wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar cation/proton exchanger 2 (Ca(2+)/H(+) antiporter CAX2) (Ca(2+)/H(+) exchanger 2) (Protein CATION EXCHANGER 2) (Q39254)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase.
Subcellular location: Vacuole membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Tonoplast.
Interaction partners:
- Cation/calcium exchanger 3
- Cation/calcium exchanger 4
- Cation/calcium exchanger 2
- Calcium-transporting ATPase 1, endoplasmic reticulum-type
- Cation/calcium exchanger 5
- Putative cadmium/zinc-transporting ATPase HMA4
- Magnesium/proton exchanger
- Cadmium/zinc-transporting ATPase HMA2
- Metal transporter Nramp3
- Cation/calcium exchanger 1
Sequence:
MSCCKVPVLIEAQVEMVSANELENKSLFRQEEDATQTKEASLMEQGSLSTSFPQHTPKAPKNSVLNSIKIVIFCNKLNLLLPFGPLAILVHYMIDSKGWVFLLTLVGITPLAERLGYATEQLACYTGPTVGGLLNATFGNVTELIISIFALKNGMIRVVQLTLLGSILSNMLLVLGCAFFCGGLVFYQKDQVFDKGIATVNSGLLLMAVMGILFPAVLHYTHSEVHAGSSELALSRFSSCIMLIAYAAYLFFQLKSQSNSYSPLDEESNQNEETSAEDEDPEISKWEAIIWLSILTAWVSLLSGYLVDAIEGASVSWNIPIAFISTILLPIVGNAAEHAGAIMFAMKDKLDLSLGVAIGSSIQISMFAVPFCVVIGWMMGQQMDLNFQLFETAMLFITVIVVAFFLQEGSSNYFKGLMLILCYLIVAASFFVHEDPHQDGI
Protein: FYN-binding protein 1 (Adhesion and degranulation promoting adaptor protein) (ADAP) (FYB-120/130) (p120/p130) (FYN-T-binding protein) (SLAP-130) (SLP-76-associated phosphoprotein) (D3ZIE4)
Organism: Rattus norvegicus (Rat)
Function: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (By similarity). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (By similarity). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O15117}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}.
Interaction partners:
- Lymphocyte cytosolic protein 2
- Src kinase-associated phosphoprotein 1
- Linker for activation of T-cells family member 1
- Integrin alpha-4
- Integrin beta-1
- Integrin subunit alpha 5
- Src kinase-associated phosphoprotein 2
- Adapter protein GRID
- Proto-oncogene vav
- NCK adaptor protein 1.
Sequence:
MDGKTDVKSLMAKFNTGSNPTEEVSTSSRPFKVAGQNSPSGIQSKKNLFDNQGNASPPAGPSNMSKFGTTKPPLAAKPTYEEKSEKEPKPPFLKPTGVSPRFGTQPNSVSRDPEVKVGFLKPVSPKPTSLTKEDSKPVILRPPGNKLHNLNQESDLKTLGPKPGSTPPVPENDLKPGFSKIAGAKSKFMPAPQDADSKPRFPRHTYGQKPSLSTEDAQEEESIPKNTPVQKGSPVQLGAKSRGSPFKPAKEDPEDKDHGTPSSPFAGVVLKPAASRGSPGLSKNSEEKKEERKTDIPKNIFLNKLNQEEPARFPKAPSKLTAGTPWGQSQEKEGDKDSATPKQKPLPPLSVLGPPPSKPSRPPNVDLTRFRKADSANSSNKSQTPYSTTSLPPPPPTQPASQPPLPASHPAHLPAPSLPPRNIKPPLDLKHPINEENQDGVMHSDGTGNLEEEQESDGEMYEDIESSKERDKKREKEEKKRLELERKEQKEREKKEQELRKKFKLTGPIQVIHHAKACCDVKGGKNELSFKQGEDIEIIRITDNPEGKWLGRTARGSYGYIKTTAVKIDYDSLKRKKNTINAVPPRPVEEDQDVYDDVAEQDAPNSHSQSGSGGMFPPPPADDDIYDGIEEEDADDGSVPQVDEKTNAWSWGILKMLKGKDERKKSIREKPKVSESDSNEGSSFPSPHKQLDVGEEVYDDVDASDFPPPPAEMSQGMSVGKTKAEEKDPKKLKKQEKEEKDLRKKFKYDGEIRVLYSTKVASSLTSKKWGTRDLQIKPGESLEVIQSTDDTKVLCRNEEGKYGYVLRSYLVDNDGEIYDDIADGCIYDND
