wanglab/gogpt-training-data huggingface dataset:
Protein: Tubby like protein 8 (F4I2T3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAGSRKVNDLLEENKGNVDTITGSLSTQKGEDKENVSPEKVSTSVETRKLDRALKSQSMKGNSGFPTEVTNFKSFSTGGRTALKQSSLQACMQKNSEVDKSSFGMKTWTSVDSEHSSSLKVWEFSDSEAAPASSWSTLPNRALLCKTLPLDVGRCTCLIVKEQSPEGLSHGSVYSLYTHEGRGRKDRKLAVAYHSRRNGKSIFRVAQNVKGLLCSSDESYVGSMTANLLGSKYYIWDKGVRVGSVGKMVKPLLSVVIFTPTITTWTGSYRRMRTLLPKQQPMQKNNNKQVQQASKLPLDWLENKEKIQKLCSRIPHYNKISKQHELDFRDRGRTGLRIQSSVKNFQLTLTVHFHNFKALIKNQSQES
Protein: Tyrosine-protein kinase receptor TYRO3 (EC 2.7.10.1) (Tyrosine-protein kinase SKY) (P55146)
Organism: Rattus norvegicus (Rat)
Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3 (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Growth arrest-specific protein 6
- Vitamin K-dependent protein S
Sequence:
MALRRSMGRPGLRPLLLAGLASLLLPGSAAAGLKLMGAPVKMTVSQGQPVKLNCSVEGMDDPDIHWMKDGAVVQNASQVSISISEQNWIGLLSLKSAERSDAGLYWCQVKDGEETKISQSVWLTVEGVPFFTVEPKDLAVPPNVPFQLSCEAVGPPEPVTIFWWRGPTKVGGPASSPSVLNVTGVTQRTEFSCEAHNIKGLATSRPAIIRLQAPPAAPFNITVTTISSSNASVAWVPGADGLALLHSCTVQVAHAPGEWEALAVVVPVPPFTCLLRNLAPATNYSLRVRCANALGPSPYGDWVPFQTKGLAPARAPQNFHAIRTDSGLILEWEEVIPEDPGEGPLGPYKLSWVQENGTQDELMVEGTTANLTDWDPQKDLVLRVCASNAIGDGPWSQPLVVSSHDHAGRQGPPHSRTSWVPVVLGVLTALITAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKEKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLASRIGENPFNLPLQTLVRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVHSDVWAFGVTMWEIMTRGQTPYAGIENAEIYNYLISGNRLKQPPECMEEVYDLMYQCWSADPKQRPSFTCLRMELENILGHLSVLSTSQDPLYINIERAGQPAENGSPELPCGEQSSSEAGDGSGMGAIGGIPSDCRYIFSPGGLAESPGQLEQQPESPLNENQRLLLLQQGLLPHSSC
Protein: Transcriptional regulatory protein PmpR (Q51423)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in regulation of the quinolone signal (PQS) system and of pyocyanine production. Negatively regulates the quorum-sensing response regulator pqsR of the PQS system by binding to its promoter region.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00693}.
Interaction partners:
- Crossover junction endodeoxyribonuclease RuvC
- Aspartate--tRNA
- Holliday junction branch migration complex subunit RuvA
Sequence:
MAGHSKWANIKHRKERQDAKKGKIFTKLIRELTVAARQGGGVPADNPRLRLAVDKALTANMTRDTIDRAIARGVGSNDADNMVELSYEGYAPSGVAIIVEAMTDNRNRTAAEVRHAFSKCGGNLGTDGSVAYMFERKGQISFAPGVDEEALMDAALEAGADDVVVNDDGSIDVFTTFADFISVNEALAAAGFKGDEAEVTMIPSTTATLDLETAQKVLKLIDMLEDLDDVQNVYSNADIPDDVMAQLG
Protein: RNA binding motif protein 28 isoform 1 (A0A024R753)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGLTLFVGRLPPSARSEQLEELFSQVGPVKQCFVVTEKGSKACRGFGYVTFSMLEDVQRALKEITTFEGCKINVTVAKKKLRNKTKEKGKNENSECPKKEPKAKKAKVADKKARLIIRNLSFKCSEDDLKTVFAQFGAVLEVNIPRKPDGKMRGFGFVQFKNLLEAGKALKGMNMKEIKGRTVAVDWAVAKDKYKDTQSVSAIGEEKSHESKHQESVKKKGREEEDMEEEENDDDDDDDDEEDGVFDDEDEEEENIESKVTKPVQIQKRAVKRPAPAKSSDHSEEDSDLEESDSIDDGEELAQSDTSTEEQEDKAVQVSNKKKRKLPSDVNEGKTVFIRNLSFDSEEEELGELLQQFGELKYVRIVLHPDTEHSKGCAFAQFMTQEAAQKCLLAASPENEAGGLKLDGRQLKVDLAVTRDEAAKLQTTKVKKPTGTRNLYLAREGLIRAGTKAAEGVSAADMAKRERFELLKHQKLKDQNIFVSRTRLCLHNLPKAVDDKQLRKLLLSATSGEKGVRIKECRVMRDLKGVHGNMKGQSLGYAFAEFQEHEHALKALRLINNNPEIFGPLKRPIVEFSLEDRRKLKMKELRIQRSLQKMRSKPATGEPQKGQPEPAKDQQQKAAQHHTEEQSKVPPEQKRKAGSTSWTGFQTKAEVEQVELPDGKKRRKVLALPSHRGPKIRLRDKGKVKPVHPKKPKPQINQWKQEKQQLSSEQVSRKKAKGNKTETRFNQLVEQYKQKLLGPSKGAPLAKRSKWFDS
