wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein T12E18_40 (Q9M2V2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVTVARLLNLTLVVPEIDKTSFFADSRSGCAVNMGALAQVVPWIPEDDLLLKNAVEAGASLESLAKGAVQFSRRFSIRELQDRWHALLYDPVVSVEAAFRMAELERTNPNFPTKFGRTGYSKENKSSSRKRNAERLRSTYHSLRKKFRTEPFNSLDLGFLVPPNDSHFMDNGDATHLGLEDSHMDIIHNAFPEILAEGGCVTTHVLPEDNLQGDIPYVEGENLTFTEHAGLSVCDVVHQDSEQKLENTAHEAKNTMASTDFLAQLSTSLFEEDMEPFMEVDGKEVDKSYYDGLSSLLVNSTNDTNREAFPNPTEQEPSIAPTHPGEATLDDHVMLELDGTIALDPHPEIVGGVICCLLNEEDPDIPCNDDIFLSNNSRPMSVSSLARRNFKDTNSPITTCVRDVSASKEKSEGYSLQAQKKKPGRLQGSTQGKPEMGQPSKGSKFRASTSTELKNTVAPGGSSSAQACSNTLLSTGTGAKDGKKETATGTLFVGSDGHGNHPEKDSENCKEKNVVPPVNESPHAKDTDDGLIEITVPELEITRAEAEAEAEAHVCESDEDLPNYSDIEAMILDMDLEPDDQDNFDLEVSKYQSQDMKRTIIRLEQAAHSYMQRAIASRGAFAVLYGRYSKHYIKKPEVLVGRSTEDLAVDIDLGREKRGSKISRRQAIIRLGDDGSFHIKNLGKYSISVNEKEVDPGQSLILKSDCLVEIRGMPFIFETNQSCMQEYLKRRGKVN
Protein: Dysfusion, isoform D (Q9VBH3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator homolog
- Phenoloxidase-activating factor 2
- MAGE
- Klingon
- Gustatory and pheromone receptor 32a
- FI08446p
- Uncharacterized protein, isoform C
- U3 small nucleolar RNA-associated protein 15 homolog
- AT01806p
- tRNA
Sequence:
MPNAIGASSITKWISQIESFEQRELVTNICKRAIDDMYADNKRGLDKVTAATPPTHALQQQQQQQHPHQQQQHLQHVLQLQQQQQQHLQQQQHHLQHQMHTHHNFQQHETSPTVSQQQHMQQQQPQTTQQQHATQQQQQQQQQTAGMFTRFDANKSTKGASKMRRDLINAEIANLRDLLPLPQSTRQRLSQLQLMALVCVYVRKANYFQQVFKRHNAMHHLHHQTATPNIGFSKALSGFLMMLTQNGKLLYISDNAAEYLGHSMEDLLIHGDSVYDIIDKQDHANIQAELNRNVPPQPGGSSQASSGGAGGAGGAGDSTSSNGSAAGAGGAGGASSLEGEHRMFLCRMNVSRNARRQMRFGDQKVVLVQGHYLSFLPLCSRNEPVFLATCTPIAMPETRECVVQGATNVFTTIHSMDMKIAHIDKNGEFHLGYDKSTLQGTSWYNLIHSDNLTEAQKKHSLIIQSEQDRSCILLVRMQRSSGEYTWVHVVLQVRDSPDSTQQPVIVCTNQVLNDREASIMLANSWLYHYYTVQSKIQFGMPLDSGIRVPPGTPSSGYYSPHSSHPPATPGGATPNLGIASSFGPHHHPHHSHHPHHHHHHHHPATAYHHHPHMGTYGGVYHAKAAIELKEDQPLFCFQEPVDYSQVNSHVNPPNATSTPNPPISKSSTPPPPKKRARKLEPLYLHAERSPAAAITPEPDCYAIHTHPAAAYATSSVVSSDASVIYATIVPTRPRLPNKSLPPDPADFIEQWNPSPPWSESAQKASLDSFGSSHELSPCITTTPPTPTSATPHQSGLGTTQTIGPAFSFEWMSDPLVPVTYQQWPPTGDHHQHLSQHLSQSQNHQNPLQQQQNEQLLLGQQPHLHQQHQHLALHHGRGEHSLEGESQGVVVVPPIPISIPIPTATGHGDAGEPVEDRDPKN
Protein: Ubiquitin-conjugating enzyme E2 K (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme K) (Huntingtin-interacting protein 2) (HIP-2) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-25 kDa) (Ubiquitin-conjugating enzyme E2(25K)) (Ubiquitin-conjugating enzyme E2-25K) (Ubiquitin-protein ligase) (P61086)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P61085}.
