wanglab/gogpt-training-data huggingface dataset:
Protein: Tegument protein VP22 (P10233)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Tegument protein that plays different roles during the time course of infection. Participates in both the accumulation of viral mRNAs and viral protein translation at late time of infection. Modulates the RNase activity of the virion host shutoff protein UL41 probably to ensure necessary levels of key cellular mRNAs and proteins. Plays a role in microtubule reorganization that occurs after viral infection by stabilizing microtubule network. Finally, may prevent nucleosomal deposition onto the viral genome by interacting with and inhibiting host SET. Plays a role in the inhibition of host innate immune system by targeting the CGAS enzymatic activity which is the principal cytosolic DNA sensor that detects invading viral DNA. Acts by mediating disruption of liquid-like droplets in which CGAS is activated, thereby preventing CGAS activity.
Subcellular location: Virion tegument {ECO:0000269|PubMed:18596102, ECO:0000269|PubMed:8659129}. Host cytoplasm {ECO:0000269|PubMed:11967313, ECO:0000269|PubMed:1312128, ECO:0000269|PubMed:18353954, ECO:0000269|PubMed:19279114}. Host nucleus {ECO:0000269|PubMed:11967313, ECO:0000269|PubMed:15795259, ECO:0000269|PubMed:18353954}. Host Golgi apparatus {ECO:0000269|PubMed:19279114}. Note=One of the most abundant tegument protein (about 2000 copies per virion). Localizes in the cytoplasm at 8 hours postinfection and in the nucleus at 16 hours postinfection. During virion morphogenesis, this protein probably accumulates at the trans-Golgi where secondary envelopment occurs.
Interaction partners:
Sequence:
MTSRRSVKSGPREVPRDEYEDLYYTPSSGMASPDSPPDTSRRGALQTRSRQRGEVRFVQYDESDYALYGGSSSEDDEHPEVPRTRRPVSGAVLSGPGPARAPPPPAGSGGAGRTPTTAPRAPRTQRVATKAPAAPAAETTRGRKSAQPESAALPDAPASTAPTRSKTPAQGLARKLHFSTAPPNPDAPWTPRVAGFNKRVFCAAVGRLAAMHARMAAVQLWDMSRPRTDEDLNELLGITTIRVTVCEGKNLLQRANELVNPDVVQDVDAATATRGRSAASRPTERPRAPARSASRPRRPVE
Protein: Endoribonuclease ToxN (EndoRNase) (EC 3.1.-.-) (Toxin ToxN) (B8X8Z0)
Organism: Pectobacterium atrosepticum (Erwinia carotovora subsp. atroseptica)
Function: Toxic component of a type III toxin-antitoxin (TA) system. An endoribonuclease which is active independently of the ribosome, cleaving between the second and third A of AAA(U/G) sequences, although not all occurrences of this tetranucleotide are cleaved. Digests many mRNA species, including its own transcript and its cognate antitoxin RNA ToxI. ToxI has 5.5 nearly identical 36 nucleotide-long repeats (a single repeat neutralizes the toxin in vivo); a single repeat folds into a pseudoknot which binds the toxin. The ToxI precursor RNA is a preferential target in vivo and is progressively degraded to single repeat lengths as ToxN-ToxI complex self-assembly occurs. In vivo expression of ToxI antitoxin inhibits endonuclease activity of ToxN. The toxin alone inhibits growth when expressed in E.coli without causing cell lysis; this bacteriostatic effect is neutralized by cognate RNA antitoxin ToxI. Non-cognate antitoxin RNA from B.thuringiensis does not inhibit this toxin. The RNA antitoxin is less stable than the proteinaceous toxin; synthesis of ToxI in the absence of new ToxN synthesis restores growth and also detectable accumulation of the ToxN protein. Negatively regulates its own operon in complex with ToxI. The toxin-antitoxin system functions in plasmid maintenance (a plasmid addiction system).
Interaction partners:
Sequence:
MKFYTISSKYIEYLKEFDDKVPNSEDPTYQNPKAFIGIVLEIQGHKYLAPLTSPKKWHNNVKESSLSCFKLHENGVPENQLGLINLKFMIPIIEAEVSLLDLGNMPNTPYKRMLYKQLQFIRANSDKIASKSDTLRNLVLQGKMQGTCNFSLLEEKYRDFGKEAEDTEEGE
Protein: Conserved protein (O07256)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- HTH cro/C1-type domain-containing protein
- SnoaL-like domain-containing protein
- Glucose-1-phosphate thymidylyltransferase
Sequence:
MRKPASSLAKVDYSSAYLEQTHAFGELIRNVDQSTPVPTCPGWSLGQLFRHVGRGDRWAAQIVRDRLDHFLDPRSVEGGKPPPDPDDAISWLYGGARLLVDAVEQTGVETPVWTFLGPRPAGWWVRRRLHEVAVHRADVAITVGGEFTLEPNVAADGISEFLERIAVQAGSGGTPLPLEDDDTLHLHATDPGLLEAGEWTVRRDERGVTWSHRHGKGAVALRGGATELLLAMVRRLSVADTGIELLGDAGVWQKWLDRTPL
Protein: Kinesin-like protein (O16048)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
GNLRHRGIMPRCLDVLFRTISDYQAKKFVFKPDKLNGFEILSEEDALLERQHEMNQRFAGSGRFAFRHKDSDPEIASQASVEPIPLLGLDEDNMYSVFVTYIEIYNNSVYDLLEDSGIQKTLESKIIREDANRHMFVHGVTEVEVKTVEDALEVFQMGQKRKRMGHTVLNAESSRSHSVFNIRLVQAPTDSQGENVVQDRQNITVSQLSLVDLAGSERSSRTKNTGVRLREAGNINNSLMTLRTCLEYLRENQLAASNGLAPKKVPYRDSKITHMFKNYFDGEGQVSMIVCINPRIEDYDENMQVMKFAEMTQEVQIARATPMKQDLGLTPGRRKANKLFKIAVNNLNELGIPEAKDLEVDVGLVYSLGPDFPAYEMDSPEAQIKIRELMHYLEQRIEKRKKLRANLDIKCDSFRQMLMNLDRDNLQLRTELASLKAVYKQERDRSAALEKKVRIHESSIDVLNNTLSKQERQIEELTFKLNEKENMLTQKEHEKEKQKKKFSSKLAVESDKNKREFELKLREQRVKLQERMRIKDEKLRLVSNILQSEDLPSLPRSQSSENILNEKDRGAYTARTEESSVPATRTDIYATPRHGAAAANNRHRRSRSAGDKWLEHRAANPVPLGTIMQPYLKNRKSVTKLTDLKELTAHGTTKYCLVSQDADTDGDVETKLYKGNVIPTCGGGAQVVFNDVECLKQKSPVHSPTRKRPSNGNISALGGGAVPSTVTSAQDVASRCNLGIEGHSSKKSKI
Protein: U3 small nucleolar RNA-associated protein 18 homolog (Protein wicked) (WD repeat protein l(2)k07824) (Q9V7P1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA. Regulation of cell size by ribosome synthesis is an important parameter for stem cell maintenance and function.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:19430468}. Note=Asymmetric segregation of expression upon mitosis both in germline stem cells (GSCs) and dividing larval neural stem cells (NSCs) (at protein level).
Interaction partners:
- LD31322p
- FI04466p
- LD47749p
- GH01043p
- U3 small nucleolar RNA-associated protein 15 homolog
- KRR1 small subunit processome component homolog
- LD47550p
- Lethal
- RE67794p
- LD10780p
Sequence:
MSSDESSDGLEELQSLKALYGQQEQEKPAKIKRERYIPKASQAKELNYVEVPMEKVLFGDRQRLLTNLAKSVGQKLPNDDEDEQEENPGQAKPGDKRKAAWSDSDDEDLQVGDVKKATKHTGPLNHLRKDKSYKEYLTARFQRTLNQPKWAEKKVKNEDDEDVSSDEELLRTVGFIDRKARNSDLPQKTLNFKRVKDLNRATYAEGNATSIQFHPTSTAALVAGMNGLATIYAVDGQKNERLHNMRFKKFPLACSRIAPCGTRAFFGSVKPFYYSYDLLEAKESKLKLPGAMEFMHRFEVSPCGKFIVTAGKFGAIHLLTAKTNELLHSFKQEGKVKGFTWSSDSKRILVCGSTSNVSVLNLRQNLIEHIFMDDGCIHGESIQLSPNQRLLATGSQEGVVNIYDYESIFASKAPQPEKRFMNLRTAITDLQFNHSSELLAMCSSEAPNAFKLAHFPSATVYSNFPAQNEKVGFVTSMAFSPHSSFLAFATKGKQVPLFRLKYFKGY
Protein: BCL2 interacting protein 2 (D3ZGE0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEGVELKEEWQDEDFPIPLPEDDSIEADILDVTDPDRQPGSLEVNGNKVRKKLVAPDISLTLDPGEDSLWSDDLDEGGEVDLDGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYAATEEKEDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQEPPKSEQ
Protein: Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2) (Q9BDI7)
Organism: Bos taurus (Bovine)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against vesicular stomatitis virus (VSV).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx1
- Interferon-induced, double-stranded RNA-activated protein kinase
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon induced protein with tetratricopeptide repeats 1
- USP domain-containing protein
- E3 ubiquitin-protein ligase TRIM21
- 25A_SYNTH_3 domain-containing protein.
- C-X-C motif chemokine 10
- 2'-5' oligoadenylate synthase
Sequence:
MSMSFRPLKYKRHTQTSTQHHPKQDIYFHQQPPGPPLGQTMSPPQWQVEESNPDFLPNNFNQLNLDPQQPEAKGGQQMSKGPENNLYRKYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIITRCPLVLKLTKRECEWTGKITYRNITQQLQNPSEVEWEIRRAQNIIAGNGLGISHELINLEITSPEVPDLTLIDLPGITRVAVENQPQDIGLQIKALIKKYIQRQETINLVVVPCNVDIATTEALSMAQEVDPDGDRTIGILTKPDLVDKGTEKGVLKVMQNLTYHLKKGYMIVKCRGQQDITNKLSLAEATRKETMFFETHPYFRILLDEGKATVPLLAERLTTELIWHINKSLPLLENQIKEKHQRATEELQQYGDDIPSDEGDKMFFLIEKIKVFNEDIGKLIEGEEIVMETESRLCNKIREEFTSWILILTTNIEKVKSILNEEVSKYEKKYRGKELLGFVNYKTFETVVKHYLGQLIDPALKMLQKAMEIVWQTFKDTAKKHFAEFCNLHQTVQNKIEDIKTKQMAEAANLIQLQFRMEKLVFCQDQIYGVVLNKVREDIFNSMGKASETPQSKQPFLNDQSSISSIVEIGVHLNAYFMETSKRLANQIPFIIQYFMLQENGDKVQKAMMQLLQDTQHYSWLLQEQSDTATKRKFLKEKIFRLTQAQQALYEFPHFKG
Protein: 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal (DHNS) (EC 4.1.3.36) (Enoyl-CoA hydratase/isomerase D) (ECHID) (Naphthoate synthase) (Q8GYN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of phylloquinone (vitamin K1). Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:20150517, ECO:0000305|PubMed:17951448}.
Interaction partners:
- 2-succinylbenzoate--CoA ligase, chloroplastic/peroxisomal
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 2
- Protein PHYLLO
- Dehydrin HIRD11
- Dehydrin ERD14
- Dehydrin ERD10
- Dehydrin Xero 2
- Dehydrin Xero 1
- Acetyl-CoA acetyltransferase 1
Sequence:
MADSNELGSASRRLSVVTNHLIPIGFSPARADSVELCSASSMDDRFHKVHGEVPTHEVVWKKTDFFGEGDNKEFVDIIYEKALDEGIAKITINRPERRNAFRPQTVKELMRAFNDARDDSSVGVIILTGKGTKAFCSGGDQALRTQDGYADPNDVGRLNVLDLQVQIRRLPKPVIAMVAGYAVGGGHILHMVCDLTIAADNAIFGQTGPKVGSFDAGYGSSIMSRLVGPKKAREMWFMTRFYTASEAEKMGLINTVVPLEDLEKETVKWCREILRNSPTAIRVLKAALNAVDDGHAGLQGLGGDATLLFYGTEEATEGRTAYMHRRPPDFSKFHRRP
Protein: Periostin (PN) (Osteoblast-specific factor 2) (OSF-2) (Q15063)
Organism: Homo sapiens (Human)
Function: Induces cell attachment and spreading and plays a role in cell adhesion. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:Q62009}. Secreted {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:18450759}. Note=Colocalizes with BMP1 in the Golgi. {ECO:0000250|UniProtKB:Q62009}.
Interaction partners:
- Fibronectin
- Bone morphogenetic protein 1
- Collagen alpha-1
- Neurogenic locus notch homolog protein 1
- Collagen alpha-2
- Lumican
- Collagen alpha-1
- Calcium-activated chloride channel regulator 1
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Plasminogen activator inhibitor 2
Sequence:
MIPFLPMFSLLLLLIVNPINANNHYDKILAHSRIRGRDQGPNVCALQQILGTKKKYFSTCKNWYKKSICGQKTTVLYECCPGYMRMEGMKGCPAVLPIDHVYGTLGIVGATTTQRYSDASKLREEIEGKGSFTYFAPSNEAWDNLDSDIRRGLESNVNVELLNALHSHMINKRMLTKDLKNGMIIPSMYNNLGLFINHYPNGVVTVNCARIIHGNQIATNGVVHVIDRVLTQIGTSIQDFIEAEDDLSSFRAAAITSDILEALGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSESIMGGAVFETLEGNTIEIGCDGDSITVNGIKMVNKKDIVTNNGVIHLIDQVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASALRPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLNELYNGQILETIGGKQLRVFVYRTAVCIENSCMEKGSKQGRNGAIHIFREIIKPAEKSLHEKLKQDKRFSTFLSLLEAADLKELLTQPGDWTLFVPTNDAFKGMTSEEKEILIRDKNALQNIILYHLTPGVFIGKGFEPGVTNILKTTQGSKIFLKEVNDTLLVNELKSKESDIMTTNGVIHVVDKLLYPADTPVGNDQLLEILNKLIKYIQIKFVRGSTFKEIPVTVYTTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETITEVIHGEPIIKKYTKIIDGVPVEITEKETREERIITGPEIKYTRISTGGGETEETLKKLLQEEVTKVTKFIEGGDGHLFEDEEIKRLLQGDTPVRKLQANKKVQGSRRRLREGRSQ
Protein: Endoplasmic reticulum transmembrane protein (G5EBI0)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}.
Interaction partners:
- Phosphofurin acidic cluster sorting protein 2
- Ubiquitin-conjugating enzyme E2 13
- FIS1-related protein fis-2
- FIS1-related protein fis-1
- Dynamin-1-like protein drp-1
- PDZ Domain containing
- Mesencephalic astrocyte-derived neurotrophic factor homolog
- Ubiquitin-like domain-containing protein
- Membrane-bound transcription factor site-2 protease
- alpha-1,2-Mannosidase
Sequence:
MTLQWTIVAGVLYAEIAITFTLLLPWIRPTLWSKLFKSRLFTALAKHAHIYSITFGFVLFILFADGVRETMKYNGLEGQMGRTAESDATHHMRLFRAQRNLYISGFALLLWLVIQRIMTLLGRAAQLEAASEAAMRQAESATKTARTLMNSADTNEEAAGLAKQIEKLKGELKSANTDRDTLKKQSEGLQREFDRVSDLLRDSAESKGDKKKD
Protein: Fibroblast growth factor-binding protein 3 (FGF-BP3) (FGF-binding protein 3) (FGFBP-3) (Q1HCM0)
Organism: Mus musculus (Mouse)
Function: Heparin-binding protein which binds to FGF2, prevents binding of FGF2 to heparin and probably inhibits immobilization of FGF2 on extracellular matrix glycosaminoglycans, allowing its release and subsequent activation of FGFR signaling which leads to increased vascular permeability.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8TAT2}.
Interaction partners:
Sequence:
MSPPRPRASLSPLTLLLLLGGCLLSAAGRDKGAAGREVTRASRPTVGSSGRFVSPEQHACSWQLLVPAPGTPTGGELALRCQTPGGASLHCAYRGHPERCAATGARRAHYWRRLLGALRRRPRPCLDPAPLPPRLCARKTAGSDLHSPAHPSLPARPSEPPRSRARSPARSRQSVRSPSSQPEKKPLLVKSNSGGRKAGSDPVPEPPAAAGFQPNGLDQNAELTETYCTEKWHSLCNFFVNFWNG
Protein: Laminin subunit gamma-1 (Q1LVF0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250}.
Interaction partners:
- Laminin, beta 1a.
- CD44 antigen
- Uncharacterized protein.
- Uncharacterized protein.
- Laminin, alpha 2.
- Integrin alpha-6 isoform X1
- Integrin, alpha 6b
- Integrin, alpha 6,-like
- Integrin beta
- Integrin beta
Sequence:
MSLFSCLLLWTLWAACSHGAMDECIDEDDRPQRCMPEFVNAAFNATVVATNTCGSPPEEFCVQTGVTGVTKSCHICNAADPRLHHGAVYLTDYNQPVQPTWWQSQTMLAGIQYPNSINLTLHLGKSFDITYVRLKFHTSRPESFAIYKRSSEDGPWTPYQYYSGSCEKTYSKNNRGFIRTGEDEQQALCTDEFSDISPLYGGNVAFSTLEGRPSAYNFDNSPVLQDWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGGRCKCNGHASECVKNEYSKLVCNCKHNTEGADCNVCKPFYNDRPWRRATAENPNECLPCNCNGKSAECYFDPELYRATGHGGHCRNCADNTDGPKCERCLANYYREASGQRCLSCGCNPVGSLSTQCDNTGRCSCKPGVMGDKCDRCQPGYHSLSEAGCRPCSCNPAGSTQECDVQTGRCQCKENVDGFNCDRCKLGYFNLDPQNPQGCTPCFCFQHSTVCESADGYSVHKITSTFDRDDEGWKGKQRDDSSVPVQWSPSSGEISLISEDYFPIYFVAPDKFLHNQLLSYGQNLTLNFRIQRHDARLSAEDVVLEGSGLRVAVPLIAQGNSYPGEETQTFVFRLHDTTDYPWRPTIKHADFQKLLYNLTSIMIRGTYSAQSAGYLDNVSLVTARRGPGTPARWVEKCTCPQGYLGQHCEQCDQGFRRSRPELRRFSTCERCNCNGHSDTCDPETGMCNCQHNTAGLSCERCKDGFYGDSTVGSSSDCKACPCPAGATCAVVPKTNEVVCTNCPTGTTGKRCELCDDGFFGDPLGEKGPVRACRACSCNNNIDPNAVGNCNRESGECLKCIYNTAGVFCDRCKQGFYGDARAANVADKCKPCKCSPYGTVDRQTACSQVTGQCPCLPHVINRDCGACELGFYNLQSGKGCERCNCNPIGSTNGQCDIVSGQCECQPGVTGQHCERCEVNFFGFSSSGCKPCDCDPEGSESAQCKEDGRCHCRPGFVGSRCDMCEENYFYNRSTPGCQQCPNCYSLVRDKVNQQRQKLLDLQNLIDSLDNTETTVSDKAFEDRLKEAEKTIMDLLEEAQASKEVDKGLLDRLNNINKTLNNQWNRLQNIKNTVDNTGAQADRARNRVRDAENLINTAREELDKAKEAISKVDIKIPTTSGDPNNMTLLAEEARKLSEKHKADADQIEKIAKDANDTSTKAYNMLKKALDGENKTSSDIDELNRKYLEAKDLAKNLEKQAAKVHAEAEEAGNKALKIYANLTSLPPINTKTLEDDANKIKKEASDLDKLIDKTEKEYNDLREDLRGKETEVRKLLDKGKTEQQTADQLLARADAAKALAEEAAKKGKSTFQEAQDILNNLRDFDKRVNDNKTAAEDAMRRIPQINATINEANDKTRRAEAALGNAAADAKDAKAKAEEAEKIANDVQKGSAKTKADAEKAFEDTMKLDKDVDKMMDQLTAAEKELEKKKAEADTDMMMASMASDNAKDAEGNARKAKSAVREVLNTINALLGQLGNIDKVDLSKLNQIDNALKDAKDKMAGSELDRKLKELNDIAKSQEDMISDYDRQIQEIRADIANLNDIKNTLPEGCFNTPSLERP
Protein: Neuronal pentraxin-1 (NP1) (47 kDa taipoxin-binding protein) (Neuronal pentraxin I) (NP-I) (P47971)
Organism: Rattus norvegicus (Rat)
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q15818}. Cytoplasmic vesicle, secretory vesicle {ECO:0000305}. Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
- Glutamate receptor 4
Sequence:
MLAGRAARTCALLALCLLGSRAQDFGPTRFICTSVPVDADMCAASVAAGGAEELRSNVLQLRETVLQQKETILSQKETIRELTTKLGRCESQSTLDAGPGEARSGGGRKQPGSGKNTMGDLSRTPASETLSQLGQTLQSLKTRLENLEQYSRLNSSSQTNSLKDLLQSKIDDLERQVLSRVNTLEEGKGGPKNDTEERAKIESALTSLHQRISELEKGQKDNRPGDKFQLTFPLRTNYMYAKVKKSLPEMYAFTVCMWLKSSAAPGVGTPFSYAVPGQANELVLIEWGNNPMEILINDKVAKLPFVINDGKWHHICVTWTTRDGVWEAYQDGTQGGNGENLAPYHPIKPQGVLVLGQEQDTLGGGFDATQAFVGELAHFNIWDRKLTPGEVYNLATCSSKALSGNVIAWAESQIEIFGGATKWTFEACRQIN
Protein: Cation efflux protein cytoplasmic domain-containing protein (H2KZN1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLYNISSTIKKWRKQKKVSQFYENQNALLEAHKEDMQTLTEEESDKAAEKEKRDLVWDSRITTLTIILNVSLIIAKSIVAYFSGSLAILASVVDSFMDITSGVVVWYACYKIEKMNKEQYPVGMRKLEPLTVVIVGMIMLFANFIVLERATVQTIEDKLDPRVDLTTLIVLCTGTATKFCLFMICRVRKSAACLVLAIDQRNDCLTNIVALLGAWIGQNWWKYADPLGAFMVSGFIIVTWFLTIREHIPYLIGRRADQEFINRITNISINHDQRIKALDTVHVYHFGEKFLVEVHAVFDEPAPLQMAHDVAESLQVKLEKLPFVERAFVHCDYKFDGDEHV
Protein: TSC22 domain family protein 4 (TSC22-related-inducible leucine zipper protein 2) (Q9EQN3)
Organism: Mus musculus (Mouse)
Function: Binds DNA and acts as a transcriptional repressor. Involved in the regulation of systematic glucose homeostasis and insulin sensitivity, via transcriptional repression of downstream insulin signaling targets such as OBP2A/LCN13. Acts as a negative regulator of lipogenic gene expression in hepatocytes and thereby mediates the control of very low-density lipoprotein release. May play a role in neurite elongation and survival.
Subcellular location: Nucleus {ECO:0000269|PubMed:20878296}. Cytoplasm {ECO:0000269|PubMed:20878296}. Cell projection, dendrite {ECO:0000269|PubMed:20878296}. Synapse {ECO:0000269|PubMed:20878296}. Note=Localizes away from the nucleus to neurite processes and synaptic termini as cerebellar granular neurons differentiate (PubMed:20878296). Accumulates in the cytoplasm of differentiated Purkinje cells (PubMed:20878296). Localized to both the cytoplasm and nucleus in immature cerebellar granular neurons and atrophic Purkinje cells (PubMed:20878296). {ECO:0000269|PubMed:20878296}.
Interaction partners:
- Nuclear receptor-binding protein
- TSC22 domain family protein 1
Sequence:
MSGGKKKSSFQITSVTTDYEGPGSPGASDSPVPPALAGPPPRLPNGDPNPDPGGRGTPRNGSPPPGAPASRFRVVKLPQGLGEPYRRGRWTCVDVYERDLEPPSFGRLLEGIRGASGGTGGRSLDSRLELASLGISTPIPQPGLSQGPTSWLRPPPTSPGPQARSFTGGLGQLAGPGKAKVETPPLSASPPQQRPPGPGTGDSAQTLPSLRVEVESGGSAAATPPLSRRRDGAVRLRMELVAPAETGKVPPTDSRPNSPALYFDASLVHKSPDPFGAAAAQSLSLARSMLAISGHLDSDDDSGSGSLVGIDNKIEQAMDLVKSHLMFAVREEVEVLKEQIRDLAERNAALEQENGLLRALASPEQLAQLPSSGLPRLGPSAPNGPSI
Protein: Dehydration-responsive element-binding protein 2E (Protein DREB2E) (Dehydration response element-binding protein 19) (O80917)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates abscisic acid-inducible transcription. Involved in the regulation of plant development and tolerance to abiotic stresses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:21069430}.
Interaction partners:
- Histone H4
- FACT complex subunit SSRP1
- High mobility group B protein 15
- Uncharacterized protein T2H7.3
- C2H2-like zinc finger protein
Sequence:
MEKEDNGSKQSSSASVVSSRRRRRVVEPVEATLQRWEEEGLARARRVQAKGSKKGCMRGKGGPENPVCRFRGVRQRVWGKWVAEIREPVSHRGANSSRSKRLWLGTFATAAEAALAYDRAASVMYGPYARLNFPEDLGGGRKKDEEAESSGGYWLETNKAGNGVIETEGGKDYVVYNEDAIELGHDKTQNPMTDNEIVNPAVKSEEGYSYDRFKLDNGLLYNEPQSSSYHQGGGFDSYFEYFRF
Protein: Pierisin (EC 2.4.2.-) (NAD--DNA ADP-ribosyltransferase) (Pierisin-1) (Q9U8Q4)
Organism: Pieris rapae (Small white butterfly) (Artogeia rapae)
Function: ADP-ribosylates double-stranded DNA by targeting the N2 amino group of dG residues; 10-fold less active on tRNA. Induces apoptosis in a range of human cell lines. May play a role in removing unnecessary or harmful cells during pupation (Probable). May play a role in defense against parasitic wasps; its habitual predator Cotesia glomerata is only susceptible after removal of its eggshell or the surface of the larval caudal vesicle, while other wasps are damaged by this protein (Probable). The wild-type catalytic domain (residues 1-233) cannot be expressed in E.coli as it is unstable probably due to its toxicity. A catalytic domain fragment (Glu-165 mutated to Gln) binds dsDNA but not ssDNA; the presence of the linker inhibits DNA-binding.
Interaction partners:
Sequence:
MADRQPYMTNGIQAAVVEWIRALDLEIISLLLSRAWPMALLATSELRWRPTVLTDTDNVVRLDRRQRLVRWDRRPPNEIFLDGFVPIVTRENPDWEETDLYGFAKNNHPSIFVSTTKTQRNKKKYVWTPRNANRGIVYQYEIYAPGGVDVNDSFSDASPWPNQMEVAFPGGIQNIYIRSARELHNGRIQRIWINPNFLDPGDLEPIVSSSRTPQVIWRMNHPDGGHRDQRSERSASSYDDLMYGGTGNVQEDTFGDEPNNPKPIAAGEFMIESIKDKNSFLDLSKNVNGGVIHSNLYSGGDNQIWVFSYDDNKKAYRIQSYQNSYLYLSWDSNASSKEMILRGYTNSGSNNQYWQIEQTGKNYRLRNLLNLDMIITAQDKPSAFGGKEVIVNTEISNSNTKISQEWKMIPFDFRPIIDGDYNIFNVDLSNQVVDFSNQPDLLVHGHIFCDNENQTWHFTYNSTYHAYKIWSGRKSNLLLTWDSNAASKEMVVRAYTESRSKNQYWRIEQTGSKSYKVRNLENSSMILGLTRVSTPYGGLNLMVEDDSDGHSDLHSDWDIKPIFYQDIPDGDYNIFNDNFPNIAIDFTNQEGSLIHGHNFCSNNNQKWSFVFDGKRKAYRIKSGVRSNLWLSWDSNASSKEMVLRAYTESGSSNQYWRLDEANDGSYRIRNLQDYYKLIALTNKNTPYGGKELIVSDNKESGNTWYLKKLGEVPLPNRKFRIATKLNYKKVIDSSTSYNLIITHDLNFASSIWELVYDSSKKAYNIYSSDINNLGWIYQNKNFFVKLGNIDGPDHGDLRYFWTIEYSMQTGCYLIRSLHDPANAVGYTDSESVITDTSTYSDNQLFHFILM
Protein: Cytochrome c peroxidase, mitochondrial (CCP) (EC 1.11.1.5) (Q6FMG7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00431}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P00431}.
Interaction partners:
- Cytochrome c
Sequence:
MSATALRIAPIASRTFQRRLGYLLAGVATGAAATVAYKAQKNNNYYKYNNNNNNNSGFKAGALAAAAGVVHLAHEEDKKTADYQKVYNLIAERLRDDDEYDNYIGYGPVLVRLAWHSSGTWDKNDNTGGSYGGTYRYKKESQDPSNAGLENAAKFLEPVKKQFPWISYGDLYTLGGVVGIQELQGPKIPWRSGRTDLPEDMTPDNGRLPDGDKDANYVRNFYKRLDFNDREVVALLGAHALGKTHLKNSGFEGPWGAANNIFTNEFYLNLLNEDWKLEKNDAGNLQYNSPKGYMMLPTDYALIQDSNYLKIVKEYAADQDAFFRDFSKAFAALLERGIDFPKNQPVHIFKTLDEQGL
Protein: Protein REVEILLE 7 (Early-phytochrome-responsive 1) (MYB-related transcription factor EPR1) (B3H5A8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in phytochrome A-mediated cotyledon opening. Controlled by the central oscillator mediated by LHY and CCA1. Part of a regulatory circadian feedback loop. Regulates its own expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:14523250}.
Interaction partners:
- Two-component response regulator-like APRR5
- Transcription factor LUX
- Two-component response regulator-like APRR1
- Two-component response regulator-like APRR9
- Two-component response regulator-like APRR7
- Protein LNK4
- Transcription factor KUA1
Sequence:
MLCFVRFQAGFVRIIVAARKRFRYFLMAAEDRSEELSSNVENGSCNSNEGINPETSSHWIENVVKVRKPYTVTKQREKWSEEEHDRFLEAIKLYGRGWRQIQEHIGTKTAVQIRSHAQKFFSKMAQEADSRSEGSVKAIVIPPPRPKRKPAHPYPRKSPVPYTQSPPPNLSAMEKGTKSPTSVLSSFGSEDQVNRCSSPNSCTSDIQSIGATSIDKKNNYTTSKQPFKDDSDIGSTPISSITLFGKIVLVAEESHKPSSYNDDDLKQMTCQENHYSGMLVDTNLSLGVWETFCTGSNAFGSVTEASENLEKSAEPISSSWKRLSSLEKQGSCNPVNASGFRPYKRCLSEREVTSSLTLVASDEKKSQRARIC