wanglab/gogpt-training-data huggingface dataset:
Protein: Mediator of RNA polymerase II transcription subunit 8 (Mediator complex subunit 8) (P38304)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. MED8 binds to the consensus sequence 5'-[AC][AG]GAAAT-3' in both the UAS of SUC2 and the DRS2 of HXK2.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 11
Sequence:
MSQSTASLVPEGNQGSLQEDVSFDFNGVPGQALDAVRMRLAQLTHSLRRIRDEMSKAELPQWYTLQSQLNVTLSQLVSVTSTLQHFQETLDSTVVYPLPKFPTTSHESLVTTLLRKKNIPEVDEWMKYVRETSGVTTALLKDEEIEKLLQQDREITNWARTTFRNEYGKHDFKNEESLSEEHASLLVRDSKPSKPFNVDDVLKFTFTGEKPIITGSTSTSSSN
Protein: Protein phosphatase 1 regulatory subunit (Q9VUF3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glycogen [starch] synthase
- Serine/threonine-protein phosphatase alpha-1 isoform
- Serine/threonine-protein phosphatase alpha-2 isoform
- Serine/threonine-protein phosphatase alpha-3 isoform
- glycogenin glucosyltransferase
- Glycogen-binding subunit 76A
Sequence:
MISHSPPIFSHSPPVSFLADFMSGHPRQSLNYNDEPNRASRYCRPQVITLASKAMVNNASAAVQGQGPSQQKAGATPLGVGSRSGRSYLERMASAPLLTNQPKSCLSRKSCLHKSQNTTASSADLSPTDTDVADSASHSCICSKDSDSNGEVSRGPKKHVIFADDEGLSLTEVRVMSEPSNVPPYWSMKFLEQITQGLVSPHPPDQWTVDFKQPASDYLSFRQKIERDFVSLENVIVKDEESIVVGTIKVKNIDFQKEIIVRVTWDDWKSQQDIFCTYARAYGPATCAHVVFDTFSFKITLPPSSKRLEFCICYRTNETEYWDNNDGKNYTISKRSPFYYNALSPYDKGQNRNSSQQIRSTLTDALAKVQDQNGWHQEPHTPYW
Protein: Angiotensin-converting enzyme (EC 3.4.-.-) (G1PXH7)
Organism: Myotis lucifugus (Little brown bat)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|PROSITE-ProRule:PRU01354}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|PROSITE-ProRule:PRU01354}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Angiotensinogen
- Dipeptidyl peptidase 4
- Transporter
- Neprilysin
- Lysosomal Pro-X carboxypeptidase
- Meprin A subunit
- Interleukin-2
- Meprin A subunit
- Transporter
- Transporter
Sequence:
MSGSSWLFLSLVAVAAAQSSTEEKAKIFLENFNSKAEDLSHESALASWNYNTNITDENVQKMNEADSKWSAFYEQQSKLAQTYPLQEIQNSTIKRQLQVLQQNGSSVLSADKSKRLNTILTTMSTIYSTGKVCNPNNPQECFTLAVTGLEEIMEKSKDYNQRLWVWEGWRSEVGKQLRPLYEEYVDLKNEMARGNNYEDYGDYWRGDYETEGEDGYNYSRNQLTEDVERIFLEIKPLYEHLHAYVRAKLVNAYPSRISPTGYLPAHLLGDMWGRFWTNLYNLTVPFEQKPNIDVTGAMVEQSWDAEKIFKEAEKFYISVGLPSMTPGFWNNSMLTEPGDGRKVVCHPTAWDLGKGDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYATQPYLLRNGANEGFHEAVGEVMSLSVATPKHLKGMGLLPPDFSEDNETEINFLLKQALNIVGTLPFTYMLEKWRWMVFKGEIPKEQWMKKWWEMKRDIVGVMEPLPHDETYCDPASLFHVANDYSFIRYFTRTIFEFQFQEALCQIAKHQGPLHKCDISNSKEAGNKLLEMLKLGKSEPWTLALDKIVGTKKMDAKPLLNYFEPLFTWLKEQNGNSVGWNSDWSPYAEQSIKVRISLQSALGEKAYKWNDNEMYLFQSSVAYAMREYFLKEKNQTIPFGVENVRVNDIKPRVSFKFYVTSPKNMSVVIPRSEVEDAIRDRMSRSRINDAFRLDDNTLEFLGIQPTLGPPNQPPVTIWLIVFGVVMGVAVIGIAVLIFTGIRDRKKKKQAGNEENPYSSVNLSKGENNPGFQNGDDVQTSF
