROWDED NUCLEI 1
- Negative regulator of systemic acquired resistance SNI1
- Protein CROWDED NUCLEI 4
- Protein CROWDED NUCLEI 2
- Calmodulin-1
- Nuclear envelope-associated protein 1
- Transcription factor TGA2
- Calmodulin-binding protein 60 G
- DNA replication ATP-dependent helicase/nuclease JHS1
Sequence:
MGAVSMESLPLGFRFRPTDEELVNHYLRLKINGRHSDVRVIPDIDVCKWEPWDLPALSVIKTDDPEWFFFCPRDRKYPNGHRSNRATDSGYWKATGKDRSIKSKKTLIGMKKTLVFYRGRAPKGERTNWIMHEYRPTLKDLDGTSPGQSPYVLCRLFHKPDDRVNGVKSDEAAFTASNKYSPDDTSSDLVQETPSSDAAVEKPSDYSGGCGYAHSNSTADGTMIEAPEENLWLSCDLEDQKAPLPCMDSIYAGDFSYDEIGFQFQDGTSEPDVSLTELLEEVFNNPDDFSCEESISRENPAVSPNGIFSSAKMLQSAAPEDAFFNDFMAFTDTDAEMAQLQYGSEGGASGWPSDTNSYYSDLVQQEQMINHNTENNLTEGRGIKIRARQPQNRQSTGLINQGIAPRRIRLQLQSNSEVKEREEVNEGHTVIPEAKEAAAKYSEKSGSLVKPQIKLRARGTIGQVKGERFADDEVQVQSRKRRGGKRWKVVATVMVAVMVGVGMGIWRTLVSS
Protein: SAP domain-containing protein (Q22145)
Organism: Caenorhabditis elegans
Interaction partners:
- Structure-specific endonuclease subunit SLX1 homolog
- DNA repair endonuclease XPF
- Crossover junction endonuclease MUS81
- ERCC1-like central domain-containing protein
- Glutamyl-tRNA
- GEN1 Holliday junction resolvase homolog
- Methionine--tRNA ligase, cytoplasmic
- proline--tRNA ligase
- Regulator of telomere elongation helicase 1 homolog
- RecQ-like DNA helicase blm-1
Sequence:
MNDSSLKKALSQNSISSAPRRPQKLGSVQSIVRNESDKNVPSPFEEITLSDDDEEAPAKKPVKCATCARDMTLWMNSRRDIHVKVCKAKQSEKEKETTRKSKTLTETIEKDDQVYEKPSSKTHLFEKPFEKPQELPKSWELSKNNVKFARIAEDDEENRKRKRPRSFAVVELAPKKCQCEVLTTLHSRFIDEFHSKSIKNQKKREEGVTEHAFQMKKMIEKISRYEQLSSDMQKVLDDNSEQLPTHIFITCSDGHRVKCQTMILKHRTSLIRLNPKSENIQVEHTKEVVKAWISFVFTANIEWNDDDKDGVRDLASKYGPVGLDLIVKNDKEEDLEKVDDVEDVVEPEAKIDSVVADPVEIEPTASHSDPIELDKSVNYFTSDDPFFGFGKAVENVEDDAEQIMEDKPHESVHSTPQKPTTNVTMDSFDEWSNQPSTNLPTTSNVITPIRNITSKAVFGSHVKILKTNDITPMPAFDSMEEAELKERMKEIGMRPKGKKAMIQILKKAYITLHPEICSGTPTIRPLVRSASLEKVSEQGGKGGRKTIKTKTLSERMIASPKKVSPKKQGVKNAISDETSKNVSNVSDDLDEDNDGDKTLNISNDEREVGKICGDDVGDDEEDDDDMSASSTSGKHDLSALKLAFLTWLRSDQNTVLHEHILSLQPVSLEEMLIRLEKADGPLGRIGKGKLVKLLEMLKITYQLPQKTGRARGGYKRRL
Protein: Baculoviral IAP repeat-containing protein 7 (EC 2.3.2.27) (Kidney inhibitor of apoptosis protein) (KIAP) (Livin) (Melanoma inhibitor of apoptosis protein) (ML-IAP) (RING finger protein 50) (RING-type E3 ubiquitin transferase BIRC7) [Cleaved into: Baculoviral IAP repeat-containing protein 7 30kDa subunit (Truncated livin) (p30-Livin) (tLivin)] (Q96CA5)
Organism: Homo sapiens (Human)
Function: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and MAP3K7/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9.
