wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisome biogenesis factor 2 (EC 2.3.2.27) (EC 2.3.2.36) (Peroxin-2) (Peroxisomal membrane protein 3) (Peroxisome assembly factor 1) (PAF-1) (P24392)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase. PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-11', a modification that acts as a signal for PEX5 extraction into the cytosol (By similarity). Required for pexophagy in response to starvation by mediating ubiquitination of peroxisomal proteins, such as PEX5 and ABCD3/PMP70. Also involved in the response to reactive oxygen species (ROS) by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of PNPLA2/ATGL, thereby regulating lipolysis (By similarity).
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:1750930}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome biogenesis factor 10
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 1 receptor
- Peroxisomal ATPase PEX6
- Peroxisomal targeting signal 2 receptor
- Peroxisomal biogenesis factor 19
- Similar to peroxisome biogenesis factor 26.
- Peroxisomal biogenesis factor 3
Sequence:
MAAREESTQSANRVLRISQLDALELNKALEQLVWSQFTQCFHGFKPGLLARFEPEVKAFLWLFLWRFTIYSKNATVGQSVLNIQYKNDSSPNPVYQPPSKNQKLLYAVCTIGGRWLEERCYDLFRNRHLASFGKAKQCMNFVVGLLKLGELMNFLIFLQKGKFATLTERLLGIHSVFCKPQSMREVGFEYMNRELLWHGFAEFLVFLLPLINIQKLKAKLSSWCIPLTSTAGSDSTLGSSGKECALCGEWPTMPHTIGCEHVFCYYCVKSSFLFDMYFTCPKCGTEVHSVQPLKSGIEMSEVNAL
Protein: Retinoschisin (X-linked juvenile retinoschisis protein homolog) (Q9Z1L4)
Organism: Mus musculus (Mouse)
Function: Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides. May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells (By similarity). Required for normal structure and function of the retina.
Subcellular location: Secreted {ECO:0000250|UniProtKB:O15537}. Cell membrane {ECO:0000269|PubMed:17325137, ECO:0000305|PubMed:20677810}; Peripheral membrane protein {ECO:0000269|PubMed:17325137, ECO:0000269|PubMed:20677810}; Extracellular side {ECO:0000269|PubMed:17325137, ECO:0000305|PubMed:20677810}. Note=Binds to phosphatidylserine-containing lipid membranes and embeds itself partially into the lipid bilayer. Lipid-binding requires the presence of Ca(2+) ions. {ECO:0000269|PubMed:20677810}.
Interaction partners:
Sequence:
MPHKIEGFFLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQVGANALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKYQDSSQWLQIDLKEIKVISGILTQGRCDIDEWVTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRSSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECASKCA
Protein: Bifocal, isoform C (Q9VYV8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}. Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004269}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004269}.
Interaction partners:
Sequence:
MESQKRPSLDLHTDVPAGLAAGGSGLGAAAEMSPTSGFLPDMPQWKKDLIQRRKTNVARTQAASITSPTDGSCGALAEANAAPGAIADFTEPATISSTSQKRNMIGSEEKSEKSSISNTNSDSTGGHHSVVAVSLSPDAAATTNVTVTPIPKQRSSLLNTRSQEREMVRYILSESGERDGELESGEQPAGVVSNSRCGEVETGTIGSPSSSANQNPNPNHLKTKCKPGQSVAEGKPSAKETIVDNSKSCSKTKSISDKLQSNKFIIQQQQQQQQQQQQQQQLSPTKVTVKPTMVAMQEMKKTTKQNGQHRHLAGKIGSVAGGDVDPQHPPTNPIPDSLDTGEDLSYGPGIVSKLRCRYLSLALRESRQQSSKQRLQRSTSLNTLLDRDDDEVEVEEPEMTNSQVRAKSTPPPILGAKPTPKPSSQHQRPVSLGANGAGSAVNPPSNSDQAQTGAVANGGAGSGQRSRHFKRGNEVMKRARSVEALLCEKSPWNSQRISTAGAAAAAAPSPPAPKATAAAPSPVTSPTCVTIEDKIHNARERLHSGTDTAPPKRLTSIIDDTERPPPDLVKQTLKMFEASANRRPRAAHRSNGVGGVASKVANYKSIIKDQKQPSSAAATPPPTGMGFASSTPLRHVHPDIIPRQVDSPVSALSVMMRRMELQEPETPERETRDAEATPQSEALSETERNDRDEGDGEVDDDNHNNNDDDHDDGDDGSDNNEQRDKMGAAAAGDKPKPPAESAAGGAQRSFAASTENAHVASGSSSSTSASVRKLSNNNDSSSGPAVTKQIGVIRPLFNSQGAGSTPLTSREIEKNRINEMKKSTATDAGGSVSGSGTVAGAGSGTSPTTSLDSVINTKEAASSETDASASPLWTLRKLRNQSQTAGGGSGPSSSLHSTENTSMVFNFSKSTKEVPDYIESDVVIYRRKRELPKPNEPGFVLLGDLSVETSTDTDYDDYSMCPPSPCDVEFENANIVIDGKSSIRQKPKESSFRVQFNDTLTSTFEYPSEASMTIEDPPYADPFGHVSKHHQMLLAEQMHLLQHQEQLELEQMHQLGLAPEQHHHVTVDEIIELPTSTAGHGHGIGLGHRSGAAGGGGTMLGNLPLDII