Protein: Polyribonucleotide 5'-hydroxyl-kinase Clp1 (EC 2.7.1.78) (Polyadenylation factor Clp1) (Polynucleotide kinase Clp1) (Pre-mRNA cleavage complex II protein Clp1) (E7F3I6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Polynucleotide kinase that can phosphorylate the 5'-hydroxyl groups of double-stranded RNA (dsRNA), single-stranded RNA (ssRNA), double stranded DNA (dsDNA) and double-stranded DNA:RNA hybrids. dsRNA is phosphorylated more efficiently than dsDNA, and the RNA component of a DNA:RNA hybrid is phosphorylated more efficiently than the DNA component. Plays a role in both tRNA splicing and mRNA 3'-end formation. Component of the tRNA splicing endonuclease complex: phosphorylates the 5'-terminus of the tRNA 3'-exon during tRNA splicing; this phosphorylation event is a prerequisite for the subsequent ligation of the two exon halves and the production of a mature tRNA. Its role in tRNA splicing and maturation is required for cerebellar development. Component of the pre-mRNA cleavage complex II (CF-II), which seems to be required for mRNA 3'-end formation. Also phosphorylates the 5'-terminus of exogenously introduced short interfering RNAs (siRNAs), which is a necessary prerequisite for their incorporation into the RNA-induced silencing complex (RISC). However, endogenous siRNAs and microRNAs (miRNAs) that are produced by the cleavage of dsRNA precursors by dicer1 already contain a 5'-phosphate group, so this protein may be dispensible for normal RNA-mediated gene silencing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- PCF11 cleavage and polyadenylation factor subunit.
- Cleavage stimulation factor, 3' pre-RNA, subunit 2.
- Cleavage stimulation factor subunit 3
- Cleavage and polyadenylation-specific factor 3.
- General transcription factor 3C polypeptide 3
- Cleavage and polyadenylation-specific factor 4.
- Pre-mRNA 3'-end-processing factor FIP1
- Cleavage and polyadenylation specificity factor subunit 2
- TSEN54 tRNA-splicing endonuclease subunit.
- Cleavage and polyadenylation specificity factor subunit 1
Sequence:
MTAEAAEKSVEEGLSSSGSAGSSGTRFDLDKETELRFEVEAGERVQLELLSGLAEIFGSELNRNKKYTFGPGSKIAVFTWQGCGVALSGKTEVAYVSKDTPMLLYLNTHAALEQMRRQAEKDNERGPRVMVVGPTDVGKSTVCRMLLNYAVRLGRRPTLVELDVGQSSVSVPGTMSALCIERPADVEEGFSVQAPLVFHFGSTTPGTNIKLYNKLTSSLADAFSQRCEVNRRASVGGCIINTCGWVKGSGYQALVHCASAFQVDVVLVLDQERLYNELKRDLPHFVRVVLLPKSGGVVERSKDCRRETRDEKIREYFYGFRGTSFYPHAFDVRFSDVRIYKIGAPSIPDSCLPLGMSQDDTQLKLVPVSPGRDLTHHVLSVSSVDDEAEVGQSRGILESPACGFIVVTAVDTQAQVMTVLSPAPRPLPRHTLLIMDIRFIDLK
