wanglab/gogpt-training-data huggingface dataset:
Protein: Ribonuclease P protein component (RNase P protein) (RNaseP protein) (EC 3.1.26.5) (Protein C5) (P0A7Y8)
Organism: Escherichia coli (strain K12)
Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
Interaction partners:
- Large ribosomal subunit protein bL34
- Putative membrane protein insertion efficiency factor
- Membrane protein insertase YidC
- Ribonuclease E
- Small ribosomal subunit protein uS10
- Beta sliding clamp
- Chromosomal replication initiator protein DnaA
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein bS20
- Small ribosomal subunit protein uS12
Sequence:
MVKLAFPRELRLLTPSQFTFVFQQPQRAGTPQITILGRLNSLGHPRIGLTVAKKNVRRAHERNRIKRLTRESFRLRQHELPAMDFVVVAKKGVADLDNRALSEALEKLWRRHCRLARGS
Protein: 205 kDa microtubule-associated protein (P23226)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play an important role in the regulation of microtubule assembly and interaction.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Note=Associated with cytoplasmic microtubules and with the mitotic spindle.
Interaction partners:
- Serine/threonine-protein kinase polo
- Protein salivary glands marred
Sequence:
MEHHEDNAQLDNYLQNRLAESLQICGGAGEHNPHLADATGGNGCAPGIAPSKSDEVDGEEDEEWKYIHEVRQSEKLQQEKLPLTKETGNGFGPGRDSDNQVHGNGAAAVFNLYEEDVEVIKNDGDFSTNSNTTTSTDEVVARQAQEPNQLPEQLQQQQQIESQGVHEDPRQEDEDEHSSVATTYGTSSLSENNSSPLDQEEVVMVAQTVGQEQLVDFDNKENSYFVKNLEENHSQLNPNAVAFVPGVGSQSSSPLPAAEDPLPGVQPRPFLPGGTLDDLVAESPRKEFARINMDGIAVPDEREFDIEADMRPHELEQESDTFGAGHLEMQLLNGIGTADQAALRDVLDHGPETSVDMELPLDQVPNDADIMKQSIYAEHNSSIEDILNSVQPLPIQTCDDKELIHVEEKEHVSKSPSTEELQFQSDFPNNQESHTLFNNTEQDPMQASFYLEHTSQKAQEGCQEQMQLPAECSDIFADQSLLLDTSAPQLSSEADSPVAKLELESQQAGIVDITPSPLSSTAEKHLVEDTKELVEEYTLDPESHFFGVVSSQAPLQLFGKHTLPSIIHSCKHRVASEQNDEENAVFESVSGYETQNFDEISSPPEGINPFAQPFTPAHLVIEQANTMMEDVGGMPIPASEDFAICDKVASKSSNEVEDHRSEQQAFVKEELLHPVGDVVAQVENLGTEKNFVVEEERLPISVSDEIPLSSASKEKLLPDTTDEQLLTSALEEKLRSVAPEESVSTAADGQSISQFDEYVIASNKPLEDILEPEKDVEVAKSLSEKTSVATVAGGAVVGATKTHSATKAGSTAASAKSKTETLVMKKTTASSTSVYGANKSAAPRPSTARLGIKSTSIATKTSTTSSLTGNPRKSLSSNVGSTVKPPTKLSGTRPATAPVSKVTLGAKTITNKPTASGTASDNVTRTTLRPLVSTNARRPATSGTGSVASSTARRPVTNAKGSAPGSAASTKVRPAATMTAPVKPKVLSPRSTISSTTTVRKVPSTSTPSFSTRSPNKQQSNGLGKNTSSTTTSTATATITKSFTARSAPKFTHSASLTYNNGSTSRRLLVPGSSSTTTTSSLRKSSPLKAAPGKAASKPLTPQSKDGTAKSSPAVLKARNSTLMGGEGVAPSNECVPTPNGQINAEEVVKLKGKGLAEEVKIIEEQKLHEQDVPAHNAEVPLLDF
Protein: GEO07743p1 (RE41137p) (Ring finger protein 11, isoform A) (Q8SX35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin-conjugating enzyme E2 N
Sequence:
MGNCLKISTSDDISLLRGNDSQISGTQPVYHQGEHYQRELYPSTSSSTTLTPSSNNRQLSDENQVKIAKRIGLMQYLPIGTYDGSSKKARECVICMAEFCVNEAVRYLPCMHIYHVNCIDDWLLRSLTCPSCLEPVDAALLTSYEST
Protein: GAG1At protein (T24D18.10 protein) (P93048)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Thermosome subunit gamma
- Transmembrane protein
- Transmembrane protein
- Transmembrane protein
- AT3g62190/T17J13_150
