wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock factor-binding protein 1 (Nasopharyngeal carcinoma-associated antigen 13) (NPC-A-13) (O75506)
Organism: Homo sapiens (Human)
Function: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.
Subcellular location: Nucleus.
Interaction partners:
- WASH complex subunit 3
- Heat shock factor protein 1
- Heat shock 70 kDa protein 4
Sequence:
MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS
Protein: 2'-5'-oligoadenylate synthase 2 ((2-5')oligo(A) synthase 2) (2-5A synthase 2) (EC 2.7.7.84) (Q5MYU0)
Organism: Rattus norvegicus (Rat)
Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation. Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (By similarity). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
Interaction partners:
- Interferon regulatory factor 7.
- Interferon-induced, double-stranded RNA-activated protein kinase
- Nucleotide-binding oligomerization domain-containing protein 2
- Interferon-induced protein with tetratricopeptide repeats 1
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx3
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon-induced protein 44
- RNA helicase
- Ribonuclease L
Sequence:
MGNWMPGWSSSGSLGVPPMPVQKLEKSVQVNLEPDEKCLSQTEVSSVPSQKLEEYIQANLKPDEESLKQIDQAVDAISDLLCSEVMIDVLKVVKGGSYGRKTVLRDCSDGTLVLFTGLFKQFQDQKKYQDKLLDLIEQRLKSHEKYKKSVKRKLSLLEVQVSIPGQSILLQLLPTFNPLCISENPSAQVYQNLKRSMDQVKASPGEFSDCFTTLQQRFFEKYPGRLKDLILLVKHWYKQLQDKWIIPSPPPLLYALELLTVYAWEQGCQTKDFDITQGIRTVLQLISQPTNLCVYWLDNYNFEDETVRNNLLHQLNSPRPVILDPTDPTNNVGKDDRFWQLLAEEAQEWLNSLRLNKPHKPCWDVLPMPFFITPSHCLDKFIKDFLQPDKVFLNQIKRAVDIICSFLKETCFQNSDIKVLKIIKGGSTAKGTALQQRSDADIIVFLSSLDSYDSLETERSQYVQEIRKQLEACQKAFNLGVKFDISKWMAPRVLSFTLESKSLKQSVEFDVLPAYDALGQLRSDYTSRLKAYKKLIELYASQDSLKGGEFSVCFTELQRDFIETRPTKLKGLIRLIKHWYKQCERKMKPKASLPPKYALELLTVYAWEHGSGTDGFDTAEGFRTVLDLVIRYRQLCVFWTVNYNFEEDHMRKFLLTQIQKKRPVILDPADPTGDVGGGDRWCWHLLAKEAKEWLSSSCFQVEPKSPVQPWKVPVVQTPGSCGAQIYPVVGGVY
Protein: Taste receptor type 2 member 13 (T2R13) (Taste receptor type 2 member 121) (Taste receptor type 2 member 7) (T2R7) (Q9JKT7)
Organism: Rattus norvegicus (Rat)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MGSSLYDILTIVMIAEFIFGNVTNGFIVLTNCIAWLSKRTLSFIGWIQLFLAISRVVLIWEMLLAWLKYMKYSFSYLAGTELRVMMLTWVVSNHFSLWLATILSIFYLLKIASFSRPVFLYLKWRVKKVLLLILLGNLIFLMFNILQINTHIEDWMDQYKRNITWDSRVNEFVGFSNLVLLEMIMFSVTPFTVALVSFILLIFSLWKHLQKMHLSSRGERDPSTKAHVNALRIMVSFLLLYATYFISFFISLIPMAHKKGLDLMFSLTVGLFYPSSHSFILILGHSNLRHSSCLVITYLRCKEKD
Protein: Placenta-specific protein 1 (EPCS26) (Q9JI83)
Organism: Mus musculus (Mouse)
