wanglab/gogpt-training-data huggingface dataset:
Protein: Protein lin-7 homolog B (Lin-7B) (hLin7B) (Mammalian lin-seven protein 2) (MALS-2) (Vertebrate lin-7 homolog 2) (Veli-2) (hVeli2) (Q9HAP6)
Organism: Homo sapiens (Human)
Function: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. May increase the amplitude of ASIC3 acid-evoked currents by stabilizing the channel at the cell surface (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O88951}; Peripheral membrane protein {ECO:0000250|UniProtKB:O88951}. Basolateral cell membrane {ECO:0000269|PubMed:11742811, ECO:0000269|PubMed:12967566}; Peripheral membrane protein {ECO:0000250|UniProtKB:O88951}. Cell junction {ECO:0000250|UniProtKB:O88951}. Postsynaptic density membrane {ECO:0000250|UniProtKB:O88951}; Peripheral membrane protein {ECO:0000250|UniProtKB:O88951}. Cell junction, tight junction {ECO:0000250|UniProtKB:O88951}. Note=Mainly basolateral in renal epithelial cells. {ECO:0000269|PubMed:11742811}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Rhotekin
- Amyloid-beta A4 precursor protein-binding family A member 1
- Protein lin-7 homolog C
- Disks large homolog 1
- Glutamate receptor ionotropic, NMDA 2B
- MAGUK p55 subfamily member 2
- MAGUK p55 subfamily member 3
- Protein PALS1
- Disks large homolog 4
Sequence:
MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEIRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEQHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHQSYSSLESRG
Protein: Alpha-mannosidase (EC 3.2.1.-) (A0A8I6AJ32)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLLRWLPLLGQLLLLWPLAARPASPIRAFVVPHSHMDVGWVYTVQESMRAYAANVYTTVVEELVRGRQRRFIAVEQEFFRLWWDGVASEQQKQQVRQLLDEGRLEFVLGGQVMHDEAVTHLDDQILQLTEGHGFLYETFGIRPQFSWHVDPFGASATTPTLFALAGFNAHLISRIDYDLKDAMQEAQGLQFVWHGSPSLSEQQEIYTHVMDLYSYCTPSHIPFSNRSGFYWNGVAVFPEPPPDGVYPNMSEPVTVDNIHLYAEALVANVKQRAAWFRTPHVLWPWGCDKQFFNASVQFDNMDPLLEYINNRSAQFGISVQYATLNDYFQALHDFNVTWDIRDHHDFLPYSSEPQQAWTGFFTSRSTLKGLARQASALLYAGESMFTRYMWPHPRGTLDPTWALQQLQQLRWAVSEVQHHDAITGTESPKVKNMYMEHLSMGMRGVHKLMASIALDRPPGSGTDTRPVGYSASVYNPLAWKITTIITLTVAFPSVSVTDELGRPVSAQIQNSTKDPSAYDLLILTTIPGLSYRHYKVRRTRGDQAGTRELVTPRANTLKFSRKLRNQTSQEGKLLVPVMNDCYTLLFDQDTNMLHSIQDRQSNRTVHMTQEFLEYRANGDVKQGPISDNYLFASNDTAEPSWEAVGMEMVVGTLATDVRQYFYRNITDQGYIYSIHTRLAHVHPSLAGELLCRRIEQQYQVGPLDLNREAILRTSSDLNSQQVLYSDNNGYQMQRRPYKAFKSNPIPRNYYPMVQSAFIEDDKSRLVLLAERPHGVSSQENGQVEVMLHRRLWNNLVWDLNYNLTLNDTSVVHPVLWLLLGPKSTTTALRPRSGVALQHRPVVLLKELTDEEETAIHRPHHPWPVTLPPSLHLQVLSLPGWQYSRNHAQHLKNLQRGSVLVNLSSRDKAPGEINSGSQGLCKEVTQEDNRSSTQP
Protein: Phosphatidylserine decarboxylase proenzyme, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase beta chain; Phosphatidylserine decarboxylase alpha chain] (Q9UG56)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity).
Subcellular location: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:30858161, ECO:0000305|PubMed:33718843}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:30858161, ECO:0000305|PubMed:33718843}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Cytoplasm {ECO:0000269|PubMed:33593792}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane {ECO:0000269|PubMed:33593792}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane {ECO:0000269|PubMed:33593792}. Lipid droplet {ECO:0000269|PubMed:33593792}. Note=Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions. {ECO:0000269|PubMed:33593792}.
Interaction partners:
- Phosphatidylserine synthase 1
- Phosphatidylserine synthase 2
- Ethanolamine-phosphate cytidylyltransferase
- Phosphatidylethanolamine N-methyltransferase
- Phospholipase D1
- Choline/ethanolaminephosphotransferase 1
- Phospholipase D2
- Ethanolaminephosphotransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
Protein: UPF0502 protein YceH (G20.3) (P29217)
Organism: Escherichia coli (strain K12)
Interaction partners:
- [Ribosomal protein uS5]-alanine N-acetyltransferase
- Putative oxidoreductase YceM
Sequence:
MKYQLTALEARVIGCLLEKQVTTPEQYPLSVNGVVTACNQKTNREPVMNLSESEVQEQLDNLVKRHYLRTVSGFGNRVTKYEQRFCNSEFGDLKLSAAEVALITTLLLRGAQTPGELRSRAARMYEFSDMAEVESTLEQLANREDGPFVVRLAREPGKRENRYMHLFSGEVEDQPAVTDMSNAVDGDLQARVEALEIEVAELKQRLDSLLAHLGD
Protein: Solute carrier family 2, facilitated glucose transporter member 3 (Glucose transporter type 3, brain) (GLUT-3) (P32037)
Organism: Mus musculus (Mouse)
Function: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate. Does not mediate fructose transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1730609, ECO:0000269|PubMed:35810171}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. Perikaryon {ECO:0000250|UniProtKB:Q07647}. Cell projection {ECO:0000250|UniProtKB:Q07647}. Note=Localized to densely spaced patches along neuronal processes. {ECO:0000250|UniProtKB:Q07647}.
Interaction partners:
- Hexokinase-1
- Cyclic AMP-responsive element-binding protein 1
- Methyl-CpG-binding protein 2
- Excitatory amino acid transporter 1
- Hexokinase-2
- Monocarboxylate transporter 4
- L-lactate dehydrogenase A chain
- Pyruvate kinase PKM
- Hexokinase-3
Sequence:
MGTTKVTPSLVFAVTVATIGSFQFGYNTGVINAPETILKDFLNYTLEERLEDLPSEGLLTALWSLCVAIFSVGGMIGSFSVGLFVNRFGRRNSMLLVNLLAIIAGCLMGFAKIAESVEMLILGRLLIGIFCGLCTGFVPMYIGEVSPTALRGAFGTLNQLGIVVGILVAQIFGLDFILGSEELWPGLLGLTIIPAILQSAALPFCPESPRFLLINKKEEDQATEILQRLWGTSDVVQEIQEMKDESVRMSQEKQVTVLELFRSPNYVQPLLISIVLQLSQQLSGINAVFYYSTGIFKDAGVQEPIYATIGAGVVNTIFTVVSLFLVERAGRRTLHMIGLGGMAVCSVFMTISLLLKDDYEAMSFVCIVAILIYVAFFEIGPGPIPWFIVAELFSQGPRPAAIAVAGCCNWTSNFLVGMLFPSAAAYLGAYVFIIFAAFLIFFLIFTFFKVPETKGRTFEDIARAFEGQAHSGKGPAGVELNSMQPVKETPGNA
Protein: Protamine-2 (Sperm histone P2) (Sperm protamine P2) (P19757)
Organism: Sus scrofa (Pig)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P07978}. Chromosome {ECO:0000250|UniProtKB:P07978}.
Interaction partners:
- Nuclear transition protein 2
- Spermatid nuclear transition protein 1
- Sperm protamine P1
Sequence:
MVRCRVRSPSESPQQGSGQQRENERQDQDQELRPEDVPVYGRTHRGRYHYRHRSHTRRRRSCRRRRRRACRHRRHRRGCRRIRRRRRCRRRL
Protein: Kinesin-like protein KIN-12C (Phragmoplast orienting kinesin 1) (Q27IK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the spatial control of cytokinesis by a proper phragmoplast guidance. Localizes TAN to the cortical division sites (CDS) during cytokinesis via direct binding.
Subcellular location: Cytoplasm, cytoskeleton, phragmoplast {ECO:0000250}.
Interaction partners:
- Probable microtubule-binding protein TANGLED
- 65-kDa microtubule-associated protein 3
- RAN GTPase-activating protein 1
- Vacuolar protein sorting-associated protein 52 A
- Kinesin-like protein KIN-14E
- 65-kDa microtubule-associated protein 4
- Kinesin-like protein KIN-10A
- Kinesin-like protein KIN-12F
- Serine-rich adhesin for platelets-like protein
- Probable serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit TON2
Sequence:
MSRNVPRIEMPESEENEFASLSLFSPSRPPLNSIPDPSQIQKANHLPHFDLVQKLEGTRAQHQRTLGPEKKFEVLEGRAGNSSDSNPKIVNRNGKSRSEPNSAQSTPTRNGARVSLGGGCATGARFLQSFGGRGRIPRGVSIAESVSFAETTPHFELNEDHSFWKDHNVQVLIRLRPLGTMERANQGYGKCLKQESPQTLVWLGHPEARFTFDHVASETISQEKLFRVAGLPMVENCLSGYNSCVFAYGQTGSGKTYTMMGEISEAEGSLGEDCGVTARIFEYLFSRIKMEEEERRDENLKFSCKCSFLEIYNEQITDLLEPSSTNLQLREDLGKGVYVENLVEHNVRTVSDVLKLLLQGATNRKIAATRMNSESSRSHSVFTCTIESLWEKDSLTRSRFARLNLVDLAGSERQKSSGAEGDRLKEAANINKSLSTLGLVIMSLVDLAHGKHRHVPYRDSRLTFLLQDSLGGNSKTMIIANVSPSLCSTNETLSTLKFAQRAKLIQNNAKVNEDASGDVTALQQEIRKLKVQLTSLLKNHDSCGALSDCISSLEESRYSGTCKVAGETRQDKCHCQVKNMNDNMIGALRREKIAESALQKSEAEIERIDCLVRDMEEDAKRIKIMLNLREEKVGEMEFCTSGSLMTKECLIEENKTLKGEIKLLRDSIDKNPELTRSALENTKLREQLQRYQKFYEHGEREALLAEVTGLRDQLLDVLEAKDESFSKHVMKENEMEKEFEDCRNMNSSLIRELDEIQAGLGRYLNFDQIQSNVVASSTRGAEQAETMPTISEIQEEVAISHSKNYDRGALVKTDEGIDRSILQFKLGKLMKDLEEARTLNCKYEKDHKSQLSQQEDIEVVREQVETETARTILELQEEVIALQSEFQRRICNLTEENQSIKDTITARESEIRALNQDWEKATLELTNFIVAGSKSIKNASTQIESIICSFPQVNAWIGDYVEKAAKNCIKKEETILLLQKSLEDARILVAEMNLKLNSLKGATIALNEFQLGGNAATTEEAFNLNNDVDRMSDEVDTLESNFKANQYSILKTERHAEAALAVTKWLSDSRDQHQMMEKVQDQSVKEFGTLSSISASLSAEGNADISLSRDGHLSDATYPKGDELSTSSSDFSNCRWQHDCALNVKCQGVSSSESDAQESNNKITSAALIAKNGSAHSVYCGEGRQSVEKPLTIMMGREETEYKCSKPLSSGVYMGLMQRMDPVRTFFDRFEEVNATMKEADLTICELVKANEKSNSVTEMWLQTHEELISKEKNLMDDLEQVKSILSACEEEKQVLLNQTHTTLADMENSVSLLEEYFQEMKRGVEETVEALFSHARLAGKELLQLISNSRPSLEQIASEFMEREFTMYATYQCHIGKLIDQILDQRKQVITPNLSGQETNQSVKINAIGYNAEDEVTKKQSREEIVTGLENDEVVQSHESLLYENLYLKKELERKEALFEGLLFDFRLLQESASNKRDIKNEMDELFDALCKVQLELELKASQVHELFVHNENLENCSIDLKTALFTSQSDLEQAKQRIQILAEQNDELRALVSDLCKEKAAAEEGLDEQRDLVNRLEKEILHLTTTAEKQLLSAVKSIKENLKKTSDEKDQIVDEICSLNNKLELAYAIADEKEAIAVEAHQESEASKIYAEQKEEEVKILEISVEELERTINILERRVYDMDEEVKRHRTTQDSLETELQALRQRLFRFENFTGTMVTTNESTEEYKSHISRSTGLQGAHSQIQVLQKEVAEQTKEIKQLKEYISEILLHSEAQSSAYQEKYKTLEVMIRDFKLEDSSSSAAETISHKTEKSSTRSRGSSSPFRCIVGLVQQMKLEKDQELTMARVRVEELESLLAVKQKEICTLNTRIAAADSMTHDVIRDLLGVKMDITSYAELIDQHQVQRVVEKAQQHAEEILSKEQEVMNLKRHIDYLFKDRESCMSELNKKDTDVLATQISLDQLQERVQLLSMQNEMLKNDKSNLLRKLAELDRTVHNAQASNHRVPQTTKDTASFKLADTDYTKRLENAQKLLSHANNELAKYRKTSNNHPSTRTQGQSSGTRYR
Protein: Glutamate receptor ionotropic, NMDA 2B (GluN2B) (N-methyl D-aspartate receptor subtype 2B) (NMDAR2B) (NR2B) (A7XY94)
Organism: Xenopus laevis (African clawed frog)
Function: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18177891, ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00960}; Multi-pass membrane protein {ECO:0000269|PubMed:25008524, ECO:0000269|PubMed:28232581}.
