wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (EC 2.4.3.3) (GalNAc alpha-2,6-sialyltransferase I) (ST6GalNAc I) (ST6GalNAcI) (Sialyltransferase 7A) (SIAT7-A) (Q9QZ39)
Organism: Mus musculus (Mouse)
Function: Protein sialyltransferase specifically expressed in goblet cells that plays a key role in intestinal host-commensal homeostasis. Conjugates sialic acid with an alpha-2-6 linkage to N-acetylgalactosamine (GalNAc) glycan chains linked to serine or threonine in glycoproteins. Catalyzes the formation of the sialyl-Tn (S-Tn) antigen, an antigen found in intestinal goblet cells. Protein sialylation in globlet cells is essential for mucus integrity and is required to protect the intestinal mucus against excessive bacterial proteolytic degradation.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NSC7}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9NSC7}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Polypeptide N-acetylgalactosaminyltransferase 6
- Polypeptide N-acetylgalactosaminyltransferase 5
- Polypeptide N-acetylgalactosaminyltransferase 1
- Polypeptide N-acetylgalactosaminyltransferase 4
- Polypeptide N-acetylgalactosaminyltransferase 3
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
Sequence:
MTRYCRGLSQRQAFLLLTVLALLFILLFVVKDPRAKDSRCQFIWKNDASAQENQQKAEPQVPIMTLSPRVHNKETTSVSSKDLKKQEREAVQGEQAEGKEKRKLETIRPAPENPQSKAEPAAKTPVSEHLDKLPRAPGALSTRKTPMATGAVPAKKKVVQATKSPASSPHPTTRRRQRLKASEFKSEPRWDFEEEYSLDMSSLQTNCSASVKIKASKSPWLQNIFLPNITLFLDSGRFTQSEWNRLEHFAPPFGFMELNQSLVQKVVTRFPPVRQQQLLLASLPTGYSKCITCAVVGNGGILNDSRVGREIDSHDYVFRLSGAVIKGYEQDVGTRTSFYGFTAFSLTQSILILGRRGFQHVPLGKDVRYLHFLEGTRDYEWLEAMFLNQTLAKTHLSWFRHRPQEAFRNALDLDRYLLLHPDFLRYMKNRFLRSKTLDTAHWRIYRPTTGALLLLTALHLCDKVSAYGFITEGHQRFSDHYYDTSWKRLIFYINHDFRLERMVWKRLHDEGIIWLYQRPQSDKAKN
Protein: Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Lymphocyte stimulatory factor 1) (Q04745)
Organism: Sus scrofa (Pig)
Function: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-4 receptor subunit alpha
- Interleukin-13
- Interleukin-10
- Interleukin-13 receptor subunit alpha-1
- Interleukin-2
- Tyrosine-protein kinase
- Interleukin-5
- Tyrosine-protein kinase
- Interferon gamma
- Interleukin-6
Sequence:
MGLTSQLIPTLVCLLACTSNFVHGHKCDITLQEIIKTLNILTARKNSCMELPVTDVFAAPENTTEKETFCRASTVLRHIYRHHTCMKSLLSGLDRNLSSMANMTCSVHEAKKSTLKDFLERLKTIMKEKYSKC
Protein: Peroxiredoxin 2 (EC 1.11.1.24) (Cytosolic thioredoxin peroxidase 1) (Thioredoxin peroxidase 1) (Thioredoxin-dependent peroxide reductase 1) (Thioredoxin-dependent peroxiredoxin 2) (Q9V3P0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11677042}.
Interaction partners:
- Sulfiredoxin
- Peroxiredoxin-5
- Thioredoxin-2
- Glyceraldehyde-3-phosphate dehydrogenase 2
- thioredoxin-dependent peroxiredoxin
- AT18092p
- Glutathione S-transferase D1
- Glutathione peroxidase
- Enolase
- Thioredoxin-1
Sequence:
MPQLQKPAPAFAGTAVVNGVFKDIKLSDYKGKYLVLFFYPLDFTFVCPTEIIAFSESAAEFRKINCEVIGCSTDSQFTHLAWINTPRKQGGLGSMDIPLLADKSMKVARDYGVLDEETGIPFRGLFIIDDKQNLRQITVNDLPVGRSVEETLRLVQAFQYTDKYGEVCPANWKPGQKTMVADPTKSKEYFETTS
Protein: 1-aminocyclopropane-1-carboxylate oxidase 4 (ACC oxidase) (EC 1.14.17.4) (Ethylene-forming enzyme) (EFE) (Q06588)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enzyme involved in the ethylene biosynthesis. May promote stem elongation by maximizing the extensibility cells, possibly by activating ethylene biosynthesis, in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
Interaction partners:
- 1-aminocyclopropane-1-carboxylate synthase 2
- 1-aminocyclopropane-1-carboxylate synthase 6
- Aconitate hydratase 1
- 1-aminocyclopropane-1-carboxylate synthase 4
- 1-aminocyclopropane-1-carboxylate synthase 7
- 1-aminocyclopropane-1-carboxylate synthase 8
- 1-aminocyclopropane-1-carboxylate synthase 9
- 1-aminocyclopropane-1-carboxylate synthase 11
- 1-aminocyclopropane-1-carboxylate synthase 5
- 1-aminocyclopropane-1-carboxylate synthase-like protein 1
Sequence:
MESFPIINLEKLNGEERAITMEKIKDACENWGFFECVNHGISLELLDKVEKMTKEHYKKCMEERFKESIKNRGLDSLRSEVNDVDWESTFYLKHLPVSNISDVPDLDDDYRTLMKDFAGKIEKLSEELLDLLCENLGLEKGYLKKVFYGSKRPTFGTKVSNYPPCPNPDLVKGLRAHTDAGGIILLFQDDKVSGLQLLKDGEWVDVPPVKHSIVVNLGDQLEVITNGKYKSVEHRVLSQTDGEGRMSIASFYNPGSDSVIFPAPELIGKEAEKEKKENYPRFVFEDYMKLYSAVKFQAKEPRFEAMKAMETTVANNVGPLATA
Protein: Protein argonaute 7 (Protein ZIPPY) (Q9C793)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA-mediated post-transcriptional gene silencing (PTGS). Main component of the RNA-induced silencing complex (RISC) that binds to a short guide RNA such as a microRNA (miRNA) or small interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide for slicer-directed cleavage of homologous mRNAs to repress gene expression. Required for the processing of 21 nucleotide trans-acting siRNAs (ta-siRNAs) derived from TAS3a transcripts. Associates preferentially with the microRNA (miRNA) miR390 which guides the cleavage of TAS3 precursor RNA. Seems to act as miR390 specific slicer. Associates mainly with small RNAs of 21 nucleotide in length and with a 5' terminal adenosine. Acts in the RDR6/SGS3/DCL4/AGO7 trans-acting siRNA pathway involved in leaf developmental timing. Does not seem to act on leaf polarity. Required for the production of the 30-40nt bacterial-induced long siRNAs (lsiRNA). Involved in antiviral RNA silencing by contributing to efficient viral RNAs clearance. Targets less structured viral RNAs than AGO1 which is capable of targeting RNAs with more compact structures.
Interaction partners:
- Dicer-like protein 4
- Endoribonuclease Dicer homolog 1
- Endoribonuclease Dicer homolog 2
- Endoribonuclease Dicer homolog 3
- RNA-dependent RNA polymerase 6
- Protein SUPPRESSOR OF GENE SILENCING 3
- Protein DCL homolog, chloroplastic
- Small RNA 2'-O-methyltransferase
- RNA-dependent RNA polymerase 2
- DNA-directed RNA polymerase IV subunit 1
Sequence:
MEEKTHHHHHSTNKHIPSSKSRTPLLHKPYHHHVQTNPPPFLLHPSSHQNLNLVASNLPSSYYYYYYCYFYSQFHNSLPPPPPPHLLPLSPPLPPLLPLPPPHSMTRFHKSLPVSQVVERKQQHQQKKKIQVSNNKVSGSIAIEEAALVVAKRPDFGGQDGSVIYLLANHFLVKFDSSQRIYHYNVEISPQPSKEIARMIKQKLVETDRNSFSGVVPAFDGRQNIYSPVEFQGDRLEFFVNLPIPSCKAVMNYGDLREKQPQKKIEKLFRVNMKLVSKFDGKEQRKEGEDWAPLPPEYIHALDVILRENPMEKCTSIGRSFYSSSMGGSKEIGGGAVGLRGFFQSLRHTQQGLALNMDLSITAFHESIGVIAYLQKRLEFLTDLPRNKGRELSLEEKREVEKALKNIRVFVCHRETVQRYRVYGLTEEITENIWFPDREGKYLRLMSYFKDHYGYEIQFKNLPCLQISRARPCYLPMELCMICEGQKFLGKLSDDQAAKIMKMGCQKPNERKAIIDKVMTGSVGPSSGNQTREFNLEVSREMTLLKGRILQPPKLKLDRPRNLKESKVFKGTRIERWALMSIGGSSDQKSTIPKFINELTQKCEHLGVFLSKNTLSSTFFEPSHILNNISLLESKLKEIQRAASNNLQLIICVMEKKHKGYGDLKRISETRIGVVTQCCLYPNITKLSSQFVSNLALKINAKIGGSMTELYNSIPSHIPRLLRPDEPVIFMGADVTHPHPFDDCSPSVAAVVGSINWPEANRYVSRMRSQTHRQEIIQDLDLMVKELLDDFYKAVKKLPNRIIFFRDGVSETQFKKVLQEELQSIKTACSKFQDYNPSITFAVVQKRHHTRLFRCDPDHENIPPGTVVDTVITHPKEFDFYLCSHLGVKGTSRPTHYHILWDENEFTSDELQRLVYNLCYTFVRCTKPISIVPPAYYAHLAAYRGRLYIERSSESNGGSMNPSSVSRVGPPKTIPLPKLSDNVKNLMFYC
Protein: B-cell CLL/lymphoma 9 protein (Bcl9) (Q67FY0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHSSNPKVRNSPSANTQSSPKSKQEAMVRSPPVMSPSSAAQMDSKLPNQGKQGGAGSQSQPSPCDPKSLSGSHTPKGPQVPIGSMGLKNGQGLSSGNGAKGKIKRERSTSVESFEQRDTGTPSNEGDQKEIGSRAKRLCVGERRLPYSGADWCSGGESDEDDPGFFNCNSADIKPDPGALSASTPTHNTVGAQSTELGSGQKPGSKVVYVFTTEMANKAADAVITGHVDNIITYHMNNISNGKGGKPQLPLNNQIGSLRSDPKQQGVPSQQQPSSHSGDQNHQAASKVAQSGQQQQPQAQPTQPQQPTHGAKPNSLPPDNAPSAGMDSKSLPSSSPQDGAGSHDSSNSAGTPGSQTSNQPPNAGPPQNFPSLDLPKGMDAKLTAQHHQQLAHEIMSSMGDNPEGLSQEQLEHRERSLQTLRDIQRMLFPDDKDMAAMGQGNMGGPPPGAVMMEGGPKKPEQGPLQAMMAQSQSLGKPGGPGGPRPDGPPFGPPGPRDMPFSPDDLGPPPPGPGPMNSHPGGEHGDHMTPEQMAWLKLQQEFYEEKKRKQEQMQHRPMGDMMLHQGGPRGMMRGPPPPYQLNPGEVWGPGGPEPFPDQMNMGPRGMHPHMQRMPGFPGMMNPDMEGGPNAMPRPGMNWPDDMPKMGDGRGFPPGQGMFGGPGGRVERFPNPQSVQEAMFHQGMGDKQGMGMPPGMMMEMNRMMGNQRPMDPGNGGGMMFPRMPGDGPMSPTSRMEFVKGLGQSRGEFGMGPGNLNVNMGPSPQMMPPKMRESQMSLSPEEIMKMRQGGGPMPDGVVPSQRMMQGPPFPDQPHPGDLNMGPNRQFPGIGPQGPGNPRGPRGEPPFGPDQRGGNGRLSHMPPLPPNQGPNSSGPPPGQRNVSRKPSDLNVQSGPANSPNVNLKSPTLRQVQSPMLGSPSGNLKSPQTPSQLAGMLSGPSAAAVAAAAAIKSPPMMGSAGASPVHMKSPSLPAPSPGWTSSPKPPMQSPGIPQNTNPPLSMTSPNMMGGVAQGGNVPPSAPPSSSSSQPGGMNVPGSLPSSSPYTMPPEPTLSQNPLSIMMSRMSKFAMPSSTPLYHDAIKTVASSDDDSPPARSPNLPSMNNSMPGMGVNHHPGHPRMMTPNSSGPMPSLSPMGMSAMGSQPLSHGMPNQLPSPNPMGPNMPPHSGPMGPGMMPHGMMMNPVSQDPVMGNNQMMSQGRMGLSHRGQGFPPGQSPPQQVPFPHNGPGHQGGFPHGMGFQGEGGPLGRMGNMPHGPGVEPGMCKPNTPGGQEFNNMPGVFGDSDLHEVMRPGASGIPEFDLSRIIPSEKPSQTLSYFPRGGDAPGGKPPHPSGPPGFAQMQGMMGEGNPRMDLPMQGMGGPPGPGHMGPQDMPMGNPGHNPMRPPGFMGQGMMGPQHRMLSPGQQPGMMGGPGMMQGKERPMYNHPGPVGSPNMMMSLQGMSGPQQTMMMPSQMRPRGMAADMGMGFNPGPGNPGNLMF
Protein: Pantoate--beta-alanine ligase (EC 6.3.2.1) (Pantoate-activating enzyme) (Pantothenate synthetase) (Q09673)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable 3-methyl-2-oxobutanoate hydroxymethyltransferase
- Pantothenate kinase
- Probable 2-dehydropantoate 2-reductase
- 4-aminobutyrate aminotransferase
- Putative aldehyde dehydrogenase-like protein C922.07c
- Putative aldehyde dehydrogenase-like protein C9E9.09c
- Uncharacterized protein C4B3.18
- Biotin--protein ligase
- Putative uridine kinase C227.14
Sequence:
MQVLKEKLLIHQQVDNWRKDGNRIAFVPTMGNLHEGHFSLVREAKRHAEKVVVSIFVNPMQFNNPQDLLLYPRTMDQDCSQLQNLGVDLVYAPTVEELYPEGSQDITFVDVPKLSTMLEGASRPGHFRGVTTVVSKLFHIVNPDVACFGEKDFQQVAIIKKMVRDLNFFIEIIQVPIVRADDGLALSSRNGYLTSEERKIAPNLYKILKKLAQELSNGNGDLEKLIAETNTELSRCRFIPDQLEICDSTTLEPFTAGTKNVVILAAAWLGKARLIDNIQTTIN
Protein: Importin subunit alpha (Q9V455)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Nuclear pore complex protein Nup153
- Regulator of chromosome condensation
- Importin subunit beta
- E3 SUMO-protein ligase RanBP2
- D-Importin 7/RanBP7
- Exportin-2
- Nuclear pore complex protein Nup50
- Exportin-1
- Ran GTPase-activating protein
- Nuclear cap-binding protein subunit 1
Sequence:
MTSMEQNRLQNFKNKGKDQDEMRRRRNEVTVELRKNKREETILKRRNVPNLDSNTDEEEQLSSSIDLKKLAKAAADATKPEQQLAAVQAARKLLSSDKNPPINDLIQSDILPILVECLKQHNHTMLQFEAAWALTNIASGTSAQTNEVVAAGAVPLFLQLLNSPAPNVCEQAVWALGNIIGDGPLLRDFVIKHGVVQPLLSFIKPDIPITFLRNVTWVIVNLCRNKDPAPPTATIHEILPALNVLIHHTDTNILVDTVWAISYLTDGGNDQIQMVIESGVVPKLIPLLGNSEVKVQTAALRAVGNIVTGSDEQTQVVLNYDALSYFPGLLSHPKEKIRKEAVWFLSNITAGNQSQVQAVINVGLLPKIIENLSKGEFQTQKEAAWAISNLTISGNREQVFTLIKEGVIPPFCDLLSCQDTQVINVVLDGLNNMLKVADSHVEAVANCIEECEGLAKIERLQSHENVEIYKLAYEIIDQYFTDEGEQTNMAPTSDGAQYNFDPHADRLTMNSFNF
Protein: Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41) (Phosphatidylglycerophosphate synthase 3) (PGP synthase 3) (Q93YW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL. Possesses high activity with PG species carrying dioleoyl groups and low activity with species carrying one or two palmitoyl groups. CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. In mitochondrial fission, CL stabilizes the protein complex of the major mitochondrial fission factors, DRP3A and DRP3B.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:24443516}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidate cytidylyltransferase 4, chloroplastic
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 5, chloroplastic
- Phosphatidate cytidylyltransferase 3
- Phosphatidate cytidylyltransferase 2
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Phosphatidylglycerophosphate phosphatase 1, chloroplastic/mitochondrial
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- N-acylphosphatidylethanolamine synthase
- Tafazzin family protein
Sequence:
MAIYRSLRKLVEINHRKTRPFFTAATASGGTVSLTPPQFSPLFPHFSHRLSPLSKWFVPLNGPLFLSSPPWKLLQSATPLHWRGNGSVLKKVEALNLRLDRIRSRTRFPRQLGLQSVVPNILTVDRNDSKEEDGGKLVKSFVNVPNMISMARLVSGPVLWWMISNEMYSSAFLGLAVSGASDWLDGYVARRMKINSVVGSYLDPLADKVLIGCVAVAMVQKDLLHPGLVGIVLLRDVALVGGAVYLRALNLDWKWKTWSDFFNLDGSSPQKVEPLFISKVNTVFQLTLVAGAILQPEFGNPDTQTWITYLSWLVASTTMASTAAYGVQYWKKRPISMIKRS
Protein: FANCD2 (E5QCJ4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKLANKKRSALKYLCDELQSVIDTLIKQKKKTPPMLLAARRAAAPTTPNSSKFYHGDSVTIWFCVKKAVEQVWGIVELVFGVFAEQSDASQELKSRVQKDMDDLGEKSLNLIHSILSGELYGGEEKLSPAERVERKSVLIRIIEKKMLSSEHLSNDSEKARVEIGKFLAKSAEFSPTPAVAVAILDVFEDLKLDEDDDAETRKIMAKYALAYLKKDWSKVDELWSKGTRYTCAVRDILHHYIRLRKEKDQLLAIQWILTNKVVQLVPEDDKRKSCVFSQQSDDDLLEKEDRKATFYCISKTTFGVIFKTLFGNLNSRCLKYDMSASAAKNGGVDIEDTLESWETASSCFLILCLLLRINKIRTTAVLTSAIKEGKQFLITVSKKSSFIFLMDNITKGTNFDTICRRVEKILSAVQQGNRVLQSIGTFAKTNKCVLLLKKFPELRAESENCLRVIHSAMVKNECLNAFTVGLVKSRSIDGDIIMDQRASEIDSDSE
Protein: Leucine-rich repeat (LRR) family protein (Similarity to elicitor-inducible receptor-like protein) (Q9FH56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLISLVLLLLLTLSSAESKTFWGDVAALKDFKNSVDAKSMSPGSCLSSWDFSVDPCDNIFSDTFTCGFRCDSVVTGSGRVTELSLDQAGYSGSLSSVSFNLPYLQTLDLSGNYFSGPLPDSLSNLTRLTRLTVSGNSFSGSIPDSVGSMTVLEELVLDSNRLYGSIPASFNGLSSLKRLEIQLNNISGEFPDLSSLKNLYYLDASDNRISGRIPSFLPESIVQISMRNNLFQGTIPESFKLLNSLEVIDLSHNKLSGSIPSFIFTHQSLQQLTLSFNGFTSLESPYYSPLGLPSELISVDLSNNQILGALPLFMGLSPKLSALSLENNKFFGMIPTQYVWKTVSPGSEFAGFQRLLLGGNFLFGVVPGPLMALKPGSANVQLAGNCFSWCPATLFFCQGQEQRSPKECRKFSRVVP
Protein: Palmitoyltransferase SWF1 (EC 2.3.1.225) (Spore wall formation protein 1) (Q04629)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs SNC1, SNC2, SYN8 and TLG1, at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15973437}; Multi-pass membrane protein {ECO:0000269|PubMed:15973437}.
Interaction partners:
- Palmitoyltransferase PFA5
- Palmitoyltransferase AKR1
- Probable palmitoyltransferase AKR2
- t-SNARE affecting a late Golgi compartment protein 1
- Ras modification protein ERF4
- Vacuolar protein 8
Sequence:
MSWNLLFVLLIGFVVLILLSPVFKSTWPFSTFYRNVFQPFLVDDQKYRWKLHLVPLFYTSIYLYLVYTYHMRVESTIKNELFLLERILIVPIIILPPVALGILAMVSRAEDSKDHKSGSTEEYPYDYLLYYPAIKCSTCRIVKPARSKHCSICNRCVLVADHHCIWINNCIGKGNYLQFYLFLISNIFSMCYAFLRLWYISLNSTSTLPRAVLTLTILCGCFTIICAIFTYLQLAIVKEGMTTNEQDKWYTIQEYMREGKLVRSLDDDCPSWFFKCTEQKDDAAEPLQDQHVTFYSTNAYDHKHYNLTHYITIKDASEIPNIYDKGTFLANLTDLI
Protein: Osteocalcin (Bone Gla protein) (BGP) (Gamma-carboxyglutamic acid-containing protein) (P83473)
Organism: Halobatrachus didactylus (Lusitanian toadfish)
Function: Binds strongly to apatite and calcium.
