wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase 1 regulatory subunit 1C (Inhibitor-5 of protein phosphatase 1) (IPP5) (Q8WVI7)
Organism: Homo sapiens (Human)
Function: May increase cell susceptibility to TNF-induced apoptosis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Sequence:
MEPNSPKKIQFAVPVFQSQIAPEAAEQIRKRRPTPASLVILNEHNPPEIDDKRGPNTQGELQNASPKQRKQSVYTPPTIKGVKHLKGQNESAFPEEEEGTNEREEQRDH
Protein: Probable CCR4-associated factor 1 homolog 7 (EC 3.1.13.4) (Q9SKZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Transcription regulator
- Transcription regulator NOT2/NOT3/NOT5 family protein
- NOT2 / NOT3 / NOT5 family
- Probable NOT transcription complex subunit VIP2
- Cell differentiation, Rcd1-like protein
- TPR repeat-containing thioredoxin TTL4
- Cell differentiation, Rcd1-like protein
- Cell differentiation, Rcd1-like protein
- CCR4-NOT transcription complex subunit 11
- AT5g35440/MOK9_2
Sequence:
MSLFLKDDSIQIREVWNDNLESEMALIREVVDDFPFVAMDTEFPGIVCRPVGTFKTNTEYHYETLKTNVNILKMIQLGLTFSDEKGNLPTCGTDNKYCIWQFNFREFDLESDIYATDSIELLRQSGIDFVKNNEFGIDSKRFAELLMSSGIVLNENVHWVTFHSGYDFGYLLKLLTCQNLPETQTGFFEMISVYFPRVYDIKHLMKFCNSLHGGLNKLAELLDVERVGICHQAGSDSLLTSCTFRKLQENFFIGSMEKYSGVLYGLGVENGQIVH
Protein: Ephrin-A3 (EHK1 ligand) (EHK1-L) (EPH-related receptor tyrosine kinase ligand 3) (LERK-3) (O08545)
Organism: Mus musculus (Mouse)
Function: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Ephrin type-A receptor 4
- Ephrin type-A receptor 1
- Ephrin type-A receptor 2
- Ephrin type-A receptor 3
- Ephrin type-A receptor 10
- Ephrin type-A receptor 5
- Ephrin type-A receptor 8
- Ephrin type-A receptor 7
- Ras GTPase-activating protein 1
- Tyrosine-protein kinase Fyn
Sequence:
MAAAPLLLLLLLVPVPLLPLLAQGPGGALGNRHAVYWNSSNQHLRREGYTVQVNVNDYLDIYCPHYNSSGPGGGAEQYVLYMVNLSGYRTCNASQGSKRWECNRQHASHSPIKFSEKFQRYSAFSLGYEFHAGQEYYYISTPTHNLHWKCLRMKVFVCCASTSHSGEKPVPTLPQFTMGPNVKINVLEDFEGENPQVPKLEKSISGTSPKREHLPLAVGIAFFLMTLLAS
Protein: Serine/threonine-protein phosphatase 6 catalytic subunit (PP6C) (EC 3.1.3.16) [Cleaved into: Serine/threonine-protein phosphatase 6 catalytic subunit, N-terminally processed] (O00743)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. During mitosis, regulates spindle positioning. Down-regulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7. Participates also in the innate immune defense against viruses by desphosphorylating RIGI, an essential step that triggers RIGI-mediated signaling activation. Also regulates innate immunity by acting as a negative regulator of the cGAS-STING pathway: mediates dephosphorylation and inactivation of CGAS and STING1. CGAS dephosphorylation at 'Ser-435' impairs its ability to bind GTP, thereby inactivating it.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:29053956}. Cytoplasm {ECO:0000269|PubMed:16769727, ECO:0000269|PubMed:17568194}.
Interaction partners:
- Serine/threonine-protein phosphatase 6 regulatory subunit 1
- Serine/threonine-protein phosphatase 6 regulatory subunit 3
- Serine/threonine-protein phosphatase 6 regulatory subunit 2
- Immunoglobulin-binding protein 1
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C
- TIP41-like protein
- Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B
- NF-kappa-B inhibitor epsilon
- Immunoglobulin-binding protein 1 family member C
Sequence:
MAPLDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQFYDLCELFRTGGQVPDTNYIFMGDFVDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL
Protein: GAS2-like protein 2 (GAS2-related protein on chromosome 17) (Growth arrest-specific protein 2-like 2) (Q8NHY3)
Organism: Homo sapiens (Human)
Function: Involved in the cross-linking of microtubules and microfilaments. Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers. Enhances ADORA2-mediated adenylyl cyclase activation by acting as a scaffold to recruit trimeric G-protein complexes to ADORA2A (By similarity). Regulates ciliary orientation and performance in cells located in the airway.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12584248, ECO:0000269|PubMed:30665704}. Cell membrane {ECO:0000250|UniProtKB:Q5SSG4}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:24706950, ECO:0000269|PubMed:30665704}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:30665704}. Note=Colocalizes with ADORA2A at neuronal processes (By similarity). Colocalizes with and tracks the tips of microtubule plus ends (PubMed:24706950). {ECO:0000250|UniProtKB:D3ZUE1, ECO:0000269|PubMed:24706950}.
Interaction partners:
- Lipase member I
- Ras-like protein family member 10A
- Sperm surface protein Sp17
- Tektin-1
- Dynein axonemal assembly factor 6
Sequence:
MSQPAGGRRKPRTLGPPVCSIRPFKSSEQYLEAMKEDLAEWLRDLYGLDIDAANFLQVLETGLVLCQHANVVTDAALAFLAEAPAQAQKIPMPRVGVSCNGAAQPGTFQARDNVSNFIQWCRKEMGIQEVLMFETEDLVLRKNVKNVVLCLLELGRRAWRFGVAAPTLVQLEEEIEEEVRRELALPPPDPSPPAPPRRQPCHFRNLDQMVQSLVSHCTCPVQFSMVKVSEGKYRVGDSNTLIFIRILRNHVMVRVGGGWDTLGHYLDKHDPCRCTSLSHKPGSFLKPPAPPVQHEVRVQDGPSQTQPTMTISRSQSPPPPVDWKTYTSSDRRLRPPTPSSPRPRRERGAGTGASREMAPFLRCQERSLIPSWRQPTAGDSPPSPQSSSTQKGRDPQCTSSGKREERYPPELPRGRIPTSWVHEETDSWGTDAGNPTPQRLRAIEATTKGISARGPSPLPRSFGPAECLGLRLPLRDEAKGAFFQFREPESVRSPTPVQGLTKIPIRLPPARPPTPGRSFPGATSGSPRTELGRDPIPLRAVTVDLAGSTHGDCSVEVRQEDQQLDIQVMAEARESWDLGLQEQEGRYTPLPLGGNKEQAIYCSLEEEILGNMKLLEVRSACPQGTRSGVIPRSGVYIPRLAGQWPEPGGPYDKAIQELAQGSPSLLKVDLEAWKAAPTGSPKPAVTPGPGSLKGKLGARQSGPRTKASLSAKGTHMRKVPPQGGQDCSASTVSASPEAPTPSPLDPNSDKAKACLSKGRRTLRKPKRVPSIYKLKLRPRIRPRRDHRPEKQPSRIPRPLAYVFLGPARQPPKDRLLRAVLGSKGGEASRVDGASVGEEEEEGKEEKEPAAPLESSPQPPEGLQPHWLNQAPLPPEEESWV
Protein: Ras-related protein Rap-2a (EC 3.6.5.2) (Q80ZJ1)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein which cycles between a GDP-bound inactive and a GTP-bound active form. In its active form interacts with and regulates several effectors including MAP4K4, MINK1 and TNIK. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it is part of several signaling cascades and may regulate cytoskeletal rearrangements, cell migration, cell adhesion and cell spreading.
Subcellular location: Midbody {ECO:0000250}. Recycling endosome membrane {ECO:0000269|PubMed:19061864}; Lipid-anchor {ECO:0000269|PubMed:19061864}; Cytoplasmic side {ECO:0000269|PubMed:19061864}. Note=Localizes to midbody at telophase. May also localize to the Golgi and the gelatinase-containing granules of neutrophils. {ECO:0000250}.
Interaction partners:
- Traf2 and NCK-interacting protein kinase
- E3 ubiquitin-protein ligase NEDD4
Sequence:
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSNEGRALAEEWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ
Protein: Transcriptional repressor of N-acetylglucosamine utilization NagR (Q8EBJ8)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
- Glutamate synthase large chain
- N-acetyl glucosamine transporter NagP
- TonB-dependent chitooligosaccharide receptor
- Phosphotransferase system
- Phosphocarrier protein HPr
- Maltose transporter MalT
- Transmembrane cytochrome oxidase associated protein
Sequence:
MKVTINDVAKYAGVSIKTVSRVTNNEPSVKQATVDKVNEAIKVLNYQPNLAARNLAGTKSYAIGFIYDNPNAYYIIDMQNGILSACKDKGYELVIHPCNAKSDTICDELTQLVKYSRLAGLVLTPPLSEDPKVLKSLNEIDANYVRIIAGEGIIEPDGLTILVNDKSGAVEITQHLIDLGHKNIAFLSGDLHHESTKERLLGYKQALTKNHLILNENYIIEGKYSFESGVEGANTLIKLKNRPTAIVACNDEIAAGALFAARLAGLDIPGDLSIVGFEDSPFSRQTWPKLTTVHQPNSEIAQVATELLIAKRREQDAKFTKTFTPEPVIRDSSASPKH
Protein: Coatomer subunit gamma (Gamma-coat protein) (Gamma-COP) (P32074)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular location: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta
- Coatomer subunit delta
- Coatomer subunit beta'
- Coatomer subunit zeta
- Coatomer subunit epsilon
- Coatomer subunit alpha
- ADP-ribosylation factor GTPase-activating protein GLO3
- ADP-ribosylation factor 1
- ARF guanine-nucleotide exchange factor 1
- Protein transport protein SEC22
Sequence:
MSAHTYKKFENSTSGDLPDKMTIYQDCMNTFNESPVNSKRCRLLISRLLRLLAQGETFPQNEATALFFSISKLFQHQNDPLRQAVYLAIKELSGISEDVLMATSSIMKDVQNGSDLIKPDAIRSLTYVLDESTAFSAERLLKSAVVSRHPSISSAALCTSYHLLPISEVTIRRFTNETQEAVLDLKQFPNQHGNSEYYPNSTYISQYHALGLLYQLKKTDKMALLKLVRHFSENNSMKNQLAKVELVKIVNDLIYRDPQLFSQFRPLLSDWLSNKFESVQLETAKLITSFATRNSRLVAPELYAAAISALQSLLTVPRVSSRFAALRILNRISMVSPEKIVVCNPELESLINDSNRNISTYAITTLLKTGTSKNISSLISTITNFIHDVSDDFKIIIIDAVRTLSLNFPQEWKSILNFLIDVLKNSEGGFKFKNSIVEALIDIVSFVPQSKELALENLCDFIEDCEFNEILVRILHLLGKEGPSAPNPSLYVRHIYNRVVLENSIIRSAAVVALSKFALTKNDPTLYESIISLLKRIANDKDDEVRDRATIALEFIDSARNKDDVIAQNLIESKYFYDIPSLESKLSSYISSNTDSFATAFDVNQVRKFTEDEMKAINLKRKQEQIFNQKSETTLDTTPEAESVPEKRADANSFAGPNLDDHQEDLLATKYADELLSIEQIKPFGQLVNSSRAISLTEPEAEFVVRGVKHLFKDNVVLQFNITNTLTDIALDNVSVVCTPEISDEAELEELFTLQVDRLLPSEEAACYVAFKKLDEIVMEGFLNNLTFTTKEINPDTNEPFDGDEGFQDEYEIDSIFLNAGDYVKSSFTGNFSATFDELPCEEVAVFNIQEDLSIQEVVDKIILNSSCLPVESTQFAPSDSNSHTLKLFGKSALTGSKVALQIKMIKSSKGLALKVHGKGEDSLLCSDLVNGLMQ
Protein: Low molecular weight T-cell antigen TB8.4 (O50430)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ESAT-6-like protein EsxH
- ESAT-6-like protein EsxB
Sequence:
MRLSLTALSAGVGAVAMSLTVGAGVASADPVDAVINTTCNYGQVVAALNATDPGAAAQFNASPVAQSYLRNFLAAPPPQRAAMAAQLQAVPGAAQYIGLVESVAGSCNNY
Protein: Calcium/calmodulin-dependent protein kinase type I (CaMK-I) (EC 2.7.11.17) (Q9P7I2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Important in cell cycle regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10617667}.
Interaction partners:
- Calmodulin
- Myosin 1 light chain cam2
- Transcriptional regulator prz1
- Serine/threonine-protein phosphatase 2B catalytic subunit
Sequence:
MQQTYKPNTSALKDGAPKATVDQKQLLPCKYRVGRVLGGGTYATVREAVHIETNKMYAAKIMNKKMMEKKQDFVKNEIAILKRVSYEHPNILHLVDFFETVNNLYLITELATGGELFDRICAKGSFYEADAAALMRTTTSAVKYLHDNGIVHRDLKPENLLYRSKDPNSDLLIADFGLSHFYEDSQYYMLMTACGTPEYMAPEVFRRTGYGKPVDMWAIGVITYFLLSGYTPFARPSQVEVIEAILANEYTFNDPCWSGISETAKDFIKKCLENDPSKRLTAADALKHPFLSEKRPATSNLLPNVRENFNARKTFRTAYNAVRAFNTWKKLENKH
Protein: Leucine-rich repeat receptor protein kinase EMS1 (EC 2.7.11.1) (Protein EXCESS MICROSPOROCYTES 1) (Protein EXTRA SPOROGENOUS CELLS) (Q9LYN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor with a serine/threonine-protein kinase activity required for the specification of the correct number of male archesporial initials and for the subsequent specification of tapetal and middle cell layer identities. In seeds, required for enhancing cell size and the rate of embryonic development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12154130, ECO:0000269|PubMed:12401166}; Single-pass type I membrane protein {ECO:0000269|PubMed:12154130, ECO:0000269|PubMed:12401166}.
Interaction partners:
- Protein TAPETUM DETERMINANT 1
- Transcription factor DYT1
- Protein SPOROCYTELESS
- Short-chain dehydrogenase reductase ATA1
- Phosphate transporter PHO1
- Transcription factor MYB35
- Transcription factor MYB80
- Cytochrome P450 703A2
- Phosphate transporter PHO1 homolog 1
- Phosphate transporter PHO1 homolog 4
Sequence:
MAFLTALFLFLFFSFSSSAIVDLSSETTSLISFKRSLENPSLLSSWNVSSSASHCDWVGVTCLLGRVNSLSLPSLSLRGQIPKEISSLKNLRELCLAGNQFSGKIPPEIWNLKHLQTLDLSGNSLTGLLPRLLSELPQLLYLDLSDNHFSGSLPPSFFISLPALSSLDVSNNSLSGEIPPEIGKLSNLSNLYMGLNSFSGQIPSEIGNISLLKNFAAPSCFFNGPLPKEISKLKHLAKLDLSYNPLKCSIPKSFGELHNLSILNLVSAELIGLIPPELGNCKSLKSLMLSFNSLSGPLPLELSEIPLLTFSAERNQLSGSLPSWMGKWKVLDSLLLANNRFSGEIPHEIEDCPMLKHLSLASNLLSGSIPRELCGSGSLEAIDLSGNLLSGTIEEVFDGCSSLGELLLTNNQINGSIPEDLWKLPLMALDLDSNNFTGEIPKSLWKSTNLMEFTASYNRLEGYLPAEIGNAASLKRLVLSDNQLTGEIPREIGKLTSLSVLNLNANMFQGKIPVELGDCTSLTTLDLGSNNLQGQIPDKITALAQLQCLVLSYNNLSGSIPSKPSAYFHQIEMPDLSFLQHHGIFDLSYNRLSGPIPEELGECLVLVEISLSNNHLSGEIPASLSRLTNLTILDLSGNALTGSIPKEMGNSLKLQGLNLANNQLNGHIPESFGLLGSLVKLNLTKNKLDGPVPASLGNLKELTHMDLSFNNLSGELSSELSTMEKLVGLYIEQNKFTGEIPSELGNLTQLEYLDVSENLLSGEIPTKICGLPNLEFLNLAKNNLRGEVPSDGVCQDPSKALLSGNKELCGRVVGSDCKIEGTKLRSAWGIAGLMLGFTIIVFVFVFSLRRWAMTKRVKQRDDPERMEESRLKGFVDQNLYFLSGSRSREPLSINIAMFEQPLLKVRLGDIVEATDHFSKKNIIGDGGFGTVYKACLPGEKTVAVKKLSEAKTQGNREFMAEMETLGKVKHPNLVSLLGYCSFSEEKLLVYEYMVNGSLDHWLRNQTGMLEVLDWSKRLKIAVGAARGLAFLHHGFIPHIIHRDIKASNILLDGDFEPKVADFGLARLISACESHVSTVIAGTFGYIPPEYGQSARATTKGDVYSFGVILLELVTGKEPTGPDFKESEGGNLVGWAIQKINQGKAVDVIDPLLVSVALKNSQLRLLQIAMLCLAETPAKRPNMLDVLKALKEI
Protein: Uncharacterized protein (Q585K7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tim10-like domain-containing protein
Sequence:
MGQDQSMAFANDTISGEQYRAHQVSRQDIIRRAFQKCVVPLNGGAGDKNGLGLDSGERACVEEFALLYSAYGKNGFAQFSQLYEQYQRDMFEKARVEMMTQQARKELSR
Protein: Oxidation resistance protein 1 (Q7KNC5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MQNVILTSQYYWSRRASQDVSSLSRSVDNLAIPVRRSKSRSVDHGLAAPFDLDSLRSKVEQRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVPDKSAKDDASSSSTHDADGASLSGKSSPVERKLSGDESREKDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSRRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: Anaphase-promoting complex subunit 13 (20S cyclosome/APC complex protein apc13) (O74358)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome.
Interaction partners:
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit cut9
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 15
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 1
Sequence:
MDSNYNYVHMNKPGVVLFASDWLKDRLPVDDVEVRVEHLPPVTEDEMTIQHSSANLILMKNKQLRHEPAWKDLELEDLVNAFAFIQGSSNAEGKNTIEDNFETDPFKSVKEAPMAPFLEANRRHQGEHASMRYFR
Protein: Uncharacterized protein (Q57WP4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase
Sequence:
MTLGAAIMSDESRERLAREHMEKARAMKTDTQEQIEEVMKHLSLAIEVKPLSVAVLLQRAHLATRIGRYHVAIADLTFTIQLEEHGIDRRRLAAAYGSRAAVYRKLNKHKESIVDYVRAADVEPDNGTWLYELGLVYAAQGMKALAHHFVAASLSEKVTGRMSEITRFRALTSLGTCKLASGDITGAVAVLTKGLEFQETAALHNLLGIAHFLRGEYEPARSRFERAVEMDHLSSEYHTNCALCLFQLGIHSEAFKQMEYAVIKSVENARYHFYRGNIALLLGLHAPAMTDVVKAIELDPQCASHYYSKALILVATQDYEEAMAILNKAIELNPTFRAAWVHSGLLHFLRKNLFEALQCFSRALELEEEDATVHECVGLVYFDIKYYDLSAASFTRCIDLIPDDPVLYFRRGTALLLCGDLQGAYDDLQKTVCKYKFRNPEVLNSLSVVVSKLGRHLEALELAKEAVALNSKNHRYLLQQAECHFAVRDYDAVLEDLANIVSLGYATAELYYLRGRSKYALRDFCGAADDLLQAATCQPLLNECSNYCYALGVAYLCSGKNINDAEKALTRAITSHSDPPSFFYDERAKARQKLGDTKGMLEDLNFMLQRDQSDPTVLLRRSLGYKALGLYDKAARDFEKAKTLNGAREVLDCVPYEKFFEIEEVLWGNEQVE
Protein: Cytochrome P450, family 81, subfamily K, polypeptide 1 (Cytochrome P450-like protein) (Q9LXB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Auxin-responsive endogenous peptide 1
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- ATP binding / aminoacyl-tRNA ligase/ nucleotide binding protein
Sequence:
MEDLWFIFFSFLTATLIFFITKKFLWSLNSKLPPSPTPLPIIGHLHLIKKYPLPQALRHLSSNYGPVLFLKFGCRNVLTLSSPDSIEECFTNHDVTLANRPKTITSDHFSYGYKNFGFAPYGDLWRTLRRLSTLEVFSSASLQKNSSIRNEEVSNLCLIIFRLSRDSRIVDLKYQFTLLTAHIMLRLVSGKRGVKKSDPESEKRFLDDFKLRFFSSMSMNVCDYFPVLRWIGYKGLEKRVIDMQRMRDEYLQRLIDDIRMKNIDSSGSVVEKFLKLQESEPEFYADDVIKGIIVLMFNGGTDTSPVAMEWAVSLLLNHPDKLEKLREEIKSNVKHKGLIQDSDLSSLPYLRCVIYETLRLYPAAPLLLPHCSSKRFNLGNYEIPENIMLLVNAWAVHRDGELWEEANVFKPERFEGFVGDRDGFRFLPFGVGRRACPAAGLGMRVVSLAVGALVQCFEWEKVEAGDIDMRPVFGVAMAKAEPLVALPKPWSEMVPILSQL
Protein: Protein-arginine N-acetylglucosaminyltransferase SseK1 (Arginine GlcNAcyltransferase SseK1) (EC 2.4.1.-) (Salmonella secreted effector K1) (Q9L9J3)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Protein-arginine N-acetylglucosaminyltransferase effector that disrupts TNF signaling in infected cells, including NF-kappa-B signaling, apoptosis and necroptosis. Acts by catalyzing the transfer of a single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in the death domain of host proteins TRADD and, to a lower extent, FADD: arginine GlcNAcylation prevents homotypic/heterotypic death domain interactions and assembly of the oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling. Also acts on host proteins without a death domain: catalyzes arginine GlcNAcylation of host GAPDH protein, thereby preventing GAPDH interaction with TRAF2, leading to inhibit NF-kappa-B signaling. Catalyzes GlcNAcylation of host tubulin-folding cofactor TBCB, thereby promoting microtubule stability. Also mediates auto-GlcNAcylation, which is required for activity toward death domain-containing host target proteins.
Subcellular location: Secreted {ECO:0000269|PubMed:15322005, ECO:0000269|PubMed:25972862}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:15322005, ECO:0000269|PubMed:28069818}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS). {ECO:0000269|PubMed:25972862}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
Sequence:
MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNIIMNTSQFTQSSWARHVQ
Protein: 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) (Q57WD8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein ZIP4 homolog
- 1-phosphatidylinositol 4-kinase
- 1-phosphatidylinositol-3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-phosphate 5-kinase alpha, putative
- Inositol/phosphatidylinositol phosphatase, putative
- Phosphoinositide phospholipase C
- phosphatidylinositol 3-kinase
- non-specific serine/threonine protein kinase
Sequence:
MDDIRFPSWVSHSPAFAFARVLGYQLRRQPLDTPATDNSPQALALGSGGPRWGDAPLAVSGREELLGPCMQEGYSGADVLFGRSRTDPWLASLSSVSMPQHLHGGAMPTTHALSVVNSGYMLLHPRVTQLFEMSQAKDLIAGQGRISGKNAPVLIALVALAVECRSLPFDRTKSFYLECVSLYTSLMQQLNATTFSLGVDIRGFVSSLVACGIHLRHASSGSGGLEREKAGCPTSTYAGKDVGDGSVELSREGLVGFGAHVVDPLLVQCIPSNADECVDNSIALGALEGIAIAGEAGNVDLGTELIEHLHNLTDTLVTSSHRRDPPYKELLCYLVEALSSVHGVCYTKLRYWCLTLLRPEYILRGLQRREGIQARLVAATLRLLMGWLKETAMSISCPGDSAARSGGNGDGGTTSCCSISNFVDRREVVEAETLIEGVWAVLQDSEDKWGKVQNRSFVLYGTSLRAVVVSLLQAELERIRCYAIVNSTCQHNAHSGQQHERGNGSGDAGYVPSMEEDALRLGVIGNIVKFLLLPKSAFAAIGTAGPVVSLHQDIAEHSAKVLAFVASTDGRALSTSTHPFSVLGAKMRRIQFSNKFYGGVEQVTHELIRCILRAGNLGIATSSNVETRSRTAALCLQGLCATNAYIRALVSTEVNDAVTRNDGLQQLGDGADEAGSNVEGRLDQGPVDVSLRFSVCFEMMNRVLLSRHHSLCNPLPYESLRRYTQLLFDTVEDTLRAHTRCIELSHTNKQFPGNELQVTADAFWHLTRRCHDRVLAMVREALRDLPHNASGDAGDEWNKSPLVEAINNEGKVLRLLLHSVLRCMINCLWPGSGIIYDTNIDGGKETQNGHHMRSDMSEVALATLSLFLQPLCLLCQLLTLLPEKDVQCLKSYRDNVQRFKQLESTDSFMHHSGIQPNSMSLPLYDDSDAAQLRSYWLMLTYYGFTSKVMLLTQAEGKGAEGSSDVKQPRGGEYVLSWNQTKCVRLLASLSPQLLRMRSTDYQQVMSDIELLERHLRNYSTDSHAIKPYRKGLLQYLEDCCPGVSSVGRRLPFSELFLFHALATLEILRASCGFISTIAQYHRFEICEFDASADFRAATSCLTAAATNRYLSALKATSPDTAAKRIEADVPQLVLLYGFAVQSVRRSAKEILSKIISAFPSFVGTCQALPLLWDVIGVLEKGSAAEVELYCQSKQMLEPPAVAADPESPERRKQLSDAVSFAVHWAQLAEQGSPIALREHAERFIVEQPTYGTVEPGIGLSLALRAHNAGGLSATSKPMCERSLIRRSNAKGHVRALFRVATHGGADQLLLQHLQEAGEDLVKTFGLSKQLREQQFVTLTNALSGEIGVDDFSRGCQGGEAEDTVHRGSWTSTCTPPSGQTLSDKLHESDTLACSAVVLLTSARLGTSMHISLLRCIVQYPIRSFSSDALAKAISCWRWILFERPGLFAAPLLAEVVEGFVWTITHRVGLFDGSRPRGLDEVESGRKPQLRRDAAIYSHDYATNSPHKLLAEFLIACYVDEGGPVSFVPPVLHLLKQLALRIVKTPSRLSTKDASFSEMTRCVLMIGLICRNLQAANECRAREGLPALTPAFFVGALRQGFYRCLMHWFQKTPPSWYFSRDRTAAEKELAALRKLMEMLDRDMKALSRSSDGFLDFASPEKSADSTLVNLTLVGSVAQRRIGEDIAGGTFTDIESLIAAERERLMSLIRLLQLLVKHEHHRLLVWLHPSDSLSTPSRDYFDAISSGEWLSHCTAASESDPAVLVALVARFPNRHVVGWAAQIVSENPELYCNIPGAVDLYLNSVTLVNGYPALHLFRNGGLVQSLRHLHARYATRYPQVSAYALRSLLCKKCDSLTFYLPQILQILSEDPIGAVPSFLKKMCKRSQTFEHQLLWSLQAEGGGDSEHARKCSQLASEIRHSFNASRKAFHDGEFNFIDRIISLSGEMMPIERPLRKGRLRLRLRDKEFHDSIGGQHLYLPTDPNWRIVALRPDTAGAMQSAAKCPIMVEFHCVPQNSRDGENAQGEATGSDKEAVTSKLCIFKMGDDCRQDQLALQLIGLFRRVFDSIQLPSFLYPYKVVATGRDCGVIECVPRAMSRDQIGKLVEGNLSEYFVQTYGYPESVRFHRARECFIRSMASYATASFVLNIKDRHNGNILIDSYGHLVHIDFGFLFDLSPGGDINFESSPFKLTLEMAQLMGYPVNEGKGKQPSPSLAKALVDLESYNLFVDLTIRCFLAVRQYAHEICVLVELMLSSGLPCFKPKKTIHDLSWRLAMHKSEAWAADFMRKRIAESRENVRTVLYDRYQNYAEGIEM