Protein: Os01g0218100 protein (Q9FTQ1)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
- Transcription factor RF2a
- Os04g0461600 protein
- Os01g0267400 protein
- Os03g0101800 protein
- Os03g0830500 protein
- Os03g0830400 protein
- Os10g0112100 protein
- Os03g0830300 protein
- Defective in exine formation protein, putative, expressed
- Expressed protein
Sequence:
MGSAPFGDAVAGGGLYEYQGYHGGFAGGHGLGQPAGRAPALDDGETEGMDASAAAAVAAMEMAKRNCGGGREEKAAMALKSHSEAERRRRERINAHLATLRTMVPCTDKMDKAALLAEVVGHVKKLKSAAARVGRRATVPSGADEVAVDEASATGGGGEGPLLLRATLSCDDRADLFVDVKRALQPLGLEVVGSEVTTLGGRVRLAFLVSCGSRGGAAAAAMASVRHALQSVLDKASSGFDFAPRAASLLGSKRRKVSTFESSSSSS
Protein: Cytoplasmic polyadenylation element-binding protein 4 (CPE-BP4) (CPE-binding protein 4) (hCPEB-4) (Q17RY0)
Organism: Homo sapiens (Human)
Function: Sequence-specific RNA-binding protein that binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism. Regulates activation of unfolded protein response (UPR) in the process of adaptation to ER stress in liver, by maintaining translation of CPE-regulated mRNAs in conditions in which global protein synthesis is inhibited (By similarity). Required for cell cycle progression, specifically for cytokinesis and chromosomal segregation. Plays a role as an oncogene promoting tumor growth and progression by positively regulating translation of t-plasminogen activator/PLAT. Stimulates proliferation of melanocytes. In contrast to CPEB1 and CPEB3, does not play role in synaptic plasticity, learning and memory (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q7TN98}. Postsynaptic density {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TN98}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q7TN98}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q7TN98}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TN98}.
Interaction partners:
- Cyclin-dependent kinase 1
- Aurora kinase A
- Serine/threonine-protein kinase PLK1
- G2/mitotic-specific cyclin-B2
- Fragile X messenger ribonucleoprotein 1
- RNA-binding protein FXR1
- RNA-binding protein FXR2
- Cytoplasmic polyadenylation element-binding protein 1
- Probable ATP-dependent RNA helicase DDX6
- Cytoplasmic polyadenylation element-binding protein 2
Sequence:
MGDYGFGVLVQSNTGNKSAFPVRFHPHLQPPHHHQNATPSPAAFINNNTAANGSSAGSAWLFPAPATHNIQDEILGSEKAKSQQQEQQDPLEKQQLSPSPGQEAGILPETEKAKSEENQGDNSSENGNGKEKIRIESPVLTGFDYQEATGLGTSTQPLTSSASSLTGFSNWSAAIAPSSSTIINEDASFFHQGGVPAASANNGALLFQNFPHHVSPGFGGSFSPQIGPLSQHHPHHPHFQHHHSQHQQQRRSPASPHPPPFTHRNAAFNQLPHLANNLNKPPSPWSSYQSPSPTPSSSWSPGGGGYGGWGGSQGRDHRRGLNGGITPLNSISPLKKNFASNHIQLQKYARPSSAFAPKSWMEDSLNRADNIFPFPDRPRTFDMHSLESSLIDIMRAENDTIKGRLNYSYPGSDSSLLINARTYGRRRGQSSLFPMEDGFLDDGRGDQPLHSGLGSPHCFSHQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLIVDWPHKAESKSYFPPKGYAFLLFQDESSVQALIDACIEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHGEIDKRVEVKPYVLDDQLCDECQGARCGGKFAPFFCANVTCLQYYCEYCWAAIHSRAGREFHKPLVKEGGDRPRHISFRWN
Protein: Minor fimbrium subunit Mfa1 (Pg-II fim a) (B2RHG1)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Structural subunit of the minor fimbriae. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Mfa1 orthologs from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable).
Subcellular location: Fimbrium {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:23809984, ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, ECO:0000269|PubMed:26437277}. Cell outer membrane {ECO:0000269|PubMed:11083792, ECO:0000269|PubMed:15972485, ECO:0000305|PubMed:9786913}. Note=Probably synthesized as a palmitoylated precursor. Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (Probable). {ECO:0000305}.
Interaction partners:
Sequence:
MKLNKMFLVGALLSLGFASCSKEGNGPDPDNAAKSYMSMTLSMPMGSARAGDGQDQANPDYHYVGEWAGKDKIEKVSIYMVPQGGPGLVESAEDLDFGTYYENPTIDPATHNAILKPKKGIKVNSAVGKTVKVYVVLNDIAGKAKALLANVNAADFDAKFKEIIELSTQAQALGTVADGPNPATAAGKIAKKNGTTDETIMMTCLQPSDALTIEAAVSEANAIAGIKNQAKVTVERSVARAMVSTKAQSYEIKATTQIGEIAAGSVLATITDIRWVVAQGERRQYLSKKRGTVPENTWVTPGSGFVPTSSTFHTNATEYYDYAGLWEDHNTNEAVISGTQVPTLADYQLQDVTGELANALSGKFLLPNTHKSGANAASSDYKRGNTAYVLVRAKFTPKKEAFIDRGKTYSDNTAVPEYVAGEDFFVGENGQFYVSMKSVTDPKVGGVAGMKAHKYVKGKVLYYAWLNPSTTSPDSWWNSPVVRNNIYHIHIKSIKKLGFNWNPLVPDPDPSNPENPNNPDPNPDEPGTPVPTDPENPLPDQDTFMSVEVTVLPWKVHSYEVDL
Protein: U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase (EC 2.1.1.346) (O42662)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: RNA N6-methyltransferase that mediates N6-methylation of adenine of U6 small nuclear RNA (U6 snRNA).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative acetyltransferase C18B11.09c
- Siroheme biosynthesis protein met8
- S-adenosylmethionine synthase
- Uncharacterized protein C2A9.02
- Intermediate cleaving peptidase 55
- ADP-ribosylation factor guanine nucleotide-exchange factor sec71
- Meiotic expression up-regulated protein 29
Sequence:
MPIYILIERSVKNGRIDFWNEDAIRTLGKAILDRDYSLRVEFPENRLCPMVPNRATYIRYIHDLLSSTSGQKDKKRIIGLDIGTGASCIYPLLGCRMYSYDFVGTEIDKFSFETAKSNILQNNMESQIKIVLRSKQDCLLPDTEGMEEFTFVMCNPPFYEHEEDFINFKQNPPSGVCTGVYHEMVTEGGEVGFANKILTESKKRKGIQWYTCMFGKKSSVPAVVDKLREQNISNYGIYELALGKTKRWIICWSFQAMRPHNELIRPSSTSLSKYFPHKVLQNWTLDPELCAQIDDILQKFLDDNKIPWSKKGSVLEISTKSITWSRKARRISKSQTSVSSLEGQMKCELNVIDNQLQCKWIEGYDYNVYESFCSALARALRDNKK
Protein: CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (P71629)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities (Probable). This CRISPR-Cas system protects bacteria against transformation with plasmids containing DNA homologous to its spacer regions.
Interaction partners:
- CRISPR system Cms protein Csm5
- CRISPR system Cms protein Csm4
- CRISPR system Cms protein Csm2
- CRISPR system Cms endoribonuclease Csm3
- CRISPR-associated endoribonuclease Cas6
- CRISPR-associated endoribonuclease Cas2
- CRISPR system endoribonuclease Csm6
- CRISPR-associated endonuclease Cas1
Sequence:
MNPQLIEAIIGCLLHDIGKPVQRAALGYPGRHSAIGRAFMKKVWLRDSRNPSQFTDEVDEADIGVSDRRILDAISYHHSSALRTAAENGRLAADAPAYIAYNIAAGTDRRKADSDDGHGASTWDPDTPLYSMFNRFGSGTANLAFAPEMLDDRKPINIPSPRRIEFDKDRYAAIVNKLKAILVDLERSDTYLASLLNVLEATLSFVPSSTDASEVVDVSLFDHLKLTGALGACIWHYLQATGQSDFKSALFDKQDTFYNEKAFLLTTFDVSGIQDFIYTIHSSGAAKMLRARSFYLEMLTEHLIDELLARVGLSRANLNYSGGGHAYLLLPNTESARKSVEQFEREANDWLLENFATRLFIATGSVPLAANDLMRRPNESASQASNRALRYSGLYRELSEQLSAKKLARYSADQLRELNSRDHDGQKGDRECSVCHTVNRTVSADDEPKCSLCQALTAASSQIQSESRRFLLISDGATKGLPLPFGATLTFCSRADADKALQQPQTRRRYAKNKFFAGECLGTGLWVGDYVAQMEFGDYVKRASGIARLGVLRLDVDNLGQAFTHGFMEQGNGKFNTISRTAAFSRMLSLFFRQHINYVLARPKLRPITGDDPARPREATIIYSGGDDVFVVGAWDDVIEFGIELRERFHEFTQGKLTVSAGIGMFPDKYPISVMAREVGDLEDAAKSLPGKNGVALFDREFTFGWDELLSKVIEEKYRHIADYFSGNEERGMAFIYKLLELLAERDDRITKARWVYFLTRMRNPTGDTAPFQQFANRLHQWFQDPTDAKQLKTALHLYIYRTRKEESE
Protein: Translation initiation factor eIF2B subunit epsilon (eIF2B GDP-GTP exchange factor subunit epsilon) (Q9GQ87)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MAQFEKEIVQAVLIADNNVWNFKPLSDEGSTALVPLVNVRMLDYALMALNRSGVEEVFVYTSLYRSSIREHIRAGIATDAAWSFKMTVHVIGGEGCRCFGDAMRDLDNKALIRGHFILLGADTVTNADLRPVLEQHKRQAKFDKGTAATLVFKECANNVRTGNEVLIAVDRRNDRLHYHQRLRMHHKENRYQLPLDVFLGNSCVALHHNLLDPQIAIGSPSMLSLFNDNFDFQTRDDFVRGLLINEELLDSRIYVALLPAAQYAHKVNNWPAYQLVSRDIINRWAYPFVPDIGLYKLQQEYVFHKDNIYKSPEAHVSKVALLQNVVIEAGSHVDSGSVISDSVIGANCRIGKNCRLTNAFLMADVTVMDNCRLEHCVVGEGAIINEDCDVSAGCVLGAKSVLPAKTTLAKTLITRTPSRRRSDDEVVVELKSIGPHAYIVSDLTTGDPEDSECEDLLPQQPLSIPKMGDLLAPLDEISYCSDFSEDDEDASRAVTPLPDDTSFPGRSIDSLTRGFREKSNPDFLVLEINSSRYAYNMSLKEVNFNVVKAVFGMQSIVEPANDNVLVAINAAFKQLGPVVSNYIKSEDSMMDCLKALEDVYEENHLVRGKISQIVHYLYDKDFVSESAIQAWYAQLDEEEHAHLRQSLAKLVAWLDQSSEEDDDEEDDD
Protein: phosphoinositide 5-phosphatase (EC 3.1.3.36) (A0A1D8PIH6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- phosphoinositide 5-phosphatase
- 1-phosphatidylinositol 4-kinase
- Phosphatidylinositol-3-phosphatase
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
- 1-phosphatidylinositol-4-phosphate 5-kinase
- Phosphatidylinositol 4-kinase
- Phosphatidylinositol 4-kinase PIK1a
- Phosphoinositide phospholipase C
- Increased rDNA silencing protein 4
Sequence:
MRLYLIEKPRTFVITTNTHALIIRHPSPTYKHSGIKGLVSGHSKDKDQNKDTKVLVEFVLKEYLDLSLYRDITPKHGGLLGLLGLLNVKGKTFIGFITRDEWTASATVTDRIYKITDTEFYCINNDEYDYLLDKEYENMSHQERERLRYPAASVQRLLSSGAFYYSKQFDMTSNIQERGFVSSDYKLIADSSFFKSFMWNGFMTEELIETRKRMSPAEQKIIDKSGLLIIVIRGYAKTVNTTVGGCEALMTLISKQSCAKEGPLFGDWGSDGDGYVSNYLESEIIIYTEKFCLSYVIVRGNVPMYWELENNFSTKTILAANGKQIAFPRSFEASQEALVRHFDRLSSQYGDIHVLNTLSDKSYKGVLNSAYEEQLKYFLQNRESTDIGYKVLYTRIPIASSRIKKIGYSGQNPYDIVSLLSNSIIDFGALFYDSKPNSFIGKQLGVFRINSFDSLNKANFLSKIISQEVIDLAFRDIGLELDRELYVKHAQLWEENDLWISKLTLNFASTSDKLHTSHNSIKSSFVKSHITKKYFGGVVESKPNEIAMLKLLGRLQDQSPVTMFNPIHNYVNKELNKRAKDFTSKLDLSVYASTFNVNGSVYEGDIDKWIYPEENDYDLIFIGLQEIVVLNAGQMVNTDFRNKTQWERKILSVLQKRNKYMVMWSGQLGGVALYFFVKESQVKYVSNVECSFKKTGLGGVSANKGGIAVSFKFSDTTICFVSAHLAAGLSNIEERHQNYKALIKGIQFSKNRRIQNHDAVIWLGDFNYRIDLTNDQVKPMILQKLYAKIFECDQLNKQMANGESFPFFSEQEINFPPTYKFDKGTKVYDTSEKQRIPAWTDRILFLSRQNLIEPLSYNSCQNLTFSDHRPVYATFKITVKIINHTIKKNLSDEIYKNYKDSHNGIFDILVKSFDNKELNEEKDASLPAPSSDKHKWWLEGGKAAKIIIPGLEDDNMVMNPWRPINPFEKSNEPEFVSKNDLEAIQN
Protein: Sialic acid-binding Ig-like lectin 10 (Siglec-10) (Sialic acid-binding Ig-like lectin G) (Siglec-G) (mSiglec-G) (Q80ZE3)
Organism: Mus musculus (Mouse)
Function: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (By similarity). Involved in negative regulation of B-cell antigen receptor signaling and specifically acts on B1 cells to inhibit Ca(2+) signaling, cellular expansion and antibody secretion. The inhibition of B cell activation is dependent on PTPN6/SHP-1. In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (By similarity). Plays a role in the control of autoimmunity. During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96LC7}; Single-pass type I membrane protein.
Interaction partners:
- Signal transducer CD24
- High mobility group protein B1
- Leukocyte surface antigen CD47
- CAMPATH-1 antigen
- E3 ubiquitin-protein ligase CBL
- B-cell receptor CD22
- Amine oxidase [copper-containing] 3
- TYRO protein tyrosine kinase-binding protein
- Tyrosine-protein phosphatase non-receptor type 11
Sequence:
MSLLLFLLSFLLDGPQGQMESYFLQVQRIVKAQEGLCIFVPCSFSSPEGKWLNRSPLYGYWFKGIRKPSLSFPVATNNKDKVLEWEARGRFQLLGDISKKNCSLLIKDVQWGDSTNYFFRMERGFERFSFKEEFRLQVEALTQKPDIFIPEVLEPGEPVTVVCLFSWTFNQCPAPSFSWMGDAVSFQESRPHTSNYSVLSFIPGLQHHDTELTCQLDFSRMSTQRTVRLRVAYAPRSLAISIFHDNVSVPDLHENPSHLEVQQGQSLRLLCTADSQPPATLSWVLEDQVLSWSSPVGSRTLALELPWVKAGDSGHYTCQAENRLGSQQHTLDLSVLYPPQDLRVTVSQANRTVLEILRNAISLPVLEGQSLCLVCVTYSNPPANVSWAWVTQTLIPIQSSEPGVLELPLVQREHEGEFTCAAQNPLGAQRISLSLSVHYPPQMSSPSCSWEAKGLHCNCSSRAWPAPSLRWRLGEGLLEGNSSNASFTVTFSSLGPWVNSSLSLLQELGPSLWLSCESWNTHGAQTTSVLLLPDKDSATAFSKGAVLGFGITALLALCLIVVIVKTLQKKGTQEEPSRPKLSRGSTILDYINVVPKTRSLARNWKAEPDAPSRSSPLDTHFPKPKKKQKDPHFTYPGCPDPTSSSQVPVSENNPEELHYAALNFSRLRLQETQDPQDTYSDYTEVRVH
Protein: Sushi-repeat-containing protein, X-linked (A0A8I6AFA8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPRGSRWGTGGLGQYLRPNRVAPAVFPKQAQIPFAAFGMAEPESLVPDTGAVFTFGKTKFAENIPSKFWFKNDVPICLSCGDEHTAIVTGNNKLYMFGSNNWGQLGLGSKSAISKPTCIKALKPEKVKLAACGRNHTLVSTDTGGVYAAGGNNEGQLGLGDTDDRDTFHQIGFFTPSDIIKQLSAGANTSAALTEDGKLFMWGDNSEGQIGLKNKSNVCIPHEVTVGKPISWISCGYYHSAFVTTDGELYTFGEPENGKLGLPNQLLINHRSPQRVLGIPDKVIQVACGGGHTVVLTEKVVYAFGLGQFGQLGLGTFLFETSEPKIIDRIKDQKISHISCGENHTALMTDIGLMYTFGDGRHGKLGLGMENFTNQFFPTLCSNFLKFTVQLIACGGCHMLVFATPRLGTIDETEFEEVYEPYMSTGSLSINDLSPGSSLNRSLSARLRRRERERPSCSASMVGTLPPLEGTSASTSASYFSPSSIPFRLSVNNYPEKSTSDSTEPLDSDYFEDKMNKETETENSSAVDLENFGETIDILNMTHMMTTSSNEKSLDFSPIQKQQNQDTVEKVVESTPYTENEDSYEYEEMSKIKEGTVYKQYLAKGIFMIRAPEILGTFSDEEGGNSLDQEELQAFTGVKSEQVGKERDEEIDSEKKTQAMEMADLKKVRESQENSKSDTFFDDLPDKDMNSESEDNKDIAEERKSSEQNMVFDSETELVEEPDSYMECKKHSEQDSAEESEQHKLVESSIEEKDDDEVETEHYLWYSRKCAEQATENELRANRFLPKYDLKHDHLSGIPEEQEGAEDAEGSVVVEQEVQAQEENMELEGDREEAKAEALSDVITEKEIPQLSESVKPEAEGMDEQISVPNVEDTVEEEGKKEKETVEEGSLPEDALPETEGSETVVPADEKPAEMVKEENSASLLQRNLREYNENPKGHMYDRVKSSSSEILGGNEPTSKDIKKAKKISFFNRMSLTGQKLMQSANDPLPEIKPIGDQIALQSDKKDANQNHMGQNLQDTATPNMEGKSKSCTIL
Protein: Pyridoxal 5'-phosphate synthase subunit PdxS (PLP synthase subunit PdxS) (EC 4.3.3.6) (Pdx1) (Superoxide-inducible protein 7) (SOI7) (P37527)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Interaction partners:
- Pyridoxal 5'-phosphate synthase subunit PdxT
- Pyridoxine kinase
- Transaldolase
- Transketolase
- Ribokinase
- Ribose-phosphate pyrophosphokinase
- Putative sugar phosphate isomerase YwlF
- Phosphoglucomutase
- Phosphopentomutase
- GMP synthase
Sequence:
MAQTGTERVKRGMAEMQKGGVIMDVINAEQAKIAEEAGAVAVMALERVPADIRAAGGVARMADPTIVEEVMNAVSIPVMAKARIGHIVEARVLEAMGVDYIDESEVLTPADEEFHLNKNEYTVPFVCGCRDLGEATRRIAEGASMLRTKGEPGTGNIVEAVRHMRKVNAQVRKVVAMSEDELMTEAKNLGAPYELLLQIKKDGKLPVVNFAAGGVATPADAALMMQLGADGVFVGSGIFKSDNPAKFAKAIVEATTHFTDYKLIAELSKELGTAMKGIEISNLLPEQRMQERGW
Protein: Interleukin-11 receptor subunit alpha (IL-11 receptor subunit alpha) (IL-11R subunit alpha) (IL-11R-alpha) (IL-11RA) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)] (Q99MF4)
Organism: Rattus norvegicus (Rat)
Function: Receptor for interleukin-11 (IL11). The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth. Restricts suture fusion and tooth number.
Subcellular location: [Interleukin-11 receptor subunit alpha]: Membrane {ECO:0000250|UniProtKB:Q14626}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Soluble interleukin-11 receptor subunit alpha]: Secreted {ECO:0000250|UniProtKB:Q14626}.
Interaction partners:
- Interleukin-11
- UDP-glucose 4-epimerase
- N-acetylgalactosamine kinase
- Galactokinase
- Interleukin-6 receptor subunit beta
- Cardiotrophin-1
- Oncostatin-M
- Ciliary neurotrophic factor
- UTP--glucose-1-phosphate uridylyltransferase
- dTDP-D-glucose 4,6-dehydratase
Sequence:
MSSSRSGLTRVLVAVATALVSSSTPCPQAWGPPGVQYGQPGRPVMLCCPGVNAGTPVSWFRDGDSRLLQGPDSGLGHRLVLAQVDSRDEGTYVCRTLDGVFGGMVTLKLGSPPARPEVSCQAVDYENFSCTWSPGRVSGLPTRYLTSYRKKTLPGAESQRESPSTGPWPCPQDPLEASRCVVHGAEFWSEYRINVTEVNPLGASTCLLDVRLQRILRPDPPQGLRVESVPGYPRRLHASWTYPASWRRQPHFLLKFRLQYRPAQHPAWSTVEPIGLEELITDAVAGLPHAVRVSARDFLDAGTWSAWSPEAWGTPSTGPLRDEVPDGSRGHEQKLEAAAQEDSPAPPSPSLQPDPRPLDHRDPLEQVAVLASLGIFSFLGLAVGALALGLWLRLRRSGKDGPQKPGFLAPMIPGDKLPGIPNLQRTPENFS
Protein: NUC153 domain-containing protein (Q38AI3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP-dependent RNA helicase
- Sas10 C-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 6 N-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 18
- Probable eukaryotic initiation factor 4A
- Nrap protein domain-containing protein
- RNA cytidine acetyltransferase
- RRM domain-containing protein
- MI domain-containing protein
- AATF leucine zipper-containing domain-containing protein
Sequence:
MKTLQSSSRGRGLHRGRGRGRGGDARFASRFTDPRFQLTRGGHRSGRGRGTVQDAARQDPRFAKHLRQIQGGEGDSEKEEEDEESDEYSDMEDGEEGAEALSDIASSLKSDNGGGMDLSDDEAEQLDGEVRAWSPSDVEYVEPKHRLAIVNCSWDHIRSVDLYAVLFYALPLGGQLLNVAVYMSDFGKRMLEYERMHGPDLWEKRDEVSVKPPADADKPIKEGSKKKDRKNKGKESGMDYGVGDNEAEEGNIEKEHTMDDDPWEDDNIAMLQEEGEDGELFSEGKHRKYERDRMKYYYAVATFDSPETAEAVYNQLDGMDIEASGVVLDLRYVDDSEVFENPVNKADRIPANYQPLAAFKAAALSQTRFRISWDQEDVFRHRSLRDSFTGETADDDLAAYIAPPDSSEEDEVDDNVENSRVNGKKMKRAKDKVRIRKKYAALLEEIGGLPEDYGGSGEDGEADEENSDESDDDSLNRFSDVEMEKSEGSCEGSPEVFGEVEATLDLDAESKAVKLQRDVRIKQQMTSSDLGSKAELKYKLRRSEMKKKKKEMIMQEREAETAKQHAEREERRQVLRAALGTDDEGAIHLSGKEKRKQHARAVKQRLAAERAEKKKMRASNNLGVTREARQRLASDAAAEAIDTRFQSKLLSDPRFHLDVAQKDRRHNPDVVGLAATVVNARQGRRQHERNEARDDGAVEYFLGRPSKKAKRE