Protein: Uncharacterized protein (C0H4H1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNILKLYINISVLLFFIISKYNPHNDHNNKSINSYNKINSSSTYTHSRILKQLEFITLEEKTVNALQEMLDSVEEDPSEKKCNRLLAKLKIRNEYHKHRKPHNYYARKNKKKEQKRQHLKKNKGKLNRLQQLEEKLFTHADLLRSAIFERTSRVPDGIFYT
Protein: Serine/threonine-protein kinase TOR (EC 2.7.11.1) (Q57UT3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Rapamycin-insensitive companion of TOR2
- Uncharacterized protein
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase TOR
- Protein artemis
- Ras-family member, GTP-binding protein, putative
- Small GTPase, putative
- Raptor N-terminal CASPase-like domain-containing protein
- Raptor N-terminal CASPase-like domain-containing protein
- Nuclear cap-binding protein subunit 2
Sequence:
MSLGYDARKVEALIRTIAVSSKCDVIYAAEVVKQAKDNQRKNQQEYENLVSCLLFCLENFDVVEGGTAEVKCALVTLATLLQLDLTANQVSQCNSYLSICLTHVQDVSVAFVASRAFGETLVTSMTSDFVQEQVEGAFLAIDLKENITHAQRVCALLMLQEVVTKIPMRILDMLDSLFEKLWGMLASSDAMIREISHLLFMDCGKLLCSRSPVNRKKTVDSLLHQLKFNLAAKSRESNMAGLLAFETVVMTSVGTASQPRYEDMSIMLVPYVMTGGSTNIAELRELLFRCLIVLCRYSTTLFITNQLKDTVGFALKSIENGYQVAASFNMLSEIIVLVTDVAFRPFVNETCNAVRYVSGKSSKPCWEAVRCFSVICHVCPPVDVESYIEPCIENIFRWGLSLPLIESMPHIIASSSAKYRSRLEEGLLDMISVTLCGLPFRQQPGSKGTITMKVESEPTESQITVALDALVQFGFSDSELMGDFLRDSVLPLIDSESVSVRTAAVRTICTLLIPPGVKGELTMARRICVDVILSRMLVVGLSNPDPVVRKGILSSFTEPFYPFLKEVQFVTSIYAALGDEDISCRVAATVLLCRMTFHDPSHILPIFRKQIVQILHTVSTSDNTGAVQSGLQLLDAAASNAPQFVMNFADGIIKALGHHFSTVNIHSSILQHLLRCCTSVAHAAHFFGNTDAIFRVEVDRAYMLLKALPLDSESVELRLWCLRFLSATLGPQIEGRSPYEVYPHLYQQLSGIVKNNDEDLDVRLEALRCAGVIGALDISIFHSTVVNRTCRHEEMKRNEPSTLSHAMCCRVVIRSIASLLDLSEKRFSGGKDNVLRVGIQTILNIAESCPDSRGEIAVVIPPVVRAVSELSACRLLGTLLHELTQIIRYVGVAALSHAHLLYNLIDESWVKSSKYRFLAVRLALTLVTLEADGKAESRRSNMRMSPIKFDALNDIESSESLRYAIIEYILKHTQTLKTCVETVVTNLLRAAQRCPIDFALSVITTLRVVCFRLHVDEFAGLIVRGLLSCLKTRLSTSMRATEQNAFVSRIMGVFCVLMTVLQSEFVKYSSEVLRTLKTLRVSNNELITLHGTLMKGGVCTLSKGFVTEHQKQVVRLLKECEGIALRHVSDLDKVLSTRGNVDEKGWNSDDGERPLPFSEKLIISTTRTAPLTKEEWLRWLNDFSCVIMQESPYRVFRCISLPLTANTSPLVDCSPQFTQDIAPHAFRALWNFASASVRSSLADFFFQVLQQAMESSAVPDEVVSALLTVAEYMDNVGMALPIAPSILSRCAWGRGMLAKALYWCEAAYRKDPRGTAKYLFSLYRELQQSGLLMVTGHSESLKLLQGCIDNERSESDGSDEYSVKWLSRQESLRRMCGVGGRSRSDANSSFNGEDVKLDPEMENEVNTLYALSEAGDYDAVLEQWKVLFQKYNGRDEQKREENTLFYVSQCAADASIRLQAWDTLEDTTRWQLNDTVSYHVSRAALSIHKRRYEEATSAINEGRKLLLEDLSGLLHQSYTRAYEGLVIAQKLSELEEIVTVKRAEVVSSTHHLSRVLRLWSQRIEMMSSTVSAWKEVLGVRGLLIPPGEDVATRLRFVNLCRREKAKQHERFILCQLLGYRCPTSEQLMHSNANPRVVMQYISFLSANGELGPKSSYGLERDLLKRMIDTHSRNENAFLLSSAYARLGSSAELSEAVQCYKAATTYCPKWFHAWRMFAESNAEMLDVTFSDATCAAAIEGYIQSIKLGNSDSTIIQDVLKLLTLLSRHCDQESGLKELRKRVFEVSPRAWKLVVPQLIARLDSGSDGSCELVAEILTTVSFDCPLSLIYPLNLCAMSNSRRRRKYANIILDKLQSKHPLVVNQGRILVDELVRTSDLLHEQWYHMLECSATAFFDRNDYKGMLDVLLPLHEKLHLSTDTIVEAEFTCKFGNKLDRAQEWLQSYLRTGSIADLHSAWNIYHAVYQQIDKQIRSQSKLHLSFCSPKLFEARNLAVGLPDAMPSEDCAVRCTASFNGTLTVIGSKQRPKRLSVTTVDGETQKYLLKGREDLRLDERVMQLFRLVNTLMMTDSRTCKNPGFQIQRYSVTPLKDTVGLIGWVSGCDTLHTLVTKYRKFRGIPPELELRMMNQIIVCDRPKTYDHLTMISKVEVMEFLADHTSGHDVRKAMWASASNCEMWLEQRQVFTTSSATTCMVGYILGLGDRHPNNVMIQRTSGLFVHIDFGDCFEVAMTRQMFPERVPFRLTRMIRNALDVFGVDGPFRSIAETAMCVLRDGSRSVLAILEAFIQDPLISWRLLNHMKKEPGDSTVHKNIDEQSEAVGPRMSSVAFPGAPVRDDMFTVDSKLTRCASIPDDDVVHKGVKVFQRVRSKLKGEEFLRTKGDTKSTDPKVQVARLIVEATDITNVAQSWAGWYPFW
Protein: Prion-like-(Q/N-rich)-domain-bearing protein (Q21648)
Organism: Caenorhabditis elegans
Interaction partners:
- RING-type domain-containing protein
Sequence:
MGCCQSKKARNNQRNNQRSDQMNRQHTQPSPNASTEQMAYPRQQPQGIPQGPPPAYAPPAAPKAPEKVVEPKNRRVTIAEPPERVAEPSPTPEDPELFTCIDQTEKEVEKEVEKRKSAPRAPVPAPTPAPQAAPQATPAAPAQAYPQQQQAAPVVYGSQPMVMGAAPVAPVVMAPPPVIMSPYPYYGGGVMFDPYYNGFYGGYGYGGFDFGYGGYGGYGCGFY
Protein: Glutathione S-transferase U24 (AtGSTU24) (EC 2.5.1.18) (GST class-tau member 24) (Q9SHH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase Z1
- Glutathione S-transferase F2
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione reductase, chloroplastic
- Glutathione S-transferase F7
- Glutathione S-transferase F8, chloroplastic
- Glutathione synthetase, chloroplastic
Sequence:
MADEVILLDFWASMFGMRTRIALAEKRVKYDHREEDLWNKSSLLLEMNPVHKKIPVLIHNGKPVCESLIQIEYIDETWPDNNPLLPSDPYKRAHAKFWADFIDKKVNVTARRIWAVKGEEQEAAKELIEILKTLESELGDKKYFGDETFGYVDIALIGFHSWFAVYEKFGNVSIESECSKLVAWAKRCLERESVAKALPESEKVITFISERRKKLGLE
Protein: Raw, isoform D (X2J5A2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMQLSMIFLLLLMTMSVFSCQNTEDTEGADEAAAQISEVLNAWRAKARCNVVPDERTQELFHELSFHPSQKQISEMLQTAKKVARKGGSGQANGLTFGQFCVLAADLKRFRASTISNQPSYCDYQSLSAGLLLPELDDPASSSNQNLQSPAATNSSPAHSSKKPDNHGTELRSTKSFSSVDDTKKKKNATNEPVEVFLGGSCNPTTWRADVAIPALKELGISFYNPQVSDWTPDLIELEHRAKEKARVLFFVMDSETRASAGAIEAAHIAGQNCKQLVLVLHPYKPNQKILNEPISQQEYLDLNRNQLILKELVSRRGLPVLDNIPLGLQRTKDILGGIRDPPSKISSILDTVRGAFDRVNPLNDLLTVEQCKRALLFLGYAQSLVNLDNLNKIIINQRESLKLLQTHSPRAVADDADADGGNCSQPILPSQELIDFDLFCVISAYLSVLQQEIHESGCISPIKGTNVPPPQVYFTNAPDVDIYYSASKNISRTSSNASVPSNSSSGIGHDLERQSLFEQLSRSRDSGTSSPQPTGSSSLGKSPRPQILLNVESIETTEIITTKTIETKPNPVTASTVVHAEEEESDSNDSVLSSNSSIASAGDILCCGGGLDLRDVYLGGSCVLRTKWRQELAVPYLQSKGVSFHTPALHESIQQMILNQEQNQDQSQQPTVPPQEQQQQQRSFVRTRRKCRGNQLQLEEQEELTVAEESLSWSLPPVAVRQSLFNPSLLDSSRVLLFVITNETRSLAPMTLAAHCIGLMYNVVLAVQMLPEDCVLGDEKLTVAAIKDYNRGRSYLIDLAKRQGVPVFSDIRAALECTVAKVKAYNNRDRC
Protein: E3 ubiquitin-protein ligase FANCL (EC 2.3.2.27) (Fanconi anemia group L protein homolog) (Proliferation of germ cells protein) (RING-type E3 ubiquitin transferase FANCL) (Q9CR14)
Organism: Mus musculus (Mouse)
Function: Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21229326}. Nucleus {ECO:0000269|PubMed:21229326}. Note=In the nucleus, colocalizes with UBE2W.
Interaction partners:
- Fanconi anemia group B protein homolog
- Fanconi anemia core complex-associated protein 100
- Fanconi anemia group C protein homolog
- Fanconi anemia group A protein homolog
- Fanconi anemia group M protein homolog
- Fanconi anemia group F protein
- Fanconi anemia group D2 protein homolog
- Fanconi anemia, complementation group E
- Ubiquitin-conjugating enzyme E2 T
- Fanconi anemia core complex-associated protein 24
Sequence:
MDEAEASLLRHFPLLLPQNREKTVYEGFISAQGSDFHLRIVLPKDLQLKKARLLCSLQLKNILNEYHQVVQQRMKHSPDLMSFMMELKMILEVALKNKQELCVQPPSCSFCKDLLTEIGAIGWDKLACVESSFSTIKLKADDASGRKHLITVKLKAKYPVEPPDCVVDFPVPFSVSWTPQSSLVDVYSQFLVALETLKVFWDVMDEIDEKTWVLEPEKPPRSATARRIALGKNVSIAIEVDPRHPTMLPEFCFLGADHVTKPLGMKLSGSIHLWDPENSLLQNLKDVLEIDFPARSILEESDFSMDCGICYARHLNGAIPDQVCNNPQCGQPFHEICLYEWLRGLSTSRQSFNVFFGDCPYCSKPITLKMSGRKP
Protein: Gig2-like protein DreI (Grass carp reovirus (GCRV)-induced gene 2i) (E7F7D7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Furry homolog b
Sequence:
MWAEDDLGPGAPPCLESYSAPVEGKVYIMYHGTSEVAAEQIAEEGFIQSSKGMLGRGVYLSRDLEKASRYPLNLPEDQRVIVRVMVDVGKVKKIDYQGHPMQKTWHDHGYDTAWCPPDCGMVPSGLEEDCVWDPERITVIDLIHPEQNEEEENGCRLF
Protein: 5'(3')-deoxyribonucleotidase, cytosolic type (EC 3.1.3.-) (Cytosolic 5',3'-pyrimidine nucleotidase) (Deoxy-5'-nucleotidase 1) (dNT-1) (Q8TCD5)
Organism: Homo sapiens (Human)
Function: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytosolic 5'-nucleotidase 3A
- Cytosolic 5'-nucleotidase 1A
- Purine nucleoside phosphorylase
- Thymidine phosphorylase
- Cytosolic purine 5'-nucleotidase
- Cytosolic 5'-nucleotidase 1B
- NAD-capped RNA hydrolase NUDT12
- Deoxycytidine kinase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- Adenosine deaminase
Sequence:
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRLLSWSDNWREILDSKRGAAQRE
Protein: Asp/Glu-specific dipeptidyl-peptidase (EC 3.4.14.-) (Dipeptidyl-peptidase 11) (DPP11) (F8WQK8)
Organism: Porphyromonas endodontalis (strain ATCC 35406 / DSM 24491 / JCM 8526 / CCUG 16442 / BCRC 14492 / NCTC 13058 / HG 370) (Bacteroides endodontalis)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Shows a strict specificity for acidic residues (Asp or Glu) in the P1 position, and has a hydrophobic residue preference at the P2 position. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
Subcellular location: Secreted {ECO:0000269|PubMed:21896480}. Cell surface {ECO:0000269|PubMed:21896480}. Note=Is observed in both cell-associated and soluble extracellular forms. {ECO:0000269|PubMed:21896480}.