Protein: Insulin receptor substrate 53 kDa, isoform A (Q8IQE6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cdc42 homolog
- Dol-P-Man:Man
- Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase Alg3
- Dolichyl-phosphate beta-glucosyltransferase
- Abelson interacting protein, isoform D
- Rho-related BTB domain containing, isoform B
- Dolichol-phosphate mannosyltransferase subunit 1
- Dreadlocks, isoform B
- Wiskott-Aldrich syndrome protein family member
- LD35927p
Sequence:
MEAEEVTKLVDGVYRNILDRFNPGARQLIAAGKSYLKALHGAATASRLFNEALAKIAMNAQQSGTGDIGSALMSVVNVNKEIQDQQMNILKAFYVDLLVPLETNLEKDTKVVQHEQKKFLQQHKVRMESYQKAVSTMKKQRKKKATPENTEKELRSLQLLEDQKKKLDVFCDQSYKNAMTQERRRYGFVLERQCSIAKHWMVYHTTGKTVIDNNFENWQEIAASREIIPPAAYESGYSTSNGHNNNNISSSSSSGNNNTSGNMRRLERIKDGDDDHLQGHGAQLKKSRSIDAPYGDMRTLHERENLSGLGGTGPAHYAQNSLPRAKSDFNLALVGTGQSSANKHKIIEEQLATLGDDQRGDQRPLVKALYAYMPSGENQLSFEEGDRIALVGGKAKGWQFGENLRTQHFGWFPVAYTNAEVAEVTTSGGRRYENMLMSYERNGGGSGSGSGGGGLRSYQQQQDYEAQLELMESHEATYRRRRNHSAEDSSPTRMFGDTIKQQKKYRPGSGANPRPGPPPTLPAPVPNGPQSQSSRMLNSSQSFCASNGGGVNAAVERRKQKLLNGVQSSKNHPSGKSGVAAKTSLHSSNDSGFANEPPPQPEVDYSDEEPATQRVAIRRRADTNSHTNTVPRDVASWTLNRNFRNSVDSQIDDKSLHRLSRQSGGVGKMRYDLIASDDEILQASSAGLKRTKSFWKFGGGRNGEDILAGMSLWQHRDLVAAPNLEEMRDRDDLERRLEEDRNGTLTKSHNSSSSQEKRERKDSLTSTELYGDEDENIYGVSPQQPPLQQQTQQHQQHQQHQQQQAQQHRSSYTPKSRMKIMKTIEIDIEEPTEAERMSTMRRGQSQDQQQQHRKLDKQVSGTGSQHKSLTLSRTKSNQQQQQQQQFPQSTDEGESDEHGTLKLSDVNNFFDGEGKNNSHGHGLVMKTVKRQDILKQYYTSEDEEDSDAELKSTSSDPYDCIVINDHLVRKDDKMRRHHQQQHQQMATNTLKKSSSKDQDSTLTRNSTASSGAPTATILPRTRLLKSSTSAGNNIGNSSATLERNSKGLAGNKSYGPWYDFWDQEQHGQKSASAKLK
Protein: Fc fragment of IgG binding protein (E9Q0B5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGSPWKWWALWAGATLLWALLTPAEASCQGIQCASGQRCQMVSGKARCVAESTAVCRAQGDPHYTTFDGRRYDMMGTCSYTMAELCGSDETLPAFSVEAKNEHRGSRQVSYVGLVTVYAYSHSVSLVRGEIGFVRIDNQRSRLPASLSEGRLRVHKSGTRGVIEMDFGLVVTYDWDGQLTLSLPKRFQDQVCGLCGNYNGDPADDFLTPDLDQAPDALEFANSWKLDDGDYLCDDGCHNSCPSCTPGQTQHYKGDRLCGMLTLSTGPFSACHEFLDPKPFLDDCVFDLCVTGGERLSLCRSLSAYAQACVELGVTLENWRLPASCPMSCPANSCYDPCSPACPPSCNSEAVPTNCSSRPCVEGCVCLPGFVASGGDCVPVSSCGCIYQGRLLAPGQEVFDDDRCRRRCTCDGATQKVTCRDTTGCPSGERCNVQNGLLGCYPDNFASCQASGDPHYVSFDGKRFDFMGTCTYLLVGSCGQNAALPAFKVLVENEHRGSQTVSYTRAVRVVAHGVEVAVRRENPGRVLVNGVLQYLPFQAAGGKIQVYRQGNDAIVSIDFGLTVTYNWDAHVTAKVPSSYAKDVCGLCGNFNGNPDDDLALKGGGQASNVLDFGNSWQEEIIPGCGATEPGDCPQLDSLVTQQIQDKKECGILADPEGPFRECHKLLNPQGAIRDCVYDLCLLPGQSGPLCDALAAYAAACQAAGGTVHPWRSEELCPLTCPPNSHYEQCSYGCPLSCGDLPVQGGCGSECREGCVCNEGFALSGESCVPLASCGCVHEGAYHAPGETFYPGPGCDSLCHCEEGGLVSCEPSSCGPQEACQPSNGVLGCVAVGTTTCQASGDPHYVTFDGRRFDFMGTCVYVLAQTCGNRPGLHQFTVLQENEAWGNGKVSVTKVITVLVANYTLRLEQSQWKVKVNGVDTKLPVMLDGGKIRVSQHGSDVVIETDFGLRVAYDLVYYVRVTIPGNYYKQMCGLCGDYNGDPKDDFQKPDGSQTTDPSDFGNSWEEAVPDSPCAPVPPCTGDDCDTECSPELQDKYHGEQFCGLLTSPTGPLAACHKLLDPQGPLQDCVFDLCLGGGNQSILCNIIHAYVSACQAAGGQVEPWRTETFCPMECPPHSHYEVCADTCSLGCWALNTPQQCPEGCAEGCECDSGFLYNGKACVPIEQCGCYHNGVYYEPEESVLIENCQQHCVCQPGKGMMCQDHSCKPGQVCEPSGGVLTCVTKDPCHGITCRPQETCKVQGGEGVCVPNYNSTCWLWGDPHYNSFDGWSFDFQGTCNYLLAGTLCPGVNAEGLTPFTVTTKNENRGSPAVSYVRQVTVTTLNTNISIHKNEIGKVRVNGVLMALPVYLAGGRISVINGGSKAVLETDFGLQVTYDWNWRVDVTLPSSYHGAVCGLCGNMDKNHQNDQVFPNGTMAPSIPTWGGSWQVPGWDPLCWHECQGSCPTCPEDRVEEYEGPGFCGPLAPGTGSPFTSCHAHVPPESFFKGCVLDVCLGGGSKDILCQALAAYAAACQAAGIKIEDWRTQAGCEITCPDNSHYELCGPPCPASCPPPARHTAPTVCDGPCVEGCQCDEGFVLSADQCVPLDGGCGCWVNGTYYEAGTEFWADTTCSKRCHCGPGGDSLVCKPASCGLGEECALLPSGEIGCQPTSITECQAWGDPHYTTLDGHRFDFQGTCEYLLSAPCHEPPTGTEYFNVTVANEHRGSQAVSYTRSVTLQIYGLSLTLSAQWPRKLQVNGEFVALPFHLDQKLSVYISGADVVVNTASGVSLAFDGDSFVRLRVPAAYAGTLCGLCGNYNKNPNDDLTAVGGKPEGWKVGGAPGCDQCEPEPCPKPCTPEEQEPFRGPDACGIITAPEGPLAPCHSLVPPTQYFEACLLDACQVQGHPGGLCPAIATYVAACQAAGAQLGEWRKPDFCPLQCPAHSHYQLCGDSCPVSCPSLSAPVGCETICREGCVCDAGFVLSGDTCVPVGQCGCLYQGRYYVLGATFYPGPECERLCECGPDGQVTCQEGADCEPYEECRIENGVQACHPTGCGHCLANGGLHYVTLDGRVYDLHGSCSYVLASVCHPKPGDEEFSIVLEKNSAGDPQRVVVTVAGQVVGLARGPQVTVDGEVVTLPVATGHVSVTAEGRNIVLQTNKGMKVLFDGDAHILMSIPSSFRGRLCGLCGNFNGNWSDDFVLPSGAVAPNVEAFGTAWRAPGSSLGCGEGCGPQGCPVCLAEETQAYEKNDACGKIRDPHGPFAACHKVLSPLEYFRQCVYDMCAHKGDKAYLCRSLAAYTAACQAAGAAVKPWRTDSVCPLQCPAHSHYSICTRSCQGSCAALSGLTGCTTRCFEGCECDDHFLLSHGVCIPAQDCGCVHNGQYMPVNSSLMSSDCSERCFCSPNNGLTCHEAGCPSGHVCEIQAGVRECQAARGLCSISVGANLTTFDGAHNAISSPGVYELSSRCPGLQKNVPWYRVLADVQPCHNNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Interferon-induced protein with tetratricopeptide repeats 2 (IFIT-2) (ISG-54 K) (Interferon-induced 54 kDa protein) (IFI-54K) (P54) (P09913)
Organism: Homo sapiens (Human)
Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Binds AU-rich viral RNAs, with or without 5' triphosphorylation, RNA-binding is required for antiviral activity. Can promote apoptosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21190939}. Endoplasmic reticulum {ECO:0000269|PubMed:21190939}.
