wanglab/gogpt-training-data huggingface dataset:
Protein: Pyruvate dehydrogenase protein X component, mitochondrial (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (E3-binding protein) (E3BP) (Lipoyl-containing pyruvate dehydrogenase complex component X) (proX) (O00330)
Organism: Homo sapiens (Human)
Function: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
- [Pyruvate dehydrogenase
Sequence:
MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA
Protein: Mandelate racemase/muconate lactonizing enzyme C-terminal domain-containing protein (A9CG74)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
- Galactose mutarotase
- ABC transporter, nucleotide binding/ATPase protein
- ABC transporter, membrane spanning protein
- ABC transporter, membrane spanning protein
- ABC transporter, substrate binding protein
- Calcium-binding protein, regucalcin
Sequence:
MKIDRMRVFVTRDKDRPRVIVALDTDDGMTGWGECYNHGPDLALPPVLDYLYNFLAGQDPTRVEFLYNLMLQQNRFPPGALGLSAISALDHCLWDLAAKAVGVPVYKLLGGEVRNRIKVYAGVYTAPDAPAARDEFDRLNEGWGFSAFKLSPWRVDIHAHRWGEVVRSSAEYFRTLRETVRADYDIAFDAHAKIFEPSAARQLGNALAPYDPLFYEEPLRPENIEMYGDLKQGLNCTLATGESLYNRNEFLRLLQVKGADIIQPDICVVGGISEMRRIATLAEAHFVSIAPHNPMGPLATAVNVHFCAVQQNFRILEYRLPKGQVYAYGGNDLVKEEDVTRYVVDPYLPRDGYLELRPDRPGWGVEMDEKAMQEDGYVHWQRRVPKRPDGSYAFA
Protein: Beta-amyrin 6-beta-monooxygenase (EC 1.14.14.64) (Cytochrome P450 716E26) (A0A3Q7HS74)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Catalyzes the C-6 beta-hydroxylation of beta-amyrin to form daturadiol. Catalyzes the C-6 beta-hydroxylation of alpha-amyrin to form 6-beta-hydroxy-alpha-amyrin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPFILYSLAFALVYISLYFIFKGNYSNNKHTNLPLGSNGWPILGENIDMAYSSSPEKFIHERMEKHSSQVFKTSLLGQKIAIFCGTSGNKFLFSNENKLLTTWWPPSLTKPLMCPTQSQSQNSVKEIALLNRGFLREILKPENLKQYIPFMDSMARDHLKQEWIPFKEVKIYPLVKKYTFSLACKLFLSIDDFRHVKKLSDPFVLVTSGMFTVPINLPGTPYNRAIKGGKMVHEELMKIIKERKINEKNNHSNDLLSQLISFSDENGQFMNDAEIYNNIIGLLVASYDTTSAAITFVLKYLAELPNIFNEVYKEQMEIAKSKGEGELLNWDDIQKMKYSWNVACEAIRLMPPAQGAFREAITDFTFGGFTVPKGWKTFWSVYSTHKNPKYFPEPEKFDPCRFEGSGPEPYTFVPFGGGPRMCPGKEYARLEILVFMYNIVTNFKLEKLVPHEKIIYKSSPVPLNGLPVRIQPIA
Protein: Ankyrin repeat-containing protein (Q551Q8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSNQQQHHNQQQQQQQHVVKPFLNSFDGSIKLEESIEDSPQFRKHLKDTEQSIDELTQNIKKMLKSSKQSCELGEDYNITFKNFVDDLLTYKGEAGSGFVRDELLEKSMIKFSTALKEICNFRELLHIEMDALITGPLQSFAENDLRQVKEQCKKYDKYSQQYDASASKLGQIKKKNSVRIEEVSQEANETLKLRVQFGLDLVESMNQVQARRRFEFLEYFSVYLHAQSTFFHQGYELFRDLEPHMRVFSDYLQATRKHFEDEKRKQTMLKAELIEKTFLNSPSSNTSMSGSPVNGGIIFTTNRTSQDTLFKKGYLFKRSEYNSYTRKFFELSNGKLSYYKTGNDTSPSHTHDLFLTTVRIREDLDRRYCFELLSPDRSIILAAETFESMQEWVQVLQNTIANLLNNCSPQGNLIVNNLSSPNSNCNNNNNNNNNNSNNLIITNNNNNNFNNNNISLSNSPSGNNIIVNSFNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNGKNIPFSDNHNGLNSSCGSTTSSSSIASISVNNSGNNINIQQQQSQQQQQQQQQQQQQQNETPISILRRIDSSNLYCADCNTRDPDWASINFGCLLCIDCSGIHRGMGVHISKVRSVILDKWEPELLNMMKCIGNEKVNKIYENKIPPGRKKPTPNDEFEIRAKWIRDKYDKRLFVNFLDKSLDDINSLFYHIASEPNASYILELIAQGADPNYKEPHHDYKSPLHNAAQHNLPQNICLLLQNGAMVDQLDSNGNTPLHTSADCGSPDSCILLLMKSVKLLSITNKDNHTPLDLAVEKGHVGCVTILRLAQLQKDEGKHSFDDAFAELLRGFVINCK
Protein: ADF-H domain-containing protein (Q54S93)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Actin-related protein 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1
- Peroxisomal multifunctional enzyme A
- Actin-related protein 2/3 complex subunit 2
- Twinfilin
- Mediator of RNA polymerase II transcription subunit 13
Sequence:
MATCTLPDEYFEEFKALKKERSPKNTAMVFMIDKSKHEFKIEETFVDISLEKLQEELSNTSPRYIVYVYKHTHPDGRQSFPMVFIYFMPKGISPAVAMTYSANKEILVNKLEIMKSFNAETVETLTEPWLKEKLAFFK
Protein: Cysteine protease StiP (EC 3.4.22.-) (Q6FAX7)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Cysteine protease that may play a role in regulating cell morphology in response to stressful conditions which likely cause oxidative damage. Appears to catalyze its own cleavage, which probably leads to its activation.
Interaction partners:
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL22
Sequence:
MAIINKDKATELILKQGFSGSYQSEQVTFLLKRTHIEPTDTAEKERLIQSGEKHYSQMISLENAPTARHLELFEQAMQQGQQRLAQEVQQLAQTLVVEFNEPIVLVSFVRAGVPLGVLLYHAIQDLGRDCVHYGISIIRDRGIDFAALETIIARHGHASIVFVDGWTGKGAIRQELQRSLGNDTRFIGKPLPLVVLSDIAGCAWLAASGDDWLIPSGILGSTISGLISRSICEGETLSADEITAENIDQWHRCIEYHHLKEFDISQQFIQRINQIRLKLNPQSNAVWAETQQQAQQDQSQQVVHKLAQEYDIQNINRIKPSIAEATRAILRRVPDLVLLRDADDEDTRLLRHLTQITKTPVQVVGDQIAPYRAITLIQKLGKG
Protein: Terpentedienyl-diphosphate synthase (EC 5.5.1.15) (Q9AJE4)
Organism: Kitasatospora griseola (Streptomyces griseolosporeus)
Function: Involved in the production of the isoprenoid antibiotic terpentecin. Converts geranylgeranyl diphosphate (GGDP) into terpentedienol diphosphate (TDP) by a protonation-initiated cyclization.
Interaction partners:
- C-5 sterol desaturase
- C-5 sterol desaturase
- Isopentenyl-diphosphate Delta-isomerase
- Polyprenyl synthetase
- Terpentetriene synthase
- Dimethylallyltranstransferase
- NUDIX hydrolase
- Phytoene synthase
- Cytochrome P450
- Geranyl geranyl diphosphate synthase
Sequence:
MKDRAADPVTKFSPSPYETGQFLRISERADVGTPQIDYLLATQRPDGLWGSVGFELVPTLGAVAGLSSRPEYADRAGVTDAVARACEKLWELALGEGGLPKLPDTVASEIIVPSLIDLLSEVLQRHRPAVGGKAGQEQEFPSPPGANAELWRQLSDRIARGQAIPKTAWHTLEAFHPLPKQFAATVTPAADGAVTCSPSSTAAWLSAVGTDAGASTRAYLDEAQSRYGGAIPMGSSMPYFEVLWVLNLVLKYFPDVPIPREIIEEIAAGFSDSGIGGGPGLPPDGDDTAYANLAGDKLGAPTHPEILMKFWAEDHFVSYPGEQTPSETVNAHALEYLNHLRMRRGITEFGAVEDACAEWVISQQTEDGCWYDKWNVSPYYSTAACVEALLDARKQDEPQLDSLRRAREWLLRHQTDSGGWGMAEPSPEETAYAVLALDLFASRGGEGAEECAAAISRAKEFFTDESRENPPLWMGKDLYTPFRIVDVTVMCGRAVVGRY
Protein: Protein phosphatase inhibitor 2 (IPP-2) (Q580S8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGRKRVMWDEKNLEDNEEYRRTHPVTMHITEPKTPFQYPEDEEDFEEALERNDDGGGDEVENGGTWDPKVNELARQVREEFRKEAPVVVAPVAPSGRPMLSDEVVSGEALEKQRAAEFKTMRKAVYADEGARVKALLGKGNTFDDDGDDGDDNNEEEEGEEGKKAEDSNGIGEK
Protein: Phospholipase A2, membrane associated (EC 3.1.1.4) (Enhancing factor) (EF) (GIIC sPLA2) (Group IIA phospholipase A2) (Phosphatidylcholine 2-acylhydrolase 2A) (P31482)
Organism: Mus musculus (Mouse)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (By similarity). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin-dependent manner (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P14555}. Cell membrane {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14555}.
Interaction partners:
Sequence:
MKVLLLLAASIMAFGSIQVQGNIAQFGEMIRLKTGKRAELSYAFYGCHCGLGGKGSPKDATDRCCVTHDCCYKSLEKSGCGTKLLKYKYSHQGGQITCSANQNSCQKRLCQCDKAAAECFARNKKTYSLKYQFYPNMFCKGKKPKC
Protein: Conserved protein (O06829)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MAEAGGGPISVIARHMQLIRDDFISELFDKMKAEIRGLDYDARMADLWRASITENFVTAVHYLDRDTPQSLVEAPAAALAYARAAAQRDIPLSGLVRAHRLGHARFLEVAMQYVSLLEPADRVSTIIELVNRSARLVDLVADQLIVAYEHEHDRWLSRRSGLQQQWVSELLADTPVDVPRAERALGYRLDGVHIAAVVWVDSAVPIGDVVAQFDQVRCLLAGELGPELGPVANSLMVPTDEREARLWFSPAPTRAFAPSRIRAAFESAGIRARLACGRVGDGLRGFRASLKQAERVKALALAGGARPGGRVMFYDDVAPVALLADDLEELRRFVTDVLGDLSVDDERNSWLRETLREFLLRNRSYVATADAMILHRNTIQYRVIQAMELCGQNLDDPDAAFRVQMALEVCRWMAPAVLRAKQ
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5 (Oligosaccharyl transferase subunit OST5) (Oligosaccharyl transferase 9.5 kDa subunit) (Oligosaccharyl transferase subunit zeta) (Q92316)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:29301962}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1
- Dol-P-Glc:Glc
- Mannosyl-oligosaccharide glucosidase
Sequence:
MTYEQLYKEFHSSKSFQPFIHLDTQPKFAICGLIVTLAVLSSALFAVGSKSSYIKKLFFYTILSVIGSLFAGLTTVFASNSFGVYV
Protein: At4g22010 (Pectinesterase-like protein) (SKU5 similar 4) (O65449)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT2G44210 protein)
- Proline-rich extensin-like family protein
- GDSL esterase/lipase 5
- Probable pectinesterase/pectinesterase inhibitor 36
- Anthranilate N-hydroxycinnamoyl/benzoyltransferase-like protein
- Probable pectate lyase 12
- Uclacyanin 1
- Putative cell wall protein
- phosphoglucomutase
- Glycerophosphodiester phosphodiesterase GDPDL4
Sequence:
MRGSCKVSIVLLLVLINGVLGDNPYRFFTWKITYGDIYPLGVKQQGILINGQFPGPHIDAITNDNIIISVFNYLKEPFLISWNGVQQRKNSWQDGVVGTTCPIPPGKNFTYVIQVKDQIGSFYYFPSLAFHKAAGAFGAIRVWSRPRIPVPFSPPDGDFWLLAGDWYKTNHYVLRRLLEAGRNLPNPDGVLINGRGWGGNTFTVQPGKTYRFRISNVGVATSLNFRIQGHTMKLVEVEGSHTVQNIYTSLDIHLGQSYSVLVTANQAPQDYYIVISSRFTRKVLTTTSILHYSNSRKGVSGPVPNGPTLDIASSLYQARTIRRNLTASGPRPNPQGSYHYGLIKPGRTIILANSAPWINGKQRYAVNGASFVAPDTPLKLADYFKIPGVFNLGSIPTSPSGGNGGYLQSSVMAANFREFIEVVFQNWENSVQSWHVSGYSFFVVGMDGGQWTPGSRAKYNLRDAVSRSTVQVYPRAWTAIYIALDNVGMWNIRSENWARQYLGQQFYLRVYTSSTSYRDEYPPPKNALMCGRAKGRHTRPF
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC4 (RNA polymerases I, II, and III subunit ABC4) (DNA-directed RNA polymerase II subunit K) (Metallothionein-I gene transcription activator) (RPB10alpha) (Q63871)
Organism: Mus musculus (Mouse)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P53803}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P53803}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MDAQKDVQPPKQQPMIYICGECHTENEIKSRDPIRCRECGYRIMYKKRTKRLVVFDAR
Protein: Uncharacterized protein (E7DNB2)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MTKRTTMMDRLKEILPTFQLSPAPMLPGVEFDEQDTDRPDDYIVLRYSHRMPSATNSLGSFAYWKVQIYVHSNSIIGIDEYSRKVRNIIKDMGYEVTYAETGDYFDTMLSRYRLEIEYRIPQGGN
Protein: J domain-containing protein required for chloroplast accumulation response 1 (Q9C9Q4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for chloroplast photorelocation movement; chloroplast accumulation upon low blue light and for chloroplast movement to the bottom of cells in darkness, by modulating chloroplast actin (Cp-actin) filaments distribution, appearance and disappearance. May mediate a slight resistance to aluminum in root hair cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16113208}.
Interaction partners:
- Protein WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT 1
- Uncharacterized protein At1g66480
- Protein PLASTID MOVEMENT IMPAIRED 1
- Protein CHUP1, chloroplastic
- At1g09520/F14J9_18
- Root phototropism protein 2
- Phototropin-2
- Iron-sulfur cluster co-chaperone protein HscB homolog
- Heat shock 70 kDa protein 9, mitochondrial
- Protein PLASTID MOVEMENT IMPAIRED 15
Sequence:
MQTLPSSETVLLGSNSAPPVLRSPGGDDVDIDFGDVFGGPPKRRSKVTSNEVTRHSFSESALRRRDVIVDVGDLLPQDEKPVFGEDTSSVRRRFTTDDFFDDIFRVNESSSLPGSRILSPAHKPESSSGTSSPSQFSLPAKATEIPTFNLAATRSLNKNKETVSSSPLSRTSSKADVVSTAKSYSDDCDDPPQVFVTGKGRQFHFSIYKWPNKGVPVVIWGSSRLSSMSKAEETTPVPLSDYRKTSVVEKLGKNEEGDGKSGLSGLKDVKKTSLKRPGVQTKEEKTETDLKSEQAFFGVSKAREANVKPLDSVESEQAFSGVSKAHEATTVKPLHSIFHEEDERQDEKIVSEREVRKGKSKAKNTRSFTEDSRTKKKSQGTKSSLDSSPIPDKSSFASSSAAPEVGKDGVKGKVSDFVKIFSKGASVGAGGESLGQSSRWRAKETPKTDIIHDGSNAKETVNIPDQQKKSTPDIPAMNRDQKPSQSTQKKDSDRESMNYKAPGDTVQEERQEPSTTHTTSEDIDEPFHVNFDVEDITQDENKMEEANKDAEEIKNIDAKIRKWSSGKSGNIRSLLSTLQYILWSGSGWKPVPLMDMIEGNAVRKSYQRALLILHPDKLQQKGASANQKYMAEKVFELLQEAWDHFNTLGPV
Protein: Aspartate ammonia-lyase (Aspartase) (EC 4.3.1.1) (P44324)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Interaction partners:
- Probable L-asparaginase periplasmic
- Phosphoenolpyruvate carboxykinase
- Bifunctional aspartokinase/homoserine dehydrogenase
- Aspartate--ammonia ligase
- Aspartate aminotransferase
- NADP-dependent malic enzyme
- Fumarate reductase flavoprotein subunit
Sequence:
MITMTQFRKEVDLLGERDVPAEAYWGIHTLRAVENFNISNVTISDVPEFVRGMVMVKKATALANGELGAIPSDIAKAIVAACDEILTTGKCLDQFPSDVYQGGAGTSVNMNTNEVVANLALEKIGHKKGEYNVINPMDHVNASQSTNDAYPTGFRIAVYNSILKLIDKIQYLHDSFDNKAKEFANILKMGRTQLQDAVPMTVGQEFKAFAVLLEEEVRNLKRTAGLLLEVNLGATAIGTGLNTPQGYTELVVKHLAEVTGLACVPAENLIEATSDCGAYVMVHGALKRTAVKLSKVCNDLRLLSSGPRAGLKEINLPELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTFASEAGQLQLNVMEPVIGQAMFESIDILTNACVNLRDKCVDGITVNKEICENYVFNSIGIVTYLNPFIGHHNGDLVGKICAQTGKGVREVVLEKGLLTEEQLDDILSVENLMNPTYKAKLNK
Protein: Pannexin-2 (Q96RD6)
Organism: Homo sapiens (Human)
Function: Structural component of the gap junctions and the hemichannels.
Subcellular location: Cell membrane {ECO:0000305|PubMed:36973289}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IMP4}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6IMP4}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Note=Localizes to Golgi apparatus and endoplasmic reticulum in multipotential neural stem and progenitor cells and to plasma membrane in terminally differentiated neurons. {ECO:0000250|UniProtKB:Q6IMP4}.
Interaction partners:
- Pannexin-1
Sequence:
MHHLLEQSADMATALLAGEKLRELILPGAQDDKAGALAALLLQLKLELPFDRVVTIGTVLVPILLVTLVFTKNFAEEPIYCYTPHNFTRDQALYARGYCWTELRDALPGVDASLWPSLFEHKFLPYALLAFAAIMYVPALGWEFLASTRLTSELNFLLQEIDNCYHRAAEGRAPKIEKQIQSKGPGITEREKREIIENAEKEKSPEQNLFEKYLERRGRSNFLAKLYLARHVLILLLSAVPISYLCTYYATQKQNEFTCALGASPDGAAGAGPAVRVSCKLPSVQLQRIIAGVDIVLLCVMNLIILVNLIHLFIFRKSNFIFDKLHKVGIKTRRQWRRSQFCDINILAMFCNENRDHIKSLNRLDFITNESDLMYDNVVRQLLAALAQSNHDATPTVRDSGVQTVDPSANPAEPDGAAEPPVVKRPRKKMKWIPTSNPLPQPFKEPLAIMRVENSKAEKPKPARRKTATDTLIAPLLDRSAHHYKGGGGDPGPGPAPAPAPPPAPDKKHARHFSLDVHPYILGTKKAKAEAVPAALPASRSQEGGFLSQAEDCGLGLAPAPIKDAPLPEKEIPYPTEPARAGLPSGGPFHVRSPPAAPAVAPLTPASLGKAEPLTILSRNATHPLLHINTLYEAREEEDGGPRLPQDVGDLIAIPAPQQILIATFDEPRTVVSTVEF
Protein: Dynactin subunit 4 (Dynactin subunit p62) (Q9QUR2)
Organism: Rattus norvegicus (Rat)
Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UJW0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UJW0}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:10607597}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10607597}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:Q8CBY8}. Note=Has a punctate cytoplasmic distribution as well as centrosomal distribution typical of dynactin (By similarity). Overexpression in cultured mammalian cells revealed colocalization with cortical actin, stress fibers, and focal adhesion sites, sites of potential interaction between microtubules and the cell cortex (PubMed:10607597). In skeletal muscles, costamere localization requires the presence of ANK2 (By similarity). {ECO:0000250|UniProtKB:Q8CBY8, ECO:0000250|UniProtKB:Q9UJW0, ECO:0000269|PubMed:10607597}.
Interaction partners:
- Dynactin subunit 6
- Dynactin subunit 5
- Dynactin subunit 2
- Actin-related protein 10
- Dynactin subunit 1
- Dynactin subunit 3
- Alpha-centractin
- Beta-centractin
- Actin, cytoplasmic 1
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MASLLQSERVLYLVQGEKKVRAPLSQLYFCRYCSELRSLECVSHEVDSHYCPSCLENMPSAEAKLKKNRCANCFDCPGCMHTLSTRATSISTQLPDDPAKTTMKKAYYLACGFCRWTSRDVGMADKSVASGGWQEPENPHAQRMNKLIEYYQQLAQKEKVERDRKKLARRRNYMPLAFSQHTIHVVDKYSLGTRLQRPRAGASISTLAGLSLREGEDQKEVKIEPAQAVAEVEPLPEDYYTRPVNLTEVTTLQQRLLQPDLQPVSASQLYPRHKHLLIKRSLRCRKCEHNLSKPEFNPTSIKFKIQLVAVNYIPEVRIMSIPNLRYMKESQVLLTLTNPVENLTHVTLLECEEGDPDNINSTAKVVVPPKELILAGKDAAAEYDELAEPQDFQDDPDIVAFRKANKVGIFIKVTPQREEGDVTVCFKMKHDFKNLAAPIRPMEESDQGTEVIWLTQHVELSFGPLLP
Protein: Coiled-coil alpha-helical rod protein 1 (Alpha-helical coiled-coil rod protein) (A0A1U9X7G6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MWPHSAGARPWASTLTGKDPRVMACWCLDGLPSGLAEPWRELWRWRSRPLHCVPPFSPLARSSRDHRNLRRRGNIDGWRQNLEPSNNVEMFPPSGHQDVSERRLDTQRPQVTMWERDVSSDRQEPGRRGRSWGLEGSQALSQQAEVIVRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELEALARAEKAGRAEAEGLRAALAGAEVVRKNLEEGSQRELEEVQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLSSLETRRAGEAKELAEAQREAELLRKQLSKTQEDLEAQVTLVENLRKYVGEQVPSEVHSQTWELERQKLLETMQHLQEDRDSLHATAELLQVRVQSLTHILALQEEELTRKVQPSDSLEPEFTRKCQSLLNRWREKVFALMVQLKAQELEHSDSVKQLKGQVASLQEKVTSQSQEQAILQRSLQDKAAEVEVERMGAKGLQLELSRAQEARRRWQQQTASAEEQLRLVVNAVSSSQIWLETTMAKVEGAAAQLPSLNNRLSYAVRKVHTIRGLIARKLALAQLRQESCPLPPPVTDVSLELQQLREERNRLDAELQLSARLIQQEVGRAREQGEAERQQLSKVAQQLEQELQQTQESLASLGLQLEVARQGQQESTEEAASLRQELTQQQELYGQALQEKVAEVETRLREQLSDTERRLNEARREHAKAVVSLRQIQRRAAQEKERSQELRRLQEEARKEEGQRLARRLQELERDKNLMLATLQQEGLLSRYKQQRLLTVLPSLLDKKKSVVSSPRPPECSASAPVAAAVPTRESIKGSLSVLLDDLQDLSEAISKEEAVCQGDNLDRCSSSNPQMSS
Protein: Argonaute RISC component 1 (Q5TA58)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.
Interaction partners:
Sequence:
MVQHFKPQIFGDRKPVYDGKKNIYTVTALPIGNERVDFEVTIPGEGKDRIFKVSIKWLAIVSWRMLHEALVSGQIPVPLESVQALDVAMRHLASMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWKMMLNIDVSATAFYKAQPVIEFMCEVLDIRNIDEQPKPLTDSQRVRFTKEIKGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLQLESGQTVECTVAQYFKQKYNLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLMKNASYNLDPYIQEFGIKVKDDMTEVTGRVLPAPILQYGGRNRAIATPNQGVWDMRGKQFYNGIEIKVWAIACFAPQKQCREEVLKNFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYSGLQLIIVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINVKLGGINNILVPHQRSAVFQQPVIFLGADVTHPPAGDGKKPSITAVVGSMDAHPSRYCATVRVQRPRQEIIEDLSYMVRELLIQFYKSTRFKPTRIIFYRDGVPEGQLPQILHYELLAIRDACIKLEKDYQPGITYIVVQKRHHTRLFCADKNERIGKSGNIPAGTTVDTNITHPFEFDFYLCSHAGIQGTSRPSHYYVLWDDNRFTADELQILTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKEHDSGEGSHISGQSNGRDPQALAKAVQVHQDTLRTMYFA