Function: May play a role in placental development.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MNLRKFLGGTVLVAFMLFSYSEQNQVNVLCSTDWFMVTVHPFLLNNDVYVHFYEVHLGLGCPPNHVHPHFYQFHYRVTECGIRIKAVSPDVVIYSSEIHYASKGSSTKYVIPVSCAAPRRSPWLTKPYSAKAPSNNMGATPKNDTSYHVFTLPEPSEQPNCSCPPYVYNQKSM
Protein: Uncharacterized protein C57A7.07c (P87138)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- S-adenosylmethionine synthase
- Cystathionine beta-lyase
- Homocysteine synthase
- Methylenetetrahydrofolate reductase 2
- Methylenetetrahydrofolate reductase 1
- Adenosylhomocysteinase
- Methylenetetrahydrofolate dehydrogenase [NAD
- Putative glycine dehydrogenase
- S-adenosylmethionine decarboxylase proenzyme
Sequence:
MLMLDGGSTAILPKLPESISESRLWTSEALVRYPEIVVKHHEEFLKVCDIISTFTYQLDASIYDEKVEGVPLKQVYANSIGLPVYAREHLGLPNKYIALCLGSHAATIPGCMEYKMIYDKPTDFEMLYNFHKNRIEAIQASNPKAFEKIDFIAFESLPHVTEAEVVCQLIQDMKGWSKRCWITCTCPERSTIERVSSIISKILSINHDSIWGIGVNCFHLSLLEPIAKMLSSLLPSNITAILYPDGRGLYQNPDGTFSPGSTDHPAPSPEEWSTITAKYSNLHNGNLILGGCCETNYNHLSLLREKTK
Protein: Respiratory nitrate reductase 2 beta chain (EC 1.7.5.1) (P19318)
Organism: Escherichia coli (strain K12)
Function: This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Respiratory nitrate reductase 2 alpha chain
- Respiratory nitrate reductase 1 alpha chain
- Respiratory nitrate reductase 2 gamma chain
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
- Nitrate/nitrite transporter NarU
- Respiratory nitrate reductase 1 gamma chain
- Respiratory nitrate reductase 1 beta chain
- Nitrate/nitrite antiporter NarK
- Nitrate reductase molybdenum cofactor assembly chaperone NarJ
- Nitrite reductase small subunit
Sequence:
MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTGREGMEYAWFNNVETKPGIGYPKNWEDQEEWQGGWVRDVNGKIRPRLGNKMGVITKIFANPVVPQIDDYYEPFTFDYEHLHSAPEGKHIPTARPRSLIDGKRMDKVIWGPNWEELLGGEFEKRARDRNFEAMQKEMYGQFENTFMMYLPRLCEHCLNPSCVATCPSGAIYKREEDGIVLIDQDKCRGWRLCISGCPYKKIYFNWKSGKSEKCIFCYPRIESGQPTVCSETCVGRIRYLGVLLYDADRIEEAASTEREVDLYERQCEVFLDPHDPSVIEEALKQGIPQNVIDAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSYADAGGLPKSEGVLPAIESLRIPVQYLANMLSAGDTGPVLRALKRMMAMRHYMRSQTVEGVTDTRAIDEVGLSVAQVEEMYRYLAIANYEDRFVIPTSHREMAGDAFAERNGCGFTFGDGCHGSDSKFNLFNSSRIDAINITEVRDKAEGE
Protein: Actin alpha cardiac muscle 1a (Actin alpha cardiac muscle 1c) (Beta-actin-like protein 2) (F1RCB6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Myosin heavy chain 7
- Tropomyosin alpha-1 chain
- Dynactin subunit 2
- Actin-related protein 10
- Slow myosin heavy chain 1
- Tropomyosin 3
- Tropomyosin 2
- Myosin, heavy chain 6, cardiac muscle, alpha
- Dynactin 4.
- Troponin T type 2a
Sequence:
MCDEEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDAGDGVTHNVPVYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNGIMKCDIDIRKDLYANNVLSGGTTMYPGIGDRMQKEITALAPSTMKIKMIAPPERKYSVWIGGSILASLSTFQQMWISKDEYEEAGPSIVHRKCF
Protein: NYN domain-containing protein (Q381V4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFAELDFDAEADNSSSAPGGVSECACSSIQDSGSSSALTPNDDALVVQLHRPGSEGFSCVAGPADGATRMYDEKLINGDSWVSDECHCVYCEVLKASSSLSKLQGRFKRDLRPTGDRVGGRKTVVLLLDLDNYGFNQFKSVPPRRSEGSNINVLDHLFVWSFFSSCFARYHGVLPDAHVVCQRNSGSEADARHSDVNNLNWGQGKKSVWKHLADEGRLHFTPCGGQQQAADGVIMQIAYAMVHMPLIVVSGDQGLLRAISERRRVAGRKTSRDIMENELTSQLEVINVCKHNKKFFPVWRDLETAVRRIIHHK
Protein: Activator of apoptosis harakiri (BH3-interacting domain-containing protein 3) (Neuronal death protein DP5) (O00198)
Organism: Homo sapiens (Human)
Function: Promotes apoptosis.
Subcellular location: Membrane; Single-pass membrane protein. Mitochondrion.
Interaction partners:
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- Induced myeloid leukemia cell differentiation protein Mcl-1
- Bcl-2-like protein 2
- Bcl-2-interacting killer
- Bcl-2-related protein A1
- Transcription factor Dp family member 3
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-modifying factor
- Bcl-2-like protein 11
Sequence:
MCPCPLHRGRGPPAVCACSAGRLGLRSSAAQLTAARLKALGDELHQRTMWRRRARSRRAPAPGALPTYWPWLCAAAQVAALAAWLLGRRNL
Protein: AT3g04420/T27C4_6 (NAC domain containing protein 48) (Q8W4R4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NAC
- At5g18300
- Transcription factor HHO6
Sequence:
MENPVGLRFRPTDKEIVVDYLRPKNSDRDTSHVDRVISTVTIRSFDPWELPCQSRIKLKDESWCFFSPKENKYGRGDQQIRKTKSGYWKITGKPKPILRNRQEIGEKKVLMFYMSKELGGSKSDWVMHEYHAFSPTQMMMTYTICKVMFKGDVREISSSSASYGSEIEQSRDSLIPLLVNDSEEEAQIEDAIPIEEWETWLTDDGVDEQVNHIMNMKDDRNNHRPQKPLTGVLIDDSSDDDDDSDLLSPTTNSIENSSTCDSFGSSDQINLVSLTQEVSQALITSIDTPEKIKSPYDDAQGTGAGGQKLGQETREKKRAGFFHRMIQIFVKKIHQCSSISRT
Protein: Cation efflux system protein CusC (P77211)
Organism: Escherichia coli (strain K12)
Function: Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:21249122}; Multi-pass membrane protein {ECO:0000269|PubMed:21249122}. Cell outer membrane {ECO:0000269|PubMed:21249122}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:21249122}.
Interaction partners:
- Cation efflux system protein CusB
- Cation efflux system protein CusF
- Cation efflux system protein CusA
- Transcriptional regulatory protein CusR
- Multidrug export protein AcrF
- Multidrug efflux pump subunit AcrB
- Probable aminoglycoside efflux pump
- Multidrug resistance protein MdtF
- Sensor histidine kinase CusS
- Multidrug efflux pump subunit AcrA
Sequence:
MSPCKLLPFCVALALTGCSLAPDYQRPAMPVPQQFSLSQNGLVNAADNYQNAGWRTFFVDNQVKTLISEALVNNRDLRMATLKVQEARAQYRLTDADRYPQLNGEGSGSWSGNLKGNTATTREFSTGLNASFDLDFFGRLKNMSEAERQNYLATEEAQRAVHILLVSNVAQSYFNQQLAYAQLQIAEETLRNYQQSYAFVEKQLLTGSSNVLALEQARGVIESTRSDIAKRQGELAQANNALQLLLGSYGKLPQAQTVNSDSLQSVKLPAGLSSQILLQRPDIMEAEHALMAANANIGAARAAFFPSISLTSGISTASSDLSSLFNASSGMWNFIPKIEIPIFNAGRNQANLDIAEIRQQQSVVNYEQKIQNAFKEVADALALRQSLNDQISAQQRYLASLQITLQRARALYQHGAVSYLEVLDAERSLFATRQTLLDLNYARQVNEISLYTALGGG
Protein: Class E basic helix-loop-helix protein 41 (bHLHe41) (Class B basic helix-loop-helix protein 3) (bHLHb3) (Differentially expressed in chondrocytes protein 2) (hDEC2) (Enhancer-of-split and hairy-related protein 1) (SHARP-1) (Q9C0J9)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes. Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY transcriptional repressors (PER/CRY loop). Both these loops are interlocked as it represses the expression of PER1 and in turn is repressed by PER1/2 and CRY1/2. Represses the activity of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer by competing for the binding to E-box elements (5'-CACGTG-3') found within the promoters of its target genes. Negatively regulates its own expression and the expression of DBP and BHLHE41/DEC2. Acts as a corepressor of RXR and the RXR-LXR heterodimers and represses the ligand-induced RXRA/B/G, NR1H3/LXRA, NR1H4 and VDR transactivation activity. Inhibits HNF1A-mediated transactivation of CYP1A2, CYP2E1 AND CYP3A11 (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Period circadian protein homolog 2
- Basic helix-loop-helix ARNT-like protein 1
- Nuclear factor interleukin-3-regulated protein
- Cryptochrome-1
- Class E basic helix-loop-helix protein 40
- Circadian locomoter output cycles protein kaput
- Neuronal PAS domain-containing protein 2
- Period circadian protein homolog 3
- Cryptochrome-2
- Nuclear receptor subfamily 1 group D member 1
Sequence:
MDEGIPHLQERQLLEHRDFIGLDYSSLYMCKPKRSMKRDDTKDTYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHLKALTALTEQQHQKIIALQNGERSLKSPIQSDLDAFHSGFQTCAKEVLQYLSRFESWTPREPRCVQLINHLHAVATQFLPTPQLLTQQVPLSKGTGAPSAAGSAAAPCLERAGQKLEPLAYCVPVIQRTQPSAELAAENDTDTDSGYGGEAEARPDREKGKGAGASRVTIKQEPPGEDSPAPKRMKLDSRGGGSGGGPGGGAAAAAAALLGPDPAAAAALLRPDAALLSSLVAFGGGGGAPFPQPAAAAAPFCLPFCFLSPSAAAAYVQPFLDKSGLEKYLYPAAAAAPFPLLYPGIPAPAAAAAAAAAAAAAAAAFPCLSSVLSPPPEKAGAAAATLLPHEVAPLGAPHPQHPHGRTHLPFAGPREPGNPESSAQEDPSQPGKEAP
Protein: Putative serine protease K12H4.7 (EC 3.4.-.-) (P34528)
Organism: Caenorhabditis elegans
Interaction partners:
- Peptidase A1 domain-containing protein
- C-type LECtin
- C-type LECtin
- Carboxypeptidase
- CUB_2 domain-containing protein
- Peptidase M20 dimerisation domain-containing protein
- DUF19 domain-containing protein
- DUF19 domain-containing protein
- CUB-like domain-containing protein
- Aspartic protease 6
Sequence:
MKTLLAVLLAACVLTQVLSAPSNEQRVRRNMIRGRPRGGMKKTPPMSSVSHMINFDNVVSSTFTQTLDHFDSSVGKTFQQRYYHNNQWYKAGGPAFLMLGGEGPESSYWVSYPGLEITNLAAKQGAWVFDIEHRFYGETHPTSDMSVPNLKYLSSAQAIEDAAAFIKAMTAKFPQLANAKWVTFGGSYSGALAAWTRAKHPELVYAAVGSSGPVQAEVDFKEYLEVVQNSITRNSTECAASVTQGFNLVASLLQTSDGRKQLKTAFHLCQDIQMDDKSLKYFWETVYSPYMEVVQYSGDAAGSFATQLTISHAICRYHINTKSTPLQKLKQVNDYFNQVSGYFGCNDIDYNGFISFMKDETFGEAQSDRAWVWQTCTEFGYYQSTSSATAGPWFGGVSNLPAQYYIDECTAIYGAAYNSQEVQTSVDYTNQYYGGRDNLNTDRILLPNGDIDPWHALGKLTSSNSNIVPVVINGTAHCADMYGASSLDSMYLTNARQRISDVLDGWLHAN
Protein: Terpenoid synthase 22 (AtTPS22) (EC 4.2.3.-) (Q9LQ27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in terpene biosynthesis in roots. Possesses sesquiterpene (C15) synthase activity in vitro. Does not seem to be involved in diterpene (C20) biosynthesis.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Uncharacterized protein At4g13230
- Probable alpha,alpha-trehalose-phosphate synthase 7
- Putative inactive
- Geranylgeranyl pyrophosphate synthase 3, chloroplastic
Sequence:
MEAARMGFRAKTLPHLGNGTRLPLKTKLSLFPMHLLQNHTTLSRRSTKLNLCVKACSKTSGVESSRPLPHSAPDLWGDHILSVPTENSEFDTLETEIESIKPKVRNMLMSSHKTDKERICLIHLLICLGTFHYFEKEIEEILEQAFRKLDMLFTDEDDLETTAIMFEVFRLYGHKISCDVFDRFKGVDAKFKEHLVSDVRGMLQLYEAAHLATPFETILDEALSFTRYHLESLAGQQATAPHISRHILNALYKPRFLKMEIIAAREYIHFYQKEGHDETLLKFAKLNFNFCQLHYVRELKTLTKWWKDIDLPYKLPYIRDRLLETFIGVMAVYLEPHYSLGRIIATKVSQVIVVMDDTCDAYGTFSEVRSLIDSLERWDPGAIDKLPSCLRIVIQSIVETMEDIEREMKPRGRSSSVQDTVEEIKIMGRAYAEISKWARAGHVPTFDDYIELGLDSSGIRCFAMYSFISMEDCEENQTNAWFKSKPKMLRALSVIFRLTNDIAGFEEEMRRGEVVNGVNCYVKQHNVTKELAVREIKKMIRDNYKIMMEEFLTIKSVSRPILVRCFNIVRLVNLYYEEGDNFTNPNGKLKDLITSLFFHPLPL
Protein: Homeobox-leucine zipper protein ANTHOCYANINLESS 2 (HD-ZIP protein ANL2) (Homeodomain protein AHDP) (Homeodomain transcription factor ANL2) (Q0WV12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the regulation of the tissue-specific accumulation of anthocyanins and in cellular organization of the primary root.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- C2H2-like zinc finger protein
- At4g14500
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- At3g13062
Sequence:
MNFGSLFDNTPGGGSTGARLLSGLSYGNHTAATNVLPGGAMAQAAAAASLFSPPLTKSVYASSGLSLALEQPERGTNRGEASMRNNNNVGGGGDTFDGSVNRRSREEEHESRSGSDNVEGISGEDQDAADKPPRKKRYHRHTPQQIQELESMFKECPHPDEKQRLELSKRLCLETRQVKFWFQNRRTQMKTQLERHENALLRQENDKLRAENMSIREAMRNPICTNCGGPAMLGDVSLEEHHLRIENARLKDELDRVCNLTGKFLGHHHNHHYNSSLELAVGTNNNGGHFAFPPDFGGGGGCLPPQQQQSTVINGIDQKSVLLELALTAMDELVKLAQSEEPLWVKSLDGERDELNQDEYMRTFSSTKPTGLATEASRTSGMVIINSLALVETLMDSNRWTEMFPCNVARATTTDVISGGMAGTINGALQLMNAELQVLSPLVPVRNVNFLRFCKQHAEGVWAVVDVSIDPVRENSGGAPVIRRLPSGCVVQDVSNGYSKVTWVEHAEYDENQIHQLYRPLLRSGLGFGSQRWLATLQRQCECLAILISSSVTSHDNTSITPGGRKSMLKLAQRMTFNFCSGISAPSVHNWSKLTVGNVDPDVRVMTRKSVDDPGEPPGIVLSAATSVWLPAAPQRLYDFLRNERMRCEWDILSNGGPMQEMAHITKGQDQGVSLLRSNAMNANQSSMLILQETCIDASGALVVYAPVDIPAMHVVMNGGDSSYVALLPSGFAVLPDGGIDGGGSGDGDQRPVGGGSLLTVAFQILVNNLPTAKLTVESVETVNNLISCTVQKIRAALQCES
Protein: Platelet glycoprotein V (GPV) (Glycoprotein 5) (CD antigen CD42d) (O08770)
Organism: Rattus norvegicus (Rat)
Function: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Glycoprotein 9
- Platelet glycoprotein Ib beta chain
- Platelet glycoprotein Ib alpha chain
- von Willebrand factor
- Tyrosine-protein kinase Lyn
- Pancreatic secretory granule membrane major glycoprotein GP2
- Glycoprotein VI
- Keratin, type I cytoskeletal 19
- Keratin, type II cytoskeletal 8
- Phosphoglucomutase-like protein 5
Sequence:
MLRSVLLSAVLSLVGAQPFPCPKTCKCVVRDAVQCSGGSVAHIAELGLPTNLTHILLFRMDRGVLQSHSFSGMTVLQRLMLSDSHISAIDPGTFNDLVKLKTLRLTRNKISHLPRAILDKMVLLEQLFLDHNALRDLDQNLFQKLLNLRDLCLNQNQLSFLPANLFSSLGKLKVLDLSRNNLTHLPQGLLGAQIKLEKLLLYSNRLMSLDSGLLANLGALTELRLERNHLRSIAPGAFDSLGNLSTLTLSGNLLESLPPALFLHVSWLTRLTLFENPLEELPEVLFGEMAGLRELWLNGTHLRTLPAAAFRNLSGLQTLGLTRNPLLSALPPGMFHGLTELRVLAVHTNALEELPEDALRGLGRLRQVSLRHNRLRALPRTLFRNLSSLVTVQLEHNQLKTLPGDVFAALPQLTRVLLGHNPWLCDCGLWPFLQWLRHHLELLGRDEPPQCNGPESRASLTFWELLQGDQWCPSSRGLPPDPPTENALKAPDPTQRPNSSQSWAWVQLVARGESPDNRFYWNLYILLLIAQATIAGFIVFAMIKIGQLFRTLIREELLFEAMGKSSN
Protein: Homeobox-leucine zipper protein PROTODERMAL FACTOR 2 (HD-ZIP protein PDF2) (Homeodomain transcription factor PDF2) (Q93V99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that binds to the L1 box DNA sequence 5'-TAAATG[CT]A-3'. Plays a role in maintaining the identity of L1 cells, possibly by interacting with their L1 box or other target-gene promoters; binds to the LIP1 gene promoter and stimulates its expression upon imbibition. Acts as a positive regulator of gibberellins (GAs)-regulated epidermal gene expression (e.g. LIP1, LIP2, LTP1, FDH and PDF1). Functionally redundant to ATML1. Involved, together with HDG proteins (e.g. HDG1, HDG2, HDG5 and HDG12), in the regulation of flower organs development by promoting the expression of APETALA 3 (AP3) in the epidermis and internal cell layers of developing flowers. Seems to promote cell differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At4g14500
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- At3g13062
- Serine/threonine-protein kinase-like protein ACR4
- Homeobox-leucine zipper protein MERISTEM L1
- Protodermal factor 1
Sequence:
MYHPNMFESHHMFDMTPKSTSDNDLGITGSREDDFETKSGTEVTTENPSGEELQDPSQRPNKKKRYHRHTQRQIQELESFFKECPHPDDKQRKELSRDLNLEPLQVKFWFQNKRTQMKAQSERHENQILKSDNDKLRAENNRYKEALSNATCPNCGGPAAIGEMSFDEQHLRIENARLREEIDRISAIAAKYVGKPLGSSFAPLAIHAPSRSLDLEVGNFGNQTGFVGEMYGTGDILRSVSIPSETDKPIIVELAVAAMEELVRMAQTGDPLWLSTDNSVEILNEEEYFRTFPRGIGPKPLGLRSEASRQSAVVIMNHINLVEILMDVNQWSCVFSGIVSRALTLEVLSTGVAGNYNGALQVMTAEFQVPSPLVPTRENYFVRYCKQHSDGSWAVVDVSLDSLRPSTPILRTRRRPSGCLIQELPNGYSKVTWIEHMEVDDRSVHNMYKPLVQSGLAFGAKRWVATLERQCERLASSMASNIPGDLSVITSPEGRKSMLKLAERMVMSFCSGVGASTAHAWTTMSTTGSDDVRVMTRKSMDDPGRPPGIVLSAATSFWIPVAPKRVFDFLRDENSRKEWDILSNGGMVQEMAHIANGHEPGNCVSLLRVNSGNSSQSNMLILQESCTDASGSYVIYAPVDIVAMNVVLSGGDPDYVALLPSGFAILPDGSVGGGDGNQHQEMVSTTSSGSCGGSLLTVAFQILVDSVPTAKLSLGSVATVNSLIKCTVERIKAAVSCDVGGGA
Protein: Poly(ADP-ribose) glycohydrolase (EC 3.2.1.143) (O88622)
Organism: Mus musculus (Mouse)
Function: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q86W56}. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q86W56}.
Interaction partners:
- Poly [ADP-ribose] polymerase 2
- Poly [ADP-ribose] polymerase 1
- ADP-ribosylhydrolase ARH3
- Protein mono-ADP-ribosyltransferase PARP3
- ADP-ribose glycohydrolase MACROD1
- DNA repair protein XRCC1
- DNA polymerase beta
- Rearranged L-myc fusion sequence
- ADP-ribose glycohydrolase MACROD2
- Proliferating cell nuclear antigen
Sequence:
MSAGPGWEPCTKRPRWGAAGTSAPTASDSRSFPGRQRRVLDPKDAPVQFRVPPSSPACVSGRAGPHRGNATSFVFKQKTITTWMDTKGPKTAESESKENNNTRIDSMMSSVQKDNFYPHKVEKLENVPQLNLDKSPTEKSSQYLNQQQTASVCKWQNEGKHAEQLLASEPPAGTPLPKQLSNANIGQSPHTDDHSDTDHEEDRDNQQFLTPIKLANTKPTVGDGQARSNCKCSGSRQSVKDCTGCQQEEVDVLPESPLSDVGAEDIGTGPKNDNKLTGQESSLGDSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPVFDEQDDRSSQTANKLSSCQAREADGDLRKRYLTKGSEVRLHFQFEGENNAGTSDLNAKPSGNSSSLNVECRSSKQHGKRDSKITDHFMRISKSEDRRKEQCEVRHQRTERKIPKYIPPNLPPEKKWLGTPIEEMRKMPRCGIHLPSLRPSASHTVTVRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALVDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEGNGRGMLQVDFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQRRCTEIVAIDALHFRRYLDQFVPEKVRRELNKAYCGFLRPGVPSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHTFLTERKLDVGKVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESSAETTDMPGQKAGT