wanglab/gogpt-training-data huggingface dataset:
Protein: Cleavage and polyadenylation specificity factor subunit 3 (EC 3.1.27.-) (Cleavage and polyadenylation specificity factor 73 kDa subunit) (CPSF 73 kDa subunit) (mRNA 3'-end-processing endonuclease CPSF-73) (P79101)
Organism: Bos taurus (Bovine)
Function: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required for entering/progressing through S-phase of the cell cycle (By similarity). Required for the selective processing of microRNAs (miRNAs) during embryonic stem cell differentiation via its interaction with ISY1 (By similarity). Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity). Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UKF6}.
Interaction partners:
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 4
- Cleavage stimulation factor subunit 2
- Pre-mRNA cleavage complex 2 protein Pcf11
- WD repeat-containing protein 82
- Pre-mRNA 3'-end-processing factor FIP1
- E3 ubiquitin-protein ligase RBBP6
Sequence:
MSAIPAEESDQLLIRPLGAGQEVGRSCIILEFKGRKIMLDCGIHPGLEGMDALPYIDLIDPAEIDLLLISHFHLDHCGALPWFLQKTSFKGRTFMTHATKAIYRWLLSDYVKVSNISADDMLYTETDLEESMDKIETINFHEVKEVAGIKFWCYHAGHVLGAAMFMIEIAGVKLLYTGDFSRQEDRHLMAAEIPNIKPDILIIESTYGTHIHEKREEREARFCNTVHDIVNRGGRGLIPVFALGRAQELLLILDEYWQNHPELHDIPIYYASSLAKKCMAVYQTYVNAMNDKIRKQININNPFVFKHISNLKSMDHFDDIGPSVVMASPGMMQSGLSRELFESWCTDKRNGVIIAGYCVEGTLAKHIMSEPEEITTMSGQKLPLKMSVDYISFSAHTDYQQTSEFIRALKPPHVILVHGEQNEMARLKAALIREYEDNDEVHIEVHNPRNTEAVTLNFRGEKLAKVMGFLADKKPEQGQRVSGILVKRNFNYHILSPCDLSNYTDLAMSTVKQTQAIPYTGPFNLLYYQLQKLTGDVEELEIQEKPALKVFKNITVIQEPGMVVLEWLANPSNDMYADTVTTVILEVQSNPKIRKGAVQKVSKKLEMHVYSKRLEIMLQDIFGEDCVSVKDGSILSVTVDGKTANINLETRTVECEEGSEDDESLREMVELAAQRLYEALTPVH
Protein: Sexual differentiation process putative amino-acid permease isp5 (P40901)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized transporter PB1C11.03
- Ribose-phosphate pyrophosphokinase 1
- Putative formamidase C869.04
- Sexual differentiation process putative subtilase-type proteinase isp6
Sequence:
MNNYGVSSIGTSLTPSPTGSIDEYTSKEVKHPEDVKVDASYEKEEVGYGELEVVPERGNLFQRWYRSFLPPEDGKPQKLKRTLTARHIQMIGIGGAIGTGVWVGSKNTLREGGAASVLICYSLVGSMVLMTVYSLGELAVAFPINGSFHTYGTRFIHPSWGFTLGWNYLASFLATYPLELITASICLQFWININSGIWITVFIALLCFVNMFGVRGYGEVEFFVSSLKVMAMVGFIICGIVIDCGGVRTDHRGYIGATIFRKNAFIHGFHGFCSVFSTAAFSYAGTEYIGIAASETKNPAKAFPKAVKQVFIRVSLFYILALFVVSLLISGRDERLTTLSATAASPFILALMDAKIRGLPHVLNAVILISVLTAANGITYTGSRTLHSMAEQGHAPKWFKYVDREGRPLLAMAFVLCFGALGYICESAQSDTVFDWLLSISNLATLFVWLSINVSYIIYRLAFKKQGKSYDEVGYHSPFGIYGACYGAFIIILVFITEFYVSIFPIGASPDAGAFFQSYLCFPVVVIVFIAHALITRQKFRKLSEIDLDTGFSKYDRLEESDKGPMTAKSLAKSVLSFCV
Protein: Cohesin subunit SA-2 (SCC3 homolog 2) (Stromal antigen 2) (O35638)
Organism: Mus musculus (Mouse)
Function: Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity).
