wanglab/gogpt-training-data huggingface dataset:
Protein: COP9 signalosome complex subunit 5 (EC 3.4.-.-) (Q5BBF1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development. Required for fruit body formation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 7
- Ubiquitin-like domain-containing protein
- Proteasome regulatory particle subunit
- RING-box protein 1
- Ubiquitin ligase subunit CulD, putative
Sequence:
MQAAQLSWELENAVTLIDPQRDSLYRYDEETHKYLSDTRPWTKDPHYFKSVRISAVALLKMVMHARSGGSLEVMGLMQGYILPNTFVVTDAFRLPVEGTETRVNAQDEANEYMVSYLQSCREAGRMENAVGWYHSHPGYGCWLSGIDVSTQDMQQMSGPFVAVVIDPERTISAGKVDIGAFRTFPKDYTPPKEEQEEDEYQTVPLNKAEDFGAHASHYYSLEVSLFKSALDTEILSLLWNKYWVATLSQSPLFTTRDYGSKQMLDLSQKTRRVARGIESNPPRGGAPTQVRDQQLERVVKDGQRIVSEEVKGLLAAEVKMQLFQGIGGKQTVEST
Protein: Serpin 28B, isoform A (Serpin 28B, isoform B) (Q9VLZ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serpin 28Da
- Serpin 38F, isoform A
- Major facilitator superfamily
- Accessory gland-specific peptide 26Aa
- glutaminyl-peptide cyclotransferase
- GH21475p
- Serpin 28F
- Accessory gland protein Acp76A
- Uncharacterized protein, isoform B
Sequence:
MKYLYLLLLATSVESGFWEDFYRILASQNAKRNLIYSPISAEIIMSMVYMASGGKTFEELRNVLKFSENKTLVANNYRSLLSDLKRRETFIILHMANRIYVNKKYCLVPEFNQLARKAFKAKAKSIRLDDPVSASAIVNSWILNRTRGMIRNIVLPKDFNSDTSAFLVNAIYFKGQWLYNFKADQTHIADFYVSANEIIPVKMMTLSASLLSGYIDDIDAKIIELPYWNSTLSMRIILPNSVDGLRKLKEKVGFIDYHLEKKSVNVKLPKFKIESKAQLKGIFENLGILDVFKPSADLNGLVLESGAKIDKIVQKAFLKIDEKGGEASAATGVLTRRKKSIDNLIQPPMEFIADHPFFYVIHDNKVIYFQGHIVEPRW
Protein: MYB-like transcription factor TCL1 (Protein TRICHOMELESS 1) (D3GKW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: MYB-type transcription factor involved in trichome cell specification. Acts as a negative regulator of trichome patterning and formation by direct binding to the cis-acting regulatory elements of GL1, thus suppressing the expression of GL1.
Subcellular location: Nucleus {ECO:0000269|PubMed:17933793}.
Interaction partners:
- Transcription factor GLABRA 3
- Homeobox-leucine zipper protein GLABRA 2
- Transcription factor EGL1
- Protein TRANSPARENT TESTA GLABRA 1
- Squamosa promoter-binding-like protein 9
- Zinc finger protein 8
- Uncharacterized protein At2g30430
- Zinc finger protein GIS2
- NAC domain-containing protein 40
- Protein TORMOZ EMBRYO DEFECTIVE
Sequence:
MDNTNRLRRLHCHKQPKFTHSSQEVSSMKWEFINMTEQEEDLIFRMYRLVGDRWDLIARRVVGREAKEIERYWIMRNCDYFSHK
Protein: Probable ATP-dependent RNA helicase DDX41 (EC 3.6.4.13) (DEAD box protein 41) (DEAD box protein abstrakt homolog) (Q9UJV9)
Organism: Homo sapiens (Human)
Function: Probable ATP-dependent RNA helicase. Is required during post-transcriptional gene expression. May be involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:26712909, ECO:0000269|PubMed:35613581}. Cytoplasm {ECO:0000269|PubMed:23222971, ECO:0000269|PubMed:25704810, ECO:0000269|PubMed:35613581}. Note=Predominantly present in the nucleus and traffics to the cytoplasm, specifically in the perinuclear region, after DNA stimulation. {ECO:0000269|PubMed:35613581}.
Interaction partners:
- Serine/threonine-protein kinase TBK1
- E3 ubiquitin-protein ligase TRIM21
- Gamma-interferon-inducible protein 16
- Interferon regulatory factor 3
- Pre-mRNA-processing factor 17
- Spliceosome RNA helicase DDX39B
- Cyclic GMP-AMP synthase
- Serine/arginine repetitive matrix protein 1
- Stimulator of interferon genes protein
- NF-kappa-B-activating protein
Sequence:
MEESEPERKRARTDEVPAGGSRSEAEDEDDEDYVPYVPLRQRRQLLLQKLLQRRRKGAAEEEQQDSGSEPRGDEDDIPLGPQSNVSLLDQHQHLKEKAEARKESAKEKQLKEEEKILESVAEGRALMSVKEMAKGITYDDPIKTSWTPPRYVLSMSEERHERVRKKYHILVEGDGIPPPIKSFKEMKFPAAILRGLKKKGIHHPTPIQIQGIPTILSGRDMIGIAFTGSGKTLVFTLPVIMFCLEQEKRLPFSKREGPYGLIICPSRELARQTHGILEYYCRLLQEDSSPLLRCALCIGGMSVKEQMETIRHGVHMMVATPGRLMDLLQKKMVSLDICRYLALDEADRMIDMGFEGDIRTIFSYFKGQRQTLLFSATMPKKIQNFAKSALVKPVTINVGRAGAASLDVIQEVEYVKEEAKMVYLLECLQKTPPPVLIFAEKKADVDAIHEYLLLKGVEAVAIHGGKDQEERTKAIEAFREGKKDVLVATDVASKGLDFPAIQHVINYDMPEEIENYVHRIGRTGRSGNTGIATTFINKACDESVLMDLKALLLEAKQKVPPVLQVLHCGDESMLDIGGERGCAFCGGLGHRITDCPKLEAMQTKQVSNIGRKDYLAHSSMDF
Protein: Calcium-activated potassium channel slowpoke (dSlo) (BK channel) (Maxi K channel) (MaxiK) (Q03720)
Organism: Drosophila melanogaster (Fruit fly)
Function: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Kinetics are determined by alternative splicing, phosphorylation status and its combination interaction with Slob and 14-3-3-zeta. While the interaction with Slob1 alone increases its activity, its interaction with both Slob1 and 14-3-3-zeta decreases its activity.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Slowpoke-binding protein
- Voltage-dependent calcium channel type D subunit alpha-1
- Potassium voltage-gated channel protein eag
- GH12235p
Sequence:
MASGLIDTNFSSTLANGMSGCDQSTVESLADDPTDSPFDADDCLKVRKYWCFLLSSIFTFLAGLLVVLLWRAFAFVCCRKEPDLGPNDPKQKEQKASRNKQEFEGTFMTEAKDWAGELISGQTTTGRILVVLVFILSIASLIIYFVDASSEEVERCQKWSNNITQQIDLAFNIFFMVYFFIRFIAASDKLWFMLEMYSFVDYFTIPPSFVSIYLDRTWIGLRFLRALRLMTVPDILQYLNVLKTSSSIRLAQLVSIFISVWLTAAGIIHLLENSGDPLDFNNAHRLSYWTCVYFLIVTMSTVGYGDVYCETVLGRTFLVFFLLVGLAMFASSIPEIIELVGSGNKYGGELKREHGKRHIVVCGHITYESVSHFLKDFLHEDREDVDVEVVFLHRKPPDLELEGLFKRHFTTVEFFQGTIMNPIDLQRVKVHEADACLVLANKYCQDPDAEDAANIMRVISIKNYSDDIRVIIQLMQYHNKAYLLNIPSWDWKQGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSPDMQSWTNDYLRGTGMEMYTETLSPTFIGIPFAQATELCFSKLKLLLLAIEIKGAEEGADSKISINPRGAKIQANTQGFFIAQSADEVKRAWFYCKACHEDIKDETLIKKCKCKNLTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNLLNRNVRRPNGTGNGTGGMHHMNNTAAAAAAAAAAGKQVNKVKPTVNVSRQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVSLPAGIADDQSKDFDFEKTEMKYDSTGMFHWSPAKSLEDCILDRNQAAMTVLNGHVVVCLFADPDSPLIGLRNLVMPLRASNFHYHELKHVVIVGSVDYIRREWKMLQNLPKISVLNGSPLSRADLRAVNVNLCDMCCILSAKVPSNDDPTLADKEAILASLNIKAMTFDDTIGVLSQRGPEFDNLSATAGSPIVLQRRGSVYGANVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSTTYFNQNALTLIRSLITGGATPELELILAEGAGLRGGYSTVESLSNRDRCRVGQISLYDGPLAQFGECGKYGDLFVAALKSYGMLCIGLYRFRDTSSSCDASSKRYVITNPPDDFSLLPTDQVFVLMQFDPGLEYKPPAVRAPAGGRGTNTQGSGVGGGGSNKDDNS
Protein: Kelch domain-containing protein 10 (Q6PID8)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC10) complex specifically recognizes proteins with a proline-glycine (Pro-Gly) at the C-terminus, leading to their ubiquitination and degradation. Participates in the oxidative stress-induced cell death through MAP3K5 activation. Inhibits PPP5C phosphatase activity on MAP3K5. Acts as a regulator of necroptosis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23102700}. Cytoplasm {ECO:0000269|PubMed:23102700}.
Interaction partners:
- Cullin-2
- Protein fem-1 homolog B
- Amyloid protein-binding protein 2
- Protein fem-1 homolog C
- Protein zer-1 homolog
- Kelch domain-containing protein 3
- Protein zyg-11 homolog B
- Protein fem-1 homolog A
- Kelch domain-containing protein 2
- Elongin-B
Sequence:
MSAAQGWDRNRRRGGGAAGAGGGGSGAGGGSGGSGGRGTGQLNRFVQLSGRPHLPGKKKIRWDPVRRRFIQSCPIIRIPNRFLRGHRPPPARSGHRCVADNTNLYVFGGYNPDYDESGGPDNEDYPLFRELWRYHFATGVWHQMGTDGYMPRELASMSLVLHGNNLLVFGGTGIPFGESNGNDVHVCNVKYKRWALLSCRGKKPSRIYGQAMAIINGSLYVFGGTTGYIYSTDLHKLDLNTREWTQLKPNNLSCDLPEERYRHEIAHDGQRIYILGGGTSWTAYSLNKIHAYNLETNAWEEIATKPHEKIGFPAARRCHSCVQIKNDVFICGGYNGEVILGDIWKLNLQTFQWVKLPATMPEPVYFHCAAVTPAGCMYIHGGVVNIHENKRTGSLFKIWLVVPSLLELAWEKLLAAFPNLANLSRTQLLHLGLTQGLIERLK
Protein: FI21236p1 (Rumpelstiltskin, isoform A) (Q9VHC7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K, isoform C
- Uncharacterized protein, isoform C
- Bub3 interacting GLEBS and zinc finger domain protein, isoform F
- Interleukin enhancer-binding factor 2 homolog
- Serine/arginine-rich splicing factor x16
- TAR DNA-binding protein 43
- LD21442p
- Small nuclear ribonucleoprotein Sm D3
- LD40489p
- LD45152p
Sequence:
MSMDASNSVESREKERDRRGRGARGSRFTDADGNGNGAGSQGGGVAARDRSRERRNCRVYISNIPYDYRWQDLKDLFRRIVGSIEYVQLFFDESGKARGCGIVEFKDPENVQKALEKMNRYEVNGRELVVKEDHGEQRDQYGRIVRDGGGGGGGGGGVQGGNGGNNGGGGGGGRDHMDDRDRGFSRRDDDRLSGRNNFNMMSNDYNNSSNYNLYGLSASFLESLGISGPLHNKVFVANLDYKVDNKKLKQVFKLAGKVQSVDLSLDKEGNSRGFAVIEYDHPVEAVQAISMLDRQMLFDRRMTVRLDRIPDKNEGIKLPEGLGGVGIGLGPNGEPLRDVAHNLPNGGQSQGQLLGNAQQGSQLGSVGSQPNSSAVSNATTNLLNNLTGVMFGNHAAVQPSPVAPVQKPSLGNNTGSGGLNLNNLNPSILAAVVGNLGNQGGNLSNPLLSSSLSNLGLNLGNSGNDDNLPPSNVGLSNNYSSGGTGGGNSYSSGNNYSGGGGSSNLGYNAYSSSGGMGGGNGGVGVDGNDYNTGNPLDVYGGGSNVGNSNVGSANAVGASRKSDTIIIKNVPITCTWQTLRDKFREIGDVKFAEIRGNDVGVVRFFKERDAELAIALMDGSRLDGRNIKVTYF
Protein: BCL-6 corepressor (BCOR protein) (A1A564)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTRPAFQPPATPAKHSSSTSSKGAKASNPEPSFKANENGLPPSSIFLSPNEAFRSPPIPYPRSYLPYPAPEGIAVSPLSLHGKGPVYPHPVLLPNGSLFPGHLAPKPGLPYGLPTGRPEFVTYQDALGLGMVHPMLIPHTPIEITKEEKPERRSRSHERARYEDPTLRNRFSEILETSSTKLHPDVPTDKNLKPNPNWNQGKTVVKSDKLVYVDLLREEPDAKTDTNVSKPSFAAESVGQSAEPPKPSVEPALQQHRDFIALREELGRISDFHETYTFKQPVFTVSKDSVLAGTNKENLGLPVSTPFLEPPLGSDGPAVTFGKTQEDPKPFCVGSAPPSVDVTPTYTKDGADEAESNDGKVLKPKPSKLAKRIANSAGYVGDRFKCVTTELYADSSQLSREQRALQVSPPT
Protein: Ribulose bisphosphate carboxylase large chain (RuBisCO large subunit) (EC 4.1.1.39) (Q31NB3)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:20304968, ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:24585024, ECO:0000269|PubMed:28616951, ECO:0000269|PubMed:28963440, ECO:0000269|PubMed:31048338, ECO:0000269|Ref.2}. Note=The CcmM short form (M35) purifies from carboxysomes in complex with both RuBisCO subunits; a second complex with full-length CcmM and RuBisCO also includes carbonic anhydrase (CA, ccaA). RuBisCO-CcmM complexes are probably associated with the carboxysome shell (PubMed:17675289). In the carboxysome RuBisCO is organized into a paracrystalline array (PubMed:28616951). This cyanobacterium makes beta-type carboxysomes (PubMed:22928045). {ECO:0000269|PubMed:17675289, ECO:0000269|PubMed:22928045, ECO:0000269|PubMed:28616951}.
Interaction partners:
- Ribulose bisphosphate carboxylase small subunit
- Carboxysome assembly protein CcmM
- RuBisCO accumulation factor 1
- Phosphoribulokinase
- Phosphoglycerate kinase
- Carboxysome shell protein CcmK2
- Phosphoglycolate phosphatase
- HAD family hydrolase
- Carboxysome assembly protein CcmO
- Glycerate kinase
Sequence:
MPKTQSAAGYKAGVKDYKLTYYTPDYTPKDTDLLAAFRFSPQPGVPADEAGAAIAAESSTGTWTTVWTDLLTDMDRYKGKCYHIEPVQGEENSYFAFIAYPLDLFEEGSVTNILTSIVGNVFGFKAIRSLRLEDIRFPVALVKTFQGPPHGIQVERDLLNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKSQAETGEIKGHYLNVTAPTCEEMMKRAEFAKELGMPIIMHDFLTAGFTANTTLAKWCRDNGVLLHIHRAMHAVIDRQRNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGDKASTLGFVDLMREDHIEADRSRGVFFTQDWASMPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRDLYREGGDILREAGKWSPELAAALDLWKEIKFEFETMDKL
Protein: LIM domain-containing protein ajuba (Q96IF1)
Organism: Homo sapiens (Human)
Function: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, mitosis, cell-cell adhesion, cell differentiation, proliferation and migration. Contributes to the linking and/or strengthening of epithelia cell-cell junctions in part by linking adhesive receptors to the actin cytoskeleton. May be involved in signal transduction from cell adhesion sites to the nucleus. Plays an important role in regulation of the kinase activity of AURKA for mitotic commitment. Also a component of the IL-1 signaling pathway modulating IL-1-induced NFKB1 activation by influencing the assembly and activity of the PRKCZ-SQSTM1-TRAF6 multiprotein signaling complex. Functions as an HDAC-dependent corepressor for a subset of GFI1 target genes. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates the Hippo signaling pathway and antagonizes phosphorylation of YAP1.
Subcellular location: Cytoplasm, cytoskeleton. Cell membrane. Cell junction. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, P-body. Note=Shuttles between the cytoplasm and the nucleus. Localizes on centrosomes during G2-M phase. Preferentially co- localizes with cadherin-adhesive complexes at sites of cell-cell contacts. Colocalizes with GFI1 in the nucleus.
Interaction partners:
- Serine/threonine-protein kinase LATS2
- Serine/threonine-protein kinase LATS1
- Protein salvador homolog 1
- LIM domain-containing protein 1
- Wilms tumor protein 1-interacting protein
- Protein aurora borealis
- Nuclear receptor corepressor 1
- Histone deacetylase 3
- Rab effector Noc2
- Aurora kinase A
Sequence:
MERLGEKASRLLEKFGRRKGESSRSGSDGTPGPGKGRLSGLGGPRKSGPRGATGGPGDEPLEPAREQGSLDAERNQRGSFEAPRYEGSFPAGPPPTRALPLPQSLPPDFRLEPTAPALSPRSSFASSSASDASKPSSPRGSLLLDGAGAGGAGGSRPCSNRTSGISMGYDQRHGSPLPAGPCLFGPPLAGAPAGYSPGGVPSAYPELHAALDRLYAQRPAGFGCQESRHSYPPALGSPGALAGAGVGAAGPLERRGAQPGRHSVTGYGDCAVGARYQDELTALLRLTVGTGGREAGARGEPSGIEPSGLEEPPGPFVPEAARARMREPEAREDYFGTCIKCNKGIYGQSNACQALDSLYHTQCFVCCSCGRTLRCKAFYSVNGSVYCEEDYLFSGFQEAAEKCCVCGHLILEKILQAMGKSYHPGCFRCIVCNKCLDGIPFTVDFSNQVYCVTDYHKNYAPKCAACGQPILPSEGCEDIVRVISMDRDYHFECYHCEDCRMQLSDEEGCCCFPLDGHLLCHGCHMQRLNARQPPANYI
Protein: Alpha-mannosidase 2 (EC 3.2.1.114) (Golgi alpha-mannosidase II) (AMan II) (Man II) (Mannosidase alpha class 2A member 1) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) (P27046)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-mannosidase 2x
- alpha-1,2-Mannosidase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Sequence:
MKLSRQFTVFGSAIFCVVIFSLYLMLDRGHLDYPRGPRQEGSFPQGQLSILQEKIDHLERLLAENNEIISNIRDSVINLSESVEDGPRGSPGNASQGSIHLHSPQLALQADPRDCLFASQSGSQPRDVQMLDVYDLIPFDNPDGGVWKQGFDIKYEADEWDHEPLQVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFMWSEISYLAKWWDIIDIPKKEAVKSLLQNGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLEKNLGVKPRSGWAIDPFGHSPTMAYLLKRAGFSHMLIQRVHYAIKKHFSLHKTLEFFWRQNWDLGSATDILCHMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLLDQYRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQCRNYEQLFSYMNSQPHLKVKIQFGTLSDYFDALEKAVAAEKKSSQSVFPALSGDFFTYADRDDHYWSGYFTSRPFYKRMDRIMESRIRAAEILYQLALKQAQKYKINKFLSSPHYTTLTEARRNLGLFQHHDAITGTAKDWVVVDYGTRLFQSLNSLEKIIGDSAFLLILKDKKLYQSDPSKAFLEMDTKQSSQDSLPQKIIIQLSAQEPRYLVVYNPFEQERHSVVSIRVNSATVKVLSDSGKPVEVQVSAVWNDMRTISQAAYEVSFLAHIPPLGLKVFKILESQSSSSHLADYVLYNNDGLAENGIFHVKNMVDAGDAITIENPFLAIWFDRSGLMEKVRRKEDSRQHELKVQFLWYGTTNKRDKSGAYLFLPDGQGQPYVSLRPPFVRVTRGRIYSDVTCFLEHVTHKVRLYNIQGIEGQSMEVSNIVNIRNVHNREIVMRISSKINNQNRYYTDLNGYQIQPRRTMSKLPLQANVYPMCTMAYIQDAEHRLTLLSAQSLGASSMASGQIEVFMDRRLMQDDNRGLGQGVHDNKITANLFRILLEKRSAVNMEEEKKSPVSYPSLLSHMTSSFLNHPFLPMVLSGQLPSPAFELLSEFPLLQSSLPCDIHLVNLRTIQSKMGKGYSDEAALILHRKGFDCQFSSRGIGLPCSTTQGKMSVLKLFNKFAVESLVPSSLSLMHSPPDAQNMSEVSLSPMEISTFRIRLRWT
Protein: Early boundary activity protein 1 (Blastoderm-specific gene 25A) (Q9VR17)
Organism: Drosophila melanogaster (Fruit fly)
Function: The heterotrimeric Elba complex is required for chromatin domain boundary function during early embryogenesis. It binds to a 8-bp sequence 5'-CCAATAAG-3' in the Fab-7 insulator or boundary element in the bithorax complex and contributes to its insulator or boundary activity. Elba1 may act as a transcriptional repressor and binds the palindromic sequence 5'-CCAATTGG-3' to mediate transcriptional repression.
Subcellular location: Nucleus {ECO:0000269|PubMed:23240086, ECO:0000269|PubMed:25561495}.
Interaction partners:
- GEO07864p1
- Early boundary activity protein 3
- Halo
- Early boundary activity protein 2
- FI01028p
- RE73577p
- RE73396p
- Serendipity locus protein alpha
- Protein brother
- Uncharacterized protein, isoform A
Sequence:
MINRRQRLEFALTLLPYDPETVQLSETQKKVEAIIARLRTDDSFTEEESDDCKVRRIQDANEFADSAMRHIEMSDSGKLSTLETLTLAAEKLLRTQRSPDQDFDDMVQDVEYSQLMRNTIQAVNEARLKLLQQWERSKRKALDLLTIEIEKVQEMDQEPEHKQSHEQDQDQEQSSEPFNAFRDGADEHNTSTPKTNDEDLGLDDDDEDYVPGGEETMGNKRKRIKKPVTSTPNAKRRCPGFEFDLDGESPMVTIGPNGTEVSRISLSAINWDMTGPSITRKLLCEIFDRDTLAHHTLSGKPSPAFRDCARPSKQQLDPLKVADLVYLMTNSLDMTPREVRTAITTKCADENKMLRSRMQRKSK
Protein: Interleukin-24 (IL-24) (Cytokine-like protein Mob-5) (Q9JI24)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional cytokine mainly produced by T-cells that plays a regulatory role in immune response, tissue homeostasis, host defense, and oncogenesis. Possesses antiviral functions and induces the type I intereferon response during influenza infection. Signals through two receptor complexes IL20RA/IL20RB or IL20RB/IL22RA1. In turn, stimulates the JAK1-STAT3 and MAPK pathways and promotes the secretion of pro-inflammatory mediators including IL8 and MMP1 (By similarity). Intracellularly, maintains endoplasmic reticulum homeostasis by restricting the eIF2alpha-CHOP pathway-mediated stress signal (By similarity). In addition, acts as a quality control mechanism for the ubiquitin proteasome system by alerting the cell to proteasome dysfunction through activation of PKR/EIF2AK2 (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q13007}.