Protein: Potassium voltage-gated channel subfamily KQT member 4 (KQT-like 4) (Potassium channel subunit alpha KvLQT4) (Voltage-gated potassium channel subunit Kv7.4) (Q9JK97)
Organism: Mus musculus (Mouse)
Function: Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea.
Subcellular location: Basal cell membrane {ECO:0000250|UniProtKB:Q9JK96}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56696}. Note=Situated at the basal membrane of cochlear outer hair cells. {ECO:0000250|UniProtKB:Q9JK96}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 3
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily KQT member 5
- Inward rectifier potassium channel 4
- ATP-sensitive inward rectifier potassium channel 12
- Inward rectifier potassium channel 2
- ATP-sensitive inward rectifier potassium channel 14
- Ubiquitin-like protein FUBI
- Potassium voltage-gated channel subfamily E member 4
Sequence:
MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGGQRSSAAQKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIIRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDTSRAYLTATWYYYDSILPSFRELALLFEHIQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSASFCPGESSRMGIKDRIRISSSQKRTGPSKQHLAPPPIPTSPSSEQVGEASSPSKVQKSWSFNDRTRFRASLRLKPRCSAEEGPSEEVAEEKSYQCELTVDDVMPAVKTVIRSVRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQARVDQIVGRGPGDRKTREKGDKGPSDTEAVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGTVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q388T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- UDP-glucose 4-epimerase
Sequence:
MPLNPPSAFSGAALACLEKMQASGVEEKCIHIFLIQHALVRKGETGYIPEKSIFPVESLPFLQGIETKGENTALLRQAVVLKLNGGLGTGMGLNGPKSLLQVKNGQTFLDFTALQLEHFRQVRNCNVPFMLMNSFSTSGETKNFLRKYPTLYEVFDSDIELMQNRVPKIRQDNFFPVTYEADPTCEWVPPGHGDVYTVLYSSGKLDYLLGKGYRYMFISNGDNLGATLDVRLLDYMHEKQLGFLMEVCRRTESDKKGGHLAYKDVIDETTGQTRRRFVLRESAQCPKEDEDSFQNIAKHCFFNTNNIWINLMELKKMMDEQLGVLRLPVMRNPKTVNPQDSQSTKVYQLEVAMGAAISLFDRSEAVVVPRERFAPVKTCSDLLALRSDAYQVTEDQRLVLCEERNGKPPAIDLDGEHYKMIDGFEKLVKGGVPSLRQCTSLTVRGLVEFGADVSVRGNVVIKNLKEEPLIIGNGRVLDNEVVVVE
Protein: Probable N-acetyltransferase san (EC 2.3.1.258) (N-epsilon-acetyltransferase san) (EC 2.3.1.-) (Protein atado) (Protein separation anxiety) (Q9NHD5)
Organism: Drosophila melanogaster (Fruit fly)
Function: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins. Autoacetylates. Required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. Required for the interaction between Scc1/vtd and SMC3, possibly by mediating N-terminal acetylation of Scc1/vtd.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14653991}. Note=During interphase, it localizes to the cytoplasm. During the entry into mitosis, it becomes distributed throughout the entire cell in a punctate pattern. From metaphase through telophase, it is distributed uniformly throughout the cell. {ECO:0000269|PubMed:14653991}.
Interaction partners:
- N
- N-terminal amino-acid N
- GEO07882p1
- N-alpha-acetyltransferase 20
- GEO02452p1
- Phagocyte signaling-impaired protein
- N-alpha-acetyltransferase 30A
- N-alpha-acetyltransferase 35, NatC auxiliary subunit homolog
- N
- N-alpha-acetyltransferase 20
Sequence:
MTRSSIELGDVTPHNIKQLKKLNTVVFPVSYNDKFYVDVLEAGELAKLAYYNDIVVGAVCCRIDNTENQRRLYIMTLGCLSPYRRLGIGTVMFEHIMNFAEKDGNFDSIFLHVQINNNGAIEFYKKFGFEIVDTKEQYYKRIEPADAHVLQKTLRRTAPNSNSTATSTTANSNSRSKARQFTFV
Protein: Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12] (Q8MKI5)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P42574}.
Interaction partners:
- E3 ubiquitin-protein ligase XIAP
- Cytochrome c
- Apoptotic protease-activating factor 1
- Poly [ADP-ribose] polymerase
- Caspase-8
- Caspase 9
- Cyclin dependent kinase inhibitor 1A.
- Baculoviral IAP repeat containing 2.
- DNA fragmentation factor subunit alpha.
- Baculoviral IAP repeat-containing protein 3
Sequence:
MENTENSVDAKSFKNAETKILHGSKSMDSGMSFDNSYKMDYPEMGLCIIINNKNFHKSTGMAPRSGTDVDAANLRETFTNLKYEVRNKNDLTCEEILELMNSVSKEDHSKRSSFVCVLLSHGDEGIIFGTNGPVDLRKVTGFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGIEDDMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSAFHGKKQIPCIVSMLTKELYLYH
Protein: Growth/differentiation factor 9 (Q6GUA6)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Zona pellucida sperm-binding protein 2
- receptor protein serine/threonine kinase
- Follicle-stimulating hormone receptor
- Lutropin-choriogonadotropic hormone receptor
- Zona pellucida sperm-binding protein 3
- Muellerian-inhibiting factor
- TGF-beta receptor type-1
- Proto-oncogene serine/threonine-protein kinase mos
Sequence:
MALPRKFFLCFCCFALFCFPVSCGSQASRREAHFATSAVLESEAEPWSLLRPPDERHRSGLPSPLFNVLYDGHGGLPRLQPDSRALRYMKRLYKTYATKEGIPKANRSHLYNTVRLFTPCAQHKQAPGDQVTGTLPSGDLRFNLDRVTAVEHLLKSVLLYTWNNSISFPSPVKCECSLVVKEPELSNKTLPKAPYSFTLNSPFTFQKKHKWIEIDVTAILQPLVVSNKREIHMSIDFTCVKDQLQHLSAQESPCNMTLLAAPSLLLYLNDTSTQAYHRWYSLPWKRRPSQGPDQKRGLSEGVPSSRHRRAQDTVSSELKKPLVPASFNLSEYFKQFLFPQNECELHDFRLSFSQLKWDNWIVAPHKYNPRYCKGDCPRAVGHRYGSPVHTMVQNIIHEKLDSSVPRPSCVPAKYSPLSVLAIEPDGSIAYKEYEDMIATKCTCR
Protein: T-complex protein 1 subunit eta (TCP-1-eta) (CCT-eta) (B6V9S8)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU365042}.
Interaction partners:
Sequence:
MMPTPVILLKEGTDSSQGIPQLVSNISACQVIAEAVRTTLGPRGMDKLIVDGRGKATISNDGATILKLLDVVHPAAKTLVDIAKSQDAEVGDGTTSVTLLAAEFLKQVKPYVEEGLHPQIIIRAFRTATQLAVNKIKEIAVTVKKQDKVEQRKLLEKCAMTALSSKLISQQKAFFAKMVVDAVMMLDDLLQLKMIGIKKVQGGALEESQLVAGVAFKKTFSYAGFEMQPKKYNNPMIALLNVELELKAEKDNAEIRVHTVEDYQAIVDAEWNILYDKLEKIYHSGAKVILSKLPIGDVATQYFADRDMFCAGRVPEEDLKRTMMACGGSIQTSVNALSPDVLGRCQVFEETQIGGERYNFFTGCPKAKTCTFILRGGAEQFMEETERSLHDAIMIVRRAIKNDSVVAGGGAIEMELSKYLRDYSRTIPGKQQLLIGAYAKALEIIPRQLCDNAGFDATNILNKLRARHAQGGMWYGVDINNEDIADNFEAFVWEPAMVRINALTAASEAACLIVSVDETIKNPRSTVDAPPAAGRGRGRGRPH
Protein: 3-oxo-5-alpha-steroid 4-dehydrogenase (EC 1.3.99.5) (Delta 4, 5-alpha steroid dehydrogenase) (Q59327)
Organism: Comamonas testosteroni (Pseudomonas testosteroni)
Function: Involved in the degradation of steroids having an A:B ring fusion in a trans configuration. Catalyzes the elimination of hydrogens located at positions 4 and 5 and the introduction of double bonds into ring A.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSNVKKHVSTINPVGEVLDVGSADEVQWSDASDVVVVGWGGAGASAAIEAREQGAEVLVIERFSGGGASVLSGGVVYAGAVPATRRKPASRFTEAMTAYLKHEVNGVVSDETLARFSRDSVTNLNWLEKQGATFASTMPGYKTSYPADGMYLYYSGNEVVPAYGNPQLLKKPPPRGHRVVAKGQSGAMFFAALQKSTLAHGARTLTQARVQRLVREKDSGRVLGVEVMVLPEGDPRTERHKKLDELVAKSACIRRRVPRRVAVNVRRSRARSARSATSVPAKVWCCPLAAISSIRNCWSMRRYKPGWLTGAAGCDGSGLRLGQSVGGIAQDLNNISAWRFITPPSVWPKGLVVNIQGERFCNEQVYGAKLGYEMMEKQGGQAWLIIDSNVRRQAAWQCLFGGLWAFQSMPALALMYKVAIKGKSVDDLAKKLRMDAAVLQLQFDRANAPARGEIEDPLGKSQDMRHEFKGGSLFAIDISISQKMFPLAVLSLGGLKVNEDNGAVIDGAGYDIPGLYAAGVPPLVWLPRVT
Protein: Inner membrane protein YiaV (P37683)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- PTS system fructose-like EIIB component 2
- Inner membrane protein YiaW
- Macrolide export ATP-binding/permease protein MacB
Sequence:
MDLLIILTYVAFAWAMFKIFKIPVNKWTIPTAALGGIFIVSGLILLMNYNHPYTFKAQKAVISIPVVPQVTGVVIEVTDKKNTLIKKGEVLFRLDPTRYQARVDRLMADIVTAEHKQRALGAELDEMAANTQQAKATRDKFAKEYQRYARGSQAKVNPFSERDIDVARQNYLAQEASVKSSAAEQKQIQSQLDSLVLGEHSQIASLKAQLAEAKYNLEQTIVRAPSDGYVTQVLIRPGTYAASLPLRPVMVFIPDQKRQIVAQFRQNSLLRLAPGDDAEVVFNALPGKVFSGKLAAISPAVPGGAYQSTGTLQTLNTAPGSDGVIATIELDEHTDLSALPDGIYAQVAVYSDHFSHVSVMRKVLLRMTSWVHYLYLDH
Protein: Glutathione S-transferase GstA (EC 2.5.1.18) (GST B1-1) (P0A9D2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase GstB
- Glutathione reductase
- Thioredoxin/glutathione peroxidase BtuE
- Maltose/maltodextrin-binding periplasmic protein
- Glutathione S-transferase YfcF
- Glutathione synthetase
- Glutathione hydrolase proenzyme
- Glutathione-specific gamma-glutamylcyclotransferase
- Bifunctional glutathionylspermidine synthetase/amidase
- Disulfide-bond oxidoreductase YfcG
Sequence:
MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENGDDYFAVNPKGQVPALLLDDGTLLTEGVAIMQYLADSVPDRQLLAPVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEEYKPTVRAQLEKKLQYVNEALKDEHWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAAFMQRMAERPEVQDALSAEGLK
Protein: Telomere-binding protein cav (Anonymous fast evolving 1G5) (HP1/ORC-associated protein) (HOAP p55) (Protein caravaggio) (Q95RV2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to chromosome ends in a sequence-dependent manner and is required for telomere capping.