Interaction partners:
- Adenylate cyclase
- Smr domain-containing protein
- Peptidase, S9A/B/C family, catalytic domain protein
Sequence:
MNKRFFPTLLLAFVCSTLAYADGGMWLMQQINGQVARMKSLGMQLEAADIYNPNGSSLKDAVVMFDGGCTGVLVSNQGLLLTNHHCGYDQIQKHSSVQHNYLKDGFWSYSLAEELVNPGLEVEIVDEITDVTAAVKKELERIKKPSGLEFLSPRYLSSLAPEIVGKKAASRPGYRYEIKAFYGGNRYYMFTKKVFRDVRLVAAPPSSIGKFGSDTDNWAWPRHTGDFSIFRLYADKNGNPAEYSKDNVPYRPKRWVKVNAQGVKEGDFALIMGYPGTTYKFFTADEVTEWSEIDNNIRIEMRGILQDVMLREMLADPKINIMYAAKYASSQNGYKRAQGANWAIRRRSLREIKLAQQQEVLAWAKQKGIATTEEAVRAISKAIEGRQDLRMRQRYLLEGILMGIEMSNAPAADSDIADHWDDPARREAGLQSIRKQFEAFFNKDYSPEVEKDQLAIALLTRYAERIPAEKQPISIREGIAEYGSAKAYVEMIFDKSIYASRERFEEFMKNPDRDRLLRDPMSRFAASVAYEHQKLAKEVAAFDAPLAAAQRSYVASVLDMKGQPNLAPDANLTLRFTYGEIKGYQPRDVVTYGAKSTLEGVMEKEDPNNWEYVVDPKLKALYEAKNYGRYANSDGSMPVNFCATTHTTGGNSGSPVMNARGELIGLNFDRNWEGVGGDIEYLPNYQRSIILDIRYLLFIIDKFAGCQRLIDEIQPQF
Protein: DUF7087 domain-containing protein (O61521)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein
- PH domain-containing protein
- Sperm-specific class P protein 34
- Membrane transporter protein
- DNA-binding protein
- Phosphoprotein
- DUF389 domain membrane protein
- PDZ domain-containing protein
- MFS domain-containing protein
- Sperm-Specific family, class S
Sequence:
MDQIPPYEFNKYVLYARGAVIVCASFELLMVLFGSLGDCNFLAKLFYFIFLGGAVAVSSHNIALNIDGREEINKVLTSSDNEVRGKSAALVLVPALAGIFVFLCVSGHAFFSLFVLIHVLAAVGQLGIEAYEFKKGQSGAPAQDPAATAPPAQDPVAAPPAQ
Protein: Lipopolysaccharide kinase (Q9HUF8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Heptose kinase
- Serine/threonine protein kinase
- Lipopolysaccharide core heptose
- UDP-glucose:
- lipopolysaccharide heptosyltransferase II
- Lipopolysaccharide heptosyltransferase 1
- Probable glycosyl transferase
- Probable carbamoyl transferase
- NADH-quinone oxidoreductase subunit C/D
- Uncharacterized protein
Sequence:
MSVFIAAQDHDLLQRNRLDSFDALWALQLDAVDEPNTERGGWSSVYRLDLGDSAYYLKRQSNHLTRSLRHPLGEPTFAREFRNIERYRALGIPALQAAFFAQQAVGGERQAILLTRALDGWQDLDTWLASWHDLAEERRRAILRAVGRLARQLHAAGQMHGCFYPKHVFLREGADGVFEACLIDLEKTRPIWFGRRDQVKDLEPMLRRAPDWSEADVHEFISAYVDEPLDSAEVEQWYRLLDQRRRRKESRR
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q8IR26)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- Uncharacterized protein, isoform B
- Uncharacterized protein, isoform B
- Probable multidrug resistance-associated protein lethal
- RING-type E3 ubiquitin transferase
- FI05221p
Sequence:
MEEPKSVSTAELPSTSTGASSSSSTLSNNVSYDKIAWTRDITEPLAEESSTSQLRPLGTSIPTNSTASELKKSNTSYSFTGDYLSGGNKADLKGGYPFGGTDTDTKANEKDKEKEHTADDSLYECNICLDTAKDAVVSMCGHLFCWPCLHQWLLTRPNRKLCPVCKAAVDKDKVIPLYGRNSTHQEDPRNKVPPRPAGQRTEPDPVPGFPGFGFGDGFHMSFGIGAFPFGFITSRLNFFEPRPPADIRRLHEDEPWALSKLFWHFVVFVIYGLLVPIVHGSSR
