wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional coenzyme A synthase (CoA synthase) [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT); Dephospho-CoA kinase (DPCK) (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (DPCOAK)] (Q9DBL7)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13057}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q13057}. Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but this protein is also present in cell lysate. {ECO:0000250|UniProtKB:Q13057}.
Interaction partners:
- Pantothenate kinase 2
- Phosphopantothenoylcysteine decarboxylase
- Pantothenate kinase 1
- Pantothenate kinase 3
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Phosphopantothenate--cysteine ligase
- DDB1- and CUL4-associated factor 17
- Endonuclease 8-like 3
Sequence:
MAVFRSGLLVLTTPLATLAARLPPILTSASRLVNHTLYVHLQPGMNLGGPAQPQASPVQATFEVLDFITHLYTGADLHRHLDVRILLTNIQTKSTFLPVLSSVQNLAHPPEVVLTDFQTLDGSQYNPVKQQLERYATSCYSCSPQLASVLLYPDYGTGELPLEPPNALLPSTIRPASPVARSPRQPVRGYHRGAVGGTFDRLHNAHKVLLSVACVLAQEQLVVGVADKDLLKSKLLPELLQPYAERVEHLTEFLVDIKPSLTFELVPLLDPYGPAGSDPTLEFLVVSEETYRGGMAVNRFRLENGKEELALYQIQLLKDQSHNENEEDKVSSSSFRQRILGNLLQPPNERPELPSGLYVLGLTGISGSGKSSVAQRLKNLGAYIIDSDHLGHRAYAPGGPAYQPVVEAFGTDILHKDGTINRKVLGSRVFGNKKQMKILTDIVWPVIAKLAREEMDVAVAKGKTLCVIDAAMLLEAGWQSMVHEVWTVVIPETEAVRRIVERDGLSEAAAQSRLQSQMSGQQLVEQSNVVLSTLWESHVTQSQVEKAWNLLQKRLPKAYQTRN
Protein: Dual specificity mitogen-activated protein kinase kinase 6 (MAP kinase kinase 6) (MAPKK 6) (EC 2.7.12.2) (MAPK/ERK kinase 6) (MEK 6) (Stress-activated protein kinase kinase 3) (SAPK kinase 3) (SAPKK-3) (SAPKK3) (P52564)
Organism: Homo sapiens (Human)
Function: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. With MAP3K3/MKK3, catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinases p38 MAPK11, MAPK12, MAPK13 and MAPK14 and plays an important role in the regulation of cellular responses to cytokines and all kinds of stresses. Especially, MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 and MAPK13 induced by environmental stress, whereas MAP2K6/MKK6 is the major MAPK11 activator in response to TNF. MAP2K6/MKK6 also phosphorylates and activates PAK6. The p38 MAP kinase signal transduction pathway leads to direct activation of transcription factors. Nuclear targets of p38 MAP kinase include the transcription factors ATF2 and ELK1. Within the p38 MAPK signal transduction pathway, MAP3K6/MKK6 mediates phosphorylation of STAT4 through MAPK14 activation, and is therefore required for STAT4 activation and STAT4-regulated gene expression in response to IL-12 stimulation. The pathway is also crucial for IL-6-induced SOCS3 expression and down-regulation of IL-6-mediated gene induction; and for IFNG-dependent gene transcription. Has a role in osteoclast differentiation through NF-kappa-B transactivation by TNFSF11, and in endochondral ossification and since SOX9 is another likely downstream target of the p38 MAPK pathway. MAP2K6/MKK6 mediates apoptotic cell death in thymocytes. Acts also as a regulator for melanocytes dendricity, through the modulation of Rho family GTPases.
Subcellular location: Nucleus {ECO:0000269|PubMed:9768359}. Cytoplasm {ECO:0000269|PubMed:9768359}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9768359}. Note=Binds to microtubules.
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase kinase kinase 7
- Mitogen-activated protein kinase kinase kinase 5
- Dual specificity mitogen-activated protein kinase kinase 3
- Mitogen-activated protein kinase kinase kinase 4
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 11
- Serine/threonine-protein kinase TAO2
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 1
Sequence:
MSQSKGKKRNPGLKIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDSVAKTIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGD
Protein: SNF1-activating kinase 1 (EC 2.7.11.1) (P38990)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase that phosphorylates SNF1, the catalytic subunit of the SNF1 kinase complex. Acts as an activator of the SNF1 kinase complex and controls its nuclear localization upon glucose and nitrogen depletion. Also required for SNF1 kinase activation under other stress conditions like alkaline pH or presence of cadmium.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
- 5'-AMP-activated protein kinase subunit gamma
- Serine/threonine-protein kinase ELM1
- SNF1 protein kinase subunit beta-1
- SNF1 protein kinase subunit beta-3
- SNF1 protein kinase subunit beta-2
- Serine/threonine-protein kinase TOS3
- Serine/threonine-protein phosphatase PP1-2
- Serine/threonine-protein kinase ATG1
- Regulatory protein MIG1
Sequence:
MDRSDKKVNVEEVNVPSNLQIELEKSGTSSSVSLRSPTKSSATNLAGMAEGARDNASIASSSVDSLNMLLERQRVRQLNHPQHQQHISSSLAKTPTTTSSFCSSGSSKNKVKETNRISLTYDPVSKRKVLNTYEIIKELGHGQHGKVKLARDILSKQLVAIKIVDRHEKKQRKFFTFIKSSKISENDKIKREIAIMKKCHHKHVVQLIEVLDDLKSRKIYLVLEYCSRGEVKWCPPDCMESDAKGPSLLSFQETREILRGVVLGLEYLHYQGIIHRDIKPANLLISGDGTVKISDFGVSLAASSTNSSDSSESLDELELAKTVGTPAFFAPEMCLGEDAFTRYNLTKENLFRGSCISFMIDIWAVGVTLYCLLFGMLPFFSDFELKLFEKIVNDPLKFPTFKEIQSNKVSKVSCEEEYEMAKDLLLKLLEKNPQKRMTIPAIKKHPFVSWDFDHVPENDEKLLSSVLEQKLRFQCNQTDQFEPISISKHELKNAVSGVGKKIKESVLKSIPLKDPSDLSNKNYLHPTETTRGRGDANVIVSEGSVLSNIKELSANDGCLNTDSDTNININDDDHYSGDDNDGHLTKRELERELNKFDDKHEAGNMVNLPINSSFASLDSFYIDNFAMARMGMSSPEAGDSVSSVPNLPSAPSSTRLGRSPVFSGVTNQPSPIRPVLPQQKSSFCATGRYDKSHNSLLRNSSSHLTSYNSGRPSSRTGRMNSRNQNLPKIPNSLSKISTTKLTELRVPKDSEIPSPAKNPNADRLRRFPVKKNTKTPAIKDPPRININSSDKSGSKNSPIKSLYQRMKQSKDNSKTFEVRRGNFFSHFNGDDDDSSSQSSVTSSGSESDSELSSTSSSCTSGTQSRNSSNNNAYSETESLPFEFGVDSEDGSGVLLRDLPNEDQIRPFLDIQPCRRMKVKSSLNLEPPSVSSSSSSSSDEDELILNVGTAGHRRRHNSSKLSELSNSPQKGSNNFMYSNGSVHDSETTITPQNMDDLTLHQALSRSQPISKPGPLVLPKRLDQKKATTETSNLTDIVEFNGNNDHRKDKNFDKVLYSRDLLKDALSSTNAGRRRSIPSNKIRGRKDASITMSTNVGNDEHARNTSCHGDKGQENGAIKQRTHERSRSLTVAELNEEKRRSALP
Protein: Hydroxyproline O-galactosyltransferase GALT5 (AtGALT5) (EC 2.4.1.-) (Beta-1,3-galactosyltransferase 18) (Q8RX55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. Utilizes UDP-galactose solely as sugar donor. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25974423}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Hydroxyproline O-galactosyltransferase HPGT2
- Hydroxyproline O-galactosyltransferase HPGT3