Subcellular location: Nucleus. Chromosome {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. At anaphase, the RAD21 subunit of cohesin is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation. In germ cells, cohesin complex dissociates from chromatin at prophase I, and may be replaced by a meiosis-specific cohesin complex (By similarity). {ECO:0000250}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 1A
- Double-strand-break repair protein rad21 homolog
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 1B
- Sister chromatid cohesion protein PDS5 homolog A
- Nipped-B-like protein
- Cohesin subunit SA-1
- Double-strand-break repair protein rad21-like protein 1
- Sister chromatid cohesion protein PDS5 homolog B
Sequence:
MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKSGNGGGKPPSGSNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSRRDPEEDGLMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDDRTRITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCAHYVILWQLAKITESTSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDSNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGMSSRGSTVRSKKSKPSTGKRKVVEGMQLALPEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMSVYPMQAEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPPSKNRRERTELKPDFFDPASIMDESVLGVSMF
Protein: D(3) dopamine receptor (Dopamine D3 receptor) (P30728)
Organism: Mus musculus (Mouse)
Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- D
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
Sequence:
MAPLSQISSHINSTCGAENSTGVNRARPHAYYALSYCALILAIIFGNGLVCAAVLRERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPSICSISNPDFVIYSSVVSFYVPFGVTVLVYARIYMVLRQRRRKRILTRQNSQCISIRPGFPQQSSCLRLHPIRQFSIRARFLSDATGQMEHIEDKPYPQKCQDPLLSHLQPLSPGQTHGELKRYYSICQDTALRHPNFEGGGGMSQVERTRNSLSPTMAPKLSLEVRKLSNGRLSTSLKLGPLQPRGVPLREKKATQMVVIVLGAFIVCWLPFFLTHVLNTHCQACHVSPELYRATTWLGYVNSALNPVIYTTFNIEFRKAFLKILSC
Protein: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I) (P26284)
Organism: Rattus norvegicus (Rat)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:19341700}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Ac1164
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Pyruvate kinase PKM
- [Pyruvate dehydrogenase
- Pyruvate kinase PKLR
- [Pyruvate dehydrogenase
Sequence:
MRKMLAAVSRVLAGAAQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFNRGHAVRAILAELTGRRGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATKFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS
Protein: Dynein axonemal assembly factor 19 (Coiled-coil domain-containing protein 103) (Protein schmalhans) (Q6DGB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Dynein-attachment factor required for cilia motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22581229}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:22581229}.
Interaction partners:
- Dynein, axonemal, heavy chain 5.
- Dynein axonemal assembly factor 11
- Dynein, axonemal, intermediate chain 1, paralog 1.
- Dynein axonemal assembly factor 1
- Zinc finger MYND domain-containing protein 10
- Coiled-coil domain-containing protein 39
- Coiled-coil domain-containing protein 40
- Dynein axonemal assembly factor 3
- Dynein regulatory complex protein 1
- Dynein regulatory complex subunit 2
Sequence:
MENSDVINFSCLEKELHSALQADRKYQRENDAKFRALNQKVASYEEFRDIVLASHLKPLDRNDISGSPRKQPWNPVACRTNYVCASSEQVQPQLSEVQPRSASEFIRDWRRFAGCSFEKYSLLVSLGGEALQKIFSTEIGLGLLGEFLLILSQCLKSGDEDRVTGVLDGLSKTGRFSINLSLLSQAEQEACEELFNKLKVAAGECHPYKDNSNTSVVCEAGLTHMEDNKTDITTTLKELAGKYGTEK
Protein: Glycine/sarcosine/dimethylglycine N-methyltransferase (SDMT) (EC 2.1.1.156) (EC 2.1.1.157) (Dimethylglycine N-methyltransferase) (Q9KJ20)
Organism: Actinopolyspora halophila
Function: Catalyzes the methylation of glycine, sarcosine and dimethylglycine to sarcosine, dimethylglycine and betaine, respectively, with S-adenosylmethionine (AdoMet) acting as the methyl donor. Shows low level of activity on glycine when expressed in E.coli.