Interaction partners:
- Interleukin 20 receptor subunit alpha
- Interleukin 22 receptor subunit alpha 1.
- Interleukin 20 receptor beta IL-20R2
- Interleukin family protein
- Interleukin family protein
- Interleukin 10 receptor subunit beta
- Interleukin-22 receptor subunit alpha-2
- Interleukin-10 receptor subunit alpha
- Interleukin 22
- Interleukin-23 receptor
Sequence:
MQTSLRQQILPGLSLILLVLNQVPELQGQEFRFGPCQVTGVVLPELWEAFWTVKNTVKTQDELTSVRLLKPQVLQNVSDAESCYLAHSLLKFYLNTVFKNYHSKIVKFKVLKSFSTLANNFLVIMSKLQPSKDNAMLPISDSARRRFLLYHRTFKQLDIEVALAKAFGEVDILLAWMQNFYQL
Protein: Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) (E9PFV2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364110}. Nucleus {ECO:0000256|RuleBase:RU364110}.
Interaction partners:
Sequence:
MVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
Protein: RNA editing complex protein MP44 (Q86MV8)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MRRAVVLRTAAPMCALTGKCVEDWESHRKSFDMRIFELLKGRLTSPTEPLPIKQIYATIANPCRLVEEFTCAKTTRRLGRLHTALSFLRRHNVLLHSLLFHVKETQTWNTTPDFDRLALYGESSLRHEVRARTLRLFPGIDSETYAALTSSVLSEEALHGLFDRLLMKALVGEKPVGKMRDWSLTPNQCGQMLCAIVGEMSWFAARTKATDRTHNNALFPPSDALILHVLCCHVLESLPAELLYNVLEPKVQRIKENWVNEPMSIPEQLHLKPRTIGSLSLSLVAKPLTEEEGRRKEVAVSAEKCQLSLTPERVFGSVRSTMLPRWNYKRFEERRYHILESDKRQVLPLAMSPVGRGDVSLASEQMPDERRRELVALALGGR
Protein: Invariant chain isoform p41 (Q6J613)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- 40S ribosomal protein S30
- MHC_II_alpha domain-containing protein.
- Macrophage migration inhibitory factor
- Major histocompatibility complex Y, class II beta BLB1
- Ribosomal protein L14.
- 40S ribosomal protein S7
- DNA-
- 40S ribosomal protein S8
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS7m
Sequence:
MAEEQRDLISSDGSSGVLPIGNSERSSLGRRTALSALSILVALLIAGQAVTIYYVYQQSGQISKLTKTSQTLKLESLQRKMPIGTQPANKMSMSTMNMPMAMKVLPLAPSVGDMPMEAMKPRSNKTEDQIRHLLLKSDPRKTFPDLKDDMLGNLKRLKKTMSAMDWQDFETWMHKWLLFEMAKGPKMEEQNTIPAEKVQTKCQAEASFGGVHPGRFRPECDENGDYLPKQCYASTGYCWCCYKNGTRIEGTATRGQLDCSAPAPTQPPSAEPEEVIFSGVDMVKAK
Protein: Polypeptide N-acetylgalactosaminyltransferase 10 (EC 2.4.1.41) (Polypeptide GalNAc transferase 10) (GalNAc-T10) (pp-GaNTase 10) (Protein-UDP acetylgalactosaminyltransferase 10) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10) (Q6P9S7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- C1GALT1-specific chaperone 1
Sequence:
MRRKEKRLLQAVALALAALVLLPNVGLWALYRERQPDGSPGGLGAAVAPAAVQELHSRQKKTFFLGAEQRLKDWHNKEAIRRDAQRVGYGEQGKPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKLYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASAATGDVVTFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVVAQKKLRVSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCTDTKLGTLGSPLRLETCIRGRGEAAWNSMQVFTFTWREDIRPGDPQHTKKFCFDAVSHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRVFMNTCNPSSLTQQWLFEHTNSTVLENFNKN