Subcellular location: Secreted {ECO:0000269|PubMed:14668966}.
Interaction partners:
Sequence:
AAAELSLVQLESLREVCEQ
Protein: HLA class II histocompatibility antigen, DR beta 3 chain (MHC class II antigen DRB3) (P79483)
Organism: Homo sapiens (Human)
Function: A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB3-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells. Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes. In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (By similarity). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (By similarity). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides. The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18305173, ECO:0000269|PubMed:19531622, ECO:0000269|PubMed:19830726}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein {ECO:0000255}. Autolysosome membrane {ECO:0000250|UniProtKB:P01911}; Single-pass type I membrane protein {ECO:0000255}. Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation (PubMed:18305173). Component of immunological synapses at the interface between T cell and APC. {ECO:0000250|UniProtKB:P01911}.
Interaction partners:
Sequence:
MVCLKLPGGSSLAALTVTLMVLSSRLAFAGDTRPRFLELRKSECHFFNGTERVRYLDRYFHNQEEFLRFDSDVGEYRAVTELGRPVAESWNSQKDLLEQKRGRVDNYCRHNYGVGESFTVQRRVHPQVTVYPAKTQPLQHHNLLVCSVSGFYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVTSALTVEWRARSESAQSKMLSGVGGFVLGLLFLGAGLFIYFRNQKGHSGLQPTGFLS
Protein: Short spindle 3, isoform B (X2J6U8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEMREVLSREGREAKNLLVYQFCDETTSSGATSGFGSTGGDVGGGSGGDGPAVGSGGVLLNGYRKPPMVPPKSPNGTPKNCQSPTSPRLKSSASVGCGGGSSGGPRVRSASTGRDKKSELQARYWALLFGNLQRAINEIYQTVECYENISSCQETILVLENYVRDFKALCEWFKVSWDYESRPLQQRPQSLAWEVRKSNPTPRVRTRSLCSPNNSGKSSPALFPGTQSGETSPFCDNGQISPRKLLRAYDQVPKGAMRLNVRELFAASKRATQGSSQSDNMEGPLDLSGDKSNFVLRSTQYAQTDLEDPHLTLADVREKMRMEAEEREAQNRIENEALEEVTIPIDNEDATESLNKQEPSSLELPIHNVADLSKEPELMEAASEATALEMTVASLESMENALLNQQANKEPTPPSTVIKPLAEILKKPQPLNPLSGNNVQNSPLKYSSVLNRPSKKMIPPPGGVAAQKTISTKPGLVKPNLTTTVNGLRSTKTATAPPAIKTTGRSGLQRHPRPSSKTECYGPPNNVASRLSARSRTMLEINGRNTNSSARTLPKKTNPGSILSTATRTKMSSRLSSREDITSSTSTLKASNEQLSNSRNTLKAENQHSEPKQIQPPTDADDGWLTVKNRRRTSMHWANRFNQPTGYASLPTLALLNEQQKEQEHKEKQKGEDDGKVIVKTISAKTKAPIEVAKAKAKTSIVITRPEIKNAKAKVNSFPVQKSNTNQVKKPEKQEKSDTTAPAAIASSSNTRNSSHSICVGRNSIIKRQKSDLTGLKMTSLHKEYMRSEKNALRKLQQKEQGNQQHNSSSSSAETVVESCNEDHSKIDIKIQTNCEFSKTIGELYESIAHCKLPSGSLKTNASTLSACDENEEQNTDDNEEERNERILGEVQESLERQIRELEQTEIDVDTETDETDCEVQLEEQDDGVDGLEMGSGDDSAVFVTMSDDENASLELRYQALLSDMSWNERAEALATLQAYVARHPGRAQELHQKLSSPSRRRSLQETLKKYQAKQARAQQKRNLLQQEKAAKLQQLFSRVEDVKAAKNQIIEDKRQKMQGRLQRAAENREQYLKQIIEKAHDEEKKLKEINFIKNIEAQNKRLDLLESSKETEGRLQDLEQERQKRVEEKLAKEAAVERRRQALEKERLLKLEKMNETRLEKEQRIGKMQEQKEKQRQALAREKARDREERLLALQVQQQQTTEELQRKILQKQMESARRHEENIEHIRQRALELTIPTRQADEGRGDQDVSEDILNGNATSTTNEDCDLSSSLSEVGGNNAHTRSYKKKMKKLKQRMNQCAAEYLESLEALPAHARRDSTVPKLLNLVVKGGGAQGLDRNLGNLLRVIPKAQTLDFLAFLCMDGLGILANHVISKGMDENSEISRKSVYLAAQLYRNACSVCPQIARHALLGNSITVLFDAINKSFQLPEEKSPQHPVELSTELMLACTEALSSSYVKKNTHPKVPERLPDMINYAVITGLIEILSRRIQKVRESIESNKSVMLSLLTTLGFLSRFIDVCQPGPADPTRLLSAAKSTELFGTVSMLYGCVMPMGECIPPRTTALAASTFHLYVSLASLDVNTFQETLTVEGPLSLKLLDVMTVILNCSLVNDQWTTNSESCPMLIDLVASMAFFCVNNRRHQDLLISEQYAVIFKRMAKLPTQFNPVIYPFLVTVSFNNPPAREFLSKDFDLTFLDEYSKSEMAQRNVVIKLINSRTKDKISAGNKKNA
Protein: Na(+)/H(+) antiporter (Q99271)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Sodium export from cell, takes up external protons in exchange for internal sodium ions.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36606}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sodium/potassium exporting P-type ATPase 1
- Endosomal/prevacuolar sodium/hydrogen exchanger
- K
- High-affinity potassium transport protein
- Low-affinity potassium transport protein
- Outward-rectifier potassium channel TOK1 channel YORK)
- Phosphopantothenoylcysteine decarboxylase subunit SIS2
- Low affinity vacuolar monovalent cation/H
- ER-derived vesicles protein ERV14
- Serine/threonine-protein phosphatase PP-Z1
Sequence:
MAIWEQLEVSKAHVAYACVGVFSSIFSLVSLYVKEKLYIGESTVAGIFGLIVGPVCLNWFNPLKWGNSDSITLEITRIVLCLQIFAVAVELPRKYMLKHWVSVTMLLLPVMTAGWLIIGLFVWILIPGLNFSASLLISACITATDPILAQSVVSGKFAQRVPGHLRNLLSAESGCNDGMAFPFLFLSMNLILHPGNGREIVKDWICVTILYECLFGCLLGCFIGYVGRITIRFAEKKNIIDRESFLAFYVVLAFMCAGFGSILGVDDLLVSFAAGATFAWDGWFSQKTQESNVSTVIDLLLNYAYFIYFGAIIPWSQFNNGEIGTNVWRLIILSIVVIFLRRIPAVMILRPLIPDIKSWREALFVGHFGPIGVGAIFAAILARGELESTFSDEPTPLNVVPSKEESKHWQLIACIWPITCFFIVTSIIVHGSSVAIITLGRHLNTITLTKTFTTHTTNGDNGKSSWMQRLPSLDKAGRSFSLHRMDTQMTLSGDEGEAEEGGGRKGLAGGEDEEGLNNDQIGSVATSGIPARPAGGMPRRRKLSRKEKRLNRRQKLRNKGREIFSSRSKNEMYDDDELNDLGRERLQKEKEARAATFALSTAVNTQRNEEIGMGGDEEEDEYTPEKEYSDNYNNTPSFESSERSSSLRGRTYVPRNRYDGEETESEIESEDEMENESERSMASSEERRIRKMKEEEMKPGTAYLDGNRMIIENKQGEILNQVDIEDRNEARDDEVSVDSTAHSSLTTTMTNLSSSSGGRLKRILTPTSLGKIHSLVDKGKDKNKNSKYHAFKIDNLLIIENEDGDVIKRYKINPHKSDDDKSKNRPRNDSVVSRALTAVGLKSKANSGVPPPVDEEKAIEGPSRKGPGMLKKRTLTPAPPRGVQDSLDLEDEPSSEEDLGDSYNMDDSEDYDDNAYESETEFERQRRLNALGEMTAPADQDDEELPPLPVEAQTGNDGPGTAEGKKKQKSAAVKSALSKTLGLNK