Interaction partners:
Sequence:
MTKSVDDLARGDQAGDEQDPVHREQQTFGDNPLEVRDTDHYMHEYVGGFVDKWDDLIDWKKRYESEGSFFIDQLRARGVETVLDAAAGTGFHSVRLLEEGFETVSADGSPQMLAKAFSNGLAYNGHILRVVNADWRWLNRDVHGEYDAIICLGNSFTHLFSERDRRKTLAEFYAMLKHDGVLIIDQRNYDSILDTGFSSKHTYYYAGEDVSAEPDHIDDGLARFKYTFPDKSEFFLNMYPLRKDYMRRLMREVGFQRIDTYGDFQETYGEDEPDFYIHVAEKSYRTEDEFVDMYSNAVHTARDYYNSEDADNFYYHVWGGNDIHVGLYQTPQEDIATASERTVQRMAGKVDISPETRILDLGAGYGGAARYLARTYGCHVTCLNLSEVENQRNREITRAEGLEHLIEVTDGSFEDLPYQDNAFDVVWSQDSFLHSGDRSRVMEEVTRVLKPKGSVLFTDPMASDSAKKNELGPILDRLHLDSLGSPGFYRKELTRLGLQNIEFEDLSEYLPVHYGRVLEVLESRENELAGFIGEEYRAHMKTGLRNWVQAGNGGSLAWGIIHARA
Protein: Guanine nucleotide-binding protein G(I) subunit alpha isoform X2 (Guanine nucleotide-binding protein G(K) subunit alpha) (W5U9Q0)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
- Lysophosphatidic acid receptor 1
- D
- Dopamine receptor D2a
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Beta-2 adrenergic receptor
- Endothelin receptor type B isoform X2
- Endothelin receptor type B
- Phosphoinositide 3-kinase regulatory subunit 5
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Sequence:
MGCTLSAEDKAAIERSKIIDRNLREDGEKASREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGDPARADDARQLFVLAGTAEEGVMTPELAGVICRLWRDNGVQSCFVRSREYQLNDSASYYLNDLERISQQSYMPTQQDVLRTRVKTTGIVETHFTFKELYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYSGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLIECGLY
Protein: Twitching motility protein PilT (O66950)
Organism: Aquifex aeolicus (strain VF5)
Interaction partners:
- Fimbrial assembly protein PilC
- Type 4 prepilin peptidase
- Fimbrial assembly protein PilC2
Sequence:
MFEKQEVEQKKELKILEIIKEAIELGASDIHLTAGAPPAVRIDGYIKFLKDFPRLTPEDTQKLAYSVMSEKHRQKLEENGQVDFSFGVRGVGRFRANVFYQRGSVAAALRSLPAEIPEFKKLGLPDKVLELCHRKMGLILVTGPTGSGKSTTIASMIDYINQTKSYHIITIEDPIEYVFKHKKSIVNQREVGEDTKSFADALRAALREDPDVIFVGEMRDLETVETALRAAETGHLVFGTLHTNTAIDTIHRIVDIFPLNQQEQVRIVLSFILQGIISQRLLPKIGGGRVLAYELLIPNTAIRNLIRENKLQQVYSLMQSGQAETGMQTMNQTLYKLYKQGLITLEDAMEASPDPKELERMIRGGR
Protein: Protein NDRG4 (Brain development-related molecule 1) (N-myc downstream-regulated gene 4 protein) (Vascular smooth muscle cell-associated protein 8) (SMAP-8) (Q9ULP0)
Organism: Homo sapiens (Human)
Function: Contributes to the maintenance of intracerebral BDNF levels within the normal range, which is necessary for the preservation of spatial learning and the resistance to neuronal cell death caused by ischemic stress (By similarity). May enhance growth factor-induced ERK1 and ERK2 phosphorylation, including that induced by PDGF and FGF. May attenuate NGF-promoted ELK1 phosphorylation in a microtubule-dependent manner.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12755708, ECO:0000269|PubMed:19592488}.
Interaction partners:
- Bone morphogenetic protein 3
Sequence:
MPECWDGEHDIETPYGLLHVVIRGSPKGNRPAILTYHDVGLNHKLCFNTFFNFEDMQEITKHFVVCHVDAPGQQVGASQFPQGYQFPSMEQLAAMLPSVVQHFGFKYVIGIGVGAGAYVLAKFALIFPDLVEGLVLVNIDPNGKGWIDWAATKLSGLTSTLPDTVLSHLFSQEELVNNTELVQSYRQQIGNVVNQANLQLFWNMYNSRRDLDINRPGTVPNAKTLRCPVMLVVGDNAPAEDGVVECNSKLDPTTTTFLKMADSGGLPQVTQPGKLTEAFKYFLQGMGYIAYLKDRRLSGGAVPSASMTRLARSRTASLTSASSVDGSRPQACTHSESSEGLGQVNHTMEVSC
Protein: HCLS1-associated protein X-1 (HS1-associating protein X-1) (Q5VYD6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLNFQVLSQRHLVRDYGRDRHFGTQCLSIQIVTSPGSLGGSWRVMQEVNPPNQHQTGAPRGHFIGLMMYGLWTPILEPERTMFLPVHLSPFFLWTLSLLLLHLSALPDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR
Protein: Corneodesmosin (A8K9C1)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGSSRAPWMGRVGGHGMLALLLAGLLLPGTLAKSIGTFSDPCKDPTRITSPNDPCLTGKGDSSGFSSYSGSSSSGSSISSARSSGGGSSGSSSGSSIAQGGSAGSFKPGTGYSQVSYSSGSGSSLQGASGSSQLGSSSSHSGSSGSHSGSSSHSSSSSSFQFSSSSFQVGNGSALPTNDNSYRGILNPSQPGQSSSSSQTFGVSSSGQSVSSNQRPCSSDIPDSPCSGGPIVSHSGPYIPSSHSVSGGQRPVVVVVDQHGSGAPGVVQGPPCSNGGPPGKPCPPITSVDKSYGGYEVVGGSSDSYLVPGMTYSKGKIYPVGYFTKENPVKGSPGVPSFAAGPPISEGKYFSSNPIIPSQSAASSAIAFQPVGTGGVQLCGGGSTGSKGPCSPSSSRVPSSSSISSSSGLPYHPCGSASQSPCSPPGTGSFSSSSSSQSSGKIILQPCGSKSSSSGHPCMSVSSLTLTGGPDGSPHPDPSAGAKPCGSSSAGKIPCRSIRDILAQVKPLGPQLADPEVFLPQGELLDSP
Protein: Copine-5 (Copine V) (Q9HCH3)
Organism: Homo sapiens (Human)
Function: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes (By similarity). Plays a role in dendrite formation by melanocytes.
Subcellular location: Perikaryon {ECO:0000250|UniProtKB:Q8JZW4}. Cell projection {ECO:0000250|UniProtKB:Q8JZW4}.
Interaction partners:
Sequence:
MEQPEDMASLSEFDSLAGSIPATKVEITVSCRNLLDKDMFSKSDPLCVMYTQGMENKQWREFGRTEVIDNTLNPDFVRKFIVDYFFEEKQNLRFDLYDVDSKSPDLSKHDFLGQAFCTLGEIVGSPGSRLEKPLTIGAFSLNSRTGKPMPAVSNGGVPGKKCGTIILSAEELSNCRDVATMQFCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVMKNTLNPVWQTFSIPVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFTTSYRELARGQSQFNIYEVVNPKKKMKKKKYVNSGTVTLLSFAVESECTFLDYIKGGTQINFTVAIDFTASNGNPSQSTSLHYMSPYQLNAYALALTAVGEIIQHYDSDKMFPALGFGAKLPPDGRVSHEFPLNGNQENPSCCGIDGILEAYHRSLRTVQLYGPTNFAPVVTHVARNAAAVQDGSQYSVLLIITDGVISDMAQTKEAIVNAAKLPMSIIIVGVGQAEFDAMVELDGDDVRISSRGKLAERDIVQFVPFRDYVDRTGNHVLSMARLARDVLAEIPDQLVSYMKAQGIRPRPPPAAPTHSPSQSPARTPPASPLHTHI
Protein: EEF1A lysine methyltransferase 4 (EC 2.1.1.-) (P0DPD7)
Organism: Homo sapiens (Human)
Function: Protein-lysine methyltransferase that efficiently catalyzes three successive methylations on 'Lys-36' in eukaryotic translation elongation factor 1 alpha (EEF1A1 or EEF1A2).