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- 22 kDa peroxisomal membrane protein
- At3g63160
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Branched-chain-amino-acid aminotransferase 3, chloroplastic
Sequence:
MGNETKTNGGPASMAGGGGFRAKMEHYVYSGEKKHVLVGIGIVTIIFGVPWYLMTQGSKHQSHQDYMDKADKARKARLSSSSSANK
Protein: KH domain-containing protein 3 (ES cell-associated transcript 1 protein) (KHDC3-like protein) (F6SZT2)
Organism: Macaca mulatta (Rhesus macaque)
Function: As part of the OOEP-KHDC3 scaffold, recruits BLM and TRIM25 to DNA replication forks, thereby promoting the ubiquitination of BLM by TRIM25, enhancing BLM retainment at replication forks and therefore promoting stalled replication fork restart. Regulates homologous recombination-mediated DNA repair via recruitment of RAD51 to sites of DNA double-strand breaks, and sustainment of PARP1 activity, which in turn modulates downstream ATM activation. Activation of ATM or ATR in response to DNA double-strand breaks may be cell-type specific (By similarity). Its role in DNA double-strand break repair is independent of its role in restarting stalled replication forks (By similarity). As a member of the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for maintenance of euploidy during cleavage-stage embryogenesis (By similarity). Required for the formation of F-actin cytoplasmic lattices in oocytes which in turn are responsible for symmetric division of zygotes via the regulation of mitotic spindle formation and positioning (By similarity). Ensures proper spindle assembly by regulating the localization of AURKA via RHOA signaling and of PLK1 via a RHOA-independent process (By similarity). Required for the localization of MAD2L1 to kinetochores to enable spindle assembly checkpoint function (By similarity). Promotes neural stem cell neurogenesis and neuronal differentiation in the hippocampus. May regulate normal development of learning, memory and anxiety (By similarity). Capable of binding RNA (By similarity).
Subcellular location: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9CWU5}. Nucleus {ECO:0000250|UniProtKB:Q9CWU5}. Mitochondrion {ECO:0000250|UniProtKB:Q9CWU5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9CWU5}. Chromosome {ECO:0000250|UniProtKB:Q587J8}. Note=Localized to centrosomes during interphase and mitosis (By similarity). Localizes to sites of DNA double-strand break repair (By similarity). {ECO:0000250|UniProtKB:Q587J8, ECO:0000250|UniProtKB:Q9CWU5}.
Interaction partners:
- Transducin-like enhancer protein 6
- NLR family pyrin domain containing 5
- Oocyte-expressed protein homolog
Sequence:
MDTPRRFPTLVQLMQPKAMPVEVLGHLPKRFSWFHSEFLKNPKVVRLEVWLVEKIFGRDRERIPHVQGMSQILIHVNRLDPNGEAEILVFGRPSYQEDTIKMIMNLADYHRQLQAKGSGKALAQDVATKKAEIQLSSTEVREAGTQRSVEVREVGTQGSPVEVRETGTQQSLEAANQSGTQRSPEAASKAVTQRFSEDTRAPVTRL
Protein: Ciliary microtubule inner protein 2C (A6NJV1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q9DAS2}.
Interaction partners:
- Cilia- and flagella-associated protein 161
- Cilia- and flagella-associated protein 276
- Protein Flattop
- Tektin-1
- Cilia- and flagella-associated protein 52
- Tektin-2
- Cilia- and flagella-associated protein 107
- Cilia- and flagella-associated protein 144
- Cilia- and flagella-associated protein 95
- Cilia- and flagella-associated protein 45
Sequence:
MASRSAGTLLTEFNAAYVPPGLMPGYQGHVPTVAFSFGAPYGTTTLKYFQDHRNRAMEKSHTPFSQGGHFPTIFSTNPNLLLMERASTRDRWLHKPSYTRFNLDSHRSTELTNFYQMVQQHRKYYQDKTGTVPRVPYFAMPVREPERYPLPTVLPPLCPKKKWHLLRLAPENLKTYQTFPSGKRVSPQERKKRDCYFEFRA
Protein: Glideosome associated protein with multiple membrane spans 3 (Q8IM26)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MWFTTRQDGLDDNCHTNRGPCFQISGFFGTTLRIGFFLEFIALTFLFMSYWSNGGKGLFSYDLKNINDEYRLDQTFRNSITLWTGVYLIGAIFIMSFQVLLADDTCWARGYRAGSKILRLASFLDTISATLQFIFYLYISKFYTRKWYVHFNEGGSEWVFFIFVRLVHAFSCLLYGLAAYLLEVYHDEGAGDLHAYINGVMFVFAGLTEIFVIFCNSGCYSNLLLWLALGAVSLWSYYFEPEVNHVSPALHETELTNDVEQQVEKFSRYTPYPQDTNQNAYYPA
Protein: PilO protein (Pilus assembly protein, PilO) (Type 4 fimbrial biogenesis protein PilO) (Type 4a pilus biogenesis protein PilO) (Q51353)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MSLASSLESLRKIDINDLDLNNIGSWPAAVKVIVCVLLTAAVLALGYNFHLSDMQAQLEQQAAEEETLKQQFSTKAFQAANLEAYKAQMKEMEESFGALLRQLPSDTEVPGLLEDITRTGLGSGLEFEEIKLLPEVAQQFYIELPIQISVVGGYHDLATFVSGVSSLPRIVTLHDFEIKPVAPGSTSKLRMSILAKTYRYNDKGLKK
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (E7EPS8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MPSGSFMLVNASGRPEGQRAHLLLPQLKENDTHCIDFHYFVSSKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWPNFYQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKEIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYLWIQLNANSINGDGPIVAREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTRPGEGGTGSPGPALRTRTKCADPMRGPRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLTVHYCYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILMNPEGRKESQELIVQTDEDLPGAVPTESIQGSTFEEKIFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNQSGRVSKLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATNQFTTKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERPRRTKKTTEILKCYPVPIHFQNASLLNSQYYFAAEFPADSLQAAQPFTIGDNKTYNGYWNTPLLPYKSYRIYFQAASRANGETKIDCVQVATKGAATPKPVPEPEKQTDHTVKIAGVIAGILLFVIIFLGVVLVMKKRKLAKKRKETMSSTRQEMTVMVNSMDKSYAEQGTNCDEAFSFMDTHNLNGRSVSSPSSFTMKTNTLSTSVPNSYYPDETHTMASDTSSLVQSHTYKKREPADVPYQTGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLNMVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNSG
Protein: Septin and tuftelin-interacting protein 1 homolog 1 (Nineteen complex-related protein 1 homolog) (AtNTR1) (Protein SPLICEOSOMAL TIMEKEEPER LOCUS 1) (Q9SHG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events (By similarity). Involved in snRNPs recycling. Required for efficient splicing of genes that act within the plant circadian clock. Part of a transcription elongation checkpoint at alternative exons. Required for correct expression and splicing of DOG1, a regulator of seed dormancy. May induce transient transcriptional pausing of polymerase II at slices sites.
Subcellular location: Nucleus {ECO:0000269|PubMed:23110899, ECO:0000269|PubMed:25568310}. Note=Excluded from the nucleolus. Co-localizes with polymerase II. {ECO:0000269|PubMed:25568310}.