Subcellular location: Nucleus {ECO:0000269|PubMed:17294084}. Cytoplasm {ECO:0000269|PubMed:17294084}. Golgi apparatus {ECO:0000269|PubMed:17294084}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively in the cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis.
Interaction partners:
- Caspase-9
- Caspase-7
- Caspase-3
- Ubiquitin-conjugating enzyme E2 D2
- Diablo IAP-binding mitochondrial protein
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Dual E2 ubiquitin-conjugating enzyme/E3 ubiquitin-protein ligase BIRC6
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MGPKDSAKCLHRGPQPSHWAAGDGPTQERCGPRSLGSPVLGLDTCRAWDHVDGQILGQLRPLTEEEEEEGAGATLSRGPAFPGMGSEELRLASFYDWPLTAEVPPELLAAAGFFHTGHQDKVRCFFCYGGLQSWKRGDDPWTEHAKWFPSCQFLLRSKGRDFVHSVQETHSQLLGSWDPWEEPEDAAPVAPSVPASGYPELPTPRREVQSESAQEPGGVSPAEAQRAWWVLEPPGARDVEAQLRRLQEERTCKVCLDRAVSIVFVPCGHLVCAECAPGLQLCPICRAPVRSRVRTFLS
Protein: IP07407p (Q1ECA7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMRAFHGACPSNMTAVGDLDMDRFKGKWYTHSIYPHLSLRVEKCQSTDFIEKEENKFSVVARELNTQTGTVKMRKADILNVEPEFGRYVLGTTSTAFPEGVLMYVLDTDYVNFAIRFMCFDASKIFSFHWAVIQTRKRLPSTQVIHMAQYFGKSAGLVIGDMSKVPQESCPYDT
Protein: CCHC-type zinc finger nucleic acid binding protein (Cellular nucleic acid-binding protein) (CNBP) (Zinc finger protein 9) (P53996)
Organism: Mus musculus (Mouse)
Function: Single-stranded DNA-binding protein that preferentially binds to the sterol regulatory element (SRE) sequence 5'-GTGCGGTG-3', and thereby mediates transcriptional repression (By similarity). Has a role as transactivator of the Myc promoter. Binds single-stranded RNA in a sequence-specific manner (By similarity). Binds G-rich elements in target mRNA coding sequences (By similarity). Prevents G-quadruplex structure formation in vitro, suggesting a role in supporting translation by resolving stable structures on mRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12706888}. Cytoplasm {ECO:0000269|Ref.2}. Endoplasmic reticulum {ECO:0000269|Ref.2}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K
- Muscleblind-like protein 1
- Suppressor of fused homolog
- Muscleblind-like protein 2
- Muscleblind-like protein 3
- Myotonin-protein kinase
- Ornithine decarboxylase antizyme 1
- CUGBP Elav-like family member 1
- Heterogeneous nuclear ribonucleoprotein A1
Sequence:
MSSNECFKCGRSGHWARECPTGGGRGRGMRSRGRGGFTSDRGFQFVSSSLPDICYRCGESGHLAKDCDLQEDEACYNCGRGGHIAKDCKEPKREREQCCYNCGKPGHLARDCDHADEQKCYSCGEFGHIQKDCTKVKCYRCGETGHVAINCSKTSEVNCYRCGESGHLARECTIEATA
Protein: DNA-(apurinic or apyrimidinic site) endonuclease 2 (EC 3.1.11.2) (APEX nuclease 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2) (Q68G58)
Organism: Mus musculus (Mouse)
Function: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:12573260}. Cytoplasm {ECO:0000269|PubMed:12573260}. Mitochondrion {ECO:0000269|PubMed:12573260}. Note=Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. {ECO:0000250|UniProtKB:Q9UBZ4}.