Interaction partners:
- Endothelin-converting enzyme 2
- EEF1A lysine methyltransferase 2
Sequence:
MASPGAGRAPPELPERNCGYREVEYWDQRYQGAADSAPYDWFGDFSSFRALLEPELRPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSSVVVAAMQARHAHVPQLRWETMDVRKLDFPSASFDVVLEKGTLDALLAGERDPWTVSSEGVHTVDQVLSEVSRVLVPGGRFISMTSAAPHFRTRHYAQAYYGWSLRHATYGSGFHFHLYLMHKGGKLSVAQLALGAQILSPPRPPTSPCFLQDSDHEDFLSAIQL
Protein: Myo-inositol transporter FST1 (W7MAT5)
Organism: Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
Function: Transporter for myo-inositol. Also appears to transport the polyketide mycotoxin fumonisin B1 (FB1). Does not appear to transport hexose sugars.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20854112, ECO:0000305|PubMed:27195938}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGKSRQNSTTTVDREKDEIQKAMGHEKAEFEALEVARHGGREIDDLIDDMERQLDEAGGLNKGFFQVQFANPKHFTWLLVAFASMGGLLSGLDQSLISGANLFLPDDLGLTEHENSLVNSGMPLGAVGGALLLSPANEYFGRKGAIIISIILYTIGAALEAGSINFGMIVSSRVILGLGVGLEGGTVPVYVAETVERRIRGNLVSLYQFNIALGEVLGYAVGAIFLNVPGNWRYILGSSLLFSTIMFFGMLFLPESPRFLIHQKRHLDAYKVWKRIRGIEDRESREEFYVMSASVVSEENAVAEGAKNHRFPWMDFFTEPRARRALVYANIMILLGQLTGVNAIMYYMSVLMNQIGFDKKESNYMSLVGGGSLLLGTIPAIFLMERFGRRFWAITMLPGFFIGLVLIGVSYQFDVETQLQTVEGLYLSGLIIYMGFFGSYACLTWVVPSEVYPTYLRSYGMTTSDALLFLASFIVTYNFTAMQNAMGKTGLALGFYGGIAFIGEIYQIFFMPETKNKTLEEIDVVFSRPTMDIVRENWAGVKETTHLLLTGHWHKVFVEQAMTDPKDQVQVSHA
Protein: Negative elongation factor D (Q24134)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex, causes transcriptional pausing.
Subcellular location: Nucleus {ECO:0000269|PubMed:12782658}. Chromosome {ECO:0000269|PubMed:12782658}. Note=Associates with polytene chromosomes. Associates with the hsp70 promoter when it is inactive, but not when it is activated. The NELF complex possibly dissociates from chromatin following phosphorylation of RNA polymerase II.
Interaction partners:
- Negative elongation factor B
- Negative elongation factor E
- Negative elongation factor A
- Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MEVEYDDSGWQGRAKGQTNPEETLEDNPQKTIQECLEKFLTPDYIMEPGIFTQLKRYFQSGGSPEEVISMLSENYKAVAQMANLLAEWLILAGVKVTEVQAMVENHLKEMILKSFDPKKADTIFTEEGETPDWLTEMIDHYTWRSLIYRLAEEYPDCLMLNFTIKLISDAGFQSEITSISTAAQQIEVFSRVLKTSIVKFLNNPDDVHGAIQECARMVCHGQHTYVYSQVLIQVLSQEQKGGFNMKRLSQEIIKYALQNNQNVTPITMALNGSAVYPQACQALTSMLTRNTLNPADITVLFRNYSGSDPPPIDLIRNPQFLELLVDALFRSGVKINPEHKPKYMFLLAYASAVIDQPAKKRPMTERMLNKEELKSTIQAIEKAHTICNVDQGSTELIAELQTLYNCIKYPVVGVGVIRWIENVVMEPSYFKLSTDSCPTHLAVLDEVAAVHPTLQQQILFLLIRLFESKQDELEILVQLEMKKMILDRMVNLLTRGCVVPVLRYIKQCCAIEDTDISLIRYFVTEVLETITHPYSPEFVQLFLPMVENEEITGTMRGEGDNDPVSEFIVHCKAHYTTV
Protein: 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2) (Q63347)
Organism: Rattus norvegicus (Rat)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC2 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P35998}. Note=Colocalizes with TRIM5 in cytoplasmic bodies. {ECO:0000250|UniProtKB:P35998}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 2
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 10B
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 8
- Proteasome
Sequence:
MPDYLGADQRKTKEDEKDDKPIRALDEGDIALLKTYGQSTYSRQIKQVEDDIQQLLKKINELTGIKESDTGLAPPALWDLAADKQTLQSEQPLQVARCTKIINADSEDPKYIINVKQFAKFVVDLSDQVAPTDIEEGMRVGVDRNKYQIHIPLPPKIDPTVTMMQVEEKPDVTYSDVGGCKEQIEKLREVVETPLLHPERFVNLGIEPPKGVLLFGPPGTGKTLCARAVANRTDACFIPVIGSELVQKYVGEGARMVRELFEMARTKKACLIFFDEIDAIGGARFDDGAGGDNEVQRTMLELINQLDGFDPRGNIKVLMATNRPDTLDPALMRPGRLDRKIEFSLPDLEGRTHIFKIHARSMSVERDIRFELLARLCPNSTGAEIRSVCTEAGMFAIRARRKIATEKDFLEAVNKVIKSYAKFSATPRYMTYN
Protein: Acyl-homoserine lactone acylase QuiP (AHL acylase QuiP) (Acyl-HSL acylase QuiP) (EC 3.5.1.97) (Quorum signal utilization and inactivation protein) [Cleaved into: Acyl-homoserine lactone acylase QuiP subunit alpha (Acyl-HSL acylase QuiP subunit alpha); Acyl-homoserine lactone acylase QuiP subunit beta (Acyl-HSL acylase QuiP subunit beta)] (Q9I4U2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the deacylation of acyl-homoserine lactone (AHL or acyl-HSL), releasing homoserine lactone (HSL) and the corresponding fatty acid. Possesses a specificity for the degradation of long-chain acyl-HSLs (side chains of seven or more carbons in length). Appears to be the acyl-HSL acylase that underlies the ability of P.aeruginosa to degrade and utilize certain acyl-HSLs as growth nutrients, including one of its own quorum signals, 3-oxo-C12-HSL. Is thought to have a role in quorum quenching.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MASPAFMRFLPRCGAAAAFGTLLGLAGCQSWLDDRYADSLPPTSGVQPIKGLAQNVSIRRNALGMPLIETGTFHDALFALGYVHASDRLSQMVSLRLLAQGRLAEMVGPGALEIDRFMRTVNLRQAAEIQYRNASPRLQRFFEVYARGVNAYLYRYRDKLPMDLAQSGYRPEYWKPEDSALVFALLNFGLAVNLQEEIASLTLAQKVGSDKLAWLTPTYPDENLPFDEAEKLKGLRLDGQVPGLAGVEGAARQVAALSMLGVAASNNWAIAPQRSRSGKSLMANDTHLPLSMPSVWNYVQIRSPKYQAAGVSIAGLPGVVAGFNGKLAWGMTMVLGDNQDLYLEQLRRQGNRLYYLADGKWQPTRERQETFFIKGQRPIREVIHETRHGPLLNSALGERKNILQPLPLKSGYGLAYRSIQQEADKTLDGFFDLSRAKTIEQAFDATREIRAMPLNIVFADEKHIGWQVTGRYPNRKEGRGLLPSPGWDGRYDWDGYADPILHPSDQDPQQGWLGTANHRTVQPGYGAQLSNSWYYPERAERIAQLAGASKSHDTQSMIRMQYDQTSLFVAKLQAMFDNPGMALPLRQAIDALPEAQRSRAREAYDRLMAFDGKLTASSSDAALYGAFLHESARQIFLDELGPEDGPAWKAFVETANLSYSAQADHLLGRDDSPFWDDTRTPQKEDKPAILARSLAAAVEFCEQRLGSERKAWQWGKLHTYEWQSDSSKMAPYLGAGERAGLGAIKGYLDRGPYPAGGDHTTLDVSAYGWGQDFDTWLIPAMRLIVDFGQSEPMIGVNSSGQSGNPASPHYADGIDAWLKGRYVSFPFQPQNLDRVYGNKRLTLTPAR