Interaction partners:
- SNW/SKI-interacting protein
- Pre-mRNA-splicing factor SYF2
- Tetratricopeptide repeat
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH3
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH2
- U2 small nuclear ribonucleoprotein A'
- RNA helicase
- Protein pleiotropic regulatory locus 1
- Crooked neck protein, putative / cell cycle protein
- Pre-mRNA-processing factor 17
Sequence:
MDEYQDMERFSMDNDYEGGRWEGDEFVYQKRKEKRKQTKNDATYGIFAESDSDSDDSGGGGSRRKRRKDRDSGRKADLTKPVNFVSTGTVMPNQEIDKDSREHNDEKDRDKIEDNDMIDEDVEVRGGLGIGSSGLGLGFNANGFDDEDNLLPGALGKKIADRAKMRGKAKVEKRGQEGGGAKGGKKNTLGSDIGQFEKSTKGIGMKLLEKMGYKGGGLGKNQQGIVAPIEAQLRPKNMGMGYNDFKEAKLPDLKKVEEKKIIGVSVSENEQSHGDRGGKNLWKKKKVRKAVYVTAEELLEKKQEAGFGGGQTIIDMRGPQVRVVTNLENLDAEEKAKEADVPMPELQHNLRLIVDLVEHEIQKIDRDLRNERESALSLQQEKEMLINEEEKQKRHLENMEYIADEISRIELENTSGNLTLDSLAIRFEDLQTSYPDDYKLCSLSTIACSLALPLFIRMFQGWDPLSDAVHGLKAISSWRKLLEVEEDHNIWVVSTPYSQLVSEVVLPAVRIAGINTWEPRDPEPMLRFLETWETLLPSSVLQTILDTVVLPKLSTAVEYWDPRRELVAIHVWVHPWLPILGQKLEFLYQIIQMKLSNVLDAWHPSDSSAYTILSPWKTVFDTTSWEQLMRRYIVPKLQLALQEFQVNPANQNLERFDWVMKWASAVPIHLMADMMERFFFPKWLDVLYHWLRAKPRFEEIQGWYYGWKELFPQELTANERIRIQLKRGLDMLMEAVEGVEVSQPRAKANERTQSVPAQAQAQAKAQMDSTEVLSLKEVLEVFAQEQELLFKPKPNRMHNGLQIYGFGNVSVIIDSVNQKLLAQKDGGWFLVTPDDLLRMHNNTTVSAKR
Protein: Solute carrier organic anion transporter family member 1A5 (Organic anion-transporting polypeptide 3) (OATP-3) (Sodium-independent organic anion transporter 3) (Solute carrier family 21 member 7) (O88397)
Organism: Rattus norvegicus (Rat)
Function: Na(+)-independent transporter that mediates the cellular uptake of a broad range of organic anions such as the endogenous bile salts cholate and deoxycholate, either in their unconjugated or conjugated forms (taurocholate and glycocholate), estrone 3-sulfate and prostaglandin E2, at the plasma membrane. Responsible for intestinal absorption of bile acids. Capable of thyroid hormone transport (both T3 or 3,3',5'-triiodo-L-thyronine, and T4 or L-tyroxine). Plays roles in blood-brain and -cerebrospinal fluid barrier transport of organic anions and signal mediators, and in hormone uptake by neural cells (By similarity). May also play a role in the reuptake of neuropeptides such as substance P/TAC1 and vasoactive intestinal peptide/VIP released from retinal neurons (By similarity). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment. Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions. May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P46721}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:P46721}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Solute carrier family 22 member 7
Sequence:
MGETEKRVATHEVRCFSKIKMFLLALTWAYVSKSLSGIYMNTMLTQIERQFDIPTSIVGFINGSFEIGNLLLIIFVSYFGTKLHRPIMIGVGCVIMGLGCFLMSLPHFLMGRYEYETTISPTSNLSSNSFLCMENRSQTLKPTQDPAECIKEMKSLMWIYVLVGNIIRGIGETPIMPLGISYIEDFAKSENSPLYIGILETGKVFGPIVGLLLGSFCASIYVDTGSVNTDDLTITPTDTRWVGAWWIGFLICAGVNILSSIPFFFFPKTLPKEGLQDDVDGTNNDKEEKHREKAKEENRGITKDFLPFMKSLSCNPIYMLLILTSVLQINAFINMFTFLPKYLEQQYGKSTAEVVLLIGVYNLPPICIGYLLIGFIMKKFKITVKKAAYMAFCLSLFEYLLYFLHFMITCDNFPVAGLTASYEGVHHPLYVENKVLADCNRGCSCSTNSWDPVCGDNGLAYMSACLAGCKKSVGTGTNMVFQNCSCIRSSGNSSAVLGLCKKGPECANKLQYFLIMSVIGSFIYSITAIPGYMVLLRCIKPEEKSLGIGLHAFCTRVFAGIPAPIYFGALIDRTCLHWGTLKCGEPGACRMYNINNFRRIYLVLPAALRGSSYLPALFILILMRKFQFPGEIDSSETELAEMKITVKKSECTDVHGSPQVENDGELKTRL
Protein: Thromboxane A2 receptor (TXA2-R) (Prostanoid TP receptor) (P21731)
Organism: Homo sapiens (Human)
Function: Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Angio-associated migratory cell protein
- Guanine nucleotide-binding protein subunit alpha-11
- Calcium-activated potassium channel subunit alpha-1
- Prostacyclin receptor
- Alpha-1B adrenergic receptor
- Trifunctional enzyme subunit beta, mitochondrial
- Alpha-1D adrenergic receptor
- Guanine nucleotide-binding protein subunit alpha-12
Sequence:
MWPNGSSLGPCFRPTNITLEERRLIASPWFAASFCVVGLASNLLALSVLAGARQGGSHTRSSFLTFLCGLVLTDFLGLLVTGTIVVSQHAALFEWHAVDPGCRLCRFMGVVMIFFGLSPLLLGAAMASERYLGITRPFSRPAVASQRRAWATVGLVWAAALALGLLPLLGVGRYTVQYPGSWCFLTLGAESGDVAFGLLFSMLGGLSVGLSFLLNTVSVATLCHVYHGQEAAQQRPRDSEVEMMAQLLGIMVVASVCWLPLLVFIAQTVLRNPPAMSPAGQLSRTTEKELLIYLRVATWNQILDPWVYILFRRAVLRRLQPRLSTRPRSLSLQPQLTQRSGLQ
Protein: Protein LSM14 homolog B-A (RNA-associated protein 46) (xRAP46) (RNA-associated protein 55B-A) (RAP55B-A) (xRAP55B) (Q68FI1)
Organism: Xenopus laevis (African clawed frog)
Function: May be involved in the storage of translationally inactive mRNAs and protect them from degradation (By similarity). Plays a role in control of mRNA translation.
Interaction partners:
Sequence:
MSSGTPYIGSKISLISKAQIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPAPPREEVYEYIIFRGSDIKDITVCEPPKASHALPQDPAIVQSSLGSAPAASYQPSVPYSPFRGMPTYSQLAATSLLSQQYAASLGLEKLGSPTASAGASSSCSSPSPQPVAPEPDVPAEPPQLSQNAGYPSIPVRKSPMVEQAVQTGPLENQAQKKVQQAKGAPVGQRGVRQSGPQSQPAPLNVPPPAAPVLGTINDENRRPPRRRSGNRRTRNRSRGQNRPTTVKENPIKFEGDFDFETANAQFNREELDKEFKDKLNFKEEKPEKEGEEKTDSGVETQNSDGNPEEDPLGPNTYYDRSKSFFDNISSEMKSRRTTWAEERKLNTETFGVSGRFLRGRSFRGGFRGGRGSAAPRRNQTTQRAGTGRV
Protein: Protein-associating with the carboxyl-terminal domain of ezrin (Ezrin-binding protein PACE-1) (SCY1-like protein 3) (Q9DBQ7)
Organism: Mus musculus (Mouse)
Function: May play a role in regulating cell adhesion/migration complexes in migrating cells.
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Colocalized with EZR/VIL2, actin and CD44 in lamellipodia. {ECO:0000250}.
Interaction partners:
Sequence:
MGSENSALKSYTLRESPFTLPSGLAVYPAILQDGKCASVFVYKRENEDKVNKAAKHLKTLRHPCLLRFLSCTVEADGIHLVTERVQPLEVALETLSPAEVCAGIYDILLALIFLHDRGHLTHNNVCLSSVFVSEDGHWKLGGMETVCQVPQATPEFLRNIQSVRDPASIPPEEMSPEFSGLPESHGHARDAYAFGALVDSLLPIFNEQVSADVLSSFLQILHSALLNPMPECRPALSTLLSHDFFRNDFLEVVNFLKSLTLKSEDEKTEFFKFLLDRVSCLSEELIASRLVPLLLNQLVFAEPVAVKSFLPYLLGPKKENAPGETPCLLSPALFQSRVIPVLLRLFEVHEEHVRMVLLSHIEAYVEHFTQEQLKKVILPQVLLGLRDTSNSIVAITLRSLAVLVSLLGPEVVVGGERTKIFKRTAPSFTKTSDLSPEGSPMHVVCSQQSRVSKVLEDPSSNVFPKWLSGNVPSSSRKRIQEECYSSLSQTGDQFSHTIKFPMNGLSDVKNTSEDNGSFPAGSNKPEEWPDWSEPEEPEQQPASIHRWPREPCDVAESQHTNLTAEEVTWDDGEASFGTEINSTATASAPVPVTSGGQSTSAALVPLTEESKPLQSSPSSKTSHRQHEEVKPPQVSQERPLKAPSGLGLGEEFTIQVKKKPVQDPELDWFADMIPEIKPSGTFLILPELRTEVMVPDKDNVSSLMQFSSKFAATEMTEGEAEGWEGEELAWEDNNW
Protein: Calmodulin (CaM) (P62157)
Organism: Bos taurus (Bovine)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250}.
Interaction partners:
- Ryanodine receptor 2
- Ryanodine receptor 1.
- Nitric oxide synthase 3
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Ras GTPase-activating-like protein IQGAP1
- Nitric oxide synthase, inducible
- calcium/calmodulin-dependent protein kinase
- calcium/calmodulin-dependent protein kinase
- Protein phosphatase 3 catalytic subunit alpha
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Protein HEXIM1 (Cardiac lineage protein 1) (Q8R409)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. Core component of the 7SK RNP complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O94992}. Cytoplasm {ECO:0000250|UniProtKB:O94992}. Note=Binds alpha-importin and is mostly nuclear. {ECO:0000250|UniProtKB:O94992}.
Interaction partners:
- La-related protein 7
- 7SK snRNA methylphosphate capping enzyme
- Cyclin-dependent kinase 9
- Cyclin-T1
- Cyclin-T2
- Protein HEXIM2
- Bromodomain-containing protein 4
- B-cell lymphoma/leukemia 11B
- Polyglutamine-binding protein 1
- AF4/FMR2 family member 1
Sequence:
MAEPLLTEHQHQPQTSNCTGAAVVHEEHTSERPPSAEERVPKEDSRWQSRASLQSGSRPGQEGEGGLKHQLPPLQTNACPELSSLEKGEKGQNGEDLSTGGASPSAEGEPMSESLVQPGHDSEATKQEAPAAGGEEPWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRVRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYPKRAAAKSDDTSDEDFVEEAGEEDGGSDGMGGDGSEFLQRDFSETYERYHAESLQNMSKQELIKEYLELEKCLSRKEDENNRLRLESKRLGGVDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD
Protein: Type III secretion target, YopN family (Q72WI3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
Sequence:
MSIDLRGVSGPAQPGLANVQDGPDGAAGTLLGRAATVVDSPLSLLADAAEELTFAADTTDDFELSERKERKSTEDAMAERIELYKELMHQAGKGEGLDRLKDSLKSQQGREQARQEALSQFPDPSDAWAALHDALQAFDDDPAIPDGVREAVRGAIADLEAEHGPAIRAGVHGALASAGFADLGDADALRDLYRGTVCDFTTVEQVFATINERYGDERFDVAIGFLYRALSSDLGSDMPSMDGTHLESVNTSLGQLRLLKSAHALCADVMTRWENVHGVKDCPLTAQGLLEQVVALRSENFLGALHIDRIAAQAKAPDIEHEVLFLQELLRMTRNVPAQLFDGTAGRMKLLDAVQDAVDRAIDREDAFLAAQEG
Protein: (-)-alpha-pinene synthase 2, chloroplastic (EC 4.2.3.119) ((-)-(1S,5S)-pinene synthase) ((-)-beta-pinene synthase 2) (EC 4.2.3.120) (Beta-geraniolene synthase) (Pinene synthase, chloroplastic) (PsTPS2) (Q6XDB5)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in monoterpene (C10) olefins biosynthesis. A mixture of alpha- and beta-pinene (35:10) is produced by this enzyme.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MALVSVAPMASRSCLHKSLSSSAHELKTICRTIPTLGMSRRGKSATPSMSMSLTTTVSDDGVQRRMGDFHSNLWNDDFIQSLSTSYGEPSYRERAERLIGEVKKMFNSMSSEDGELISPHNDLIQRVWMVDSVERLGIERHFKNEIKSALDYVYSYWSEKGIGCGRESVVADLNSTALGFRTLRLHGYAVSADVLNLFKDQNGQFACSPSQTEEEIRSVLNLYRASLIAFPGEKVMEEAEIFSAKYLEESLQKISVSSLSQEIRDVLEYGWHTYLPRMEARNHIDVFGQDTQNSKSCINTEKLLELAKLEFNIFHSLQKRELEYLVRWWKDSGSPQMTFCRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITILDDMYDTFGTVDELELFTAAMKRWDPSAADCLPEYMKGVYLILYDTVNETSREAEKAQGRDTLDYARRAWDDYLDSYMQEAKWIATGYLPTFAEYYENGKVSSGHRTSALQPILTMDIPFPPHILKEVDFPSKLNDLASAILRLRGDTRCYKADRARGEEASSISCYMKDNPGATEEDALDHINAMISDVIRGLNWELLNPNSSVPISSKKHVFDISRAFHYGYKYRDGYSVANIETKSLVRRTVIDPVTL
Protein: Transcription antiterminator LicT (P39805)
Organism: Bacillus subtilis (strain 168)
Function: Mediates positive regulation of the glucanase operon (licST) by functioning as an antiterminator factor of transcription. Prevents termination at terminator lic-t.
Interaction partners:
- PTS system beta-glucoside-specific EIIBCA component
- Aryl-phospho-beta-D-glucosidase BglH
- Beta-glucanase
- Transcriptional regulatory protein LevR
- PTS system sucrose-specific EIIBC component
- DNA-binding transcriptional repressor ScoC
- Mannitol-specific phosphotransferase enzyme IIA component
- PTS system glucose-specific EIICBA component
- Probable PTS system sucrose-specific EIIBC component
- Hut operon positive regulatory protein
Sequence:
MKIAKVINNNVISVVNEQGKELVVMGRGLAFQKKSGDDVDEARIEKVFTLDNKDVSEKFKTLLYDIPIECMEVSEEIISYAKLQLGKKLNDSIYVSLTDHINFAIQRNQKGLDIKNALLWETKRLYKDEFAIGKEALVMVKNKTGVSLPEDEAGFIALHIVNAELNEEMPNIINITKVMQEILSIVKYHFKIEFNEESLHYYRFVTHLKFFAQRLFNGTHMESQDDFLLDTVKEKYHRAYECTKKIQTYIEREYEHKLTSDELLYLTIHIERVVKQA