wanglab/gogpt-training-data huggingface dataset:
Protein: EGF-like domain-containing protein (A8WFH5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRLLFLVFILAEIMLQNEIMADHRTINQSFRGNFFRRRNYDGPRAYQIAPDLTCSYDNQCAGYPLAICHSVCQCVKGALNTGTTCIASSTAIQTSVACPAGQTYIREAGVCMTVQQPGEPCQYSQQCSALEPGAYCLKMRCECVYGMKKSSNGCTFVNNDCKERGHIFISEIGECREVFPPGGKGCSHNLQCSGAYPDATCFMQTCTCPPNLPVAADGTCGRSCPNNQVYSGVTGECLPEKQPGQDCIYSSQCQASFGGLVCDKNTCRCPNGLVFDGLKCSHGCPPHKRVIDKEICVEGCPSGIVEVAGRCVKQVSIGQPCVANAQCNFGSFCQSGTCQCPPGFYVQDEQCQAIESEPNESCQNNEKCTKGSVCYNGKCSCPRNHELINGHCQQNRAAAHAYNTALENIRKIRLRFASQSKSRNSSPQLTDVENDNDTVPIGSACVRIGVTCDGGSVCVAGICVCPLGKTPRNGVCIEHVAARPGTSCQNEEECVDHSYCSPETNKCECMKASQMVIGGECRERLKAHPGYGCTMGEMCVGNSVCVNGKCACVDGKVEINKICIDQVSAKPGDTCGKGIICEGGSYCNTDSGKCACRRGENSINGICKGFTFVYPGDLCTDITSRCTGGSYCARGRCECPPRMSAIDKKCVHQQTAAPGEPCSEKVACSPFSVCENNVCKCVNNMMIRDKMCVQRRKVNIGNSCNNEDQCLGNSTCMDNNCQCGIGFVASMDVCVLRKTVTPGYLCNPEDICTGQSVCIKGVCQCQPDYKQMHNICVKKNIGIEGSPCSSRDDCGEGLMCGASGKCSCPEGLFSVNGKCRSYVQLGQTCTSDDRCAERNAQCQENYCTCRTGYTNINGQCAANIVTPAEPETLSQVKSGLLGHICTSNDHCKIAHSQCRRNVCQCIDGYRIFGSTQCIPRPGKPKERKTEKESKLVELGDKCDKLSLCSKGAICEKGVCSCPETFFESDGACVKNVAKIKVVVPPLSSCLGGEECSGNSECVHGICFCKEEFTLFEGKCQRLRIIEKLTVLESKKLIKPIKAHTTPTAASNTTPIPVKTTTTLQTTTATTLPENYVSSSTNRPLTPIIISMKLGSTSSPSPQITSNPEYKWRLSKPGHMCDNKTHCTNCSVCVNGFCRCPEGLVHYGDKCVSEIDATKCLASNQCPSGAQCVKGECRCKPGLGITRYGFCVPITFAEPGTSCAYGEHCQKDSHCEDGLCTCNEPLVLKENKCVVSPREQTRRRQPSRLLTECPRDGSCRLPSCFCTSTGKIPPNNFDTKQVPQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSGRTQERWYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLVSSPYWPQTLDHKLAWECDGNCPTQSHKAIWEIPIQNIQANDTRWYKTLTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDNGAVYALRDFLKFIVQKQDVFVVTGSQIIDYMRNPVDLNNIKSLRSWQCKPQMKDEANPCENPTTCSFSGRARGQFAHSFRMCGVCPKSYPWI
Protein: VP2 (Coat protein VP2) (VP2 protein) (Q27XI9)
Organism: Human bocavirus
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MSDTDIQDQQPDTVDAPQNTSGGGTGSIGGGKGSGVGISTGGWVGGSHFSDKYVVTKNTRQFITTIQNGHLYKTEAIETTNQSGKSQRCVTTPWTYFNFNQYSCHFSPQDWQRLTNEYKRFRPKAMQVKIYNLQIKQILSNGADTTYNNDLTAGVHIFCDGEHAYPNASHPWDEDVMPDLPYKTWKLFQYGYIPIENELADLDGNAAGGNATEKALLYQMPFFLLENSDHQVLRTGESTEFTFNFDCEWVNNERAYIPPGLMFNPKVPTRRVQYIRQNGSTAASTGRIQPYSKPTSWMTGPGLLSAQRVGPQSSDTAPFMVCTNPEGTHINTGAAGFGSGFDPPSGCLAPTNLEYKLQWYQTPEGTGNNGNIIANPSLSMLRDQLLYKGNQTTYNLVGDIWMFPNQVWDRFPITRENPIWCKKPRADKHTIMDPFDGSIAMDHPPGTIFIKMAKIPVPTASNADSYLNIYCTGQVSCEIVWEVERYATKNWRPERRHTALGMSLGGESNYTPTYHVDPTGAYIQPTSYDQCMPVKTNINKVL
Protein: Non-histone chromosomal protein HMG-17 (High mobility group nucleosome-binding domain-containing protein 2) (P09602)
Organism: Mus musculus (Mouse)
Function: Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in a unique chromatin conformation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Cytoplasmic enrichment upon phosphorylation. {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL32
Sequence:
MPKRKAEGDAKGDKTKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDANNPAENGDAKTDQAQKAEGAGDAK
Protein: Tubulin beta chain (Q18817)
Organism: Caenorhabditis elegans
Interaction partners:
- Tubulin alpha chain
- Tubulin alpha-3 chain
- Tubulin alpha chain
- Tubulin alpha-2 chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha-8 chain
- Serine/threonine-protein kinase zyg-8
Sequence:
MREIVHVQAGQCGNQIGAKFWEVISDEHGIQPDGTYKGESDLQLERINVYYNEANGGKYVPRAVLVDLEPGTMDSVRSGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDNVLDVVRKEAEGCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMSSFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETFCIDNEALYDICFRTLKLSNPTYGDLNHLVSVTMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLSAKGAQAYRALTVAELTQQMFDAKNMMAACDPRHGRYLTVAAMFRGRMSMREVDDQMMNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEATAEEDGELDGTDGDAE
Protein: Myosin light chain 3 (Cardiac myosin light chain 1) (CMLC1) (Myosin light chain 1, slow-twitch muscle B/ventricular isoform) (MLC1SB) (Ventricular myosin alkali light chain) (Ventricular myosin light chain 1) (VLCl) (Ventricular/slow twitch myosin alkali light chain) (MLC-lV/sb) (P08590)
Organism: Homo sapiens (Human)
Function: Regulatory light chain of myosin. Does not bind calcium.
Interaction partners:
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin-7
- Myosin-6
- Actin, alpha cardiac muscle 1
- Myosin light chain kinase 2, skeletal/cardiac muscle
- Myosin-binding protein C, cardiac-type
- Myosin light chain 4
- Troponin I, cardiac muscle
- Troponin T, cardiac muscle
- Tropomyosin alpha-1 chain
Sequence:
MAPKKPEPKKDDAKAAPKAAPAPAPPPEPERPKEVEFDASKIKIEFTPEQIEEFKEAFMLFDRTPKCEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPRQEELNTKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMSS
Protein: U3 small nucleolar RNA-associated protein 15 homolog (H0Y8P4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
XVIFARRSVRCVCRRLLEGPCDFYASAAELCRVGSWHSPINCPWVEVSRRTLWGSVETPVQIKEFGAVSKVDFSPQPPYNYAVTASSRIHIYGRYSQEPIKTFSRFKDTAYCATFRQDGRLLVAGSEDGGVQLFDISGRAPLRQFEGHTKAVHTVDFTADKYHVVSGADDYTVKLWDIPNSKEILTFKEHSDYVRCGCASKLNPDLFITGSYDHTVKMFDARTSESVLSVEHGQPVESVLLFPSGGLLVSAGGRYVKVWDMLKGGQLLVSLKNHHKTVTCLCLSSSGQRLLSGSLDRKVKVYSTTSYKVVHSFDYAASILSLALAHEDETIVVGMTNGILSVKHRKSEAKKESLPRRRRPAYRTFIKGKNYMKQRDDILINRPAKKHLELYDRDLKHFRISKALDRVLDPTCTIKTPEITVSIIKELNRRGVLANALAGRDEKEISHVLNFLIRNLSQPRFAPVLINAAEIIIDIYLPVIGQSPVVDKKFLLLQGLVEKEIDYQRELLETLGMMDMLFATMRRKEGTSVLEHTSDGFPENKKIES
Protein: Iron-sulfur cluster biogenesis chaperone, mitochondrial (EC 3.6.4.10) (P22774)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Assisted by the DnaJ-like co-chaperone jac1 and the nucleotide exchange factor mge1, it mediates ATP-dependent Fe-S cluster transfer from the scaffold proteins isu1/isu2 to grx5.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:26545917}.
Interaction partners:
- GrpE protein homolog
- Heat shock protein 60, mitochondrial
- Mitochondrial import inner membrane translocase subunit tim44
- DnaJ homolog 1
- Mitochondrial import inner membrane translocase subunit tim14
- Uncharacterized protein C24H6.02c
- Mitochondrial import inner membrane translocase subunit tim17
- Mitochondrial import inner membrane translocase subunit tim23
- Mitochondrial protein import protein mas5
- Iron sulfur cluster assembly protein 1, mitochondrial
Sequence:
MISSRFTNVVRSGLRFQSKGASFKIGASLHGSRMTARWNSNASGNEKVKGPVIGIDLGTTTSCLAIMEGQTPKVIANAEGTRTTPSVVAFTKDGERLVGVSAKRQAVINPENTFFATKRLIGRRFKEPEVQRDIKEVPYKIVEHSNGDAWLEARGKTYSPSQIGGFILSKMRETASTYLGKDVKNAVVTVPAYFNDSQRQATKAAGAIAGLNVLRVVNEPTAAALAYGLDKKNDAIVAVFDLGGGTFDISILELNNGVFEVRSTNGDTHLGGEDFDVALVRHIVETFKKNEGLDLSKDRLAVQRIREAAEKAKCELSSLSKTDISLPFITADATGPKHINMEISRAQFEKLVDPLVRRTIDPCKRALKDANLQTSEINEVILVGGMTRMPRVVETVKSIFKREPAKSVNPDEAVAIGAAIQGGVLSGHVKDLVLLDVTPLSLGIETLGGVFTRLINRNTTIPTRKSQVFSTAADGQTAVEIRVFQGERELVRDNKLIGNFQLTGIAPAPKGQPQIEVSFDVDADGIINVSARDKATNKDSSITVAGSSGLTDSEIEAMVADAEKYRASDMARKEAIENGNRAESVCTDIESNLDIHKDKLDQQAVEDLRSKITDLRETVAKVNAGDEGITSEDMKKKIDEIQQLSLKVFESVYKNQNQGNESSGDNSAPEGDKK
Protein: ER membrane protein complex subunit 4 (O94520)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 6
- TPR repeat protein oca3
- UPF0620 protein C83.10
- ER membrane protein complex subunit 5
- Vacuolar protein sorting-associated protein 28 homolog
- Ubiquitin-conjugating enzyme E2-18 kDa
Sequence:
MHINEETDWIDLVKPALAKKPKKIVDNSDKFPTPRGFQQKSLVSKNIHSGNSASSTSIFAKREEELQKDLLLKKAWELAYSPLKQIPMNAILAYMSGNSLQIFSIMTTLMLLVNPLKAITSTGSAFTPFKGTHPGTLWPAMGAYILFQLLLMGIGVYKLQRMGLLPTTTSDWLAWEVSKVFMDRSYGPSKTVL
Protein: Basic leucine zipper transcriptional factor ATF-like (B-cell-activating transcription factor) (B-ATF) (O35284)
Organism: Mus musculus (Mouse)
Function: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs.
Subcellular location: Nucleus. Cytoplasm. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells.
Interaction partners:
- Transcription factor Jun
- Interferon regulatory factor 4
- Basic leucine zipper transcriptional factor ATF-like 2
- Transcription factor JunB
- Basic leucine zipper transcriptional factor ATF-like 3
- PR domain zinc finger protein 1
- Nuclear receptor ROR-gamma
- Transcription factor JunD
- Transcription regulator protein BACH2
- Signal transducer and activator of transcription 3
Sequence:
MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP
Protein: Sphingosine N-acyltransferase lac1 (EC 2.3.1.24) (Meiotically up-regulated gene 83 protein) (O59735)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ceramide synthase complex required for C26-CoA-dependent ceramide synthesis. Facilitates ER-to-Golgi transport of GPI-anchored proteins (By similarity). Has a role in meiosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Sphingolipid delta
- Sphingoid long chain base kinase 4
- PIGF/3-ketodihydrosphingosine reductase fusion protein
- Sphingosine N-acyltransferase lag1
- Dihydrosphingosine 1-phosphate phosphatase C823.11
- Sphingolipid C4-hydroxylase sur2
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 1
- Copper-transporting ATPase ccc2
Sequence:
MGNNTSRRSQSQKFKNIPSISAGSFSTMPVQHRGRRRRSKSIVGRAAQNAVLRSKEKTWIVPLILLTLLVGWYFVNPNGYIKYGIFLSYPIPGTNPAQYGKGRLDIAFCLFYALFFTFCREFIMQEIIARIGRHFNIRAPAKLRRFEEQAYTCLYFTVMGSWGLYVMKQTPMWFFNTDAFWEEYPHFYHVGSFKAFYLIEAAYWIQQALVLILQLEKPRKDFKELVVHHIITLLLIGLSYYFHFTWIGLAVFITMDTSDIWLALSKCLNYVNTVIVYPIFVIFVFVWIYMRHYLNFKIMWAVWGTMRTINSFDLDWAAEQYKCWISRDVTLILLTALQLVNIYWLILILRIGYRAFTTNDTHDERSEDEDEEVSDEKSSAKKND
Protein: Mediator of RNA polymerase II transcription subunit 7a (Q9LYW3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 pre-initiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10a
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 10b
- Mediator of RNA polymerase II transcription subunit 22a
- Mediator of RNA polymerase II transcription subunit 22b
Sequence:
MATATYPPPPPYYRLYKDYSENPNSAPEPPPPIEGTYVCFGGNYTTEDVLPSLEEQGVPQLYPKDSNLDYKNELRSLNRELQLHILELADVLVDRPSQYAKRIGEISSIFKNLHHLLNSLRPHQARATLIHIMELQIQQRKQAVEDIKRRREEAQRLLKDAYLTLDGQ
Protein: Profilaggrin (Q8CIU0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MSTLLESITSMIDIFQQYSNNDKEEETLSKEELKELLEGELQAVLKNPNDQDIAEVFMQMLDVDHDDKIDFTEYLLMVLKLAQAYYETSKKRRSQTKESGKRNEHDYKGHEERREKVQRRHRRRNSGTDGKQENERSKSPRGRGKKRRGSSTISEESDTIRNSDTENKRHHHGSNRRQRRGSNSSDRKETRSKKHREVKETNAGIYNDGKDGQDWEVNYENCYYKTEESYRELREGQNHKTKESHSESEGSGGQAGRRGTAATRHTSRPEQSPDTAGRTGSSRGQQSAQRHADSTPGSTRTGSRGRGESPAGQQSPDRARHIESRRGRTREAGASQSSDSEAISGAHAGIGQGQTSTTHRRAGSSSGSQRASAGGQAADTSSRSGASQGQASGQGRAGSRSREAQGIARHGQLTDSHRHSGAGQAQAHTATSIDSRRPRGSSESQASDSEGHSDYSEAHTQGAHGGIQTSQRHEQRPSRGQQGSGHPQVYYYGVEETEDES
Protein: Envelope glycoprotein E (G3G924)
Organism: Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain Kaplan))
Subcellular location: Host Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004152}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004152}. Host cell junction {ECO:0000256|ARBA:ARBA00004315}. Host cell membrane {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane {ECO:0000256|ARBA:ARBA00004235}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004235}. Virion membrane {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004563}.
Interaction partners:
Sequence:
MRPFLLRAAQLLALLALALSTEAPSLSAETTPGPVTEVPSPSAEVWDLSTEAGDDDLDGDLNGDDRRAGFGSALASLREAPPAHLVNVSEGANFTLDARGDGAVVAGIWTFLPVRGCDAVAVTTVCFETACHPDLVLGRACVPEAPERGIGDYLPPEVPRLRREPPIVTPERWSPHLTVQRATPNDTGLYTLHDASGPRAVFFVAVGDRPPAPLAPVGPARHEPRFHALGFHSQLFSPGDTFDLMPRVVSDMGDSRENFTATLDWYYARAPPRCLLYYVYEPCIYHPRAPECLRPVDPTCSFTSPARARLVARRAYASCSPLLGDRWLTACPFDAFGEEVHTNATADESGLYVLVMTHNGHVATWDYTLVATAAEYVTVIKELTAPARAPGTPWGPGGGDDAIYVDGVTTPAPPARPWNPYGRTTPGRLFVLALGSFVMTCVVGGGVWLCVLCSRRRAASRPFRVPTRAGTRMLSPVYTSLPTHEDYYDGDDDDEEAGVARRRPSSPGGDSGYEGPYVSLDAEDEFSSDEDDGLYVRPEEAPRSGFDVWFRDPEKPEVTNGPNYGVTASRLLNARPA
Protein: Autoinducer 2-binding periplasmic protein LuxP (P54300)
Organism: Vibrio harveyi (Beneckea harveyi)
Function: Binds to the signaling molecule autoinducer 2 (AI-2), a furanosyl borate diester, (3a-methyl-5,6-dihydrofuro-[2,3d][1,3,2]dioxaborole-2,2,6,6a-tetraol). This complex then interacts with the LuxQ sensor protein.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Autoinducer 2 sensor kinase/phosphatase LuxQ
- S-ribosylhomocysteine lyase
- Phosphorelay protein LuxU
- Heme ABC exporter, ATP-binding protein CcmA
- Branched-chain amino acid transport system / permease component family protein
- D-ribose pyranase
- Luminescence regulatory protein LuxO
- histidine kinase
- Autoinducer 1 sensor kinase/phosphatase LuxN
- Autoinducer 2-binding periplasmic protein LuxP
Sequence:
MKKALLFSLISMVGFSPASQATQVLNGYWGYQEFLDEFPEQRNLTNALSEAVRAQPVPLSKPTQRPIKISVVYPGQQVSDYWVRNIASFEKRLYKLNINYQLNQVFTRPNADIKQQSLSLMEALKSKSDYLIFTLDTTRHRKFVEHVLDSTNTKLILQNITTPVREWDKHQPFLYVGFDHAEGSRELATEFGKFFPKHTYYSVLYFSEGYISDVRGDTFIHQVNRDNNFELQSAYYTKATKQSGYDAAKASLAKHPDVDFIYACSTDVALGAVDALAELGREDIMINGWGGGSAELDAIQKGDLDITVMRMNDDTGIAMAEAIKWDLEDKPVPTVYSGDFEIVTKADSPERIEALKKRAFRYSDN
Protein: Early E1A protein (Early E1A 29.5 kDa protein) (P03259)
Organism: Human adenovirus A serotype 12 (HAdV-12) (Human adenovirus 12)
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1 (By similarity).
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03255}.
Interaction partners:
Sequence:
MRTEMTPLVLSYQEADDILEHLVDNFFNEVPSDDDLYVPSLYELYDLDVESAGEDNNEQAVNEFFPESLILAASEGLFLPEPPVLSPVCEPIGGECMPQLHPEDMDLLCYEMGFPCSDSEDEQDENGMAHVSASAAAAAADREREEFQLDHPELPGHNCKSCEHHRNSTGNTDLMCSLCYLRAYNMFIYSPVSDNEPEPNSTLDGDERPSPPKLGSAVPEGVIKPVPQRVTGRRRCAVESILDLIQEEEREQTVPVDLSVKRPRCN
Protein: Laccase-1 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase 1) (Conidial laccase) (Diphenol oxidase 1) (Laccase I) (Urishiol oxidase 1) (P17489)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for the conversion of the yellow polyketide pigment synthesized by wA to the conidial green pigment.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q70KY3}.
Interaction partners:
- Conidial yellow pigment biosynthesis polyketide synthase
Sequence:
MYLSTVLFPLLALNLGLSHARFVRETLELTWEYGSPNGGTPREMVFTNGEYPGPDLIFDEDDDVEVLVINNLPFNTTVHWHGLEMRETPEADGVPGLTQTPIEPGATFTYRFRAYPAGTFWYHSHYKGLMQDGQVGAMYIRRKPDALRPYAVITEDPRELAEIQYAEDNPYLMLATDWTYLTSAEYHNIEVESGYNVFCVDSLLINGRGSVYCPGYQYLEEVSDDGLTAVLEGTHLTEKGCLQPDLHNVQGDYGPWNLSAVPTEVVFNCTPSSVEPPVIYVDPEFNGWVSLNFIGGAAQKAITFSVDNHPMWVYEVDGQFVEPREVEMVGVYSGARYAVMIKLDQTPGDYAIRIAVNGGDQVMSVYAILSYVNQDWIHRENVPKAAIGPHTDTVGYMNYGGGNTSADVRQLLFTENLPAFGVPPPPPSSEVSTTLRTGMIRVNNSYSWSLGNNVLYEPEMTSSTPLLFEPDPLAVIAPKYALTTENNTWVDIVLEITADPRDLIHPPHPIHKHGNRAYIIGNGVGKFRWENVSAAEAEVPDLFYVNETAALRDTFVTDFFDSRLMDGAWIVIRYFVQDKFPSILHCHIASHQMGGMALALLDGVDVWDS
Protein: Co-chaperone protein p23-2 (Atp23-2) (Q6ID70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a co-chaperone for HSP90. Controls root development through the modulation of auxin distribution in the root meristem.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21735091}. Nucleus {ECO:0000269|PubMed:21735091}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP40
- Protein SGT1 homolog B
- Peptidyl-prolyl cis-trans isomerase FKBP42
- Serine/threonine-protein phosphatase 5
- Co-chaperone protein p23-1
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
- Heat shock protein 90-4
- Heat shock protein 90-2
- Heat shock protein 90-6, mitochondrial
- SH3 domain-containing protein
Sequence:
MSRNPEVLWAQRSDKVYLTVALPDAKDISVKCEPQGLFSFSALGAQGERFEFSLELYGKIMTEYRKNVGLRNIIFSIQKEERSWWTRLLKSEEKPAPYIKVDWNKWCDEDEEVNSETASDDESAFVNQDSESSDDDGLLYLPDLEKARNK
Protein: Alpha-ketoglutarate dehydrogenase component 4 (Alpha-ketoglutarate dehydrogenase subunit 4) (Q9CQX8)
Organism: Mus musculus (Mouse)
Function: May be necessary to recruit DLD/E3 to the mitochondrial 2-oxoglutarate dehydrogenase complex (OGDC) core composed of OGDH/E1-DLST/E2, hence stabilizes the complex.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:36854377, ECO:0000305|PubMed:25165143}.
Interaction partners:
- Small ribosomal subunit protein bS21m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein mS39
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein mL65
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein mS38
- Small ribosomal subunit protein mS31
Sequence:
MGSKMASATRVVQVVKPHAPLIKFPNRRDKPKLSASEALGSAALPSHSSAISQHSKGSTSPDLLMHQGPPDTAEIIKSLPQKYRRKPMSQEEMEFIQRGGPE
Protein: Polypyrimidine tract-binding protein 1 (PTB) (Heterogeneous nuclear ribonucleoprotein I) (hnRNP I) (Pyrimidine-binding protein) (PYBP) (Q00438)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. Binds to polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon inclusion of CFTR exon 9. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform.
Subcellular location: Nucleus.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoprotein K
- Serine/arginine-rich splicing factor 1
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoproteins A2/B1
- ELAV-like protein 1
- Serine/arginine-rich splicing factor 3
- Transformer-2 protein homolog beta
- Heterogeneous nuclear ribonucleoprotein D0
- Serine/arginine-rich splicing factor 7
Sequence:
MDGIVPDIAVGTKRGSDELFSTCVSNGPFIMSSSASAANGNDSKKFKGDNRSTGVPSRVIHVRKLPSDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMSTEEAANTMVNYYTSVAPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGAPGIMSASPYAGAGFPPTFAIPQAAGLSVPNVHGALAPLAIPSAAAAAAAAGRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGSQAQLAMSHLNGHKLHGKSVRITLSKHQSVQLPREGQEDQGLTKDYGSSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEDDLKSLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIELHNHDLGENHHLRVSFSKSTI