wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-1 receptor accessory protein (IL-1 receptor accessory protein) (IL-1RAcP) (EC 3.2.2.6) (Interleukin-1 receptor 3) (IL-1R-3) (IL-1R3) (Q9NPH3)
Organism: Homo sapiens (Human)
Function: Coreceptor for IL1RL2 in the IL-36 signaling system (By similarity). Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD (By similarity). May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (Probable).
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
Interaction partners:
- Interleukin-33
- Interleukin-1 receptor type 1
- Interleukin-1 receptor-like 1
- Interleukin-1 beta
- Interleukin-1 receptor type 2
- Interleukin-1 alpha
- Interleukin-1 receptor-like 2
- Receptor-type tyrosine-protein phosphatase delta
- Myeloid differentiation primary response protein MyD88
- Interleukin-18 receptor 1
Sequence:
MTLLWCVVSLYFYGILQSDASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIALISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDITIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAAKVKQKVPAPRYTVELACGFGATVLLVVILIVVYHVYWLEMVLFYRAHFGTDETILDGKEYDIYVSYARNAEEEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGIVTDETLSFIQKSRRLLVVLSPNYVLQGTQALLELKAGLENMASRGNINVILVQYKAVKETKVKELKRAKTVLTVIKWKGEKSKYPQGRFWKQLQVAMPVKKSPRRSSSDEQGLSYSSLKNV
Protein: Complex 1 LYR protein domain-containing protein (Q386F8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- NADH-ubiquinone oxidoreductase complex I subunit
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 8
- Uncharacterized protein
- FAD-binding domain-containing protein
- Uncharacterized protein
Sequence:
MQISPPFCGCLSEMYARSLVKQGAFSCFRSCVRVGSVAIIGGEAHMFKQLYKRDEKLRLYRSLIKGASRFPLRSRRDIVTEEVRSSFRHPLNDSLTNEEVDRKLVLGWERAEAIKTYAQNMYWFHSRDEVSKEMMHHSLERDRQRVREMERCNTVGAAPRKTPEVTEFKSSMYNVHPDYYEKIGQKPLTHTRDIWRARGQYGSDVGGPRQKFFVRRFKALFPQGW
Protein: Nucleolar protein 3 (Apoptosis repressor with CARD) (Q62881)
Organism: Rattus norvegicus (Rat)
Function: Apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly. Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation. Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors. Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis. Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation. Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner. Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I (By similarity). Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia (By similarity). Inhibits too myoblast differentiation through caspase inhibition.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O60936, ECO:0000269|PubMed:10590251, ECO:0000269|PubMed:12191471}. Mitochondrion {ECO:0000269|PubMed:10590251, ECO:0000269|PubMed:12191471, ECO:0000269|PubMed:16639714}. Sarcoplasmic reticulum {ECO:0000269|PubMed:23382383}. Membrane {ECO:0000250|UniProtKB:O60936}; Lipid-anchor {ECO:0000250|UniProtKB:O60936}. Note=Phosphorylation at Thr-149 results in translocation to mitochondria (PubMed:12191471). Colocalized with mitochondria in response to oxidative stress (PubMed:16639714). {ECO:0000269|PubMed:12191471, ECO:0000269|PubMed:16639714}.
Interaction partners:
Sequence:
MGNMQERPSETIDRERKRLVETLQADSGLLLDALVARGVLTGPEYEALDALPDAERRVRRLLLLVQSKGEAACQELLRCAQQTVSMPDPAWDWQHVGPGYRDRSYDPPCPGHWTPEAPSSGTTCPGLPRASEEEEIGGPEDSEAVQPRTPEEPELEAEATKGDEPDLEQEMEPEPEPEVEPEPEPEPEPEPEPEPEPEPEPEPEREPDFQEGDESEGCENT
Protein: Pesticidal crystal protein Cry6Aa (Crystaline entomocidal protoxin) (Crystal protein) (Insecticidal delta-endotoxin CryVIA(a)) (Q45757)
Organism: Bacillus thuringiensis
Function: Pore-forming toxin with nematicidal activity. In infected C.elegans, induces an increase in intracellular Ca(2+) resulting in necrosis of host intestinal cells. Also, induces the expression of aspartic protease asp-1.
Subcellular location: Secreted {ECO:0000305}. Host cell membrane {ECO:0000305|PubMed:27576487}. Note=Probably secreted as a soluble protein that then inserts into the host membrane and forms pores. {ECO:0000305|PubMed:27576487}.
Interaction partners:
Sequence:
MIIDSKTTLPRHSLIHTIKLNSNKKYGPGDMTNGNQFIISKQEWATIGAYIQTGLGLPVNEQQLRTHVNLSQDISIPSDFSQLYDVYCSDKTSAEWWNKNLYPLIIKSANDIASYGFKVAGDPSIKKDGYFKKLQDELDNIVDNNSDDDAIAKAIKDFKARCGILIKEAKQYEEAAKNIVTSLDQFLHGDQKKLEGVINIQKRLKEVQTALNQAHGESSPAHKELLEKVKNLKTTLERTIKAEQDLEKKVEYSFLLGPLLGFVVYEILENTAVQHIKNQIDEIKKQLDSAQHDLDRDVKIIGMLNSINTDIDNLYSQGQEAIKVFQKLQGIWATIGAQIENLRTTSLQEVQDSDDADEIQIELEDASDAWLVVAQEARDFTLNAYSTNSRQNLPINVISDSCNCSTTNMTSNQYSNPTTNMTSNQYMISHEYTSLPNNFMLSRNSNLEYKCPENNFMIYWYNNSDWYNNSDWYNN
Protein: Traf2 and NCK-interacting protein kinase (EC 2.7.11.1) (P83510)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19816403}. Cytoplasm {ECO:0000269|PubMed:19816403}. Recycling endosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression. {ECO:0000250}.
Interaction partners:
- SH2/SH3 adapter protein Nck1
- Ras-related protein Rap-2a
- Striatin-4
- Catenin beta-1
Sequence:
MASDSPARSLDEIDLSALRDPAGIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDDQLWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPATEQLMKHPFIRDQPNERQVRIQLKDHIDRTKKKRGEKDETEYEYSGSEEEEEENDSGEPSSILNLPGESTLRRDFLRLQLANKERSEALRRQQLEQQQRENEEHKRQLLAERQKRIEEQKEQRRRLEEQQRREKELRKQQEREQRRHYEEQMRREEERRRAEHEQEYKRKQLEEQRQAERLQRQLKQERDYLVSLQHQRQEQRPLEKKPLYHYKEGMSPSEKPAWAKEVEERSRLNRQSSPAMPHKVANRISDPNLPPRSESFSISGVQPARTPPMLRPVDPQIPQLVAVKSQGPALTASQSVHEQPTKGLSGFQEALNVTSHRVEMPRQNSDPTSENPPLPTRIEKFDRSSWLRQEEDIPPKVPQRTTSISPALARKNSPGNGSALGPRLGSQPIRASNPDLRRTEPVLESSLQRTSSGSSSSSSTPSSQPSSQGGSQPGSQAGSSERSRVRANSKSEGSPVLPHEPSKVKPEESRDITRPSRPADLTALAKELRELRIEETNRPLKKVTDYSSSSEESESSEEEEEDGESETHDGTVAVSDIPRLIPTGAPGNNEQYNMGMVGTHGLETSHADTFGGSISREGTLMIRETAEEKKRSGHSDSNGFAGHINLPDLVQQSHSPAGTPTEGLGRVSTHSQEMDSGAEYGIGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAAALFTSELLRQEQAKLNEARKISVVNVNPTNIRPHSDTPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYNLINRRRFQQMDVLEGLNVLVTISGKKNKLRVYYLSWLRNRILHNDPEVEKKQGWITVGDLEGCIHYKVVKYERIKFLVIALKNAVEIYAWAPKPYHKFMAFKSFADLQHKPLLVDLTVEEGQRLKVIFGSHTGFHVIDVDSGNSYDIYIPSHIQGNITPHAIVILPKTDGMEMLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIHSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVFFMTLNRNSMMNW
Protein: Adenylate cyclase activating polypeptide 1 (Pituitary) receptor type I (A0A090N8F8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAGVVHVSLAALLLLPMAPAMHSDCIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVGEMVLVSCPELFRIFNPDQVWETETIGESDFGDSNSLDLSDMGVVSRNCTEDGWSEPFPHYFDACGFDEYESETGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSNHCFISTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWATLRLYFDDTGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIVILVQKLQSPDMGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFAVDFKHRHPSLASSGVNGGTQLSILSKSSSQIRMSGLPADNLAT
Protein: Outer dynein arm-docking complex subunit 4 (Tetratricopeptide repeat protein 25) (TPR repeat protein 25) (Q9D4B2)
Organism: Mus musculus (Mouse)
Function: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Plays an essential role for the assembly of ODA-DC and for the docking of ODA in ciliary axoneme.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:25860617}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96NG3}.
Interaction partners:
- Outer dynein arm-docking complex subunit 3
- Outer dynein arm-docking complex subunit 1
- Outer dynein arm-docking complex subunit 2
- Calaxin
- Tektin-1
- Dynein regulatory complex subunit 7
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
- Axonemal dynein light intermediate polypeptide 1
- Dynein axonemal assembly factor 4
- Piercer of microtubule wall 2 protein
Sequence:
MSDGDILRSTFPSYMAEGERLYLCGEFTKAIQSFTNALHLQSGDKNCLVARSKCYLKMGDLEKSLNDAEASLRNDPTFCKGILQKAETLYTMGDFEFALVFYHRGYKLRPDREFKVGIQKAQEAINNSVGSPSSIKLENKGDLSFLSKQAESKKAQQKHLPIKQLSYSTKHEIKRKGSLKSEKTVRQLLGELYVDKEYLEKLLLDEDLIKGTIKSGLTVEDLIMTGINYLDTRSNFWRQQKPIYARERDRKLMQEKWLRDRKRSPSQTAHYILKSLEDIDMLLTSGSADGSLQKAEKVLKKVLEWNQEEVPNKDELVGNLYSCIGNAQIELGQMVAALQSHRKDLEIAKEHDLPDAKSRALDNIGRVFARVGKFQQAIDTWEEKIPLAKTTLEKTWLFHEIGRCYLELDQAWQAQSYGEKSQQYAEEEGDLEWQLNASVLVAQAQVKLRDFESAVNNFEKALERAKLVHNNEAQQAIISALDDANKGIIEELKKTNYREILREKAERQDIMSQMDLQGASEKEPLRGREEQERVVKQWERDQESEREATDDEQDRKSSGGLSKKLLGDGHSSNLGIRRESREIYRRLSDYSSHLPSEDGSQKQEKKQAEAAKGEVQKLEKTKEE
Protein: BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex) (M0R2I2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLVRLVSNFQPQGRILASPVRVPSSHTGAMEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPP
Protein: Sestrin-2 (EC 1.11.1.-) (P58043)
Organism: Mus musculus (Mouse)
Function: Functions as an intracellular leucine sensor that negatively regulates the TORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents TORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via TORC1. May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1. May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress. Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein (By similarity). Was originally reported to contribute to oxidative stress resistance by reducing PRDX1 (By similarity). However, this could not be confirmed (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P58004}.
Interaction partners:
- GATOR2 complex protein WDR24
- GATOR1 complex protein DEPDC5
- GATOR2 complex protein MIOS
- GATOR2 complex protein WDR59
- Nucleoporin SEH1
- E3 ubiquitin-protein ligase RBX1
- Protein SEC13 homolog
- Serine/threonine-protein kinase ULK1
- Sestrin-1
- Sequestosome-1
Sequence:
MIVADSECHSEIKGYLPFTRGGVAGPETREEHREGQARRGSRGPSAFIPVEEILREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYLSSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMTEFLQTGGDPEWLLGLHRAPEKLRKLSEVNKLLAHRPWLITKEHIQALLKTGEHSWSLAELIQALVLLTHCHSLASFVFGCGILPEGDAEGSPASQAPSPPSEQGTPPSGDPLNNSGGFEAARDVEALMERMRQLQESLLRDEGASQEEMENRFELEKSESLLVTPSADILEPSPHPDILCFVEDPAFGYEDFTRRGTQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQVACSLTYNTIAMHSGVDTSMLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKIYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT
Protein: Dethiobiotin synthetase BioD (EC 6.3.3.3) (DTB synthetase) (DTBS) (Dethiobiotin synthase) (P9WPQ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. Can use a range of NTPs; has highest affinity for CTP (KD is measured as 17.2 uM or 0.160 uM in 2 different papers) while KD for ATP is 331 uM or 75 uM in the same papers. Gly-169 plays a role in NTP discrimination.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}.
Interaction partners:
- 8-amino-7-oxononanoate synthase 1
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Biotin synthase
- Conserved protein
- GTPase HflX
- Putative 8-amino-7-oxononanoate synthase 2
- Uncharacterized methyltransferase Rv0089
- Biotin--[acetyl-CoA-carboxylase] ligase
- Adenosylcobinamide-GDP ribazoletransferase
- Probable aminotransferase Rv3329
Sequence:
MTILVVTGTGTGVGKTVVCAALASAARQAGIDVAVCKPVQTGTARGDDDLAEVGRLAGVTQLAGLARYPQPMAPAAAAEHAGMALPARDQIVRLIADLDRPGRLTLVEGAGGLLVELAEPGVTLRDVAVDVAAAALVVVTADLGTLNHTKLTLEALAAQQVSCAGLVIGSWPDPPGLVAASNRSALARIAMVRAALPAGAASLDAGDFAAMSAAAFDRNWVAGLVG
Protein: Neurogranin (Ng) (RC3) [Cleaved into: NEUG(55-78)] (P60761)
Organism: Mus musculus (Mouse)
Function: Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.
Subcellular location: Cytoplasm. Synapse. Cell projection, dendritic spine. Note=Restricted to dendritic spines of a subset of neurons. {ECO:0000250}.
Interaction partners:
- Calmodulin-1
- Calmodulin 5
- Calmodulin-4
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Neuromodulin
Sequence:
MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD
Protein: Cingulin (Q9PTD7)
Organism: Xenopus laevis (African clawed frog)
Function: Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier, possibly by linking ZO proteins to the actomyosin cytoskeleton.
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:P59242}. Note=Localizes to the apical junction complex composed of tight and adherens junctions. {ECO:0000250|UniProtKB:P59242}.
Interaction partners:
Sequence:
MERDIYGDMADQHIPVGQGVQIRFIGDLKENGKPRGKRSKQDSYGVAVRVQGIDGQPFVVLNSGDKAKSSFGVQIKSQEPYLNASNTSPPNYQNYSSKPRGPSRSISSESELPENPYGSRGYRPSSSHYSSASDEEQKPRGNIRGSDGLSSLPRPLQASRREELRRSQSHSSLLEPDVEESYDYDHHYSERSSTLDTTYSQSSRDSAWSRSSQKKIDNGDYPSLGYRSATSQQSTSVSNKTKKNGLSTSSPSNQSNEDIDTKPLSSVDSLINKFDIKGQVRGRTARRSQALKDERKRSQSLDGRKNYHDTADSREIIVEKQNEVQTMREPVNASNRSFNRQTLERGDISKTRLTKEWLDQDREEPVILKQQRTVQSEFQLKSTPDLLRDQQPDGSDPTREMIFGILREGSLESENTLRKKTSILLEKLPSLQVQPGEDTISLGSQKKELERKVAELQRQLDDEMKQRMKLETSQGRPKAGMQRLEIELEESKEECSRLKELYEKKKNELSAMSQELMEVRMGKEQVETKLRTMEDKLMDSKEELSHLRAKGGTSPDKLALLKELEEVQDELDEVLQIRQKQEELLRQKDRELTALKGALKDEVANHDKDLDRVREQYQNDMQQLRKNMDNVSQDQLSLESERQKINQVVRNLQRELEESSDEISQWKEMFQKNKEELRSTKQELLQMKLEKEESEDELKETRDRFSLLQSELAQVKKGSVDPGEVASVRKELQRVQDQLKQLSVDKQKVEENLQQREREMSALKGTLKEEVSGRDRETVRLREQLQSEVMHVKKENEGLAKESRRIQDQLKQVLLEKQRHEETVHQRERELSVLKGALKDEVSGRDRETEKLRERLEQDALMTKRSYEELVKINKRLESEKTDLERVRQVIENNLQESREENDDLRRKILGLEAQLKETNTFCDDLQRAESRLKDKINKLEAERKRMEDSLGEVADQEQELAFVKRDLESKLDEAQRSLKRLSLEYEELQECYQEEMKQKDHLKKTKNELEEQKRLLDKSMDKLTRELDNMSNESRGSLQLLQTQLEEYREKSRKEIGEAQKQAKEKTAEAERHQFNSSRMQEEVQKLKLALQELQVEKETVELDKQMISQRLQSLEQDIESKKRVQDDRSRQVKVLEDKLKRMEAELDEEKNTVELLTDRVNRSRDQMEQQRAELNQERSRGQDLECDKISLERQNKELKNRLASMEGQQKPSVNVSHLEAKLQEIQERLQLEEREKATLLSTNRKLERKLKELNIQLEDERLQVNDQKDQLNLRVKALKRQVDEAEEEIERLEGLRKKAVREMEEQQEINEQLQTRVKVMEKESKRKPIRPAHDDDLSSDGEFGGPYDPSSITSLLTESNLQTSSC
Protein: Protein ENDOSPERM DEFECTIVE 1 (Protein EMBRYO DEFECTIVE 3116) (QWRF motif-containing protein 5) (O80588)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Microtubule-associated protein required for seed development and for microtubule function in the endosperm. Associates with nuclear microtubules during mitosis. Binds to microtubules of the spindle and spindle-poles and to midzone microtubules out of which the phragmoplast emerges. Not associated with cortical microtubules. Required for endosperm cellularization. May be bound and sequestered by GRF5 in an inactive soluble form during the early stages of mitosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19151224}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19151224}. Note=Microtubule-associated.
Interaction partners:
- 65-kDa microtubule-associated protein 3
- AUGMIN subunit 6
- Kinesin-like protein KIN-12A
- Pentatricopeptide repeat-containing protein At1g03540
- Cytochrome b561 and DOMON domain-containing protein At4g12980
- At4g28310
- Cyclin-B1-2
- Filament-like plant protein 2
- At1g76620/F14G6_22
- Transcription factor MYB3R-5
Sequence:
MEARIGRSMEHPSTPAINAPAPVPPPSTRRPRVREVSSRFMSPISSSSSSSSSSSAGDLHQLTSNSPRHHHQHQNQRSTSAQRMRRQLKMQEGDENRPSETARSLDSPFPLQQVDGGKNPKQHIRSKPLKENGHRLDTPTTAMLPPPSRSRLNQQRLLTASAATRLLRSSGISLSSSTDGEEDNNNREIFKSNGPDLLPTIRTQAKAFNTPTASPLSRSLSSDDASMFRDVRASLSLKNGVGLSLPPVAPNSKIQADTKKQKKALGQQADVHSLKLLHNRYLQWRFANANAEVKTQSQKAQAERMFYSLGLKMSELSDSVQRKRIELQHLQRVKAVTEIVESQTPSLEQWAVLEDEFSTSLLETTEALLNASLRLPLDSKIKVETKELAEALVVASKSMEGIVQNIGNLVPKTQEMETLMSELARVSGIEKASVEDCRVALLKTHSSQMEECYLRSQLIQHQKKCHQQECTTSV
Protein: Hydantoin racemase (EC 5.1.99.5) (Q00924)
Organism: Pseudomonas sp. (strain NS671)
Function: Involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes the racemization via enolization of D- and L-5-monosubstituted hydantoins. Is able to racemize 5-substituted hydantoins having either aromatic or aliphatic substituents such as D- and L-5-(2-methylthioethyl)hydantoin.
Interaction partners:
Sequence:
MKIKVINPNTTLAMTKGIEHAAKSAARSDTQIVAVSPKMGPASIESYYDEYLSIPGVIEEIKKGEEEGVDAFVIACWGDPGLHAAREVTDKPVVGIAESSVYLASMLAARFSVVTVLPRIKTMLEDLVDSYGMQKRVLNIRTTPMGVLDFERDPEAGIEMLRQEGKRAVEEDNAEAILLGCAGMAEFADSLEKELGVPVIDGVVAGVKFAETIVDLGKKTSKLKTYKYPEKKEYVGALENFGRNQTTTK
Protein: Protein kinase C eta type (EC 2.7.11.13) (PKC-L) (nPKC-eta) (P23298)
Organism: Mus musculus (Mouse)
Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11106751, ECO:0000269|PubMed:21346190}. Note=Associates with cell membrane during keratinocytes differentiation.
Interaction partners:
- Transient receptor potential cation channel subfamily V member 4
Sequence:
MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTAGTSDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQVNGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDAKIAEQRFGINIPHKFNVHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLISRSTLRRQGKEGSKEGNGIGVNSSSRFGIDNFEFIRVLGKGSFGKVMLARIKETGELYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHEKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHEILRHPFFKEIDWAQLNHRQLEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQL
Protein: LD35209p (Q9VX15)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Replication factor C subunit 2
- Enhanced level of genomic instability 1
- Replication factor C subunit 3
- Activator 1 subunit 5
- Rad17
- Replication factor C subunit 1
- Proliferating cell nuclear antigen
- Chromosome transmission fidelity protein 18 homolog
- Cell cycle checkpoint control protein Rad9
- Checkpoint protein Hus1-like
Sequence:
MQAFLKTGKSTAGSGDKSQGTPAARRKPPAPWVEKYRPRNVDDVVEQSEVVAVLRKCVEGGDLPNMLLYGPPGTGKTSTILAASRQIFGDMFKDRILELNASDERGINVVRTKIKNFSQLSASSVRPDGKPCPPFKIIILDEADSMTHAAQSALRRTMEKESRSTRFCLICNYVSRIIVPITSRCSKFRFKALGEDKVIDRLKYICEMEGVKIEDDAYKSIVKISGGDLRRAITTLQSCYRLKGPEHIINTADLFEMSGVIPEYYLEDYLEVCRSGNYERLEQFVREIGFSAYSVGQMMEQFVEFIVHHPGLNDPQKATICDKLGECCFRLQDGGSEYLQIMDLGCCIILALK