- Beta-glucuronosyltransferase GlcAT14C
- Fasciclin-like arabinogalactan protein 4
- Beta-glucuronosyltransferase GlcAT14B
- LRR receptor-like serine/threonine-protein kinase FEI 2
- Beta-glucuronosyltransferase GlcAT14A
- LRR receptor-like serine/threonine-protein kinase FEI 1
- Beta-1,3-galactosyltransferase 7
- Hydroxyproline O-galactosyltransferase HPGT1
Sequence:
MKKPKLSKVEKIDKIDLFSSLWKQRSVRVIMAIGFLYLVIVSVEIPLVFKSWSSSSVPLDALSRLEKLNNEQEPQVEIIPNPPLEPVSYPVSNPTIVTRTDLVQNKVREHHRGVLSSLRFDSETFDPSSKDGSVELHKSAKEAWQLGRKLWKELESGRLEKLVEKPEKNKPDSCPHSVSLTGSEFMNRENKLMELPCGLTLGSHITLVGRPRKAHPKEGDWSKLVSQFVIELQGLKTVEGEDPPRILHFNPRLKGDWSKKPVIEQNSCYRMQWGPAQRCEGWKSRDDEETVDSHVKCEKWIRDDDNYSEGSRARWWLNRLIGRRKRVKVEWPFPFVEEKLFVLTLSAGLEGYHINVDGKHVTSFPYRTGFTLEDATGLTVNGDIDVHSVFVASLPTSHPSFAPQRHLELSKRWQAPVVPDGPVEIFIGILSAGNHFSERMAVRKSWMQHVLITSAKVVARFFVALHGRKEVNVELKKEAEYFGDIVLVPYMDSYDLVVLKTVAICEHGALAFSAKYIMKCDDDTFVKLGAVINEVKKVPEGRSLYIGNMNYYHKPLRGGKWAVTYEEWPEEDYPPYANGPGYVLSSDIARFIVDKFERHKLRLFKMEDVSVGMWVEHFKNTTNPVDYRHSLRFCQFGCVENYYTAHYQSPRQMICLWDKLLRQNKPECCNMR
Protein: Flagellar basal-body rod protein FlgG (Distal rod protein) (P23446)
Organism: Bacillus subtilis (strain 168)
Subcellular location: Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Flagellar motor switch phosphatase FliY
- Flagellar M-ring protein
- FlaA locus uncharacterized protein YlxG
- Flagellar basal body rod protein FlgB
- Flagellar hook-basal body complex protein FliE
- Flagellar basal-body rod protein FlgC
- Flagellum-specific ATP synthase
- Flagellar biosynthetic protein FlhB
Sequence:
MLRSLYSGISGMKNFQTKLDVIGNNIANVNTVGFKKSRVTFKDMVSQTIAGGSAAGATIGGTNSKQIGLGSSSGTIDTIHSTSATQSTGRTLDLAIDGDGYFRIDTGDGTAYTRAGNFYLDNTGTLVTGDGYHVLNMNGGTIKIPTDAQSFSIGSDGKVSIVDAEGKTQDGGQIGIVTFANSDGLDKIGSNLYRESLNSGTASAANQPGDGGTGALKSGFLEMSNVDLTDEFTEMIVAQRGFQSNSKIITTSDEILQELVNLKR
Protein: Probable WRKY transcription factor 47 (WRKY DNA-binding protein 47) (Q9ZSI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
- P-loop nucleoside triphosphate hydrolase superfamily protein
Sequence:
MEEHIQDRREIAFLHSGEFLHGDSDSKDHQPNESPVERHHESSIKEVDFFAAKSQPFDLGHVRTTTIVGSSGFNDGLGLVNSCHGTSSNDGDDKTKTQISRLKLELERLHEENHKLKHLLDEVSESYNDLQRRVLLARQTQVEGLHHKQHEDVPQAGSSQALENRRPKDMNHETPATTLKRRSPDDVDGRDMHRGSPKTPRIDQNKSTNHEEQQNPHDQLPYRKARVSVRARSDATTVNDGCQWRKYGQKMAKGNPCPRAYYRCTMAVGCPVRKQVQRCAEDTTILTTTYEGNHNHPLPPSATAMAATTSAAAAMLLSGSSSSNLHQTLSSPSATSSSSFYHNFPYTSTIATLSASAPFPTITLDLTNPPRPLQPPPQFLSQYGPAAFLPNANQIRSMNNNNQQLLIPNLFGPQAPPREMVDSVRAAIAMDPNFTAALAAAISNIIGGGNNDNNNNTDINDNKVDAKSGGSSNGDSPQLPQSCTTFSTN
Protein: Chalcone isomerase-like protein 2 (HlCHIL2) (EC 5.5.1.6) (A0A2U7XUE3)
Organism: Humulus lupulus (European hop)
Function: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Involved in anthocyanin biosynthesis (By similarity). Polyketide binding proteins (PBP) which promotes the catalytic activities of CHS_H1 and PT1L and triggers demethylxanthohumol (DMX) production.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29760092}.
Interaction partners:
Sequence:
MENNMVMVHEIPFPPEIKTTKPLSLLGYGITDMEIHFLQVKFTAIGVYLDSDVVKHLQQWKGKKGNELAEDDDFFDALISAPVEKYLRIVVIKEIKGSQYGVQLESSVRDRLAAEDMYEEEEEAALEKIVEFLQSKYFKKDTLITFHFPATSPTAEIVVTLEGKEESKLKVENKNVVDMIKKWYLGGTSGVSPSTISSLADNLSAELSK
Protein: Cyclin-like domain-containing protein (O17869)
Organism: Caenorhabditis elegans
Interaction partners:
- Cyclin-dependent kinase 12
- Probable cyclin-dependent kinase 9
- Cyclin-H
- Transcription elongation factor SPT5
- Cyclin-dependent kinase 7
- DNA-directed RNA polymerase II subunit RPB1
- Cell division cycle protein 73
- Protein lin-11
- Cyclin-C
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
Sequence:
MSDWIWPLEALKTTPSIRAGLTKEQELLWRREGIKLLSEVGNALNCKPRPTIGVAAVYFHRFYMIHSFQSFSREVTALSCLFLAGKVEDFPKKCKDVCQAAVTHYPEIYSKYQNLVDDVMGLERVLLHSLKFDLHVALPYDALLDYKMMFPDMNREKITDAVQIAWTFINDSIYTTLCITTEPQMIAIALLHLAFTVKGYQPVQKNMDPCWWSADVSNWPQESVDKACHLVLDFYAATKEKPVLEKKKLTTF
Protein: Protein CUP-SHAPED COTYLEDON 2 (NAC domain-containing protein 98) (ANAC098) (NAC domain-containing protein CUC2) (O04017)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator of STM and KNAT6. Involved in molecular mechanisms regulating shoot apical meristem (SAM) formation during embryogenesis and organ separation. Required for the fusion of septa of gynoecia along the length of the ovaries. Activates the shoot formation in callus in a STM-dependent manner. Controls leaf margin development and required for leaf serration. Involved in axillary meristem initiation and separation of the meristem from the main stem. Regulates the phyllotaxy throughout the plant development. Seems to act as an inhibitor of cell division.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:15500463}.
Interaction partners:
- Transcription factor TCP4
- Floral homeotic protein APETALA 2
- Basic leucine zipper 8
- Transcription factor AS1
- Protein WUSCHEL
- Protein ASYMMETRIC LEAVES 2
- Protein VASCULATURE COMPLEXITY AND CONNECTIVITY
- Homeobox protein knotted-1-like 6
- Homeobox protein knotted-1-like 2
- Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 3
Sequence:
MDIPYYHYDHGGDSQYLPPGFRFHPTDEELITHYLLRKVLDGCFSSRAIAEVDLNKCEPWQLPGRAKMGEKEWYFFSLRDRKYPTGLRTNRATEAGYWKATGKDREIFSSKTCALVGMKKTLVFYKGRAPKGEKSNWVMHEYRLEGKFSYHFISRSSKDEWVISRVFQKTTLASTGAVSEGGGGGGATVSVSSGTGPSKKTKVPSTISRNYQEQPSSPSSVSLPPLLDPTTTLGYTDSSCSYDSRSTNTTVTASAITEHVSCFSTVPTTTTALGLDVNSFSRLPPPLGFDFDPFPRFVSRNVSTQSNFRSFQENFNQFPYFGSSSASTMTSAVNLPSFQGGGGVSGMNYWLPATAEENESKVGVLHAGLDCIWNY
Protein: Endoplasmic reticulum-Golgi intermediate compartment protein 2 (Q96RQ1)
Organism: Homo sapiens (Human)
Function: Possible role in transport between endoplasmic reticulum and Golgi.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cytoplasm. Nucleus. Note=Cycles between the endoplasmic reticulum and the Golgi. According to a report, localizes to the nucleus (PubMed:11445006). Another report shows a partial localization in the nucleus (PubMed:17980171). {ECO:0000269|PubMed:11445006, ECO:0000269|PubMed:17980171}.
Interaction partners:
- Endoplasmic reticulum-Golgi intermediate compartment protein 3
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- Derlin-2
- Derlin-3
- Ubinuclein-1
- Protein sel-1 homolog 1
- Protein sel-1 homolog 2
- Protein sel-1 homolog 3
Sequence:
MRRLNRKKTLSLVKELDAFPKVPESYVETSASGGTVSLIAFTTMALLTIMEFSVYQDTWMKYEYEVDKDFSSKLRINIDITVAMKCQYVGADVLDLAETMVASADGLVYEPTVFDLSPQQKEWQRMLQLIQSRLQEEHSLQDVIFKSAFKSTSTALPPREDDSSQSPNACRIHGHLYVNKVAGNFHITVGKAIPHPRGHAHLAALVNHESYNFSHRIDHLSFGELVPAIINPLDGTEKIAIDHNQMFQYFITVVPTKLHTYKISADTHQFSVTERERIINHAAGSHGVSGIFMKYDLSSLMVTVTEEHMPFWQFFVRLCGIVGGIFSTTGMLHGIGKFIVEIICCRFRLGSYKPVNSVPFEDGHTDNHLPLLENNTH
Protein: Probable pectinesterase/pectinesterase inhibitor 44 [Includes: Pectinesterase inhibitor 44 (Pectin methylesterase inhibitor 44); Pectinesterase 44 (PE 44) (EC 3.1.1.11) (Pectin methylesterase 44) (AtPME44)] (Q9SMY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Secreted, cell wall {ECO:0000250}.
Interaction partners:
- Probable pectate lyase 22
- Probable pectate lyase 15
- Non-specific lipid transfer protein GPI-anchored 2
- Probable pectate lyase 8
- Non-specific lipid transfer protein GPI-anchored 1
- Non-specific lipid-transfer protein 5
- Cytosolic endo-beta-N-acetylglucosaminidase 1
- Rop guanine nucleotide exchange factor 5
- Protein IQ-DOMAIN 18
- Endoglucanase 8
Sequence:
MSCLKYFLILLMLGLCVSSEENFQYDYLKVPASEFVSSINTIVVVIRQVSSILSQFADFSGDRRLQNAVSDCLDLLDFSSEELTWSASASENPKGKGNGTGDVGSDTRTWLSAALSNQATCMEGFDGTSGLVKSLVAGSLDQLYSMLRELLPLVQPEQKPKAVSKPGPIAKGPKAPPGRKLRDTDEDESLQFPDWVRPDDRKLLESNGRTYDVSVALDGTGNFTKIMDAIKKAPDYSSTRFVIYIKKGLYLENVEIKKKKWNIVMLGDGIDVTVISGNRSFIDGWTTFRSATFAVSGRGFLARDITFQNTAGPEKHQAVALRSDSDLSVFFRCAMRGYQDTLYTHTMRQFYRECTITGTVDFIFGDGTVVFQNCQILAKRGLPNQKNTITAQGRKDVNQPSGFSIQFSNISADADLVPYLNTTRTYLGRPWKLYSRTVFIRNNMSDVVRPEGWLEWNADFALDTLFYGEFMNYGPGSGLSSRVKWPGYHVFNNSDQANNFTVSQFIKGNLWLPSTGVTFSDGLYI
Protein: Laminin subunit gamma-2 (Cell-scattering factor 140 kDa subunit) (CSF 140 kDa subunit) (Epiligrin subunit gamma) (Kalinin subunit gamma) (Kalinin/nicein/epiligrin 100 kDa subunit) (Ladsin 140 kDa subunit) (Laminin B2t chain) (Laminin-5 subunit gamma) (Large adhesive scatter factor 140 kDa subunit) (Nicein subunit gamma) (Q13753)
Organism: Homo sapiens (Human)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
Interaction partners:
- Laminin subunit beta-3
- Laminin subunit alpha-3
- Laminin subunit alpha-4
- Integrin beta-4
- CD44 antigen
- Laminin subunit beta-2
- Collagen alpha-1
- Collagen alpha-1
- Laminin subunit alpha-5
- Integrin alpha-6
Sequence:
MPALWLGCCLCFSLLLPAARATSRREVCDCNGKSRQCIFDRELHRQTGNGFRCLNCNDNTDGIHCEKCKNGFYRHRERDRCLPCNCNSKGSLSARCDNSGRCSCKPGVTGARCDRCLPGFHMLTDAGCTQDQRLLDSKCDCDPAGIAGPCDAGRCVCKPAVTGERCDRCRSGYYNLDGGNPEGCTQCFCYGHSASCRSSAEYSVHKITSTFHQDVDGWKAVQRNGSPAKLQWSQRHQDVFSSAQRLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAHDVILEGAGLRITAPLMPLGKTLPCGLTKTYTFRLNEHPSNNWSPQLSYFEYRRLLRNLTALRIRATYGEYSTGYIDNVTLISARPVSGAPAPWVEQCICPVGYKGQFCQDCASGYKRDSARLGPFGTCIPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQPCQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPMGSEPVGCRSDGTCVCKPGFGGPNCEHGAFSCPACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ
Protein: Probable LRR receptor-like serine/threonine-protein kinase At1g56130 (EC 2.7.11.1) (C0LGH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Cell wall RBR3-like protein
Sequence:
MTRIRRSPCLLLLIIWFMCIAGSVQVVQSQNQTGATTHPDEARALNSIFAAWKIQAPREWNISGELCSGAAIDASVLDSNPAYNPLIKCDCSFQNSTICRITNIKVYAIDVVGPIPPELWTLTYLTNLNLGQNVLTGSLPPAIGNLTRMQWMTFGINALSGPVPKEIGLLTDLRLLGISSNNFSGSIPDEIGRCTKLQQMYIDSSGLSGRIPLSFANLVQLEQAWIADLEVTDQIPDFIGDWTKLTTLRIIGTGLSGPIPSSFSNLTSLTELRLGDISSGSSSLDFIKDMKSLSVLVLRNNNLTGTIPSTIGEHSSLRQVDLSFNKLHGPIPASLFNLSQLTHLFLGNNTLNGSFPTQKTQSLRNVDVSYNDLSGSLPSWVSLPSLKLNLVANNFTLEGLDNRVLPGLNCLQKNFPCNRGKGIYSDFSINCGGPEKRSVTGALFEREDEDFGPASFFVSAGQRWAASSVGLFAGSSNNIYIATSQSQFVNTLDSELFQSARLSASSVRYYGLGLENGGYTVTLQFAEIQILGSTSTTWKGLGRRRFDIYVQGRLVEKDFDVRRTAGDSTVRAVQRVYKANVSENHLEVHLFWAGKGTCCIPIQGAYGPLISAVSATPDFTPTVANKPPSKGKNRTGTIVGVIVGVGLLSILAGVVMFTIRKRRKRYTDDEELLGMDVKPYIFTYSELKSATQDFDPSNKLGEGGFGPVYKGNLNDGRVVAVKLLSVGSRQGKGQFVAEIVAISSVLHRNLVKLYGCCFEGEHRMLVYEYLPNGSLDQALFGDKTLHLDWSTRYEICLGVARGLVYLHEEASVRIVHRDVKASNILLDSRLVPQISDFGLAKLYDDKKTHISTRVAGTIGYLAPEYAMRGHLTEKTDVYAFGVVALELVSGRPNSDENLEEEKKYLLEWAWNLHEKSRDIELIDDKLTDFNMEEAKRMIGIALLCTQTSHALRPPMSRVVAMLSGDVEIGDVTSKPGYVSDWRFDDTTGSSLSGFQIKDTTGYSMSLVAPGSEISPRDSDFKPMLGSKINEGR
Protein: Reticulon-3 (Homolog of ASY protein) (HAP) (Neuroendocrine-specific protein-like 2) (NSP-like protein 2) (Neuroendocrine-specific protein-like II) (NSP-like protein II) (NSPLII) (O95197)
Organism: Homo sapiens (Human)
Function: May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. Induces the formation of endoplasmic reticulum tubules. Also acts as an inflammation-resolving regulator by interacting with both TRIM25 and RIGI, subsequently impairing RIGI 'Lys-63'-linked polyubiquitination leading to IRF3 and NF-kappa-B inhibition.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12811824, ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:17031492, ECO:0000269|PubMed:17182608, ECO:0000269|PubMed:17191123, ECO:0000269|PubMed:24262037, ECO:0000269|PubMed:29117567, ECO:0000269|PubMed:34313226}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16054885, ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:29117567}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Reticulon-4
- Beta-secretase 1
- Beta-secretase 2
- Receptor expression-enhancing protein 5
- Atlastin-3
- Translocation protein SEC62
- Reticulophagy regulator 1
- Gamma-aminobutyric acid receptor-associated protein
- Cell cycle progression protein 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
Sequence:
MAEPSAATQSHSISSSSFGAEPSAPGGGGSPGACPALGTKSCSSSCADSFVSSSSSQPVSLFSTSQEGLSSLCSDEPSSEIMTSSFLSSSEIHNTGLTILHGEKSHVLGSQPILAKEGKDHLDLLDMKKMEKPQGTSNNVSDSSVSLAAGVHCDRPSIPASFPEHPAFLSKKIGQVEEQIDKETKNPNGVSSREAKTALDADDRFTLLTAQKPPTEYSKVEGIYTYSLSPSKVSGDDVIEKDSPESPFEVIIDKAAFDKEFKDSYKESTDDFGSWSVHTDKESSEDISETNDKLFPLRNKEAGRYPMSALLSRQFSHTNAALEEVSRCVNDMHNFTNEILTWDLVPQVKQQTDKSSDCITKTTGLDMSEYNSEIPVVNLKTSTHQKTPVCSIDGSTPITKSTGDWAEASLQQENAITGKPVPDSLNSTKEFSIKGVQGNMQKQDDTLAELPGSPPEKCDSLGSGVATVKVVLPDDHLKDEMDWQSSALGEITEADSSGESDDTVIEDITADTSFENNKIQAEKPVSIPSAVVKTGEREIKEIPSCEREEKTSKNFEELVSDSELHQDQPDILGRSPASEAACSKVPDTNVSLEDVSEVAPEKPITTENPKLPSTVSPNVFNETEFSLNVTTSAYLESLHGKNVKHIDDSSPEDLIAAFTETRDKGIVDSERNAFKAISEKMTDFKTTPPVEVLHENESGGSEIKDIGSKYSEQSKETNGSEPLGVFPTQGTPVASLDLEQEQLTIKALKELGERQVEKSTSAQRDAELPSEEVLKQTFTFAPESWPQRSYDILERNVKNGSDLGISQKPITIRETTRVDAVSSLSKTELVKKHVLARLLTDFSVHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRIYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE
Protein: Paired box 6 (A0A1W2PNS7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQY