wanglab/gogpt-training-data huggingface dataset:
Protein: Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC 2.7.12.1) (Q92630)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro).
Subcellular location: Cytoplasm. Nucleus. Note=Translocates into the nucleus following DNA damage.
Interaction partners:
- DDB1- and CUL4-associated factor 1
- DNA damage-binding protein 1
- E3 ubiquitin-protein ligase UBR5
- Cellular tumor antigen p53
- Serine-protein kinase ATM
- DDB1- and CUL4-associated factor 7
- E3 ubiquitin-protein ligase Mdm2
Sequence:
MLTRKPSAAAPAAYPTGRGGDSAVRQLQASPGLGAGATRSGVGTGPPSPIALPPLRASNAAAAAHTIGGSKHTMNDHLHVGSHAHGQIQVQQLFEDNSNKRTVLTTQPNGLTTVGKTGLPVVPERQLDSIHRRQGSSTSLKSMEGMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRRLPKPPTGEKTSVKRITESTGAITSISKLPPPSSSASKLRTNLAQMTDANGNIQQRTVLPKLVS
Protein: Calreticulin (EhCRT) (P83003)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Plays a role in host cell phagocytosis, possibly by acting as a receptor for host C1q. Binding to C1q prevents the activation of the host classical complement pathway. Also, binds to apoptotic host cells independently of host C1q and collectins.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:18160113, ECO:0000269|PubMed:20922421, ECO:0000269|PubMed:22473608}. Cell projection, uropodium {ECO:0000269|PubMed:18160113}. Cell surface {ECO:0000269|PubMed:22473608, ECO:0000269|PubMed:24860808}. Cell projection, phagocytic cup {ECO:0000269|PubMed:22473608}. Note=During the early stages of host cell phagocytosis, localizes to the phagocytic cup. {ECO:0000269|PubMed:22473608}.
Interaction partners:
Sequence:
MFTLFLLIALSSAKVYFHETFENRDKWIDSTSSGKALGPFKIVSGKWYGDANNKGLQTSEDNKFYIAAAKLDEEFSNKDKNLIVQYNLKFEQGIDCGGGYIKLLPKKSIESEEKFTPESEYNIMFGPDVCGGSKRTHVIMNYKGKNNLIRKEIKCESDDISHLYTLIIRPNNTYVVKIDGVEKQEGKFDEDWDMLAPKEIDDPNVSKPADWVDEKEIDDPNDKKPEGWDDIPKTIVDPNAKKPEEWNDEDDGEWEAPTIENPEYKGEWKPKRIPNPAYKGEWVHPQIANPDYVYDPELYKYDSFAYIGIDVWQVKAGTIYDDILITDDIEEAEKEAKVILERNAAEKKMRDEIKEAEKQKEEEAKKEAEKQKEEETKEEIKKEENKEEL
Protein: FCS-Like Zinc finger 10 (Q9LYE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway. Negatively regulates KIN10 leading to a repression of the SnRK1 signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29406622}. Nucleus {ECO:0000269|PubMed:29406622}. Endoplasmic reticulum {ECO:0000269|PubMed:29406622}. Note=Co-localized with ER marker when associated with KIN11. {ECO:0000269|PubMed:29406622}.
Interaction partners:
- FCS-Like Zinc finger 12
- FCS-Like Zinc finger 16
- FCS-Like Zinc finger 17
Sequence:
MSQHSNYQMTTASDYYSTKPVLSAIRSHKLISSVFEGKCPSDYESAWSPTSPLDFRLFSTLGNPFAASSSRSIWRGKQRSWDSGKVGLSIVHSLVDDHHTDSSATIVLPSPDSKNIIFGSLMRSGQKPHLLSQPFTKALMPKDVIPNAVFEIGHDVIDVLELRKSGSVDAAYCSGAENFSVNNNACQVTKQDPGSLNGGTESDMEISEDYTCVISHGPNPKTTHFYGDQVMESVEREELKNRCCKNEKESIFAVAPLDLTTPVDVLPPKDFLSFCYGCSKKLGMGEDIYMYSGYKAFCSSECRSKEIDLDEEMEDGDEEEAIKSVSSSDKESKKKSNGVFFTVG
Protein: Uncharacterized protein C4B3.03c (Q9USJ3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- GMP synthase
- Putative glutamine amidotransferase-like protein C13C5.04
Sequence:
MSLLRIRKASLYGFSTVFILLQSYAVAYPLRAFRQNDGIGIAMNPSQDGGFVSAEKDSDFEYWMKLIISAVLILLGGVFAGLTIGLMGCDDLHLQVLEQSGDASERVHARKVLKLLRRGKHWVLVTLLLGNVIVNETLPIVFDSIIGGGWPAVLISTAMIVIFGEVIPQATCVRYGLSIGAKLEPIVLFMMYLLWPIAYPTALILDACLGESQSTMYKKSGLKTLVTLHRDLGIDKLNQDEVTIITAVLDLREKHAESIMTPIEDVFTLPMDRILDEDLIGEIICAGYSRIPVHKPGFPHDFIGMLLTKTLIGYDPDDKWPVGKFALATLPQTWPNTSCLDLLNYCQEGKSHMILISNSPGEPHGAIGVITLEDIIEELIGEEIIDETDVYIDVHKGLPRVGENNDFWNRMLHRSHLSTMAALHKSQRSHDLAANEHAPILNPKNSALNPRLVTNDRVKVKSPSLIQSSTGYGSMSQSPSRSDLPSKISRVNAELQAHGSQRSSIDVSKENKSSVADGPSSQAHNGPSTQPPEALPNGTDPSSSKTTENNGNQQSERTESADGKKDNSGSISSNSSKTFTGKRVRLGNVIESNVVSPDGTNRIVIEPFERSVDPNNADIVEMVERNGIVVPKVTVTSHEDDVDSVHNTPMSVSSTLSVKTSSSKVPRNKRKRRKGKSKK
Protein: Coxsackievirus and adenovirus receptor homolog (CAR) (rCAR) (Q9R066)
Organism: Rattus norvegicus (Rat)
Function: Component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. Also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. Upon epithelial CXADR-binding, JAML induces downstream cell signaling events in gamma-delta T-cells through PI3-kinase and MAP kinases. It results in proliferation and production of cytokines and growth factors by T-cells that in turn stimulate epithelial tissues repair (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P78310}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:P78310}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P78310}. Note=In epithelial cells localizes to the apical junction complex composed of tight and adherens junctions. In airway epithelial cells localized to basolateral membrane but not to apical surface. {ECO:0000250|UniProtKB:P78310}.
Interaction partners:
- Junctional adhesion molecule-like
Sequence:
MALLLCFVLLCGVADFTSSLSITTPEQRIEKAKGETAYLPCKFTLEPEDQGPLDIEWLISPSDNQKVDQVIILYSGDKIYDNYYPDLKGRVHFTSNDVKSGDASINVTNLQLSDIGTYQCKVKKAPGVANRKFLLTVLVKPSGTRCFVDGSGEIGNDFKLKCEPKEGSLPLQYEWQKLSDSQKMPTPWLAEMTSPVISVKNASSEYSGTYSCTVQNRVGSDQCMLRLDVVPPSNRAGTIAGAVIGTLLALVLIGAILFCCHKKRREEKYEKEVHHDIREDVPPPKSRTSTARSYIGSNHSSLGSMSPSNMEGYSKTQYNQVPSEDFERAPQSPTLAPAKVAAPNLSRMGAVPVMIPAQSKDGSIV
Protein: Acyl-protein thioesterase 1 (EC 3.1.2.22) (Lysophospholipase 1) (Lysophospholipase I) (Palmitoyl-protein hydrolase) (Q6IAQ1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
Protein: NFkB (Q20KN1)
Organism: Carcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus rotundicauda)
Interaction partners:
Sequence:
MDTSVSHVTSKMVPTNPTPYVRLVEQPASRALRFRYECEGRSAGSIPGANSTAECKTYPTIQVVNYKGSAVVVVSCVTKEGPPFRPHPHNLVGREGCKKGICTMVINNHDMTCSFSSLGIQCVKRKDIEESLKLREMIKVDPYRTGFDHRLQTSNIDLNVVRLCFQVFIEGPQQGKYTVPLPPVVSDPIFDKKAICELTINKLSHYSAPVCGGSEVILLCDKVAKDDIKVRFYEERAGRVEWESFGEFHPNEVHKQVAIPFRTPRYRDENVQQPIPVFIQLYRPSDGSSSDPRPFQLLPVNRDPEGLSRKRQKIEDGCLDRFLKENIFGAARDAGGPLTPHTIPRTIKQATRTVLKPETVLEGKSNPMPELFLQPSQLPHLPVFTPELRAGATSGGVVTVGVASTVTTCSGLSATSIVEHQDRVGLCSPFYPNTTLSTASSQDILAIATKQVSSIPKSEPSSVLGHQSAEMSLEETTEKLDSLDLGIEPLDIQNILDYGETGNISLNLSQSLFDSGNNLPVSNMLVATSVDYMNASTNSFSFLQNELETLNVLCKSRTNEST
Protein: Receptor-like protein 9DC3 (Q5MR23)
Organism: Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium)
Function: Involved in plant defense. Confers resistance to the fungal pathogen C.fulvum through recognition of the AVR9 elicitor protein.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGCVKLVFFMLYVFLFQLVSSSSLPHLCPEDQALALLQFKNMFTVNPNAFHYCPDITGREIQSYPRTLSWNKSTSCCSWDGVHCDETTGQVIALDLRCSQLQGKFHSNSSLFQLSNLKRLDLSNNNFIGSLISPKFGEFSDLTHLDLSDSSFTGVIPSEISHLSKLHVLLIGDQYGLSIVPHNFEPLLKNLTQLRELNLYEVNLSSTVPSNFSSHLTTLQLSGTGLRGLLPERVFHLSDLEFLDLSYNSQLMVRFPTTKWNSSASLMKLYVHSVNIADRIPESFSHLTSLHELDMGYTNLSGPIPKPLWNLTNIESLDLRYNHLEGPIPQLPIFEKLKKLSLFRNDNLDGGLEFLSFNTQLERLDLSSNSLTGPIPSNISGLQNLECLYLSSNHLNGSIPSWIFSLPSLVELDLSNNTFSGKIQEFKSKTLSAVTLKQNKLKGRIPNSLLNQKNLQLLLLSHNNISGHISSAICNLKTLILLDLGSNNLEGTIPQCVVERNEYLSHLDLSKNRLSGTINTTFSVGNILRVISLHGNKLTGKVPRSLINCKYLALLDLGNNQLNDTFPNWLGHLSQLKILSLRSNKLHGPIKSSGNTNLFTRLQIMDLSYNGFSGNLPESILGNLQAMKKIDESTRTPEYISDPYDFYYNYLTTITTKGQDYDSVRILDSNMIINLSKNRFEGRIPSIIGDLVGLRTLNLSHNVLEGHIPASFQNLSVLESLDLSSNKISGEIPQQLASLTFLEVLNLSHNHLVGCIPKGKQFDSFGNTSYQGNDGLCGFPLSKLCGGDDQVTTPAELDQEEEEEDSPMISWQGVLVGYGCGLVIGLSVIYIMWSTQYPAWFSRMHLKLEQIVTTRMKKHKKRY
Protein: Vacuolar protein-sorting-associated protein 25 (ESCRT-II complex subunit VPS25) (Q9CQ80)
Organism: Mus musculus (Mouse)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Endosome membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Distributes diffusely throughout the cytoplasm and nucleoplasm, but exhibits a punctate distribution on coexpression with CHMP6. {ECO:0000250}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein SNF8
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 28 homolog
- Charged multivesicular body protein 3
- Charged multivesicular body protein 2a
- Tumor susceptibility gene 101 protein
- Vacuolar protein sorting-associated protein 37A
- Vacuolar protein sorting-associated protein 37B
- Charged multivesicular body protein 7
Sequence:
MAMSFEWPWQYRFPPFFTLQPNVDTRQKQLAAWCSLVLSFCRLHKQSSMTVMEAQESPLFNNVKLQRKLPVESIQIVLEELRKKGNLEWLDKNKSSFLIMWRRPEEWGKLIYQWVSRSGQNNSVFTLYELTSGEDTEDEEFHGLDEATLLRALQALQQEHKAEIITVSDGRGVKFF
Protein: Rho-related GTP-binding protein RhoJ (Ras-like protein family member 7B) (Tc10-like GTP-binding protein) (Q9H4E5)
Organism: Homo sapiens (Human)
Function: Plasma membrane-associated small GTPase specifically involved in angiogenesis. Required for endothelial cell migration during vascular development via its interaction with GLUL. Elicits the formation of F-actin-rich structures, thereby regulating endothelial cell migration.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27660391, ECO:0000269|PubMed:30158707}; Lipid-anchor {ECO:0000269|PubMed:30158707}; Cytoplasmic side {ECO:0000305}. Note=Localization to the plasma membrane is regulated by GLUL. {ECO:0000269|PubMed:30158707}.
Interaction partners:
- Dedicator of cytokinesis protein 8
- Serine/threonine-protein kinase PAK 1
- Serine/threonine-protein kinase PAK 2
- Partitioning defective 6 homolog beta
- Actin nucleation-promoting factor WAS
- Protein kinase C iota type
- Dedicator of cytokinesis protein 11
- Serine/threonine-protein kinase PAK 3
- Partitioning defective 6 homolog gamma
- Actin nucleation-promoting factor WASL
Sequence:
MNCKEGTDSSCGCRGNDEKKMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVTVTVGGKQHLLGLYDTAGQEDYNQLRPLSYPNTDVFLICFSVVNPASYHNVQEEWVPELKDCMPHVPYVLIGTQIDLRDDPKTLARLLYMKEKPLTYEHGVKLAKAIGAQCYLECSALTQKGLKAVFDEAILTIFHPKKKKKRCSEGHSCCSII
Protein: UDP-glycosyltransferase 76E1 (EC 2.4.1.-) (Q9LTH3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase and 7-O-glucosyltransferase activities in vitro.
Interaction partners:
Sequence:
MEELGVKRRIVLVPVPAQGHVTPIMQLGKALYSKGFSITVVLTQYNRVSSSKDFSDFHFLTIPGSLTESDLKNLGPFKFLFKLNQICEASFKQCIGQLLQEQGNDIACVVYDEYMYFSQAAVKEFQLPSVLFSTTSATAFVCRSVLSRVNAESFLLDMKDPKVSDKEFPGLHPLRYKDLPTSAFGPLESILKVYSETVNIRTASAVIINSTSCLESSSLAWLQKQLQVPVYPIGPLHIAASAPSSLLEEDRSCLEWLNKQKIGSVIYISLGSLALMETKDMLEMAWGLRNSNQPFLWVIRPGSIPGSEWTESLPEEFSRLVSERGYIVKWAPQIEVLRHPAVGGFWSHCGWNSTLESIGEGVPMICRPFTGDQKVNARYLERVWRIGVQLEGELDKGTVERAVERLIMDEEGAEMRKRVINLKEKLQASVKSRGSSFSSLDNFVNSLKMMNFM
Protein: Nuclear transcription factor Y subunit nfya-1 (CAAT box DNA-binding protein subunit nfya-1) (G5EEG1)
Organism: Caenorhabditis elegans
Function: Component of the sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types. In association with the components in the nfya-1-NF-Y complex, represses the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues. May act to repress txb-2 expression in conjunction with tbx-2 itself, which has an autoregulatory role (Probable). With the components in this complex, negatively regulates the expression of the homeobox protein egl-5 to spatially restrict its expression in tissues such as the head. May regulate egl-5 expression in association with the mes-2-mes-3-mes-6 complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:17574230}.
Interaction partners:
- Nuclear transcription factor Y subunit nfyc-1
- Nuclear transcription factor Y subunit nfyb-1
- RNA polymerase I associated factor, A49-like protein
Sequence:
MNGASRGDVQRPTPVQAPAKRPIPPTVFRFEKASKIGTSLDTTPKELPIRRPVPLPGPRFVKDVNPSPPATSSPNVQTQCHQPPVVRSQTHQASVSQTTPTQTTPSQYTPASVSTARAPQFHRSSHVTPSQQQRIEQAFGPAPVSQSQPQNGSYIQYNEPSTSVASTTTSFYSPNESEPVFTHAISFKPNEPENGQKAREQLELLDSGKINEINQSKVPTTIELPPNCKLFQYSWVLDGIPRTLLVPMPMDATEEDVKAMLPKTLEMDSNLFNNARPRDELPVLSFPNGTVPNVEMIGPKVQQPMLVNPKQFNRIMRRREMRQQLEASGRLPLARQKYLHESRHLHALKRKRGLDGRFDNTKTAESSSMVSSTTSPRKLKRRNRLPGEETSDSSSIVLPSPVEIQPKGGIVNSSMPSTSTGYINNGMDHQTDYIEHQQPMSTYDQYHDHVQYIAPDGNVNYHNNHDNGVDLTGSDGQSFTNL
Protein: 3-isopropylmalate dehydrogenase (3-IPM-DH) (IMDH) (EC 1.1.1.85) (Beta-IPM dehydrogenase) (P18869)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Subcellular location: Cytoplasm.
Interaction partners:
- 3-isopropylmalate dehydratase
- Orotidine 5'-phosphate decarboxylase
- Phosphoribosylaminoimidazole carboxylase
- Probable acetolactate synthase small subunit
- Acetolactate synthase, mitochondrial
- Homoaconitase, mitochondrial
- Threonine dehydratase, mitochondrial
- Histidinol-phosphate aminotransferase
- L-2-aminoadipate reductase
- 2-isopropylmalate synthase
Sequence:
MCAKKIVVLPGDHIGPEIVASALEVLKVVEKKRPELKLEFEEHKIGGASIDAYGTPLTDETVKACLEADGVLLGAVGGPEWTNPNCRPEQGLLKLRKSMGVWANLRPCNFASKSLVKYSPLKPEIVEGVDFCVVRELTGGCYFGERTEDNGSGYAMDTWPYSLEEVSRIARLAAWLAETSNPPAPVTLLDKANVLATSRLWRKTVAKIFKEEYPHLTLKNQLIDSAAMLLVKSPRTLNGVVLTDNLFGDIISDEASVIPGSLGLLPSASLSGVVGKSEEKVHCLVEPIHGSAPDIAGKGIVNPVGTILSASLLLRYGLNAPKEAEAIEAAVRKVLDDTSIGGRGLYTRDLGGEASTADITKAVVEELEKIL
Protein: T cell receptor gamma, variable 3 (A0A0G2JEW2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLLLRMFTSCCCLWVFGLGQLEQTELSVTRATDESAQISCIVSLPCFSNTAIHWYRQKPNQQFEYLIYVETNYNQQPLGGKNKKIEASKDFQTSTSTLKINYLKKEDEATYYCAVWI
Protein: Phenazine antibiotic resistance protein EhpR (Q8GPH6)
Organism: Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Function: Required for resistance to the phenazine antibiotic D-alanylgriseoluteic acid (AGA), an antibiotic produced by E.agglomerans itself, and thus protects the bacterium against phenazine toxicity. Probably binds AGA and acts as a chaperone that works in tandem with a membrane transporter for subsequent antibiotic secretion.
Interaction partners:
Sequence:
MTDLAGPTITPNLQLVYVSNVERSTDFYRFIFKKEPVFVTPRYVAFPSSGDALFAIWSGGEEPVAEIPRFSEIGIMLPTGEDVDKLFNEWTKQKSHQIIVIKEPYTDVFGRTFLISDPDGHIIRVCPLD
Protein: CAP-Gly domain containing linker protein family member 4 (E7EW06)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTIEDLPDFPLEGNPLFGRYPFIFSASDTPVIFSISAAPMPSDCEFSFFDPNDASCQEILFDPKTSVSELFAILRQWVPQVQQNIDIIGNEILKRGCNVNDRDGLTDMTLLHYTCKSGAHGIGDVETAVKFATQLIDLGADISLRSRWTNMNALHYAAYFDVPELIRVILKTSKPKDVDATCSDFNFGTALHIAAYNLCAGAVKCLLEQGANPA
Protein: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 (SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily d, member 1) (Smarcd1 protein) (Q802C8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily c, member 2.
- Brahma protein-like protein 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1-A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF complex subunit SMARCC1 isoform X1
- Actin-like 6A
- PHD finger protein 10
- AT-rich interactive domain 1B
- Actin-like 6B
Sequence:
MAARSGFQPSTPGGGGAPMGPGPPVAGAGPGMGPGTPSGRMGPGGPQNHMYRSPMPGYPRPGMPPASRMTPQGPSMGPPGYGASPVSRPGMPVMDPSRKRPAPNQIQQVQQQNRNQHAKKKKMADKILPQRIRELVPESQAYMDLLAFERKLDQTIMRKRLDIQEALKRPIKQKRKLRIFISNTFNPAKPDAEDGEGTVASWELRVEGRLLEDTAVSKYEATKQKRKFSSFFKSLVIELDKDLYGPDNHLVEWHRTATTQETDGFQVKRPGDVGVRCTVLLMLDYQPPQYKLDPRLARLLGIHTQTRPVIIQALWQYVKTHKLQDPHEREFINCDKYLQQIFETQRMKFSEIPQRLHALLMPPEPIIINHVISVDPNDQKKTACYDIDVEVDDTLKTQMNSFLLSTASQQEIAGLDNKIHETIETINQLKTQREFMLSFARDPQGFINDWLQSQCRDLKTMTDVVGNPEEERRAEFYYQPWAQEAVCRYFYSKVQQRRQELEQALGIRNT
Protein: ABC-type organic anion transporter ABCA8B (EC 7.6.2.-) (ATP-binding cassette sub-family A member 8B) (Q8K440)
Organism: Mus musculus (Mouse)
Function: Mediates cholesterol and taurocholate efflux. Through the interaction with ABCA1 potentiates the cholesterol efflux to lipid-free APOA1, in turn regulates high-density lipoprotein cholesterol levels (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O94911}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O94911}. Basolateral cell membrane {ECO:0000269|PubMed:29300488}. Note=Predominantly expressed on the sinusoidal plasma membrane in hepatocytes. {ECO:0000269|PubMed:29300488}.
Interaction partners:
- ABC-type organic anion transporter ABCA8A
Sequence:
MIKREISVRQQTCALLQKNLLKKWRLKRESLMEWVSSLLLLLFLYWYPHGHGATDLSSVPTKDLGRVDSFRQSGFMIGYTPVTSMTQQIMEKVAATPFMADKKVLGLLDEENIKELTESHAEIIRVIFSDTFSYHLKFQFDQRIPTSRELRDHNAHCDGLYEDVNCLIAIFWKEGFVALQAAINAAIIETTTNHSVMEELLSVSGKFMKIHPFVRQEGILTDFFIFTCIISFSPITYYVSINVARERKRMKGLMMMMGLRDPAFWLSWGLLYAGFVFIMALSLALVIKSVQFFILTSFMVVFSLFLLYGLSMITLAFLMSALVRKSVLTGLSVFLLTIFWGSLGFTSLYRYLPAPVEWTLSLFSPFAFTLGMAQLLRVDYDLNSNAPPDPASGSNLIIATNFMLVFDAFLYLALMMYFEKVLPNEYGHQHSPLFFLKSSFWLQTRKPAHVILEDGIDPVPSSGDSFEPVSPEFHGKESIRIRNISKEYKGKPNKIEALKDLTLDIYEGQITAVLGHSGAGKSTLLNILSGLSVPTKGSVTIYNNNLSEMADLENILRIAGVCPQANVQFDFLTVRENLRLFAKIRGIPPQDVEKEVQRVLLELEMKNIQNILAQNLSGGQKRKLTFGIAILGDSQIFLLDEPTAGLDPFSRHRVWNLLKERRADRVVLFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWGVGYHLSLQLKEVCVPENITSLVKQHIPAAKLSAEGEGKLLYTLPLETTYRFPELCQSLDSCPGLGIENYGVSMTTLNEVFLKLEGKASIDEPEVDIVGEGQTERSGDTERLMEMEQTLSSLRETEKTDGMALWRQQTCAIAKVRLLKLKHERKTLLSVLLILVVGICPFLFENISTKIRQSSYTWELSPHDYFLAPGQQPQGMLTQLLIINKTEASIDDFIHSVERQNIALEVDASGTRDGTDDPSYNGALIVSGNEKNHSFSFACNTKRLNCFPVLMDILSNGLLGMVKPSARIQTDRSTYLMDETIHPLEDLWKTAFWLILTSACPPYIAMSSVTDYKNRAWFQLRVSGLFPSAYWVGQAMVDIPLYCFVFLFMSLMDYLFRFPDTMFSIISHVIQIPCSVGYAISLIFLTYVISFISRKGKKNSGIWSLSFYIITVFSVAVILLAFDVDGTQYYIIFLIPPSTLVGCLILSLHLFIGQIFEEGQVIEPFLVFLIPFLHVFIFIFTLRCLEWKFGKKTMRKDPIFRISPRNNDVYQNPEEPEDEDEDVQMERMRTANALVSTSFDEKPVIIASCLRKEYAGKQKHCLSKKKAKIATRNVSFCVRKGEILGLLGHNGAGKSTSLKMISGDTKVTAGQVLLKGSREGDTPGFLGYCPQENALWPNLTVKEHLEIFAAVRGLRKSHAAVAITRLADALKLQDQLKSPVKTLSEGVKRKLCFVLSILGNPSILLLDEPSTGLDPEGQQQIWQAIRAIIKNTDRGALLTTHYMAEAEALCDRVAILVSGRLRCIGSIQHLKSKFGKDYLLEMKVKTLEQVEPLNTEILRLFPQASRQERYSSLMAYKLPVEAVQPLSQAFFKLEKVKQTFDLEEYSLSQSTLEQVFLELSKEQELDGLELEELDSSIKWKLLPQEEA
Protein: AT08706p (Q8T495)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRQKLKNYLPSVWEQQLRLVQTAKKAGGSKKLGPDRPPIIDPPKGYEPNCKTKFGPLDDCDRVFQNLYGRHDWRLHGACQRGDWHRTAELLEQGPEWIMKQWEFLRQTKSEKVPKMVIVNCAEGEPGTCKDRDILRHEPHKLIEGILLVGVAMGCGRAIVYIRNRFYNEACNLHFALAEAYHHGLLGNSVCGTGIKFDVMVQRGDRYLCGEETAMINCLMGKLGRPRRRPPFLTEKGYFEHPSLVINAESIAVVPTILRRGSQWWAGLGRSYNTGTKLYCLSGQVNNPCTVEEEMSIPLKDLIERHAGGVKGGWDNLAAVFPGGLSTPLLDPSTAGKVLMDFDSLTDAGSGFGCGAVIVMTKDCDPLAIMLRSIQFFEKHTCKQCSYCRDGAIWLPEIFARFVKGQTHPHEIDWTLVIADKMRNSKPICALAYSQVSVAESLVRMFSRQIEERLLKYAKGS
Protein: Tetranectin (TN) (C-type lectin domain family 3 member B) (Plasminogen kringle 4-binding protein) (P43025)
Organism: Mus musculus (Mouse)
Function: Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis (By similarity). Plays a role in retinal function (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Plasminogen
- Tumor necrosis factor
Sequence:
MGFWGTYLLFCLFSFLSQLTAESPTPKAKKAANAKKDLVSSKMFEELKNRMDVLAQEVALLKEKQALQTVCLKGTKVNLKCLLAFTQPKTFHEASEDCISQGGTLGTPQSELENEALFEYARHSVGNDANIWLGLNDMAAEGAWVDMTGGLLAYKNWETEITTQPDGGKAENCAALSGAANGKWFDKRCRDQLPYICQFAIV