Subcellular location: Nucleus {ECO:0000269|PubMed:11408576, ECO:0000269|PubMed:12510197, ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}. Chromosome {ECO:0000269|PubMed:11408576, ECO:0000269|PubMed:12510197, ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}. Chromosome, telomere {ECO:0000269|PubMed:11408576, ECO:0000269|PubMed:12510197, ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}. Note=Enriched at interphase, polytene and mitotic chromosome telomeres (PubMed:11408576, PubMed:12510197, PubMed:12826664, PubMed:19181850, PubMed:20057353, PubMed:26110638). Localized predominantly at telomeres and diffusely throughout regions of pericentric heterochromatin (PubMed:11408576, PubMed:12510197, PubMed:12826664, PubMed:19181850). Colocalizes with moi/modigliani at telomeres (PubMed:19181850). Telomere localization is not dependent on peo/pendolino, tea, ver/verrocchio or moi/modigliani (PubMed:19181850, PubMed:19240120, PubMed:20679394, PubMed:26110638, PubMed:27835648). Telomere localization is enhanced by, but not dependent on, Su(var)205/HP1 (PubMed:12510197). Telomere localization is enhanced by the activity of tefu/ATM and the MRN complex (PubMed:20057353). {ECO:0000269|PubMed:11408576, ECO:0000269|PubMed:12510197, ECO:0000269|PubMed:12826664, ECO:0000269|PubMed:19181850, ECO:0000269|PubMed:19240120, ECO:0000269|PubMed:20057353, ECO:0000269|PubMed:20679394, ECO:0000269|PubMed:26110638, ECO:0000269|PubMed:27835648}.
Interaction partners:
- HP1-HOAP-interacting protein
- Protein modigliani
- Heterochromatin protein 1
- Protein telomere ends associated
- Protein verrocchio
- Without children, isoform B
- FI06908p
- Serine/threonine-protein kinase ATM
Sequence:
MLLLLCVNMSGTQMSAFLRKYLADEDKKIRAQFKESDPNNKLILWMHEKTRITEEDLARPYTEDEVKELCLRTKVKVDMTAWNCLWEAKKRFEAKGRFVNKSERFINRMYMKAVRRKMVQPYPEEFVAQRREIVAAETKKQNISRLDRWQKKKSQNLSAPESSPDAHASSNDAVQSHEDQANTNLSSLSQMNFQVEAMAPPGVSSSDLSGIGDDEDEQQQSGFQDENINRPETEINENSVRCDPINLGRMRTGCINSQANNSFRNTESDPDYYMFGTQLSTLVRPTSTQEPDDQVNCPETEMNESWVRCDQINSESLSIGPSIDSEGTITFQNTESEPIDVTSIA
Protein: Negative regulator of flagellin synthesis (Anti-sigma-D factor) (P39809)
Organism: Bacillus subtilis (strain 168)
Function: Allows the coupling of early and late flagellar synthesis through the repression of RNA polymerase sigma-D factor-dependent transcription.
Interaction partners:
- Uncharacterized protein YvyG
- Flagellar hook-associated protein 1
- RNA polymerase sigma-D factor
- Flagellar secretion chaperone FliS
- Uncharacterized protein YvyF
- Flagellar hook-associated protein 2
- Flagellar hook-associated protein 3
- Flagellin
- Flagellar basal body rod protein FlgB
- Flagellar FliJ protein
Sequence:
MKINQFGTQSVNPYQKNYDKQAVQKTVAQPQDKIEISSQAKEMQHASDAVTGSRQEKIAQLKAQIENGSYKVDANHIAKNMINFYKKQ
Protein: Endolysin (EC 3.2.1.17) (Lysis protein) (Lysozyme) (Muramidase) (P00720)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04110}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04110}.
Interaction partners:
Sequence:
MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL
Protein: Putative pectinesterase/pectinesterase inhibitor 26 (AtPMEpcrC) [Includes: Pectinesterase inhibitor 26 (Pectin methylesterase inhibitor 26); Pectinesterase 26 (PE 26) (EC 3.1.1.11) (Pectin methylesterase 26) (AtPME26)] (Q9LUL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable pectate lyase 5
- SelT-like protein
- Pectate lyase
- Probable pectate lyase 9
- Probable pectate lyase 7
- Probable pectate lyase 3
- Probable pectate lyase 19
- Vacuolar protein sorting-associated protein 20 homolog 1
- Probable pectate lyase 6
- Thioredoxin O1, mitochondrial
Sequence:
MDTVKSINKGYGKVDETQDLALKRKTRKRLYQIGISVAVLVAIIISSTVTIAIHSRKGNSPHPTPSSVPELTPAASLKTVCSVTNYPVSCFSSISKLPLSNTTDPEVIFRLSLQVVIDELNSIVELPKKLAEETDDEGLKSALSVCEHLLDLAIDRVNETVSAMEVVDGKKILNAATIDDLLTWLSAAVTYHGTCLDALDEISHTNSAIPLKLKSGMVNSTEFTSNSLAIVAKILSTISDFGIPIHGRRLLNSSPHATPISVPKLTPAASLRNVCSVTRYPASCVSSISKLPSSNTTDPEALFRLSLQVVINELNSIAGLPKKLAEETDDERLKSSLSVCGDVFNDAIDIVNDTISTMEEVGDGKKILKSSTIDEIQTWLSAAVTDHDTCLDALDELSQNKTEYANSPISLKLKSAMVNSRKFTSNSLAIIAKFPIHERHGVQSPRLRKSPHPTPSSVLRTVCNVTNYPASCISSISKLPLSKTTTDPKVLFRLSLQVTFDELNSIVGLPKKLAEETNDEGLKSALSVCADVFDLAVDSVNDTISSLDEVISGGKKNLNSSTIGDLITWLSSAVTDIGTCGDTLDEDNYNSPIPQKLKSAMVNSTEFTSNSLAIVAQVLKKPSKSRIPVQGRRLLNSNSFPNWVRPGVRRLLQAKNLTPHVTVAADGSGDVRTVNEAVWRVPKKGKTMFVIYVKAGTYVENVLMKKDKWNVFIYGDGRDKTIISGSTNMVDGVRTFNTSTFATEGKGFMMKDMGIINTAGPEKHQAVAFRSDSDRSVYYRCSFDGYQDTLYTHSNRQYYRNCDVTGTVDFIFGAGTVVFQGCSIRPRQPLPNQFNTITAEGTQEANQNTGISIHQCTISPNGNVTATTYLGRPWKLFSKTVIMQSVIGSFVNPAGWIAWNSTYDPPPRTIFYREYKNSGPGSDLSKRVKWAGYKPISSDDEAARFTVKYFLRGDDNWIPKAVMGMPPL
Protein: Clusterin-associated protein 1 (Q8R3P7)
Organism: Mus musculus (Mouse)
Function: Required for cilia biogenesis. Appears to function within the multiple intraflagellar transport complex B (IFT-B). Key regulator of hedgehog signaling.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:23351563}. Nucleus {ECO:0000250|UniProtKB:Q96AJ1}.
Interaction partners:
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 56
- TRAF3-interacting protein 1
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 70A2
Sequence:
MSFRDLRNFTEMMRALGYPRHISMENFRTPNFGLVSEVLLWLVKRYEPQTDIPSDIETEQDRVFFIKAIAQFMATKAHIKLNTKKLYQADGYAVKELLKITSVLYNAMKTKGMEGSNVGEEDISKFKFDLGSKIADLKAARQLASEITAKGASLYDLLGKEVELRELRTEAIARPLEINETEKVMRIAIKDLLAQVQKTKDLLNNVASDEANLEAKIEKRKLELERNRKRLQTLQSVRPAFMDEYEKVEEDLQKQYDVYLEKFRNLAYLEQQLEDHHRMEQERFEEAENTLRLMQNKLKEEEKRLLKSGSNDDSDIDIQEDDESDSELEDRRMSKPRTAMEVLMQGRPSKRIVGAMQGGDSDEDEDSEDSEIDMEDDEEDDDDLEDESIALSPAKPSRRIRKPEPLDESDNDF
Protein: Histocompatibility 2, T region locus 13 (V9GXI4)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAQRTLFLLLAAALTMIETRAGPHSMRYFETAVFRPGLGEPRFISVGYVDNTQFVSFDSDAENPRSEPRAPWMEQEGPEYWERETQIAKDNEQSFGWSLRNLIHYYNQSKGVRL