Protein: ATP-dependent RNA helicase mak5 (EC 3.6.4.13) (O74393)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Uncharacterized RNA-binding protein C4F6.14
- Probable rRNA-processing protein ebp2
- Ribosome biogenesis protein nsa1
- Probable nucleolar complex protein 14
- ATP-dependent RNA helicase has1
- Uncharacterized AAA domain-containing protein C16E9.10c
- Ribosome biogenesis protein ytm1
- Ribosome biogenesis protein erb1
- 25S rRNA
- ATP-dependent RNA helicase dbp9
Sequence:
MPKKAALDELKWKEVKLPDHLDDFDGFMGLEEIEGVDIKYQPKGAMKEVIYELPEVHEKKDKKPEKRKKDQKEASEKKKKGKRTSPTIEMTSLGSKVTSKNYNEFSTLEEEDEHNSHGVDVSAWAHFSLSPEMLGSLSKAGFSKPMPIQSLVIPEASIGFDIIGKADTGSGKTLAFGIPILEHCLRNVDAKYVQALVVAPTRELAHQICQHFELIKPSPNIRVMSITGGLAVQKQQRLLNKHPHVVVATPGRLWSVINENNLTGNFKKIKCLVLDEADRLLQKSHFEELSKLLEILGNPMHTQRQTFIFSATFDEGLQQRLKKNMKGNITEKYNSPMENMLKEVRFFGKPKFLDANPQSAVASRVLEGLIECAPAEKDLYLYYLIMRYPGKTMVFANGIEDIKRITPFLNELKVPSYPLHAQLDQKKRLQSLEKFKNNPKGVLVCTDVAARGIDIPSVTHVIHYHVPHTADMYVHRSGRTARANEDGVSILMCGPKELSQLKRLCYRLKKKIETFINFPVDMSILDILKTRVVLAHKIVNLTRKDGRVGREEAWLKSMAQELGVESSDDEDPDLPKKSESSKNKKQIAHLRSELAPLLHEKIRTGFSGRYLTSGLVNMAEKLANEEVHDNIIGMDSISALEVLQKRKK
Protein: Protein-arginine deiminase type-4 (EC 3.5.3.15) (HL-60 PAD) (Peptidylarginine deiminase IV) (Protein-arginine deiminase type IV) (Q9UM07)
Organism: Homo sapiens (Human)
Function: Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci. Required for the formation of neutrophil extracellular traps (NETs); NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15629448}. Nucleus {ECO:0000269|PubMed:15629448}. Cytoplasmic granule {ECO:0000269|PubMed:11435484}. Note=Cytoplasmic granules of eosinophils and neutrophils. {ECO:0000269|PubMed:11435484}.
Interaction partners:
- Histone H3.2
- Histone H3.1
- Histone H3-7
- Histone H3.1t
- Histone H3.3
- Histone H3.3C
- Neutrophil elastase
- Tyrosine-protein phosphatase non-receptor type 22
- Cellular tumor antigen p53
- Myeloblastin
Sequence:
MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTMKVASGSTGDQKVQISYYGPKTPPVKALLYLTGVEISLCADITRTGKVKPTRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDMSLMTLSTKTPKDFFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMVPGGKHNMDFYVEALAFPDTDFPGLITLTISLLDTSNLELPEAVVFQDSVVFRVAPWIMTPNTQPPQEVYACSIFENEDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAPHKTLPVVFDSPRNRGLKEFPIKRVMGPDFGYVTRGPQTGGISGLDSFGNLEVSPPVTVRGKEYPLGRILFGDSCYPSNDSRQMHQALQDFLSAQQVQAPVKLYSDWLSVGHVDEFLSFVPAPDRKGFRLLLASPRSCYKLFQEQQNEGHGEALLFEGIKKKKQQKIKNILSNKTLREHNSFVERCIDWNRELLKRELGLAESDIIDIPQLFKLKEFSKAEAFFPNMVNMLVLGKHLGIPKPFGPVINGRCCLEEKVCSLLEPLGLQCTFINDFFTYHIRHGEVHCGTNVRRKPFSFKWWNMVP