Interaction partners:
- DNA repair nuclease/redox regulator APEX1
- Uracil-DNA glycosylase
- Tyrosyl-DNA phosphodiesterase 1
- Endonuclease III-like protein 1 lyase)
- Flap endonuclease 1
- DNA repair endonuclease XPF
- N-glycosylase/DNA lyase
Sequence:
MLRVVSWNINGIRSPLQGLACQEPSSCPTALRRVLDELDADIVCLQETKVTRDVLTEPLAIVEGYNSYFSFSRSRSGYSGVATFCKDSATPVAAEEGLSGVFATLNGDIGCYGNMDEFTQEELRVLDSEGRALLTQHKIRTLEGKEKTLTLINVYCPHADPGKPERLTFKMRFYRLLQMRAEALLAAGSHVIILGDLNTAHRPIDHCDASSLECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSYRYLHPKQQRAFTCWSVVSGARHLNYGSRLDYVLGDRALVIDTFQASFLLPEVMGSDHCPVGAVLNVSCVPAKQCPALCTRFLPEFAGTQLKILRFLVPLEQEPVREQQVLQPSHQIQAQRQPRKACMHSTRLRKSQGGPKRKQKNLMSYFQPSSSLSQTSGVELPTLPLVGPLTTPKTAEEVATATVLEEKNKVPESKDEKGERTAFWKSMLSGPSPMPLCGGHREPCVMRTVKKTGPNFGRQFYMCARPRGPPSDPSSRCNFFLWSRPS
Protein: Aquaporin TIP1-2 (Tonoplast intrinsic protein 1-2) (ZmTIP1-2) (ZmTIP1;2) (Q9ATM0)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Vacuole membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Tonoplast.
Interaction partners:
Sequence:
MPVSRIAVGAPGELSHPDTAKAAVAEFISTLIFVFAGSGSGMAFSKLTDGGAATPAGLIAASLAHALALFVAVSVGANISGGHVNPAVTFGAFVGGNISLLKALVYWVAQLLGSVVACLLLKIATGGAALGAFSLSAGVGAMNAVVLEMVMTFGLVYTVYATAVDPKKGDLGVIAPIAIGFIVGANILAGGAFDGASMNPAVSFGPAVVTGVWENHWVYWVGPLAGAAIAALVYDIIFIGQRPHQQLPTTAADY
Protein: Melanoma-associated antigen E1 (Alpha-dystrobrevin-associated MAGE Protein) (DAMAGE) (Hepatocellular carcinoma-associated protein 1) (MAGE-E1 antigen) (Q9HCI5)
Organism: Homo sapiens (Human)
Function: May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=In the skeletal muscle, found at the postsynaptic membrane and is associated with a subset of myonuclei. May reside within nuclei and/or in perinuclear compartments. In peripheral nerves, colocalizes with DTNA in the Schwann cell membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Dystrobrevin alpha
- EP300-interacting inhibitor of differentiation 2B
- Alpha-1-syntrophin
Sequence:
MSLVSQNSRRRRRRVAKATAHNSSWGEMQAPNAPGLPADVPGSDVPQGPSDSQILQGLCASEGPSTSVLPTSAEGPSTFVPPTISEASSASGQPTISEGPGTSVLPTPSEGLSTSGPPTISKGLCTSVTLAASEGRNTSRPPTSSEEPSTSVPPTASEVPSTSLPPTPGEGTSTSVPPTAYEGPSTSVVPTPDEGPSTSVLPTPGEGPGTSVPLAATEGLSTSVQATPDEGPSTSVPPTATEGLSTPVPPTRDEGPSTSVPATPGEGPSTSVLPAASDGQSISLVPTRGKGSSTSVPPTATEGLSTSVQPTAGEGSSTSVPPTPGGGLSTSVPPTATEELSTSVPPTPGEGPSTSVLPIPGEGLSTSVPPTASDGSDTSVPPTPGEGASTLVQPTAPDGPGSSVLPNPGEGPSTLFSSSASVDRNPSKCSLVLPSPRVTKASVDSDSEGPKGAEGPIEFEVLRDCESPNSISIMGLNTSRVAITLKPQDPMEQNVAELLQFLLVKDQSKYPIRESEMREYIVKEYRNQFPEILRRAAAHLECIFRFELRELDPEAHTYILLNKLGPVPFEGLEESPNGPKMGLLMMILGQIFLNGNQAKEAEIWEMLWRMGVQRERRLSIFGNPKRLLSVEFVWQRYLDYRPVTDCKPVEYEFFWGPRSHLETTKMKILKFMAKIYNKDPMDWPEKYNEALEEDAARAFAEGWQALPHFRRPFFEEAAAEVPSPDSEVSSYSSKYAPHSWPESRLESKARKLVQLFLLMDSTKLPIPKKGILYYIGRECSKVFPDLLNRAARTLNHVYGTELVVLDPRNHSYTLYNRREMEETEEIVDSPNRPGNNFLMQVLSFIFIMGNHARESAVWAFLRGLGVQAGRKHVITCRYLSQRYIDSLRVPDSDPVQYEFVWGPRARLETSKMKALRYVARIHRKEPQDWPQQYREAMEDEANRADVGHRQIFVHNFR
Protein: Chymotrypsin-like elastase family member 3A (EC 3.4.21.70) (Elastase IIIA) (Elastase-3A) (Protease E) (P09093)
Organism: Homo sapiens (Human)
Function: Efficient protease with alanine specificity but only little elastolytic activity.
Interaction partners:
- Carboxypeptidase A1
- Carboxypeptidase A2
- Carboxypeptidase B
- Colipase
- Pancreatic triacylglycerol lipase
- Bile salt-activated lipase
- Chymotrypsinogen B2
- Chymotrypsin-like protease CTRL-1
- Chymotrypsin-C
- Pancreatic polypeptide prohormone
Sequence:
MMLRLLSSLLLVAVASGYGPPSSHSSSRVVHGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISRDLTYQVVLGEYNLAVKEGPEQVIPINSEELFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNKTPCYITGWGRLYTNGPLPDKLQQARLPVVDYKHCSRWNWWGSTVKKTMVCAGGYIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVSAFGCNFIWKPTVFTRVSAFIDWIEETIASH
Protein: Intercellular adhesion molecule 5 (ICAM-5) (Telencephalin) (Q60625)
Organism: Mus musculus (Mouse)
Function: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2).
Subcellular location: Membrane {ECO:0000269|PubMed:7794412}; Single-pass type I membrane protein {ECO:0000269|PubMed:7794412}.
Interaction partners:
- Integrin alpha-L
- CD209 antigen-like protein A
- Integrin beta-2
- Integrin alpha-D
- Integrin beta-1
- CD209 antigen-like protein B
Sequence:
MPGPSPGLRRALLGLWAALGLGILGISAVALEPFWADLQPRVALVERGGSLWLNCSTNCPRPERGGLETSLRRNGTQRGLRWLARQLVDIREPETQPVCFFRCARRTLQARGLIRTFQRPDRVELVPLPSWQPVGENFTLSCRVPGAGPRASLTLTLLRGGQELIRRSFVGEPPRARGAMLTARVLARREDHRVNFSCLAELDLRPHGLGLFANSSAPRQLRTFAMPPHSPSLIAPRVLEVDSERPVTCTLDGLFPAPEAGVYLSLGDQRLNPNVTLDGDSLVATATATASAEQEGTKQLMCVVTLGGESRETQENLTVYSFPTPLLTLSEPEAPEGKMVTISCWAGARALVTLEGIPAAVPGQPAELQLNVTKNDDKRGFFCDAALDVDGETLRKNQSSELRVLYAPRLDDLDCPRSWTWPEGPEQTLHCEARGNPEPSVHCARPEGGAVLALGLLGPVTRALAGTYRCTAVNGQGQAVKDVTLTVEYAPALDSVGCPEHITWLEGTEASLSCVAHGVPPPSVSCVRSGKEEVMEGPLRVAREHAGTYRCEAINARGSAAKNVAVTVEYGPSFEELGCPSNWTWVEGSGKLFSCEVDGKPEPRVECVGSEGASEGIVLPLVSSNSGPRNSMTPGNLSPGIYLCNATNRHGSTVKTVVVSAESPPQMDESSCPSHQTWLEGAEATALACSARGRPSPRVHCSREGAARLERLQVSREDAGTYRCVATNAHGTDSRTVTVGVEYRPVVAELAASPPSVRPGGNFTLTCRAEAWPPAQISWRAPPGALNLGLSSNNSTLSVAGAMGSHGGEYECAATNAHGRHARRITVRVAGPWLWVAVGGAAGGAALLAAGAGLAFYVQSTACKKGEYNVQEAESSGEAVCLNGAGGTPGAEGGAETPGTAESPADGEVFAIQLTSS
Protein: Lipopolysaccharide core galacturonosyltransferase RgtB (LPS core GalA transferase RgtB) (EC 2.4.1.-) (Dodecaprenyl phosphate-beta-galacturonate:lipopolysaccharide core alpha-galacturonosyltransferase RgtB) (Dodecaprenyl-P-GalA:LPS core galacturonosyltransferase RgtB) (Galacturonic acid transferase RgtB) (GalAT RgtB) (Q1MJ97)
Organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium leguminosarum bv. viciae)
Function: Involved in the modification of the lipopolysaccharide (LPS) inner core. Catalyzes the transfer of a galacturonic acid (GalA) residue to the 5-position of the outer Kdo (3-deoxy-D-manno-octulosonic acid) residue of the LPS inner core, using dodecaprenyl phosphate-GalA as the donor substrate. Acts after the other GalA transferase RgtA.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:16497671, ECO:0000305|PubMed:16497674}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTESNRRDISWIFALLAAYFVLQVGVRLATSHSLDLDEAEQAFRSQWLAAGYGPQPPFYNWLQYTVFQFAGVSLTALSIVKNLLLFISYLLYGLTARLVLRDKALVAIATLGLLTIPQMAFEMQRDLTHTVAVFFSASIFFYGFIRSLKQPSLASYLIAGIGIGFGLLAKYNFAILPAAALIAALSDARLRPRIFDWRLGLTAAVALVITLPHLFWLKDNLDFATARTLEKMTASGDASYLTQVAMGVSSLALAIISFAALTVAVFAIVFGKSLRPALGSGSEWTRLLERMMLVFLAGILLLIVFGGAAGIKDRWLVPMLFILPLYFCLKIEAAGVETGKALRRFIPVVAVIMIGVPAALYGSVAAARFTGHYERLNRPYAGMLEILRKQAEPAAILAGDSLLAGNLRQDIPGVPILSADYPGFNPDLTSRRPLLLVWLLPKGGSEALPPDMAEWLQANLGTSAPEASVIDVPYFYGRGDDRYRFGYAWVNQPG
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (A0A0G2K6M9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPVPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPCFWIDGQYLCCSQTAKNAMGCQILENRNGSLKPGSSHRKTKKPLPPTPEEDQILKKPLPPEPTAAPISTSELKKVVALYDYMPMNANDLQLRKGEEYFILEESNLPWWRARDKNGQEGYIPSNYVTEAEDSIEMYEWYSKHMTRSQAEQLLKQEGKEGGFIVRDSSKAGKYTVSVFAKSTGEPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLISRLKYPVSKQNKNAPSTAGLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIREGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKIPYERFTNSETAEHIAQGLRLYRPHLASDRVYTIMYSCWHEKADERPSFKILLSNILDVMDEES
Protein: 26S proteasome regulatory subunit RPN13 (AtRPN13) (26S proteasome non-ATPase regulatory subunit 13) (O48726)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as a proteasomal ubiquitin receptor. Binds and presumably selects ubiquitin-conjugates for destruction. Prefers multiubiquitin chains rather than single ubiquitins, with a binding affinity for 'Lys-63'-linked ubiquitin chains.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU01265}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU01265}.
Interaction partners:
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 14 homolog
- 26S proteasome regulatory subunit 4 homolog B
- ARM repeat superfamily protein
- 26S proteasome non-ATPase regulatory subunit 3 homolog A
- 26S proteasome regulatory subunit 6A homolog A
Sequence:
MSSSEAFPVMQEIMLEFRAGKMSLQGTRVVPDARKGLVRIARGDEGLIHFQWLDRNQNTVEDDQIVFPDEALFEKVNQSSDRVYILKFNSDDRKLFFWMQEPRAEGDAELCSSVNQYLNQPLEFPGEEGLAAAITEELEDMAEDNTSSRAGNLVVPNLSSEVSDVTSSSGPVKLADLQRILNNLSGGPVGIAGDQDEGLALGDILKPELIMPLLEALPVQERLSSHLPEGHSRAEDILELLQSPPFRQQVDAFTYVLRTGQIDLTQFGIDPSKYKFTVDSFLEALEDSVSTQSRDAMDES
Protein: Alanine aminotransferase (EC 2.6.1.2) (Alanine transaminase) (Transaminase A) (P9WQ91)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- NAD-specific glutamate dehydrogenase
- Alanine dehydrogenase
- Dihydroxy-acid dehydratase
- 2-isopropylmalate synthase
- Arginine biosynthesis bifunctional protein ArgJ
- Branched-chain-amino-acid aminotransferase
- Amino-acid acetyltransferase
- Probable histone acetyltransferase Rv0428c
- Alanine racemase
- Isocitrate dehydrogenase 1
Sequence:
MDNDGTIVDVTTHQLPWHTASHQRQRAFAQSAKLQDVLYEIRGPVHQHAARLEAEGHRILKLNIGNPAPFGFEAPDVIMRDIIQALPYAQGYSDSQGILSARRAVVTRYELVPGFPRFDVDDVYLGNGVSELITMTLQALLDNGDQVLIPSPDYPLWTASTSLAGGTPVHYLCDETQGWQPDIADLESKITERTKALVVINPNNPTGAVYSCEILTQMVDLARKHQLLLLADEIYDKILYDDAKHISLASIAPDMLCLTFNGLSKAYRVAGYRAGWLAITGPKEHASSFIEGIGLLANMRLCPNVPAQHAIQVALGGHQSIEDLVLPGGRLLEQRDIAWTKLNEIPGVSCVKPAGALYAFPRLDPEVYDIDDDEQLVLDLLLSEKILVTQGTGFNWPAPDHLRLVTLPWSRDLAAAIERLGNFLVSYRQ
Protein: Uncharacterized protein (Q583R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYRTLTPSCKKFSGFYTTFPRRCNTTILIPFRIFSILLYLTALICVAGSSDDFVLIESRDNEVSGGGDRVDLRRSVNVYLVVSFMLLFVTCWGIFTGRTLRSGTVNFMHCCSHTTAAIALIVIWCLKLHLHRMWHVFYAFGAIPTAMEVCALCASYYRGLDSYL
Protein: Innexin (C8JQR7)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction, gap junction {ECO:0000256|ARBA:ARBA00004610}. Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}.
Interaction partners:
Sequence:
MYHSKQANTKYIKKAQKLLDGSHQLRIDSHHVGSAGHGAGQGHGHKKEFGPAMILYYLASAFRALYPRLDDDFVDKLNYYYTTTILASFALLVSAKQYVGFPIQCWVPATFTDAMEQYTENYCWVQNTYWVPMQEDIPREIYSRRNRQIGYYQWVPFILAIEALLFYVPCILWRGLLYWHSGINLQGLVQMACDARLMDSEIKTRTVYTMARHMQDEVQLTNIDRQGHSRSCFSNLQLGANCGRHCGCYVTMLYIGIKVLYSANVLLQFFLLNHLLGSNDLAYGFSLLKDLMHAIEWEQTGMFPRVTLCDFEVRVLGNIHRHTVQCVLMINMFNEKIFLFLWFWFLTCGIVTVCNTMYWILIMFIPSQGMSFVRKYLRVLPDHPAKPIADDVTLRKFTNNFLRKDGVFMLRMISTHAGELMSSELILALWQDFNNVDRSPTQFWDAEHGQGTID
Protein: Solute carrier family 53 member 1 (Phosphate exporter SLC53A1) (Protein SYG1 homolog) (Xenotropic and polytropic murine leukemia virus receptor X3) (X-receptor) (Xenotropic and polytropic retrovirus receptor 1) (Q9UBH6)
Organism: Homo sapiens (Human)
Function: Plays a role in phosphate homeostasis. Mediates phosphate export from the cell. Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23791524, ECO:0000269|PubMed:31043717}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma
- Bile acid receptor
- Peroxisome proliferator-activated receptor alpha
- Phospholipid-transporting ATPase ABCA1
- Oxysterols receptor LXR-beta
- Sterol regulatory element-binding protein 2
- ATP-binding cassette sub-family G member 5
- ATP-binding cassette sub-family G member 8
- E3 ubiquitin-protein ligase MYLIP
- Sodium-dependent phosphate transporter 2
Sequence:
MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQRRFATLQNELQSSLDAQKESTGVTTLRQRRKPVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSRGADWRVAHVEVAPFYTCKKINQLISETEAVVTNELEDGDRQKAMKRLRVPPLGAAQPAPAWTTFRVGLFCGIFIVLNITLVLAAVFKLETDRSIWPLIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFAPISVIPTYVYPLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSLELKWDESKGLLPNNSEESGICHKYTYGVRAIVQCIPAWLRFIQCLRRYRDTKRAFPHLVNAGKYSTTFFMVTFAALYSTHKERGHSDTMVFFYLWIVFYIISSCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLLPHSGDIIATVFAPLEVFRRFVWNFFRLENEHLNNCGEFRAVRDISVAPLNADDQTLLEQMMDQDDGVRNRQKNRSWKYNQSISLRRPRLASQSKARDTKVLIEDTDDEANT