Interaction partners:
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Huntingtin
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-protein ligase E3A
- SUMO-conjugating enzyme UBC9
- Breast cancer type 1 susceptibility protein
Sequence:
MANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN
Protein: Protection of telomeres protein 1 (A0A3B2WCZ2)
Organism: Mus musculus (Mouse)
Subcellular location: Chromosome, telomere {ECO:0000256|ARBA:ARBA00004574}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSAPVAPSTYTPLNLLKEGTVVNVCGVVKFFKPPYLSKGTDYCSVVTIVDQTNVKLTCMLFSRDYDTLPSVYKVGDIVCFQGLKIQAYKNELQAISKFGFASLTFDGTLGAPIILRTLSKRFNFTAQDYSMVEALRTWASTHISASSNLVQLSDAQPMQYYDLTCQLLGKAQVDGVSFLLKVWDGTRTKIPSWRVCIQDVAFEGDLSHILQLQNLVVDIVVYDNHVQVAKSLKIGSFLRIYSLHTKLQPINSESTTSLVRLEFHLHGGTSYGRGIRVLPESNYDVDQLKKALESVDLEAIQTSDDTYQSDNVENCLTSSSSESDLVSLYEVERCQPLCATSKPFSSVVTDT
Protein: Mitochondrial fission regulator (H0YF01)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU369053}.
Interaction partners:
Sequence:
XPPPPPPLPPPALGLHQSTSAVDLIKERREKRANAGKTLVKNNPKKPEMPNMLEILKEMNSVKLRSVKRSEQDVKPKPVDATDPAALIAEALKKKFAYRYRSDSQDEVEKGIPKSESEATSERVLKRLVKVRTCWTRRPMANPTEDKFISLKRIRTMTKTIQTTIIHGRKYCGIYIIKWLRSFFC
Protein: 2b protein (C1KKL7)
Organism: Cucumber mosaic virus (cucumber mosaic cucumovirus)
Interaction partners:
Sequence:
MELNEGAMTNVELQLARMVEAKRQRRRSHKKNRRERCYKSPSERARSNLRLFRFLPFYQVDGSELIEMYCHVNVAELSESEAPCFTLPAEDDHDFDDTDWLAGNEWAEGAF
Protein: Hyaluronidase-3 (Hyal-3) (EC 3.2.1.35) (Hyaluronoglucosaminidase-3) (Q8VEI3)
Organism: Mus musculus (Mouse)
Function: Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm. Involved in follicular atresia, the breakdown of immature ovarian follicles that are not selected to ovulate. Induces ovarian granulosa cell apoptosis, possibly via apoptotic signaling pathway involving CASP8 and CASP3 activation, and poly(ADP-ribose) polymerase (PARP) cleavage. Has no hyaluronidase activity in embryonic fibroblasts in vitro. Has no hyaluronidase activity in granulosa cells in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:20586096}. Cell membrane {ECO:0000269|PubMed:20586096}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:20586096}. Endoplasmic reticulum {ECO:0000269|PubMed:18234732}. Early endosome {ECO:0000269|PubMed:18234732}. Note=Mostly present in low-density vesicles. Low levels in higher density vesicles of late endosomes and lysosomes. Localized in punctate cytoplasmic vesicles and in perinuclear structures, but does not colocalize with LAMP1 (PubMed:18234732). Localized on the plasma membrane over the acrosome and on the surface of the midpiece of the sperm tail (PubMed:20586096). {ECO:0000269|PubMed:18234732, ECO:0000269|PubMed:20586096}.
Interaction partners:
- Alpha-L-iduronidase
- Beta-glucuronidase
- Arylsulfatase B
Sequence:
MIMHLGLMMVVGLTLCLMHGQALLQVPEHPFSVVWNVPSARCKAHFGVHLPLDALGIVANHGQHFHGQNISIFYKNQFGLYPYFGPRGTAHNGGIPQAVSLDHHLARAAHQILHSLGSSFAGLAVLDWEEWYPLWAGNWGPHRQVYLAASWVWTQQMFPGLDPQEQLHKAHTSFEQAARALMEYTLQLGRTLRPSGLWGFYRYPACGNGWHKMASNYTGHCHAAITTRNTQLRWLWAASSALFPSIYLPPRLPLAYRQAFVRHRLEEAFRVALLEHSHPLPVLAYSRLTHRSSGRFLSLDDLMQTIGVSAALGTAGVVLWGDLSFSSSEEKCWRLHDYLVGTLGPYVINVTKAAMACSHQRCHGHGRCARKDPGQMEAFLHLQPDDSLGAWNSFRCHCYSGWAGPTCLEPKP
Protein: Cytochrome P450, family 2, subfamily r, polypeptide 1 (F7FAJ1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.
Interaction partners:
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- 1,25-dihydroxyvitamin D
- Vitamin D-binding protein
- 7-dehydrocholesterol reductase
- Vitamin D3 receptor
- Sterol 26-hydroxylase, mitochondrial
Sequence:
MFQLPGVQTCAGALAGAFLLLLLVLVVRQLLRQRRPAGFPPGPPRLPFIGNICSLALSADLPHVYMRKQSRVFGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWIDHRRLAVNSFHYFGSGQKSFESKILEETWSLIDAIETYKGRPFDLKQLITNAVSNITNLILFGERFTYEDTDFQHMIELFSENVELAASAPVFLYNAFPWIGILPFGKHQRLFRNADVVYDFLSKLIEKAAVNRKPHLPQNFVDAYLDEMDKGQNDPLSTFSKENLIFSVGELIIAGTETTTNVLRWAVLFMALYPNIQGQVHKEIDLIMGHDRRPSWEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWKDPDMFYPERFLDSSGYFTKKEALIPFSLGHWGILAPG
Protein: Histone H4 (P59259)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- Histone H3.1
- Histone H3-like 1
- Histone H3-like 3
- Histone H3.3
- Histone H3-like 2
- Histone H3-like 5
- Histone H3-like 4
- Histone H2B.6
- Histone H3-like centromeric protein CENH3
Sequence:
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG
Protein: Grainyhead-like protein 1 homolog (G5EDF0)
Organism: Caenorhabditis elegans
Function: Probable transcription factor that binds a motif with the core sequence 5'-C[ACT][TG]G-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- T-box transcription factor tbx-8
Sequence:
MSFQLDQSTSVIKTAPPGRLEFKNEPIDIASSNIQDLAKMQTLDGYYQQTSLQLPQSQQYHRMYENVYNNQQILYAQTQNFQYPSTLLTNGSLAQTEWRGQQMDTSAYSNTGYSRSSTSQQPQYTQQVTENERIVYKPVDMPSPVDSGIGGDISILNPKEEFFTSADGGSMLERSSERTLSHRDSPLVIPKLYNNLGFQYVLEAPISTSVRRDDDRMTYVNKGQFYTVSLEYTPDLNKCLKSQTVKSQLMVVFREDKTYEEEIKTWQSWHARQHVSKQRILEIDSKNSSGMIGQIEEIGNNAVQFYWNPSDPSGVRISIAVQCLSTDFSTQKGVKGLPLHVQIDTYDGENDKVPFHRGYCQIKVFCDKGAERKLRDEDKRAQKRKVQEYTAGALPGGRKKSDGEYHDQCERSEFYHMRELDKPAALFIAPEEFEPRYVDSTSLSFDMSEIEPIPTKRPRTSERIMLYVRKRDEQIYQPLHVVPASLSGLALAIANKFGADPDKMSGVYKRCAKGITVKVDDEMLRLYCNEDTFIIDVEHATDGSTAATLIEVAPTNPNSYSNS
Protein: Lysine-specific demethylase 4 (EC 1.14.11.66) (EC 1.14.11.69) (JmjC domain-containing histone demethylation protein 2) (ceJMJD2) ([histone H3]-trimethyl-L-lysine(36) demethylase 4) ([histone H3]-trimethyl-L-lysine(9) demethylase 4) (Q9U297)
Organism: Caenorhabditis elegans
Function: Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. Involved in the negative regulation of lifespan in a germline-dependent fashion.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537}.