Interaction partners:
- Interferon-induced protein with tetratricopeptide repeats 3
- Antiviral innate immune response effector IFIT1
- Antiviral innate immune response receptor RIG-I
- Interferon-induced helicase C domain-containing protein 1
- Ubiquitin-like protein ISG15
- Interferon-induced GTP-binding protein Mx1
- Interferon-induced protein 44
- Signal transducer and activator of transcription 1-alpha/beta
- 2'-5'-oligoadenylate synthase-like protein
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
Sequence:
MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAVAHLKKADEANDNLFRVCSILASLHALADQYEDAEYYFQKEFSKELTPVAKQLLHLRYGNFQLYQMKCEDKAIHHFIEGVKINQKSREKEKMKDKLQKIAKMRLSKNGADSEALHVLAFLQELNEKMQQADEDSERGLESGSLIPSASSWNGE
Protein: RuvB-like helicase (EC 3.6.4.12) (Q581V4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RuvB-like helicase
- SNF2 DNA repair protein, putative
- HIT-type domain-containing protein
- RNA polymerase II-associated protein 3
- Histone H2A
- Nucleolar RNA binding protein, putative
- Proteasome regulatory ATPase subunit 6
- Histone H2A
- High mobility group protein, putative
- uracil phosphoribosyltransferase
Sequence:
MSGIKIEEVISTTKKERVAAHSHVKGLGLDADGVAKPTADGFVGQVKAREAAGIVVELTRTKKMAGRALLFAGPPGTGKTALALGVAKELGPKVPFCPMVGSEVYSAEVKKTEVLMENFRRAIGLRIKEQKEVYEGEVTELRAEETDNPLGGYGKSISHVIVTLKSVKGSKQLKLDAAIYESLEKEKVAVGDVIYIESSTGAVKRVGRSDAYIGDHDLEADEYVPLPKGDVHKKKEIIQDVTLHDLDAANAKPNQGQDALSIVNSLMKQKKTEITEKLRHEINKVVNKYIDQGVAELVPGVLFIDEVHMLDIECFTFLNKALESTLAPVVIFATNRGSCRIRGTDVRSPHGIPTDLLDRLLIVRTSNYSIEEVVAIVDIRARVEGVSVSDAALELLGQIGDRTSLRYVAQLLTPALIIAETNGRSTIEVEDVTLVDGLFKDAKASAQMLHENAEDYVYQ
Protein: MSP7-like protein (Q8IDY3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKSKKIICSSCLFLIFLSVIFCSEPDTNSFDENVKKNEVFNALNEHLESISNIVKVNIMDALSNNPSLIKKTYEAVEINDDDYVLEYVGDSTGKYGEGSIFYDESKKYNYRKYLDIENELRNMKGEDDDDFDEDDDDFDEDDEDDEDDEDDEDDVDDEDDLDVEDNVDDEYDDEHNHNYNDDKLSENPEKYSNYNKNIHEDKKKDNLNEPHFKQTHYIYSSNHDNNETSRFPKKNVPKYDEKLNNEFKTYLRRPEKKEETKEYPNNGCSVVQISIVTNEDFLKKVRERNKKRNNKKRTNIYDSDEESESSEETSKDPYSSGPYTVDHKNENCFPYKQNSDIHPNINNDNNDNNENNDNNENNDNNIPVNNKKNSHTPHVPKDTKNNIEKNHSNYNYKPINQENLSMYFNNNNKKKNKKNSQKNNQKNNQKNNQKHNQDLYNIKKNNDLPQYEESNKTYKKIFSNEHEPRPMITTSRYENKISNDNNNNNYNLNEQERKLIKNMIDIFIYTYKLNYTNSKSISKLFKNNLLKKNFRTYFTNYIYTLFNYGKTYNFLTPYNKDNDHMYRQLFDEAVQMMDLLINKMDLALNPTKL
Protein: Trafficking protein particle complex subunit 9 (E9PU02)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex 2
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 2B
Sequence:
MSVPDYMQCAEDHQTLLVVVQAVGIVSEENFFRIYKRICSVSQLSVRDSQRALFIRYRHHYPPENNEWGDFQTHRKVVGLITITDCFSPKDWPQTFEKFHVQKEIYGSTLYDSRLFVFGLQGDVAEQPRPDVAFYPNYDDCDSVEKRIEDFIESLFIVLESKRLDRATDKSGDKIPLLCVPFEKKDFVGLDTDSRHYKKRCQGRMRKHVGDLCLQAGMLQDALVHYHMSVELLRSVNDFLWLGAALEGLCSASVIYHYPGGTGGKTGARRLPGNSLPSEAANRHRPGALTTNGINPDTSTEIGRAKNCLSPEDIIDKYKEAISYYSKYKNAGVIELEACVKAVRVLAIQKRGMEASEFLQNAVYINLRQLSEEEKIQRYSILSELYELIGFHRKSAFFKRVAAMQCVAPSIAEPGWRACYKLLLETLPGYSLSLDPKDFNKGTHRGWAAVQMRLLHELVYASRRMGNPALSVRHLSFLLQTMLDFLSDQEKKDVTQSLENYTAKCPGTMEPITLPDGLTLPPVPFTKLPIVRCVKLLSLPTSLRPQKVKSLLGQSMSTKSPFIYSPIIAHNRGEERNKKIDFQWVQGDVCEVQLMVYNPMPFELRVENMGLLTSGVEFESLPAALSLPAESGLYPVTLVGVPQTTGMITVNGYHTTVFGVFSDCLLDNLPGLKTSGSTVEVIPALPRLQISTSLPRSAHSLQPSAGDEIATNVSVQLFNGETQQLAITLENIGLEPLEQLEVTSKLLTTKEKLYGDFLSWKLEETLAQFPLQPGKVATFTINIKAKLDFSCQENLLQDLSDDGISVSGFPLSSPFRQVVRPRVESRPTNPSEGSKTGDLGHVKTLEAILNFKYSGGPGHVEGYYRNLSLGLHVEVEPSVFFTRVSTLPATSTRQCHLLLDVFNSTEHELTVCARNNSELVLHASECQRMAIQVDKFNFESVPESPGEKGHFANLKQLEEERQEARGLEISSKLDIRWRIPSLKRSGEASVEGLLNQLILEHLQLAPLQWDVLVDGQPCDCEVAAACQVGDPVRLEVRLTNRSPRSVGPFALTVVPFQDHQNGVHNYDLHDVISFVGSSTFYLDTVQPSGQSACLGALLFLYTGDFFLNIRFHEDCKSKELPPSWFCLPSVHVRALEAQA
Protein: T-cell antigen CD7 (CD antigen CD7) (P50283)
Organism: Mus musculus (Mouse)
Function: Not yet known.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- T-cell surface glycoprotein CD5
- T-cell surface glycoprotein CD4
- Aminopeptidase N
- Receptor-type tyrosine-protein phosphatase C
- Neural cell adhesion molecule 1
- Leukosialin
- Myeloid cell surface antigen CD33
- B-lymphocyte antigen CD19
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- Secreted and transmembrane protein 1A
Sequence:
MTQQAVLALLLTLAGILPGPLDAQDVHQSPRLTIASEGDSVNITCSTRGHLEGILMKKIWPQAYNVIYFEDRQEPTVDRTFSGRINFSGSQKNLTITISSLQLADTGDYTCEAVRKVSARGLFTTVVVKEKSSQEAYRSQEPLQTSFSFPAAIAVGFFFTGLLLGVVCSMLRKIQIKKLCASGIKESPCVVYEDMSYSNRKTPCIPNQYQ
Protein: Protein NLP6 (AtNLP6) (NIN-like protein 6) (Nodule inception protein-like protein 6) (Q8RWY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00852}.
Interaction partners:
- Transcription factor TCP20
- LOB domain-containing protein 37
- Nitrate reductase 1
- Ferredoxin--nitrite reductase, chloroplastic
- Protein NRT1/ PTR FAMILY 6.3
- Nitrate regulatory gene2 protein
- High-affinity nitrate transporter 2.1
- Transcription factor TGA1
- Transcription factor HRS1
- MADS-box transcription factor ANR1
Sequence:
MELDDLDLSGSWPLDQITFASNFKSPVIFSSSEQPFSPLWSFSETSGDVGGELYSAAVAPTRFTDYSVLLASSESETTTKENNQVPSPSWGIMPLENPDSYCAIKAKMTQALRYFKESTGQQHVLAQVWAPVKNRGRYVLTTSGQPFVLGPNSNGLNQYRMVSLTYMFSLDGERDGELGLPGRVFRKKLPEWTPNVQYYSSKEFSRLGHALHYNVQGTLALPVFEPSRQLCVGVVELIMTSPKINYAPEVEKVCKALEAVNLKTSEILNHETTQICNEGRQNALAEILEILTVVCETYKLPLAQTWVPCRHRSVLAFGGGFKKSCSSFDGSCMGKVCMSTSDLAVYVVDAHVWGFRDACAEHHLQKGQGVAGRAFQSGNLCFCRDVTRFCKTDYPLVHYARMFKLTSCFAVCLKSTYTGDDEYVLEFFLPPAITDKSEQDCLLGSLLQTMKQHYSSLKVVSETELCENNMSLEVVEASEDGMVYSKLEPIRIHHPAQISKDYLELNAPEQKVSLNSDFMENNEVDDGVERFQTLDPIPEAKTVKKSERKRGKTEKTISLEVLQQYFAGSLKDAAKSLGVCPTTMKRICRQHGISRWPSRKINKVNRSLTRLKHVIDSVQGADGSLNLTSLSPRPWPHQIPPIDIQLAKNCPPTSTSPLSNLQDVKIENRDAEDSAGSSTSRASCKVNPICETRFRLPTHNQEPSRQVALDDSDSSSKNMTNFWAHLTCQDTASPTILQHKLVSIKATYREDIIRFKISPESVSITELKQQVAKRLKLETAAFELKYLDDDREWVSVSCDADLSECLDTSAAKANTLRLSVHDVTFNFGSSCESSEETMMCL
Protein: 20beta-hydroxysteroid dehydrogenase type 2 (Hydroxysteroid (20-beta) dehydrogenase 2) (A2BFP6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Aromatase
- FabG like.
- Estradiol 17-beta-dehydrogenase 1
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Cytochrome P450 1A
Sequence:
MGDNAECCWYSIVLCGIGCVTVVYYMLRWSWQCWHGFKVYVISEIWRTDLRTYGRWAVVTGATSGIGRAYAEELAKRGLNIVLISRSEEKLHRVAKEIEDKYNQKTHVIQADFTEGHSIYSTITKQLEGLEIGILVNNVGMNYIGVLANFLDVPDPDQRITQVLNCNTLSVTQMCRVILPGMVERGKGLIINISSEAGYQPVPMVSLYSATKAFVTYFSLGLNAEYRSKGITVQCVAPFMVSTNMTHNVPVNPLVKSAASFARDALNTVGYTTYTSGCLTHALQHIVLSIVFPGWLRLTSFCVQRMEKFARRIEPQLNELMAENKTKQE
Protein: Inactive glutathione hydrolase 2 (Gamma-glutamyltransferase 2 pseudogene) (Inactive gamma-glutamyltranspeptidase 2) (GGT 2) (P36268)
Organism: Homo sapiens (Human)
Function: Lacks catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:23682772}. Endoplasmic reticulum {ECO:0000269|PubMed:23682772}. Note=Co-localizes with calnexin in the endoplasmic reticulum.
Interaction partners:
- N
- Gamma-glutamylcyclotransferase
- Alkaline phosphatase, germ cell type
- Killer cell immunoglobulin-like receptor 3DL2
Sequence:
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAMAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTGKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLWYVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVCSPVSGILFNNEWTTSALPAFTNEFGAPPSPANFIQPGKQPLLSMCLTIMVGQDGQVRMVVGAAGGTQITTDTALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAALDSRKGGEPAGY
Protein: Solute carrier family 12 member 4 (Electroneutral potassium-chloride cotransporter 1) (Erythroid K-Cl cotransporter 1) (hKCC1) (Q9UP95)
Organism: Homo sapiens (Human)
Function: Mediates electroneutral potassium-chloride cotransport when activated by cell swelling. May contribute to cell volume homeostasis in single cells. May be involved in the regulation of basolateral Cl(-) exit in NaCl absorbing epithelia (By similarity).
Subcellular location: Cell membrane {ECO:0000305|PubMed:10913127}; Multi-pass membrane protein {ECO:0000269|PubMed:31649201, ECO:0000269|PubMed:34031912}.
Interaction partners:
- Serine/threonine-protein kinase WNK3
- Serine/threonine-protein kinase H1
- Serine/threonine-protein kinase WNK1
- Serine/threonine-protein kinase WNK4
Sequence:
MPHFTVVPVDGPRRGDYDNLEGLSWVDYGERAELDDSDGHGNHRESSPFLSPLEASRGIDYYDRNLALFEEELDIRPKVSSLLGKLVSYTNLTQGAKEHEEAESGEGTRRRAAEAPSMGTLMGVYLPCLQNIFGVILFLRLTWMVGTAGVLQALLIVLICCCCTLLTAISMSAIATNGVVPAGGSYFMISRSLGPEFGGAVGLCFYLGTTFAAAMYILGAIEILLTYIAPPAAIFYPSGAHDTSNATLNNMRVYGTIFLTFMTLVVFVGVKYVNKFASLFLACVIISILSIYAGGIKSIFDPPVFPVCMLGNRTLSRDQFDICAKTAVVDNETVATQLWSFFCHSPNLTTDSCDPYFMLNNVTEIPGIPGAAAGVLQENLWSAYLEKGDIVEKHGLPSADAPSLKESLPLYVVADIATSFTVLVGIFFPSVTGIMAGSNRSGDLRDAQKSIPVGTILAIITTSLVYFSSVVLFGACIEGVVLRDKYGDGVSRNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAIAKDNIIPFLRVFGHGKVNGEPTWALLLTALIAELGILIASLDMVAPILSMFFLMCYLFVNLACAVQTLLRTPNWRPRFKYYHWALSFLGMSLCLALMFVSSWYYALVAMLIAGMIYKYIEYQGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLLKLDEDLHVKYPRLLTFASQLKAGKGLTIVGSVIQGSFLESYGEAQAAEQTIKNMMEIEKVKGFCQVVVASKVREGLAHLIQSCGLGGMRHNSVVLGWPYGWRQSEDPRAWKTFIDTVRCTTAAHLALLVPKNIAFYPSNHERYLEGHIDVWWIVHDGGMLMLLPFLLRQHKVWRKCRMRIFTVAQMDDNSIQMKKDLAVFLYHLRLEAEVEVVEMHNSDISAYTYERTLMMEQRSQMLRQMRLTKTEREREAQLVKDRHSALRLESLYSDEEDESAVGADKIQMTWTRDKYMTETWDPSHAPDNFRELVHIKPDQSNVRRMHTAVKLNEVIVTRSHDARLVLLNMPGPPRNSEGDENYMEFLEVLTEGLERVLLVRGGGREVITIYS
Protein: CUE domain-containing protein 2 (Q9H467)
Organism: Homo sapiens (Human)
Function: Down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway, regardless of the presence of 17 beta-estradiol. Also involved in 17 beta-estradiol-induced ESR1 degradation. Controls PGR protein levels through a similar mechanism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17347654}. Nucleus {ECO:0000269|PubMed:17347654}.
Interaction partners:
- Progesterone receptor
- TATA-box-binding protein
- Estrogen receptor
Sequence:
MELERIVSAALLAFVQTHLPEADLSGLDEVIFSYVLGVLEDLGPSGPSEENFDMEAFTEMMEAYVPGFAHIPRGTIGDMMQKLSGQLSDARNKENLQPQSSGVQGQVPISPEPLQRPEMLKEETRSSAAAAADTQDEATGAEEELLPGVDVLLEVFPTCSVEQAQWVLAKARGDLEEAVQMLVEGKEEGPAAWEGPNQDLPRRLRGPQKDELKSFILQKYMMVDSAEDQKIHRPMAPKEAPKKLIRYIDNQVVSTKGERFKDVRNPEAEEMKATYINLKPARKYRFH
Protein: Caerin-3.1 (P86505)
Organism: Litoria rothii (Roth's tree frog) (Hyla rothii)
Function: Antibacterial peptide with narrow spectrum of activity. Inhibits the formation of NO by neuronal nitric oxide synthase.
Subcellular location: Secreted {ECO:0000269|PubMed:16124032}.
Interaction partners:
Sequence:
GLWQKIKDKASELVSGIVEGVK
Protein: At2g46730/F19D11.1 (Death domain associated protein) (Expressed protein) (Q8VYU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MWTVKPAAMPVQFHMRPTVATSVAYSQPPPHNYDGIHRRFINVPTKSQTSESVGGLGQQILLRTVDSNPRKPIPKETEISGSDVLWAIQRATAQRKRTNAGKKKTKNRLSGVELSSSAGEPTGDNGVDYSNVTPLRIKSDWGHRLEEFEKLLKEFQNTEL
Protein: Immunoglobulin kappa variable 1-16 (Ig kappa chain V-I region BAN) (P04430)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVLAQLLGLLLLCFPGARCDIQMTQSPSSLSASVGDRVTITCRASQGISNYLAWFQQKPGKAPKSLIYAASSLQSGVPSKFSGSGSGTDFTLTISSLQPEDFATYYCQQYNSYP
Protein: Beta-amylase 1, chloroplastic (EC 3.2.1.2) (1,4-alpha-D-glucan maltohydrolase) (Beta-amylase 7) (Thioredoxin-regulated beta-amylase) (TR-BAMY) (Q9LIR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Beta-amylase activity. Can use p-nitrophenyl maltopentaoside (PNPG5) as substrate only in reduced form. Can play a minor role in the starch degradation and maltose metabolism in chloroplasts during the night. More active on phosphorylated glucan. Interacts directly with starch or other alpha-1,4-glucan.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16698902, ECO:0000269|PubMed:18390594}.
Interaction partners:
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- Alpha-amylase 1
- Probable alpha-amylase 2
- Alpha-amylase 3, chloroplastic
- Isoamylase 3, chloroplastic
- alpha-D-xyloside xylohydrolase
- Isoamylase 1, chloroplastic
- Isoamylase 2, chloroplastic
- Phosphoglucan phosphatase LSF1, chloroplastic
Sequence:
MALNLSHQLGVLAGTPIKSGEMTDSSLLSISPPSARMMTPKAMNRNYKAHGTDPSPPMSPILGATRADLSVACKAFAVENGIGTIEEQRTYREGGIGGKKEGGGGVPVFVMMPLDSVTMGNTVNRRKAMKASLQALKSAGVEGIMIDVWWGLVEKESPGTYNWGGYNELLELAKKLGLKVQAVMSFHQCGGNVGDSVTIPLPQWVVEEVDKDPDLAYTDQWGRRNHEYISLGADTLPVLKGRTPVQCYADFMRAFRDNFKHLLGETIVEIQVGMGPAGELRYPSYPEQEGTWKFPGIGAFQCYDKYSLSSLKAAAETYGKPEWGSTGPTDAGHYNNWPEDTQFFKKEGGGWNSEYGDFFLSWYSQMLLDHGERILSSAKSIFENMGVKISVKIAGIHWHYGTRSHAPELTAGYYNTRFRDGYLPIAQMLARHNAIFNFTCIEMRDHEQPQDALCAPEKLVNQVALATLAAEVPLAGENALPRYDDYAHEQILKASALNLDQNNEGEPREMCAFTYLRMNPELFQADNWGKFVAFVKKMGEGRDSHRCREEVEREAEHFVHVTQPLVQEAAVALTH