wanglab/gogpt-training-data huggingface dataset:
Protein: Plexin-B3 (Q9ULL4)
Organism: Homo sapiens (Human)
Function: Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:16122393}; Single-pass type I membrane protein {ECO:0000269|PubMed:15218527, ECO:0000269|PubMed:16122393}. Note=Colocalizes with RIT2/RIN at the plasma membrane.
Interaction partners:
- Semaphorin-5A
- Semaphorin-4D
- Rho guanine nucleotide exchange factor 12
- Semaphorin-4A
- Hepatocyte growth factor receptor
- Semaphorin-4F
- Semaphorin-4C
- Semaphorin-4G
- Ras-related protein R-Ras
- Semaphorin-4B
Sequence:
MCHAAQETPLLHHFMAPVMARWPPFGLCLLLLLLSPPPLPLTGAHRFSAPNTTLNHLALAPGRGTLYVGAVNRLFQLSPELQLEAVAVTGPVIDSPDCVPFRDPAECPQAQLTDNANQLLLVSSRAQELVACGQVRQGVCETRRLGDVAEVLYQAEDPGDGQFVAANTPGVATVGLVVPLPGRDLLLVARGLAGKLSAGVPPLAIRQLAGSQPFSSEGLGRLVVGDFSDYNNSYVGAFADARSAYFVFRRRGARAQAEYRSYVARVCLGDTNLYSYVEVPLACQGQGLIQAAFLAPGTLLGVFAAGPRGTQAALCAFPMVELGASMEQARRLCYTAGGRGPSGAEEATVEYGVTSRCVTLPLDSPESYPCGDEHTPSPIAGRQPLEVQPLLKLGQPVSAVAALQADGHMIAFLGDTQGQLYKVFLHGSQGQVYHSQQVGPPGSAISPDLLLDSSGSHLYVLTAHQVDRIPVAACPQFPDCASCLQAQDPLCGWCVLQGRCTRKGQCGRAGQLNQWLWSYEEDSHCLHIQSLLPGHHPRQEQGQVTLSVPRLPILDADEYFHCAFGDYDSLAHVEGPHVACVTPPQDQVPLNPPGTDHVTVPLALMFEDVTVAATNFSFYDCSAVQALEAAAPCRACVGSIWRCHWCPQSSHCVYGEHCPEGERTIYSAQEVDIQVRGPGACPQVEGLAGPHLVPVGWESHLALRVRNLQHFRGLPASFHCWLELPGELRGLPATLEETAGDSGLIHCQAHQFYPSMSQRELPVPIYVTQGEAQRLDNTHALYVILYDCAMGHPDCSHCQAANRSLGCLWCADGQPACRYGPLCPPGAVELLCPAPSIDAVEPLTGPPEGGLALTILGSNLGRAFADVQYAVSVASRPCNPEPSLYRTSARIVCVTSPAPNGTTGPVRVAIKSQPPGISSQHFTYQDPVLLSLSPRWGPQAGGTQLTIRGQHLQTGGNTSAFVGGQPCPILEPVCPEAIVCRTRPQAAPGEAAVLVVFGHAQRTLLASPFRYTANPQLVAAEPSASFRGGGRLIRVRGTGLDVVQRPLLSVWLEADAEVQASRAQPQDPQPRRSCGAPAADPQACIQLGGGLLQCSTVCSVNSSSLLLCRSPAVPDRAHPQRVFFTLDNVQVDFASASGGQGFLYQPNPRLAPLSREGPARPYRLKPGHVLDVEGEGLNLGISKEEVRVHIGRGECLVKTLTRTHLYCEPPAHAPQPANGSGLPQFVVQMGNVQLALGPVQYEAEPPLSAFPVEAQAGVGMGAAVLIAAVLLLTLMYRHKSKQALRDYQKVLVQLESLETGVGDQCRKEFTDLMTEMTDLSSDLEGSGIPFLDYRTYAERAFFPGHGGCPLQPKPEGPGEDGHCATVRQGLTQLSNLLNSKLFLLTLIHTLEEQPSFSQRDRCHVASLLSLALHGKLEYLTDIMRTLLGDLAAHYVHRNPKLMLRRTETMVEKLLTNWLSICLYAFLREVAGEPLYMLFRAIQYQVDKGPVDAVTGKAKRTLNDSRLLREDVEFQPLTLMVLVGPGAGGAAGSSEMQRVPARVLDTDTITQVKEKVLDQVYKGTPFSQRPSVHALDLEWRSGLAGHLTLSDEDLTSVTQNHWKRLNTLQHYKVPDGATVGLVPQLHRGSTISQSLAQRCPLGENIPTLEDGEEGGVCLWHLVKATEEPEGAKVRCSSLREREPARAKAIPEIYLTRLLSMKGTLQKFVDDTFQAILSVNRPIPIAVKYLFDLLDELAEKHGIEDPGTLHIWKTNSLLLRFWVNALKNPQLIFDVRVSDNVDAILAVIAQTFIDSCTTSEHKVGRDSPVNKLLYAREIPRYKQMVERYYADIRQSSPASYQEMNSALAELSGNYTSAPHCLEALQELYNHIHRYYDQIISALEEDPVGQKLQLACRLQQVAALVENKVTDL
Protein: E3 ubiquitin-protein ligase At1g12760 (EC 2.3.2.27) (RING finger protein At1g12760) (RING-type E3 ubiquitin transferase At1g12760) (Q9LN71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates E2-dependent protein ubiquitination in vitro.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nucleic acid-binding, OB-fold-like protein
- Protein PARTING DANCERS
- Pentatricopeptide repeat-containing protein At1g12775
- Ubiquitin-conjugating enzyme E2 36
- Tetratricopeptide repeat
- Uncharacterized protein At1g63310
- Pentatricopeptide repeat
- F3F19.7
- At1g63230
- Ubiquitin-conjugating enzyme E2 35
Sequence:
MSTETTTGNSSLIPASSSSSSSDAIDPAPLLFNGDDNEGNNGGGGGERRSVRRQGLREAARFLSRASSGRVMREPSMLVREAAAEQLEERQSDWAYSKPVVVLDIVWNLAFVSVATAILVMSRKEHPIMPLRVWLLGYALQCVLHMVCVCVEYRRRNRRRTNRTTTTTPPRSRSSSSSSSSSSLEEEALGSRRNSGVQDLSLGHLDTESSSVAKHLESANTMFSFIWWIIGFYWVSAGGQELAQESPRIYWLSIVFLGFDVFFVVFCVALACVIGIAVCCCLPCIIAVLYAVADQEGASKEDIEQLTKFKFRKLGDANKHTNDEAQGTTEGIMTECGTDSPIEHTLLQEDAECCICLSAYEDGTELRELPCGHHFHCSCVDKWLYINATCPLCKYNILKSSNLDREEV
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (Q6FHX6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000256|HAMAP-Rule:MF_03140}.
Interaction partners:
Sequence:
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK
Protein: Bacteriocin glycocin F (GccF) (E9K9Z1)
Organism: Lactiplantibacillus plantarum (Lactobacillus plantarum)
Function: Has antibacterial activity against L.plantarum ATCC 8014. In purified form, the activity is bacteriostatic (IC(50)=2 nM) rather than bactericidal.
Subcellular location: Secreted {ECO:0000269|PubMed:21251913}.
Interaction partners:
Sequence:
MSKLVKTLTISEISKAQNNGGKPAWCWYTLAMCGAGYDSGTCDYMYSHCFGIKHHSSGSSSYHC
Protein: Terminase, small subunit (DNA-packaging protein gp3) (P04893)
Organism: Salmonella phage P22 (Bacteriophage P22)
Function: The terminase small subunit binds to the packaging initiation site and regulates the ATPase activity of the terminase large subunit. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by neck proteins.
Interaction partners:
Sequence:
MAAPKGNRFWEARSSHGRNPKFESPEALWAACCEYFEWVEANPLWEMKAFSYQGEVIQEPIAKMRAMTITGLTLFIDVTLETWRTYRLREDLSEVVTRAEQVIYDQKFSGAAADLLNANIIARDLGLKEQSQVEDVTPDKGDRDKRRSRIKELFNRGTGRDS
Protein: Octaketide synthase 3 (OKS 3) (EC 2.3.1.-) (Polyketide synthase 5) (C4NF91)
Organism: Aloe arborescens (Kidachi aloe)
Function: Catalyzes the iterative condensations of 8 molecules of malonyl-CoA to produce aromatic octaketides, SEK4 and SEK4b, the products of the minimal polyketide synthase for the benzoisochromanequinone actinorhodin. May be involved in the biosynthesis of the octaketide barbaloin.
Interaction partners:
Sequence:
MGSIAESSPLMSRENVEGIRKAQRAEGTATVMAIGTAHPPHIFPQDTYADFYFRATNSEHKVELKKKFDRICKKTMIGKRYFNYDEEFLKKYPNITSFDEPSLNDRQDICVPGVPALGKEAALKAIEEWGQPLSKITHLVFCTSCGVDMPSADFQLAKLLGLNTNVNKYCVYMQGCYAGGTVLRYAKDLAENNRGSRVLVVCAELTIIGLRGPNESHLDNAIGNSLFGDGAAALIVGADPIVGIEKPIFEIVCAKQTVIPDSEDVIHLHLREAGLMFYMSKDSPETISNNVEGCLVDIFKSVGMTPPADWNSLFWIPHPGGRAILDEVEARLKLRPEKFRATRHVLWEYGNMVSACVLYILDEMRNKSAADGLGTYGEGLEWGVLLGFGPGMTVETILLHSLPPV
Protein: Ribose-5-P isomerase B (EC 5.3.1.6) (RpiB-type ribose-5-P isomerase) (Q92EU5)
Organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Function: Catalyzes the interconversion of ribulose-5-P and ribose-5-P.
Interaction partners:
- Transketolase
- Triosephosphate isomerase 2
- NAD-dependent glycerol dehydrogenase
- Transketolase
- Transketolase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Putative ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 1
- PEP-dependent dihydroxyacetone kinase 2, ADP-binding subunit DhaL
- Phosphopentomutase
Sequence:
MKIAIGCDEMGYELKQTLITRLKEKNIEFTDFGSFENEKVLYPSIAEKVALEVKNNDYDRGILICGTGIGMAITANKIHGIRAAQIHDSYSAERARKSNDAHIMTMGALVIGPSLAVSLLDTWLDSDFSGGRSQAKVDLMEEIDQKNR
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (Q382B0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSLRIRKTRPPPLGFSLALPPPSVVGEVRVQQGNELFINVDDTNISPIITMDGSLPTGQFVHVTNTNLFVLVDGASLFTEAKTTQREEPQSNHIGDLVDNSASAEKGRSPQRSPCSNLGASVDSVEAAIRGIEDDSGEVRRDLSSSFSLLPKTEGDSPVLSRCSSRCRMSCQGTKGVKYHGGASLPHQYTALFTKGAGAVSGLAAATAGANRVGNREVRCNVLRGKIRGFLPWYVVEQNWTTSPKCSNASTSGTLGAATGTSAVASQSSASSVLVDTAVGDKVDKHAKRKNTLLARGRGNNSRSASLYEVGRTNRSLDLKEVEVLGFVGKGTQGAVYRVLLDNKLYGLKCIDVRELTEASSLVEHQSRKGGLVKELNMIRLQRSKSPPQYLLRLFDASVTRDREKLHLHILMELMSFSVEDAQRMVSRIPSDEMVKLTESAFRKHMAGSHSVKLKPDTFLQRNSESCVHLTGRRSYKTPEDWEMNIDRQTPVPEIILSMLAADVLGGLKELHEDYAIVHCDIKPANILIDYDMERFRLADFGCGCQMDPQSRKTRPVTFDLGSKLYKAPERLSNELYNAGVEGGLSEVEFSFDADVWSLGVTLLELRNGVHPCHPFKSDYWNYRNNLKLSRMVKPVSWSYSFYDFIVRCLMRKPEQRWSVSRLLQHPFIVKYSELPRAKLRVWMEKLRSESETFQRRQQRELLEEHILLSTGRKGPDMYRHRSRSSWESFTKFLKVAPHYQDDEKFPHLC
Protein: Peroxidase 71 (Atperox P71) (EC 1.11.1.7) (ATP15a) (ATPO2) (Q43387)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- Berberine bridge enzyme-like 10
- UDP-glycosyltransferase 72E2
- UDP-glycosyltransferase 72E1
- Berberine bridge enzyme-like 11
- Cinnamyl alcohol dehydrogenase 4
- Cinnamyl alcohol dehydrogenase 5
Sequence:
MGLVRSLCLLITFLNCLIISVHGQATARPGPVSGTRIGFYLTTCPRAETIVRNAVNAGFSSDPRIAPGILRMHFHDCFVQGCDGSILISGANTERTAGPNLNLQGFEVIDNAKTQLEAACPGVVSCADILALAARDTVILTQGTGWQVPTGRRDGRVSLASNANNLPGPRDSVAVQQQKFSALGLNTRDLVVLVGGHTIGTAGCGVFRNRLFNTTGQTADPTIDPTFLAQLQTQCPQNGDGSVRVDLDTGSGSTWDTSYYNNLSRGRGVLQSDQVLWTDPATRPIVQQLMAPRSTFNVEFARSMVRMSNIGVVTGANGEIRRVCSAVN
Protein: Salivary androgen-binding protein alpha subunit (Q63930)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
GLCPALQRKVDLFLNGTTEEYVQYLKQFNENRDVLDNAANIKKCSDRTLTEEDKAQATSLINKITASRTC
Protein: DNA damage-binding protein 1 (D-DDB1) (Damage-specific DNA-binding protein 1) (Protein piccolo) (Q9XYZ5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (By similarity). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (By similarity). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (By similarity). Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (By similarity). Required for degradation of gig. Required for genomic stability in the face of endogenous DNA lesions and for the response to MMS-induced DNA damage. Required for normal wing development.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-4A
- Protein lethal
- Protein cereblon
- DET1- and DDB1-associated protein 1
- Abnormal oocyte
- RING-box protein 1A
- Cullin homolog 1
- DDB1- and CUL4-associated factor 11 homolog
- COP9 signalosome complex subunit 5
- Protein mahjong
Sequence:
MSHHYVVTAQKPTAVVACLTGNFTSPTDLNLIIARNNQVEIDLVTPEGLRPLKEININGTIAVMRHFRPPDSNKDLLFILTRRYNVMILEARMVNDVITVVTKANGNVSDSVGIPSEGGVIAAIDPKARVIGMCLYQGLFTIIPMDKDASELKATNLRMDELNVYDVEFLHGCLNPTVIVIHKDSDGRHVKSHEINLRDKEFMKIAWKQDNVETEATMLIPVPSPIGGVIVIGRESIVYHDGSNYHAVAPLTFRQSTINCYARVSSNGLRYLLGNMDGQLYMLFLGTAETSKGVTVKDIKVEQLGEISIPECITYLDNGFLYIGARHGDSQLVRLNSEAIDGSYVVPVENFTNLAPILDIAVVDLDRQGQGQIITCSGSFKDGSLRIIRIGIGIQEHACIDLPGIKGMWSLKVGVDESPYENTLVLAFVGHTRILTLSGEEVEETEIPGFASDLQTFLCSNVDYDQLIQVTSDSVRLVSSATKALVAEWRPTGDRTIGVVSCNTTQILVASACDIFYIVIEDGSLREQSRRTLAYEVACLDITPLDETQKKSDLVAVGLWTDISAVILSLPDLETIYTEKLSGEIIPRSILMTTFEGIHYLLCALGDGSMYYFIMDQTTGQLTDKKKVTLGTQPTTLRTFRSLSTTNVFACSDRPTVIYSSNHKLVFSNVNLKEVNHMCSLNAQAYPDSLALANKNAVILGTIDEIQKLHIRTVPLGEGPRRIAYQESSQTFAVSTLRIDVHGRGGAKPLRNSASTQAQNITCSSNFLPKPGGGNSTAANAEVGQEIDVHNLLVIDQNTFEVLHAHQFVAPETISSLMSAKLGDDPNTYYVVATSLVIPEEPEPKVGRIIIFHYHENKLTQVAETKVDGTCYALVEFNGKVLAGIGSFVRLYEWTNEKELRMECNIQNMIAALFLKAKGDFILVGDLMRSITLLQHKQMEGIFVEIARDCEPKWMRAVEILDDDTFLGSETNGNLFVCQKDSAATTDEERQLLPELARFHLGDTVNVFRHGSLVMQNVGERTTPINGCVLYGTCNGAIGIVTQIPQDFYDFLHGLEERLKKIIKSVGKIEHTYYRNFQINSKVEPSEGFIDGDLIESFLDLSRDKMRDAVQGLELTLNGERKSADVEDVIKIVEDLTRMH
Protein: Oxidative stress-responsive serine-rich protein 1 (Oxidative stress-responsive protein 1) (Peroxide-inducible transcript 1 protein) (Q703I1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKSEAKDGEEESLQTAFKKLRVDASGSIVSLSVGEGTSVRASVRTTVDDTKPKTMCAPKDSWHGSTRKSSRGAVRIQRRRRSKSPVLHPPKFIHCSTTASPSSSQLKQRSQTEPLDGSSGRGISTPKEFSTGENSTSLDINHTGAAIEPLRSSVLRLPSESKTEELSDATQVSPESLTANDLSDFQSVSKLSQGKPCVCVGKACQCKRWHDMEVYSFSGLQNVPPLAPERRSLEDYSQSLHTRTLSGSPRSCSEQARVYVDDVTIEDLAGYMEYYLYIPKKMSHMAEMMYT
Protein: Ribonuclease P/MRP subunit p21 (TRIM39-RPP21 readthrough) (A0A096LP39)
Organism: Homo sapiens (Human)
Interaction partners:
- cGMP-dependent protein kinase 1
- Gamma-butyrobetaine dioxygenase
- E3 ubiquitin-protein ligase TRIM39
Sequence:
MAETSLLEAGASAASTAAALENLQVEASCSVCLEYLKEPVIIECGHNFCKACITRWWEDLERDFPCPVCRKTSRYRSLRPNRQLGSMVEIAKQLQAVKRKIRDESLCPQHHEALSLFCYEDQEAVCLICAISHTHRAHTVVPLDDATQEYKEKLQKCLEPLEQKLQEITRCKSSEEKKPGELKRLVESRRQQILREFEELHRRLDEEQQVLLSRLEEEEQDILQRLRENAAHLGDKRRDLAHLAAEVEGKCLQSGFEMLKDVKSTLEKCEKVKTMEVTSVSIELEKNFSNFPRQYFALRKILKQLIADVTLDPETAHPNLVLSEDRKSVKFVETRLRDLPDTPRRFTFYPCVLATEGFTSGRHYWEVEAAHCVLAQDPENQALARFYCYTERTIAKRLVLRRDPSVKRTLCRGCSSLLVPGLTCTQRQRRCRGQRWTVQTCLTCQRSQRFLNDPGHLLWGDRPEAQLGSQADSKPLQPLPNTAHSISDRLPEEKMQTQGSSNQ
Protein: N-lysine methyltransferase KMT5A-A (EC 2.1.1.-) (Histone-lysine N-methyltransferase KMT5A-A) (EC 2.1.1.361) (Lysine-specific methylase 5A-A) (SET domain-containing protein 8-A) (Q071E0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NQR1}. Chromosome {ECO:0000250|UniProtKB:Q9NQR1}. Note=Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms (By similarity). {ECO:0000250|UniProtKB:Q9NQR1}.
Interaction partners:
- Cellular tumor antigen p53
- Lysine methyltransferase 5C.
- Round spermatid basic protein 1.
- Histone-lysine N-methyltransferase SETD7
- Histone-lysine N-methyltransferase KMT5B
Sequence:
MFPAVNEIKVQTWRRDQRGECPRRSAQCRLFSCAHRECAPAARSLENRGPENRTARPEATMSGDVLCNGHSAFHRLLKHSSSRTHEALVVKIIQENKNTPLFCTAPEPRRDSGVNGEFLLNSAELQDEQTLPLHCIHSAADITSSKHRKPARRKVKRSTKRAAESKSPANRKVTDYFPIRRSSRKSKSELKYEEKQHIDTLISNGIEDGMMVRFIEGKGRGVFATQPFQKGQYVVEYHGDLLQITDAKQREALYAQDPSTGCYMYYFQYLSKTYCVDATKESDRLGRLINHSKNGNCQTKLHAIAGKPHLILVASRDIQEGEELLYDYGDRSKSSIEAHPWLKH
Protein: Possible SOJ/para-related protein (O05853)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable chromosome-partitioning protein ParB
- Conserved alanine valine rich protein
- PE-PGRS family protein PE_PGRS7
- Putative isochorismate synthase MenF
- Acid phosphatase
- PE-PGRS family protein PE_PGRS4
Sequence:
MTDTRVLAVANQKGGVAKTTTVASLGAAMVEKGRRVLLVDLDPQGCLTFSLGQDPDKLPVSVHEVLLGEVEPNAVLVTTMEGMTLLPANIDLAGAEAMLLMRAGREYALKRALAKFSDRFDVVIIDCPPSLGVLTLNGLTAADKAIVPLQCEMLAHRGVGQFLRTVADVQQITNPNLRLLGALPTLYDSRTTHTRDVLLDVADRYDLQVLAPPIPRTVRFAEASASGSSVMAGRKNKGAVAYRELAQALLKHWKTGRPLPTFTVDL
Protein: Bifunctional hemolysin/adenylate cyclase (AC-HLY) (ACT) (Cyclolysin) [Cleaved into: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase); Hemolysin] (J7QLC0)
Organism: Bordetella pertussis (strain ATCC 9797 / DSM 5571 / CCUG 30873 / LMG 14455 / NCTC 10739 / 18323)
Function: Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization. It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function.
Subcellular location: Secreted {ECO:0000269|PubMed:2905265}.; SUBCELLULAR LOCATION: [Hemolysin]: Host cell membrane {ECO:0000305|PubMed:7525549}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPSGRSKFSPDVLETVPASPGLRRPSLGAVERQDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSVDVFVDRFVQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLDVIGGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQTTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASALGVDYYDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTVDYSQTGAHAGIAAGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGRDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRNIENAVGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR
Protein: Probable transcription factor At2g01370 (Storekeeper-like protein At2g01370) (Q9ZU30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKGITKKLLVSRSLKRLTAKKNRRKIHRETNKRLKPEEDPSMVKRRQDSDSDSLEKEVSVVVTKTSDDEMVSTDTKKNYFQRIWSDDDEIVLLQGMVDFENDKGKSPYDDMTGFIDTVKNFISFQANQHQFTTKIRRLKDKFLKKWNNGVDENSLVNAHDRKCFQLSKVIWEPTTKVEEVGDWFVNSYLVGSIARLGVSEDVMKQSWSMVPIETKKEVEEKFKLLKDEESENLRLKTSFLQKVNSMIIEATN
Protein: LD33277p (Q95TP4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGVAVSQQVIPGQAGILPPGAGGMSPSTVAVPSPVSGGAGAGGMGGMTSPHPHQPGIGMKPGGGHSPSPNVLQVVKQVQEEAARQQVSHGGGFGKGVPMAPPVMNRPMGGAGPNQNVVNQLGGMGVGVGGVGGVGVGGVGGVGVNQLNSGGGNTPGAPISGPGMNVNHLMSMDQWGGGGAGGGGANPGGGNPQARYANNTGGMRQPTHVMQTNLIPPQQQQQMMGGLGGPNQLGGGQMPVGGQHGGMGMGMGAPPMAGTVGGVRPSPGAGGGGGSATGGGLNTQQLALIMQKIKNNPTNESNQHILAILKQNPQIMAAIIKQRQQSQNNAAAGGGAPGPGGALQQQQAGNGPQNPQQQQQQQQQQQVMQQQQMQHMMNQQQGGGGPQQMNPNQQQQQQQVNLMQQQQQGGPGGPGSGLPTRMPNMPNALGMLQSLPPNMSPGVSTQGGMVPNQNWNKMRYMQMSQYPPPYPQRQRGPHMGGAGPGPGQQQFPGGGGGAGNFNAGGAGGAGGVVGVGGVPGGAGTVPGGDQYSMANAAAASNMLQQQQGQVGVGVGVGVKPGPGQQQQQMGVGMPPGMQQQQQQQQPLQQQQMMQVAMPNANAQNPSAVVGGPNAQVMGPPTPHSLQQQLMQSARSSPPIRSPQPTPSPRSAPSPRAAPSASPRAQPSPHHVMSSHSPAPQGPPHDGMHNHGMHHQSPLPGVPQDVGVGVGVGVGVGVNVNVGNVGVGNAGGALPDASDQLTKFVERL
Protein: Carnitine O-palmitoyltransferase 2, mitochondrial (EC 2.3.1.21) (Carnitine palmitoyltransferase II) (CPT II) (P18886)
Organism: Rattus norvegicus (Rat)
Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:17585909}; Peripheral membrane protein {ECO:0000269|PubMed:17585909}; Matrix side {ECO:0000269|PubMed:17585909}.
Interaction partners:
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Mitochondrial carnitine/acylcarnitine carrier protein
- Peroxisomal acyl-coenzyme A oxidase 3
- Carnitine O-palmitoyltransferase 1, liver isoform
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Palmitoyl thioesterase CPT1C
- 3-ketoacyl-CoA thiolase, mitochondrial
Sequence:
MMPRLLFRAWPRCPSLVLGAPSRPLSAVSGPDDYLQHSIVPTMHYQDSLPRLPIPKLEDTMKRYLNAQKPLLDDSQFRRTEALCKNFETGVGKELHAHLLAQDKQNKHTSYISGPWFDMYLTARDSIVLNFNPFMAFNPDPKSEYNDQLTRATNLTVSAVRFLKTLQAGLLEPEVFHLNPSKSDTDAFKRLIRFVPPSLSWYGAYLVNAYPLDMSQYFRLFNSTRIPRPNRDELFTDTKARHLLVLRKGHFYVFDVLDQDGNIVNPLEIQAHLKYILSDSSPVPEFPVAYLTSENRDVWAELRQKLIFDGNEETLKKVDSAVFCLCLDDFPMKDLIHLSHTMLHGDGTNRWFDKSFNLIVAEDGTAAVHFEHSWGDGVAVLRFFNEVFRDSTQTPAITPQSQPAATNSSASVETLSFNLSGALKAGITAAKEKFDTTVKTLSIDSIQFQRGGKEFLKKKQLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASIFTKRCSEAFVRDPSKHSVGELQHMMAECSKYHGQLTKEAAMGQGFDRHLYALRYLATARGLNLPELYLDPAYQQMNHNILSTSTLNSPAVSLGGFAPVVPDGFGIAYAVHDDWIGCNVSSYSGRNAREFLHCVQKCLEDIFDALEGKAIKT
Protein: Siderophore triacetylfusarinine C esterase (EC 3.1.-.-) (Q4WF29)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Displays specific TAFC esterase activity but does not hydrolyze fusarinine C, which has the same core structure as TAFC. Hydrolysis optimizes but is not essential for TAFC-mediated iron uptake.Both extra- and intracellular siderophores have been shown to be crucial for the virulence. Subsequent to chelation of iron and uptake, FsC and TAFC are hydrolyzed and the iron is transferred to the metabolism or to the intracellular siderophore ferricrocin (FC) for transport and storage of iron. Hydrolyzes both TAFC and DF-TAFC with equal efficiencies, suggesting that its function might not be restricted to the release of iron from the siderophore but might also include the degradation of the iron-free chelator to protect cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17586718}.
Interaction partners:
Sequence:
MGDRPTPVPLPNSEQFYLENDRGEPYLIQVSWPLHWEDKQTGRGPLPIIYIVDGNALFLTATEAAWRRAAASHFAGGGIIVAIGYPLKGKLYDARRRSFDLTPPTACAPVGYGGADVFLDFIENSVRPAVQARFPQVSLAREALYGHSYGGLLALHALFTRPQSFDCYIASSPSIWWNSLCILHEAKAFVETKKVSHDQSPSLMVSWGSWEQHPPRWADELLDHYEARKRTAAELRMADNALDLCAMLHGCSRLHALIKTEYEGEDHTSVMSCSVSRGLTMFFEDWPFHQSG
Protein: Annexin I (Q54PW0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MEYKEKEINTSSPSSPSKTQISNIENDSISEKAQEPISEKVQDPISEKAQESISEKEHIESNNVSEIIDLIKSGDQHLNNNNNNNNNNNNNNNNNNNEEENQEINYNDNQLSNEEIVEDVKNSNINNNNTIEKGNSSQNNNKNNNNNYHTEKCDYCLICKCYDYGEITHNIVEDSEILKQSIRYSYVDDTSINSILAHRNYAEKEAIMKKFNDKYNKSLETELASHTHQKYRRTLISILTEPSIYDTLNIENSIKTKNSNTLLEILLTRTNEQKELIKRIYLVKYGKNIEHDIIAKFSNGANVNGNMMKQLLISMLNNDRDSNSNQSLDMNLINTDSNRLYQAGEHKKGTDHEVFIEILSKRSFSHLSELDRVYENSNPKGHSLRKAIELEFGVSKSIKQVKISLLDILLFSKEPSKYWAEQFNRALTSGSWGINEIDLTRLTITQQHQASKIKQAYISHYDNSLINEVSSKTSFRYKKIILSMLTV