Interaction partners:
- JmjC domain-containing histone demethylation protein 1
- JmjC domain-containing protein
- Lysine-specific demethylase 7 homolog
- Lysine-specific histone demethylase 1
- Glucosamine 6-phosphate N-acetyltransferase
- Histone-lysine N-methyltransferase set-2
- Histone-lysine N-methyltransferase set-26
- MYND-type domain-containing protein
- Lysine-specific histone demethylase
- Lysine-specific demethylase jmjd-3.1
Sequence:
MASAATTTHFPSSRIPSEPCASSGPLFPDDVLFTTEASSASSSSCHVENDSRPLSPTMFTDGRTPVNISAKHLKDHPLHEPTGTSEVLTFYPTMREFKNFSQYIKKIEQNGGHLKAGIAKIVAPEGWTPRPTRKDFSDVDDYEITQPARETIEATEKPGAYFKRNVTCRRKMPVREFRTLANSAQYRNPRPDLKGSEIEKHYFDNILHGEPIYGADTEGSFYDAQVEEWNMNRLGTILEDTNYEIKGVNTVYLYFGMYKTTFPWHAEDMDLYSINFLHFGAPKYWFAISSEHADRFERFMSQQFSYQNEYAPQCKAFLRHKTYLVTPELLRQAGIPYATMVQRPNEFIITFPRGYHMGFNLGYNLAESTNFASQRWIDYGKDAVLCDCNKDSVKIDMTHFMAKYRPDEYTTWWTYWYGGGRELWIPKKKKEVPKKRRQSLADASKIAKRARLGASSTATDSDGSSGSSGSEEATEGSSFMRALPAGYTVHNWQLRPDYDELLRKYKKETKLLRSDTRIDFYQEREFNHARRAEWPHCAVCQYFQPPHMNAINHTVPNSSRRLIPKWCFSKTDTKKHEDHHEPPPPLDRLLTCSNCHVTVHSHCCSGGGGGGGDDDDVTSSGEPWRCPRCRNRTDVEIRTTSCQLCELRGGALIPCQIGTDSTWAHVACALFNRRAIFDCPNRPGACFVEPSPRQQSETPRMPPRRLSEEYRAELGDLYENSRWECVVCHRTDEGLAPCVLCIEEQATTSLPTLAHVTCARRVGFVCEVRDYPRGVVMICHKHEHSYLVNKTTQQQAYTNVKVGDFVFVEDVVEPPQKLFTRGAIVRADKKETVVVDFLDNSCSRDNHVEDIISCECLFCENGDHQYGARVKVVWDDKQVYDAYFRGKGQMIEYTVRLEDGREVRHPRNRLKTKRELNAYLKK
Protein: Integrin beta-8 (Q0VBD0)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin (By similarity). It recognizes the sequence R-G-D in its ligands (By similarity). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation on the surface of activated regulatory T-cells (Tregs). Required during vasculogenesis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P26012}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Integrin alpha-V
- Vitronectin
- Proto-oncogene tyrosine-protein kinase Src
- Integrin alpha-6
- Transforming growth factor beta-1 proprotein
- Integrin alpha-7
- Integrin beta-1
- Focal adhesion kinase 1
- Fibronectin
- Integrin alpha-5
Sequence:
MCGSALAFLTAALLSLHNCQRGPALVLGAAWVFSLVLGLGQSEHNRCGSANVVSCARCLQLGPECGWCVQEDFVSGGSGSERCDTVSSLISKGCPVDSIEYLSVHVVTSSENEINTQVTPGEVSVQLHPGAEANFMLKVRPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSKKMALYSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGAIAGEIESKAANLNNLVVEAYKKIISEVKVQLENQVHGVHFNITAICPDGARKPGISGCGNVTSNDEVLFNVTVVMKTCDIMGGKNYAIIKPIGFNETTKVHIHRSCSCQCENHRGLKGQCAEAAPDPKCPQCDDSRCHFDEDQFPSETCKPQEDQPVCSGRGVCICGKCLCHKTKLGRVYGQYCEKDDFSCPYLHGDVCAGHGECEGGRCQCFSGWEGDRCQCPSASAQHCVNSKGQVCSGRGTCVCGRCECTDPRSIGRLCEHCPTCHLSCSENWNCLQCLHPHNLSQAALDQCKSSCAVMEQHRMDQTSECLSGPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNNNKIKSSSDYRMSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAQEAFRCNF
Protein: Ly6/PLAUR domain-containing protein 8 (Q6UX82)
Organism: Homo sapiens (Human)
Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabilis, thereby inhibiting bacterial motility in the intestinal lumen. Segregation of intestinal bacteria and epithelial cells in the colon is required to preserve intestinal homeostasis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9D7S0}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D7S0}. Secreted {ECO:0000250|UniProtKB:Q9D7S0}. Note=Secreted into the lumen of the colon following cleavage of the GPI-anchor. {ECO:0000250|UniProtKB:Q9D7S0}.
Interaction partners:
Sequence:
MKGILVAGITAVLVAAVESLSCVQCNSWEKSCVNSIASECPSHANTSCISSSASSSLETPVRLYQNMFCSAENCSEETHITAFTVHVSAEEHFHFVSQCCQGKECSNTSDALDPPLKNVSSNAECPACYESNGTSCHGKPWKCYEEEQCVFLVAELKNDIESKSLVLKGCSNVSNATCQFLSGENKTLGGVIFRKFECANVNSLTPTSAPTTSHNVGSKASLYLLALASLLLRGLLP
Protein: Primosome protein PriC (Primosomal replication protein n'') (P23862)
Organism: Escherichia coli (strain K12)
Function: PriA recognizes a specific hairpin sequence on bacteriophage phi X174 ssDNA. This structure is then recognized and bound by proteins PriB and PriC. Formation of the primosome proceeds with the subsequent actions of DnaB, DnaC, DnaT and primase.
Interaction partners:
- Replication restart protein DnaT
- Replication restart protein PriB
- Replicative DNA helicase DnaB
- Replicative helicase loader DnaC
- DNA primase
- Uncharacterized protein YbaM
- Chromosomal replication initiator protein DnaA
- ATP-dependent DNA helicase RecQ
- DNA polymerase III subunit psi
- Single-stranded DNA-binding protein
Sequence:
MKTALLLEKLEGQLATLRQRCAPVSQFATLSARFDRHLFQTRATTLQACLDEAGDNLAALRHAVEQQQLPQVAWLAEHLAAQLEAIAREASAWSLREWDSAPPKIARWQRKRIQHQDFERRLREMVAERRARLARVTDLVEQQTLHREVEAYEARLARCRHALEKIENRLARLTR
Protein: Retrotransposon-derived protein PEG10 (A0A087WZG9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGPDCPPPPPPPPPNNNNNNNSKHTGHKSACVPNMTERRRDELSEEINNLREKVMKQSEENNNLQSQVQKLTEENTTLREQVEPTPEDEDDDIELRGAAAAAAPPPPIEEECPEDLPEKFDGNPDMLAPFMAQCQIFMEKSTRDFSVDRVRVCFVTSMMTGRAARWASAKLERSHYLMHNYPAFMMEMKHVFEDPQRREVAKRKIRRLRQGMGSVIDYSNAFQMIAQDLDWNEPALIDQYHEGLSDHIQEELSHLEVAKSLSALIGQCIHIERRLARAAAARKPRSPPRALVLPHIASHHQVDPTEPVGGARMRLTQEEKERRRKLNLCLYCGTGGHYADNCPAKASKSSPAGNSPAPL
Protein: ACB domain-containing protein (Q9XTZ5)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein EEED8.3
- ACB domain-containing protein
Sequence:
MSVFETAVFIVQNLPKDGPIKTSTDEKLNFYALFKQATHGKCDLPKPSFYDIQGVYKWNAWNKLDNMTMDEAKQAYVDSIVQKIREVQKEYKTEEWMKGDTYELLAPKFEVLGVLEGKDQAVEHPKKTENKETENETDNVETPNSSACILSDNEYADAIDDEIQSRSSSFTEPHNSFNRRISRQSSLKSSCHRLEKELKVITESIDKLGKAVEERHNLLIGLMKKATVYVLVPRVTSWKTIIFFVFWPFVTKFLLRWLRRFLRLLM
Protein: Peroxisomal targeting signal 1 receptor (PTS1 receptor) (PTS1R) (PTS1-BP) (Peroxin-5) (Peroxisomal C-terminal targeting signal import receptor) (Peroxisome receptor 1) (Q920N5)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins. PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16314507, ECO:0000269|PubMed:16428307, ECO:0000269|PubMed:17040904}. Peroxisome matrix {ECO:0000269|PubMed:16314507, ECO:0000269|PubMed:16428307}. Note=Cycles between the cytosol and the peroxisome matrix (By similarity). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (By similarity). Cys-11 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle (By similarity). {ECO:0000250|UniProtKB:A0A1L8FDW4, ECO:0000250|UniProtKB:P50542}.
Interaction partners:
Sequence:
MAMRELVEGECGGANPLMKLATHFTQDKALRQEGLRPGPWPPGASAAETVSKPLGVGSEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVAQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGSSTTDRWYDDYHPEEDLQHTASDFVSKVDDPKLANSEFLKFVRQIGEGQVSLESAAGSGRAQAEQWAAEFIQQQGTSEAWVDQFTRSGNTSALDVEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSASYDKGYQFEEENPLRDHPQAFEEGLRRLEEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRYSPAYAHLVTPGEEGASGAGLGPSKRVLGSLLSDSLFLEVKELFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLLWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYGAADARDLSALLAMFGLPQ
Protein: Melanoma-associated antigen D1 (MAGE tumor antigen CCF) (MAGE-D1 antigen) (Neurotrophin receptor-interacting MAGE homolog) (Q9Y5V3)
Organism: Homo sapiens (Human)
Function: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA co-regulator, modulating the expression of core clock genes such as BMAL1 and NFIL3, induced, or NR1D1, repressed.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase Praja-1
- UBX domain-containing protein 1
- FAS-associated factor 2
- Tumor necrosis factor receptor superfamily member 16
- Netrin receptor UNC5A
- Protein AATF
- E3 ubiquitin-protein ligase XIAP
- Homeobox protein DLX-5
- Neuronal PAS domain-containing protein 4
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
Sequence:
MAQKMDCGAGLLGFQAEASVEDSALLMQTLMEAIQISEAPPTNQATAAASPQSSQPPTANEMADIQVSAAAARPKSAFKVQNATTKGPNGVYDFSQAHNAKDVPNTQPKAAFKSQNATPKGPNAAYDFSQAATTGELAANKSEMAFKAQNATTKVGPNATYNFSQSLNANDLANSRPKTPFKAWNDTTKAPTADTQTQNVNQAKMATSQADIETDPGISEPDGATAQTSADGSQAQNLESRTIIRGKRTRKINNLNVEENSSGDQRRAPLAAGTWRSAPVPVTTQNPPGAPPNVLWQTPLAWQNPSGWQNQTARQTPPARQSPPARQTPPAWQNPVAWQNPVIWPNPVIWQNPVIWPNPIVWPGPVVWPNPLAWQNPPGWQTPPGWQTPPGWQGPPDWQGPPDWPLPPDWPLPPDWPLPTDWPLPPDWIPADWPIPPDWQNLRPSPNLRPSPNSRASQNPGAAQPRDVALLQERANKLVKYLMLKDYTKVPIKRSEMLRDIIREYTDVYPEIIERACFVLEKKFGIQLKEIDKEEHLYILISTPESLAGILGTTKDTPKLGLLLVILGVIFMNGNRASEAVLWEALRKMGLRPGVRHPLLGDLRKLLTYEFVKQKYLDYRRVPNSNPPEYEFLWGLRSYHETSKMKVLRFIAEVQKRDPRDWTAQFMEAADEALDALDAAAAEAEARAEARTRMGIGDEAVSGPWSWDDIEFELLTWDEEGDFGDPWSRIPFTFWARYHQNARSRFPQTFAGPIIGPGGTASANFAANFGAIGFFWVE
Protein: RAB11-binding protein RELCH (LisH domain and HEAT repeat-containing protein KIAA1468) (RAB11-binding protein containing LisH, coiled-coil, and HEAT repeats) (Q148V7)
Organism: Mus musculus (Mouse)
Function: Regulates intracellular cholesterol distribution from recycling endosomes to the trans-Golgi network through interactions with RAB11 and OSBP. Functions in membrane tethering and promotes OSBP-mediated cholesterol transfer between RAB11-bound recycling endosomes and OSBP-bound Golgi-like membranes.
Subcellular location: Recycling endosome {ECO:0000269|PubMed:29514919}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9P260}. Note=Colocalization with RAB11A in recycling endosomes (PubMed:29514919). Translocated to the trans-Golgi network area in an OSBP-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9P260, ECO:0000269|PubMed:29514919}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MAAMAPGGGGSGSGVNPFLSDSDEDDDEVAATEDRRAGLRLGAGVGLDPGSAGSLSPQDPMALGSSARPGLAVEMSAAPAALGGSGETPARLSIDAIAAQLLRDQYLLTALELHTELLESGRELPRLRDYFSNPGNFERQSGTPPGMGAPGIPGASIVGGAGGREPSTTSGGGQLNRAGSISTLDSLDFARYSDDGNRETDERVAVLEFELRKAKETIQALRANLTKAAEHEVPLQERKNYKSSPEIQEPIKPLEKRALNFLVNEFLLKNNYKLTSITFSDENDDQDFELWDDVGLNIPKPPDLLQLYRDFGNHQVTGKDLVDVASGVDEDELEALTPILGNVPPTLDTPLPIENTLLVQKLEDKISLLNNEKWSLMEQIRRLESEMDILKAEHFATPAVGDSVQPSLVWSSQKDSEDNRQSPAVNSSDQEKTKDVHLEIPDAADSFIPKENSSGSFPRKEREELPPSSVSNKTTLHFDQPNRKLSPAFHQALLSFCRMSADSRLGSEVSRIADSEKSVMLMLGRCLPHIVPNVLLAKREELIPLILCTACLHPEPKERDQLLHILFNLIKRPDDEQRQMILTGCVAFARHVGPTRVEAELLPQCWEQINHKYPERRLLVAESCGALAPYLPKEIRSSLVLSMLQQMLMEDKADLVREAVIKSLGIIMGYIDDPDKYQQGFELLLSALGDPSERVVSATHQVFLPAYAAWTTELGNLQSHLIPTLLNKIEKLLREGEHGLDEHKLHMYLSALQSLIPSLFALVLQNAPFSSKAKLHGEVPHIEVTRFPRPMSPLQDVSTIIGSREQLAVLLQLYDYQLEHEGTTGWESLLWVVNQLLPQLIEIVGKINVTSTACVHEFSRFFWRLCRTFGKIFTNTKVKPQFQEILRLSEENIDSSAGNGVLTKATVPIYATGVLTCYIQEEDRKLLVGFLEDVMTLLSLSHAPLDSLKASFVELGANPAYHELLLTVLWYGVVHTSALVRCTAARMFELLVKGVNETLVAQRVVPALITLSSDPEISVRIATIPAFGTIMETVIQRELLERVKMQLASFLEDPQYQDQHSLHTEVIRTFGRVGPNAEPRFRDEFVIPHLHKLALVNNLQIVDSKKLDIATHLFEAYSALSCCFISEDLMVNHFLPGLRCLRTDMEHLSPEHEVILSSMIKECEQKVENKTVQEPPGSMSIAASLVSEDTKTKFLNKMGQLTTSGAMLANVFQRKK