Interaction partners:
- Glutamate receptor ionotropic, NMDA 1
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Glutamate receptor
- Xnr-2
- TGF_BETA_2 domain-containing protein.
- Peripheral plasma membrane protein CASK
- Peripheral plasma membrane protein CASK
- Uncharacterized protein.
Sequence:
MRPTEACCYLKISLIILFYMGCYAQKHPNMDIAVILVGTTEEVAIKDVHEKDDFHHLPVTPRVALVTMNESDPKSIITRICDLMSDKKVQGVVFGDDTDQEAIAQILDFISVQTLTPILGIHGGSSMIMADKEEASMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFENKVRSTIENSFVGWELEEVIHLDMSLDDIDSKIQNQLKKLQSPVILLYCTKEEATYIFEVAHSVGLTGYGFTWIVPSLVAGDTDTVPDEFPTGLISVSYDEWDYDLPARVRDGIAIITTAASTMLSEHNSIPQSKSSCNNIQESRVYEAHMLKRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNQERKWERVGKYKDRSLKMKYYVWPVFDLYPNSEEHKDEHLSIVTLEEAPFVIVEDVDPLSGTCMRNTVPCRKQIRPENRTEEGGNYIKRCCKGFCIDILKKIAKTVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVTKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPAFRFGTVPNGSTERNIRNNYLEMHSYMVKFNQRSVQDALLSLKSGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFATTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFIMEHLFFWQLRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEDRQSALDSPSATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSFQPEENLFSDYISEVERTFGNLQLKDSNVYQDHFHHHRPHSIGSNSSIDGLYDCDNAPFTTQPRSLSKKPLDIGLPSKHPSPQIGDLYGKFSFKSDHYGAPDDLIRSDVSDISTHTVTYGNIEGNAKRRKQYKDSLKKRPASAKSRREFDEIELAYRRRQRSPDHKRYFRDKEGLRDFYLDQFRTKENNPHWEHVDLTHIYAERADDFKHDTSCSNRQHQKHVGEFVQTDRKHGSGGNAWEKNMSNIEWEDRASSNFCRNCPSKMHNYTGQNTNRPACIRCEVCKKAGNLYDISEDNSLQDLEARPIQAPNSKYPQSPNGKAQKRNRSKLHRQHSYDTFVDLQKEDVTLAPRSVSLKDKERFLDGSPYAHMFEMPNETSFTSKSHGPTHNPGGYMLSRSLYPDRVTQNPFIPTFGDDQCLLHGSKPYYFRQPAIGGLKGRADFRGAGKSLSAQHSGPSGHFQKDICIGNQPNACVSNNKNPRSFNNSTNGHVYEKLSSIESDV
Protein: Cadherin-2 (Neural cadherin) (N-cadherin) (CD antigen CD325) (Q9Z1Y3)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P15116}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000269|PubMed:21617128}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes (By similarity). Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P15116}.
Interaction partners:
- Catenin beta-1
- Cadherin-1
- Catenin delta 1
- Junction plakoglobin
- Glutamate receptor 2
- Gap junction alpha-1 protein
- Catenin alpha-1
- Vinculin
- Cadherin 11
- Neural cell adhesion molecule 1
Sequence:
MCRIAGGPRTLLPLLAALLQASLEASGELALCKTGFPEDVYSAVLPKTVHEGQPLLNVKFSNCNRKRKVQYESSEPADFKVDEDGTVYAVRSFPLSAEQAKFLIYAQDKETQEKWQVAVNLSLEPSLTEEPMKEPHEIEEIVFPRQLAKHSGALQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDRELIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGSVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDVIVANLTVTDKDQPHTPAWNAAYRISGGDPTGRFAILTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTLTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPEPNSINITALDYDIDPNAGPFAFDLPLSPATIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIVITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGTIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRLDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGDQDYDYLNDWGPRFKKLADMYGGGDD
Protein: Immunoglobulin heavy constant gamma 4 (Ig gamma-4 chain C region) (P01861)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
ASTKGPSVFPLAPCSRSTSESTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTKTYTCNVDHKPSNTKVDKRVESKYGPPCPSCPAPEFLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIVPDYRNMIRQGA
Protein: Uncharacterized protein (Q580B3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRNNIEAAGVHLADCTLLWCRHETKTEEERLAADVQRRISLLGEEYPPTARDIAKQEASPHVRVDGEIVATNLALRYLTRAEEERKARFEEERRQREEREALGKKQDEIRHIIIDNWAFGMEELEKLQWIEHGVVKGKERRRLYVDWYDSGVQQHLVDEARLWSDLEQVIGREREAGRKAYELSKGKP
Protein: WD repeat-containing protein 76 (Q9H967)
Organism: Homo sapiens (Human)
Function: Specifically binds 5-hydroxymethylcytosine (5hmC), suggesting that it acts as a specific reader of 5hmC.
Interaction partners:
- Lymphoid-specific helicase
- DNA damage-binding protein 1
- Poly [ADP-ribose] polymerase 1
- Thymocyte nuclear protein 1
- Cullin-4A
- Chromobox protein homolog 3
- DDB1- and CUL4-associated factor 8
- DNA repair protein complementing XP-C cells
- ATPase family AAA domain-containing protein 2
- X-ray repair cross-complementing protein 5
Sequence:
MSRSGAAAEKADSRQRPQMKVNEYKENQNIAYVSLRPAQTTVLIKTAKVYLAPFSLSNYQLDQLMCPKSLSEKNSNNEVACKKTKIKKTCRRIIPPKMKNTSSKAESTLQNSSSAVHTESNKLQPKRTADAMNLSVDVESSQDGDSDEDTTPSLDFSGLSPYERKRLKNISENADFFASLQLSESAARLREMIEKRQPPKSKRKKPKRENGIGCRRSMRLLKVDPSGVSLPAAPTPPTLVADETPLLPPGPLEMTSENQEDNNERFKGFLHTWAGMSKPSSKNTEKGLSSIKSYKANLNGMVISEDTVYKVTTGPIFSMALHPSETRTLVAVGAKFGQVGLCDLTQQPKEDGVYVFHPHSQPVSCLYFSPANPAHILSLSYDGTLRCGDFSRAIFEEVYRNERSSFSSFDFLAEDASTLIVGHWDGNMSLVDRRTPGTSYEKLTSSSMGKIRTVHVHPVHRQYFITAGLRDTHIYDARRLNSRRSQPLISLTEHTKSIASAYFSPLTGNRVVTTCADCNLRIFDSSCISSKIPLLTTIRHNTFTGRWLTRFQAMWDPKQEDCVIVGSMAHPRRVEIFHETGKRVHSFGGEYLVSVCSINAMHPTRYILAGGNSSGKIHVFMNEKSC
Protein: Pyruvate ferredoxin oxidoreductase B (G9BQS2)
Organism: Trichomonas vaginalis
Interaction partners:
Sequence:
RLIVDVIESGEVKGELKDLFEQLLKVWDQDKESGDLAEKIKPLLAKVQNPSEKLFDLKSQADILAKKQVWIVGGDGWAYDIGYGGLDHVLASGENVKIIIYDTEVYSNTGGQCSKATSRGAVANFSAAGYTNAKKDLGAIAMTYKNIYVASTCLLADPNQALKALQEAKEYNGPAIIINYSPCINHGIKKGLGSTPKHCKDLLKTGYLNLFRYNPSKDKPLTVDTKQPNYNLDPLVKGENRFAALNDIYPNEAETKFPLLINDMKTRYEGYKK
Protein: Xylan O-acetyltransferase 5 (EC 2.3.1.-) (Protein trichome birefringence-like 13) (OsTBL13) (A0A0P0WL81)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Xylan acetyltransferase required for 2-O- and 3-O-monoacetylation of xylosyl residues in xylan. Catalyzes the 2-O-acetylation of xylan, followed by nonenzymatic acetyl migration to the O-3 position, resulting in products that are monoacetylated at both O-2 and O-3 positions (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q2QYU2}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRIPRRKGGAGPLVGAPSRRAQVAAVFALALLLGVSVLYDSAHIAASLRRHGVGGGGSSGGGGGGGGDGARAYTNTKLSATTEEAEAEAAEVRSPPAQGVESAVEATDRGEAPPEQPVAADSGASSAETPPSLLEQVTETPPPSPSSSSAAAAAAEAQVGGDHGGESCDVYKGRWVYDEANAPLYKESACEFLTEQVTCMRNGRRDDDYQKWRWQPDGCDLPRFDAKLLLEKLRNKRLMFVGDSLNRNQWESMVCLVQSEAPWEKKSLVKNDSLNVFRLEEYNATIEFYWSPFLVESNSDDPNMHSIVDRIIKPTSIAKHAANWEGVDYLIFNTYIWWMNTPEMKILHGGSFSKKPVKYDEMERVAAYRKVLKTWSRWVEKHVDPKRSTVFFMSVSPVHMQSEGWGKPDAIKCFSETQPAINYTKKLEVGTDWDLFSTAHHVTKAMKRVPVHFINITALSEIRKDAHTSVNTLRQGKLLTKEQKANPRKFADCIHWCLPGLPDTWNEFIYGHIVSSPQRRPVEPIENQPQR
Protein: Anthranilate N-hydroxycinnamoyl/benzoyltransferase, putative (HXXXD-type acyl-transferase family protein) (Q8LF28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATLEITDIALVQPSHQPLSNDQTLSLSHLDNDNNLHVSFRYLRVYSSSSSTVAGESPSAVVSASLATALVHYYPLAGSLRRSASDNRFELLCSAGQSVPLVNATVNCTLESVGYLDGPDPGFVERLVPDPTREEGMVNPCILQVTMFQCGGWVLGASIHHAICDGLGASLFFNAMAELARGATKISIEPVWDRERLLGPREKPWVGAPVRDFLSLDKDFDPYGQAIGDVKRDCFFVTDDSLDQLKAQLLEKSGLNFTTFEALGAYIWRAKVRAAKTEEKENVKFVYSINIRRLMNPPLPKGYWGNGCVPMYAQIKAGELIEQPIWKTAELIKQSKSNTSDEYVRSFIDFQELHHKDGINAGTGVTGFTDWRYLGHSTIDFGWGGPVTVLPLSNKLLGSMEPCFFLPYSTDAAAGSKKDSGFKVLVNLRESAMPEFKEAMDKFHKGEFALS
Protein: Angiopoietin-4 (ANG-4) (Angiopoietin-3) (ANG-3) (Q9WVH6)
Organism: Mus musculus (Mouse)
Function: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Angiopoietin-1 receptor
- Angiopoietin-2
- Angiopoietin-1
- Vascular endothelial growth factor receptor 2
- Tyrosine-protein kinase receptor Tie-1
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 3
- Platelet-derived growth factor receptor beta
- Platelet-derived growth factor receptor alpha
- Mast/stem cell growth factor receptor Kit
Sequence:
MLCQPAMLLDGLLLLATMAAAQHRGPEAGGHRQIHQVRRGQCSYTFVVPEPDICQLAPTAAPEALGGSNSLQRDLPASRLHLTDWRAQRAQRAQRVSQLEKILENNTQWLLKLEQSIKVNLRSHLVQAQQDTIQNQTTTMLALGANLMNQTKAQTHKLTAVEAQVLNQTLHMKTQMLENSLSTNKLERQMLMQSRELQRLQGRNRALETRLQALEAQHQAQLNSLQEKREQLHSLLGHQTGTLANLKHNLHALSSNSSSLQQQQQQLTEFVQRLVRIVAQDQHPVSLKTPKPVFQDCAEIKRSGVNTSGVYTIYETNMTKPLKVFCDMETDGGGWTLIQHREDGSVNFQRTWEEYKEGFGNVAREHWLGNEAVHRLTSRTAYLLRVELHDWEGRQTSIQYENFQLGSERQRYSLSVNDSSSSAGRKNSLAPQGTKFSTKDMDNDNCMCKCAQMLSGGWWFDACGLSNLNGIYYSVHQHLHKINGIRWHYFRGPSYSLHGTRMMLRPMGA