wanglab/gogpt-training-data huggingface dataset:
Protein: Agamous-like MADS-box protein AGL14 (Protein XAANTAL 2) (Q38838)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that regulates root development by controlling meristem size and patterning of the root apical meristem. Regulates auxin transport and gradients in the root meristematic cells via direct regulation of the auxin efflux carrier PIN1 and PIN4 gene expression. Binds specifically to the CArG-box DNA sequences in the promoter regions of PIN1 and PIN4 genes. Involved in the regulation of shoot apical meristem (SAM) cell identities and transitions. Promotes flowering transition and participates in flower meristem maintenance and determinacy. Positively regulates TFL1 and WUS expression. Binds directly to the TFL1 regulatory sequences.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Protein TERMINAL FLOWER 1
- MADS-box protein AGL24
Sequence:
MVRGKTEMKRIENATSRQVTFSKRRNGLLKKAFELSVLCDAEVALIIFSPRGKLYEFSSSSSIPKTVERYQKRIQDLGSNHKRNDNSQQSKDETYGLARKIEHLEISTRKMMGEGLDASSIEELQQLENQLDRSLMKIRAKKYQLLREETEKLKEKERNLIAENKMLMEKCEMQGRGIIGRISSSSSTSELDIDDNEMEVVTDLFIGPPETRHFKKFPPSN
Protein: S-adenosylmethionine synthase 1 (AdoMet synthase 1) (EC 2.5.1.6) (Methionine adenosyltransferase 1) (MAT 1) (P23686)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Homocysteine S-methyltransferase 3
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- S-adenosylmethionine decarboxylase proenzyme 1
- At1g77670
- S-adenosylmethionine decarboxylase proenzyme 2
- S-adenosylmethionine decarboxylase proenzyme 3
Sequence:
METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATVDYEKIVRDTCRAIGFVSDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKCPEEIGAGDQGHMFGYATDETPELMPLSHVLATKLGARLTEVRKNGTCAWLRPDGKTQVTVEYYNDKGAMVPIRVHTVLISTQHDETVTNDEIARDLKEHVIKPVIPEKYLDEKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFVDTYETGLIPDKEILKIVKESFDFRPGMMTINLDLKRGGNGRFLKTAAYGHFGRDDPDFTWEVVKPLKWDKPQA
Protein: Catalase (EC 1.11.1.6) (Q8GB51)
Organism: Edwardsiella tarda
Interaction partners:
Sequence:
MAGMVIYPIVNIDFLQFLEKTQLNKPSQHATTTEESAMNIVNGINGLIAKKNVLFFLTSLAISPSVLADTLTRDNGAPVGDNQNSQTAGPNGPVMLQDVQLLQKLQRFDRERVPERVVHARGTGAHGVFTPTADISDLTVAKVFTPGSTTPVFVRFSSVVHGTHSPETLRDPRGFATKFYTAEGNWDLVGNNFPTFFIRDAIKFPDMVHAFKPDPRTNLDNDARRFDFFSHLPESTRTLTLLYSNEGTPLSYRNMDGNSVHAYKLINDKGESPLCEVHWKTRQGIKNLDPQQVEQIQGKDYSHMTQDLVTAINRGDYPKWDLYIQVLRPADLKNFDFDPLDATKAWPDVPERKIGEMVLNKNPDNVFQETEQVAMAPSNLIPGIEPSEDKLLQGRLFAYADTQFYRIGANGLSLPINKPHSVVNNGNQDGQLNSGHTLDKGVNYQPSRIYPREELVSSRYSQTPLSGTTQQSKIQREQNFKQAGELYRSYSKKEQNDLINSLGTSLASADTVSKNIMLSYFYKADKDYGTRLTSVANGDLPTVKNLADKLQD
Protein: Netrin-1 (Q924Z9)
Organism: Rattus norvegicus (Rat)
Function: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (By similarity). Involved in dorsal root ganglion axon projection towards the spinal cord (By similarity). It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in colorectal tumorigenesis by regulating apoptosis (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:O95631}. Cytoplasm {ECO:0000250|UniProtKB:O95631}. Note=Mainly secreted. {ECO:0000250|UniProtKB:O95631}.
Interaction partners:
- Netrin receptor DCC
- Netrin receptor UNC5B
- Netrin receptor UNC5C
- Neogenin
- Netrin receptor UNC5A
- Cell adhesion molecule DSCAM
- Netrin receptor UNC5D
- Draxin
- Slit homolog 1 protein
- Repulsive guidance molecule BMP co-receptor a
Sequence:
MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNSSDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYYYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGFYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSMEEPEDCDSYCKASKGKLKMNMKKYCRKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIAXKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSXLVIQWRDTWARRXRKFQQREKKGKCKKA
Protein: Rifin (Q8I3D2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFAFPLNILVTLYHVNTHKKLSTTTCDIQTTRLLCECELYAPANYDNDPQMKEVMDKFSKQTQQRFEEYDERLQEKRQICKDKCDKEIQKIILKDKIEKQMQEQFATLQTDIQSDSIPTCVCEKSLADKFEKTCLKCGGVLGGGVAPELGLIGGTALYGISVWKPKAIASAIVEAQKAGEAAGKAAGDIAGVAEVISGLKSKFSLDTLFGTTLDKFITTKNYVNETVISGAVKLQYQVSCATDPLGETSVLCFYKTIGEPNATAAVVENAKIVVTDAIQEASEVAFKVTASKTAEFKEINIATVESICNSYNTAIIASIATIVVIILVMIVIYLILRYSRKKKMKKKLQYIKLLNQ
Protein: Pleckstrin homology domain-containing family G member 5 isoform X3 (Pleckstrin homology domain-containing, family G (with RhoGef domain) member 5a) (A0A0R4ISX1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MHRYGSPPKSWLGLRLRLCEKPAPEQKPGLLCQHPNCPEQRLASKVCHHPSCQDLRDGSPLHLCESCDSICHPAAHDGMIFDRHPRFDLQPQGSILARNVSTRSCPPRTGPPSDMEDGEDGCSDLGDRRSGGMKLVKKKTRRRHTDDPSKECFTLKFDLNFEVSMEIVPAVKKKTLREVLGAVFERKGIELSRVNLFLDQSNTPLSLGFEAYRFGGHYLRVRARPGEDLRVERCVKDPRSLSLPIMRSSSNTHSSSTDRAEHGSLGRREAADLLVGLVGHAAYIQKNGGQTRRRKNMPEFLGDSSISNQDSLSQLSGSLPGSITGPDRWRNRAASRFSGLFSSNSGNGSLGKECDRVEQLQSKLYSYTMFGLPKMPPQLSFHRDSWEEEPNLELEESWKQLLENPEILTRRQCHQQEAIWELLQTESDYIKKLHVITDLFLCGLLNLQESGLLTEVEPTRLFSNIQDIVQLHSSLWTEVMLPALEKARQKRTMLNPTELHQGFSTFGFRFKPYIRYCMEEEGCMEYMRTLLKDNELFRIYVTWAETHKQCNRLKLTDMLVKPHQRLTKYPLLLKSVLKKTDDPPTREAINRMVAAVECFINSVDSQMRHREEKQKLAAIAGRIEAYEAVEGASEEVERILKEYNNFDLMAPVMGAPPEETRQLLLEGALKMKEGKESRMDVYCFLFTDVLLITKPVKRVEKVKVIRQPLVIHNVVCRELKDPGSFLLIYLNEFGCAVASYCFQANSGAQGRSWIEAIYNAQNQLQRLRSETQRDESDEKDEDETESSMSTSSSPSIHHRETLSKSLSLSPSHSDGSTETLSVAAMDEVDEVVGSTVQTASMRNSLLSDDSFSTSDSKTLQALGDLIVTDLDPESRSLSIDSAYGTLSPQSMITELDLKGGVCQSEGEETDAGEEEEAFEDDEDDDDDGDDSITWNGSQITVNESYILDTNSEELNRRNDFSGMAQVVAGCRSQTLRRRSPVQPRPDYLQHFTLRSRSEDDLLQCLTDPLLLRPTGKNNVSKSLTHLAKQKSHSDEVFQTDEDELLEDAKTLSSKLSNTLQRAEARQVQRTLSCPNGQADSEGSDAETAPPGGMEEKKDLVVVQQTHQQHKKLTVAQLHKIRATMVLNSTLTASEV
Protein: Cleavage and polyadenylation specificity factor 30 kDa subunit (Q382Q6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Suppressor of forked domain-containing protein
- Cleavage and polyadenylation specificity factor-like protein, putative
- Cleavage and polyadenylation specificity factor subunit, putative
- C3H1-type domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Nucleic acid binding protein, putative
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 5
- Cleavage stimulation factor 50 kDa subunit
Sequence:
MFTDNAAHTSLAFEDTLPVEAPATAKRSEICQPFQHGKCRNGAACPERHVLSQFKSMRLEVCKHWLRGACVNGENCVYLHEYDDRYVPACAFYQRLGECSNPECPFQHVVQVERQPECAAYRRGFCPLGPKCRLRHVFRPPCVFYLTGFCPLGPKCALGHPVQQLYNRNDVSERLRQRMLIERADDPSFNKNATCYRCFDPGHLSPNCPGMQSGLLRRLLMALQEPGEQLYFQSDGRAARKCCFFCGEEGHEVRDCPKKQKPQQWGGHRRGDATGRQ
Protein: Serine incorporator 3 (Tumor differentially expressed protein 1) (Q13530)
Organism: Homo sapiens (Human)
Function: Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm.
Subcellular location: Cell membrane {ECO:0000269|PubMed:37474505}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9QZI9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9QZI9}.; SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000305|PubMed:26416734}. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (Probable). {ECO:0000305|PubMed:26416734}.
Interaction partners:
- Probable non-functional immunoglobulin heavy variable 3-16
- Glutaredoxin domain-containing cysteine-rich protein 1
Sequence:
MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVVPTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEGVQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS
Protein: EscB (Q4G4D3)
Organism: Edwardsiella tarda
Interaction partners:
Sequence:
MTSAPLSTQAENVARRCLALLEGRETQRPLSGASQDEMEAGYARGCQALNDGDLREATATFAFLALQQPLERRFTFAFACALQQQQEYRQALTLFSYALALRANDPFTPFHMAECLFALREPDAAMDALDATIALCYGQADGNPGYTLLRQRAQDLLDTLNQP
Protein: Poly(A) polymerase PAPa (EC 2.7.7.19) (Polynucleotide adenylyltransferase a) (Q9UW26)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA polyadenylation factor FIP1
- Cleavage and polyadenylation specificity factor subunit 2
- mRNA 3'-end-processing protein YTH1
- Protein CFT1
- RNA-processing protein
- Polyadenylation factor subunit 2
- Endoribonuclease YSH1
- Cleavage polyadenylation factor subunit
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Serine/threonine-protein phosphatase
Sequence:
MNNQAYGVTPPISVANSTPKENELNDSLIKELKSRGSFESETATKKRVEVLNILQSMTEEFVYKVSIKKNISEGMARDVGGKIFTFGSYRLGVYGPGSDIDTLVVVPKHVSRNDFFEVFYELLKGRSELEEIAPVPDAFVPIIKIEFAGISIDLIFARLDIPRVPRDLTLDDKNLLKNIDEKDLRALNGTRVTDEILQLVPKPTVFKHALRCIKMWAQQRAVYGNIFGFPGGVAWAMLVARICQLYPNAVSAVIVEKFFHIYSQWAWPQPVLLKQIEDGPLQVRVWNPRLYALDRQHRMPVITPAYPSMCATHNITSSTQKVILSEFQRGIELMNDINVGKKSWSDLLERHDFFFRYKFYLCIVAATRSTYAEHLKYSGMVESKLRLLVQKLELVEGIELAHPYVKSFENGYYCDNAEEAHEIMNLYGTSKGDDRVKGVLHAENNDNNKENVENKVELHMTKLFIGLKLDLSKEGEKKLDIQYPCAEFFNICKGWQDFDSEKHFIQIKNVKLYDLSDDVYVDGETRPIKIAKRKRAVSKNEGKKKPKSVGTVSAA
Protein: L-type lectin-domain containing receptor kinase VI.2 (LecRK-VI.2) (EC 2.7.11.1) (Lectin receptor kinase A4.1) (Q9M021)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in negative regulation of abscisic acid response in seed germination.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18987212}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Concanavalin A-like lectin family protein
- Concanavalin A-like lectin family protein
- Copper transport protein family
Sequence:
MGTQRSMFIVSFLFKLFLFLSVHVRAQRTTTNFAFRGFNGNQSKIRIEGAAMIKPDGLLRLTDRKSNVTGTAFYHKPVRLLNRNSTNVTIRSFSTSFVFVIIPSSSSNKGFGFTFTLSPTPYRLNAGSAQYLGVFNKENNGDPRNHVFAVEFDTVQGSRDDNTDRIGNDIGLNYNSRTSDLQEPVVYYNNDDHNKKEDFQLESGNPIQALLEYDGATQMLNVTVYPARLGFKPTKPLISQHVPKLLEIVQEEMYVGFTASTGKGQSSAHYVMGWSFSSGGERPIADVLILSELPPPPPNKAKKEGLNSQVIVMIVALSAVMLVMLVLLFFFVMYKKRLGQEETLEDWEIDHPRRLRYRDLYVATDGFKKTGIIGTGGFGTVFKGKLPNSDPIAVKKIIPSSRQGVREFVAEIESLGKLRHKNLVNLQGWCKHKNDLLLIYDYIPNGSLDSLLYTVPRRSGAVLSWNARFQIAKGIASGLLYLHEEWEKIVIHRDVKPSNVLIDSKMNPRLGDFGLARLYERGTLSETTALVGTIGYMAPELSRNGNPSSASDVFAFGVLLLEIVCGRKPTDSGTFFLVDWVMELHANGEILSAIDPRLGSGYDGGEARLALAVGLLCCHQKPASRPSMRIVLRYLNGEENVPEIDDEWGYSKSSRSEFGSKLVGYVSSTSITRVSSTSRISQ
Protein: Interferon-induced GTP-binding protein Mx2 (RBTMx2) (Q91196)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Does not inhibit strain RB-1 of the fish pathogen, infectious hematopoietic necrosis virus (IHNV).
Subcellular location: Nucleus {ECO:0000269|PubMed:9188599}. Cytoplasm {ECO:0000269|PubMed:9188599}. Note=Displays highly punctate staining of the nucleus. In some cells, punctate staining is observed in both nucleus and cytoplasm. {ECO:0000269|PubMed:9188599}.
Interaction partners:
Sequence:
MNYTLNQHYEEKVRPSIDLIDSLRSLGVEKDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLELKMKRKKEGEEWHGKISYQDREEEIEDPSDVENKIRKAQDEMAGVGVGISDDLISLEIGSPDVPDLTLIDLPGIARVAVKGQPENIGEQIKRLIRKFITKQETINLVVVPCNVDIATTEALKMAQEVDPDGERTLGILTKPDLVDKGTEETVVDIVHNEVIQLTKGYMIVKCRGQKEIMERVSLTEATEREKAFFKEHAHLSTLYDEGHATIPKLAEKLTLELVQHIEKSMPRLKEQIEEKLEETRTALEKCGTGPPEDPKERLYFLIDKVTLFTQDAINLSTGEELKSGDINVFSTLRTEFGKWKAYVDRSGKNFNKKIEKEVADYEKRYRGRELPGFINYKTFEVIVKDQIKQLEEPAVKKLKELSDAARKAFILLAQNSFTGFPILLKTAKTKIETIKQEKESTAESTLRTQFKMELIVYTQDSTYSSSLKKRKREEEELEEGELVKNNLGSWKGLPVVSVRSTVNGLDTHATLREMMLHLKSYYHIASQRLADQIPMVIRYLVLQEFASQLQREMLQTLQEKDNIEQLLKEDIDIGSKRAALQSKLKRLMKAHNYLVEF
Protein: Transmembrane protein 200A (Q86VY9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIATGGVITGLAALKRQDSARSQQHVNLSPSPATQEKKPIRRRPRADVVVVRGKIRLYSPSGFFLILGVLISIIGIAMAVLGYWPQKEHFIDAETTLSTNETQVIRNEGGVVVRFFEQHLHSDKMKMLGPFTMGIGIFIFICANAILHENRDKETKIIHMRDIYSTVIDIHTLRIKEQRQMNGMYTGLMGETEVKQNGSSCASRLAANTIASFSGFRSSFRMDSSVEEDELMLNEGKSSGHLMPPLLSDSSVSVFGLYPPPSKTTDDKTSGSKKCETKSIVSSSISAFTLPVIKLNNCVIDEPSIDNITEDADNLKSRSRNLSMDSLVVPLPNTSESFQPVSTVLPRNNSIGESLSSQYKSSMALGPGAGQLLSPGAARRQFGSNTSLHLLSSHSKSLDLDRGPSTLTVQAEQRKHPSWPRLDRNNSKGYMKLENKEDPMDRLLVPQVAIKKDFTNKEKLLMISRSHNNLSFEHDEFLSNNLKRGTSETRF
Protein: Stevor (O96283)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNIYYINMLVMSILLIVLFLSYNVNNHNKKYNVGYIQNNRQMIMMKSRRLAEIQLPKCPHYNNDPELKKIIDKLNEERIKKYIETNNSFEELHGLLVKERTKSLYENGMKKSSNMEKELLKKYDDSIRDEHNVISKSGIYTSDYRKLYDKSCDYQNQKILRDELASCCKVHDNYLDNLKKGCFGGVGICTLCSLLVSNIGIGYAVTAAKEVITGLYSLDIANKFTKALAGIYFFFSSSIENAGVSGVTIFYWDSMRMASIASSTINPYGIAALVLIVLVVVLIVLYIWLYRRRKKSWKHECKKHLST
Protein: Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 2 (Q8BM65)
Organism: Mus musculus (Mouse)
Function: Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis.
Interaction partners:
Sequence:
MIPSKMMSANPEEDPLDTFFQYIEDMGMKAYDGLVIQNASDIARENDRLRNETKLAYLKEKNEKRRRQEETIKRIGGEVGRGQDASYAGKHFRMGFMTMPAPQDRLPHPCSSGFTVRSQSLHSVGGTEDDSSCGSRRQPPPKPKRDPSTKLSTSSETVNSTAASKSGRSLERAEGKFTVPASHSPPRASTSGHLFPSPGSQERNIKVSAKPRPHSDEYSKKIPPPKPKRNPNTQLSTSFDETYIKKHVPRRTSLPRDSSLSQVCSPAADPEEEEPVYIEMVGNILRDFRKEEDDQSEAVYEEMKYPIFDDLGHDSKCDFDHHSCSSQCATPTVPDLDFVKSSGPCTPKGLLCDIPPPFPNLLSHRPPLLVFPPAPVHCSPNSDESPLTPLEVTKLPVLENVSYMKQPPGACPSSLPSHGSSHAKDQTGALGPAPGASILSSSPPPPSTLYRTQSPHGYPKSHSTSPSPVSMGRSLTPLSLKRPPPYDAVHSGSLSRSSSSVPHTTPRPVSQDGAKMVNAAVNTYSAAQSGSRSRTPTSPLEELTSLFTSGRSLLRKSSSGRRSKEPAEKSTEELKVRSHSTEPLPKLDSKERGHYGSSSSREPVKAQEWDGTPGPPVVTSRMGRCSVSPTLLAGNHSSEPKVSCKLGRSASTSGVPPPSVTPLRQASDLQQSQVPSSLANRD
Protein: Lysozyme-like protein 2 (O62416)
Organism: Caenorhabditis elegans
Function: Involved in resistance to Gram-positive bacteria P.aeruginosa or B.thuringiensis infection.
Interaction partners:
- Transient-receptor-potential-like protein
- Histone H2A
- C-type lectin domain-containing protein
- C-type LECtin
- C-type lectin domain-containing protein
- CUB-like domain-containing protein
Sequence:
MIKLLVSFTILFVLSSARPQEIDSNQAAIANTEANEAPVIVNNDASMGNAVDFSFPTNVQVMNCLKKAKYQVVFLRGFVPTGNGAFDSNCVGNIRNAYSAGLGIETYMTPQPISSWQGYQQLDLLYNGLNNNGITIRSVWIQVTSPANWPNNPTANVNFINSIISRAQQYGLSVGIYTNQYDWSQITGNSANINSNVMLWYWNVLGGGTSGETKPTFADFRAFGPFKKASVKQYAQVETVCNLVVNRDVYAVGIPAAAPKTEVNMADGEKIVVGGFVGN
Protein: Small ribosomal subunit protein uS11m (28S ribosomal protein S11, mitochondrial) (MRP-S11) (S11mt) (Q9DCA2)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82911}.
Interaction partners:
- Small ribosomal subunit protein uS5m
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS7m
Sequence:
MQVLRNSGSWLLLSWAGHGMTRFVGIAPAKNIHTGAPRLEDSAARQNTEREAAPSRFSLYPPVPGQESSLQWAGMKFEDVPIAHIKATYNNTQIQVVSATNASLARASCGTEGFRNAKKGTGIAAQTAGIAAAAKATGKGVTHIRVVVKGMGPGRWSAIKGLTMGGLEVISITDNTPVPHNGCRPRKARRL
Protein: Sphingoid long-chain bases kinase 2, mitochondrial (AtLCBK2) (LCB kinase 2) (EC 2.7.-.-) (O82359)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the production of sphingoid long-chain base (LCB). Is required for the cold-induced accumulation of phytosphingosine-phosphate, the regulation of the cold-responsive MPK6 and reduction of root growth at moderate low temperature.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18643979}.
Interaction partners:
- Sphingosine kinase 1
- Sphingosine kinase 2
- Neutral ceramidase 1
- Long chain base biosynthesis protein 1
- Alkaline ceramidase
- Long chain base biosynthesis protein 2a
- Ceramide kinase
- serine C-palmitoyltransferase
- Long chain base biosynthesis protein 2b
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2B
Sequence:
MLRSTCCTPLCPFTAKQPSFLRKQQRITSDRFTFRGGGGGDAAAVVSSSGLRDLVFVVNPQGANGRTAKEWKKLLPHLRSRLGKDCNVSELLTSGPSHAIDITREAIRDGADAVIAVGGDGTLHEVVNGFFWEGKPVGYLSGEASRSTALGLIPLGTGSDFARTFGWNNDPCEAVERIARGMRSRIDVGVIDKEGKDLHYFINVADVHLSAKAGFYASKYKKFGNLCYVIGALQAFMGHHNQDMRIRVNGGEWEIYPQVTALCVGNAKYFGGGMKITPNAIPGNGNLEVVVLQNFKWYDFVLKLHKLYNGTHLSVNNVTSRSVQSIEVEEITDSGSIYVQSDGEHLGFLPRKFQVLPGAIDIIS
Protein: N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)] (O70249)
Organism: Rattus norvegicus (Rat)
Function: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. {ECO:0000250}.
Interaction partners:
- Nei endonuclease VIII-like 1
- DNA repair protein XRCC1
- Endonuclease III-like protein 1 lyase)
- DNA repair nuclease/redox regulator APEX1
- Endonuclease 8-like 2 lyase Neil2)
- Adenine DNA glycosylase
- Flap endonuclease 1
- Uracil-DNA glycosylase
- Endonuclease 8-like 3
- DNA polymerase beta
Sequence:
MLFSSSLSSSMRHRTLTSSPALWASIPCPRSELRLDLVLASGQSFRWREQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDKGQVGRPTLEELETLHKYFQLDVSLTQLYSHWASVDSHFQSVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLVQLDDVTYHGFPNLHALAGPEVETHLRKLGLGYRARYVCASAKAILEEQGGPAWLQQLRVASYEEAHKALCTLPGVGTKVADCICLMALDKPQAVPVDIHVWQIAHRDYGWQPKTSQTKGPSPLANKELGNFFRNLWGPYAGWAQAVLFSADLRQQNLSREPPAKRKKGSKKTEG
Protein: Basigin (5A11 antigen) (Blood-brain barrier HT7 antigen) (Neurothelin) (P17790)
Organism: Gallus gallus (Chicken)
Function: Essential for normal retinal maturation and development (By similarity). Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors. In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:25957687}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P18572}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P18572}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:2357963}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Basolateral cell membrane {ECO:0000250|UniProtKB:P35613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
Interaction partners:
- Cytosolic endo-beta-N-acetylglucosaminidase
- Monocarboxylate transporter 4
Sequence:
MAAGADVPCAVLALLVLGSLAAGGDATAGFIKSPLSQRRLTQDSVELHCEAVGSPIPEIQWWFEGNEPNETSAQLWDGAWQDRVQINATYNLHSTSTIYIANLTSDDSGTYECRASNDPDRNHLSKSPKVKWIRSQANVLVIERPVITGQYSSSADKVVLSCNISAPPTLIKGHKWMLGDKVLKTDESDASSYISYTIEGKVEDHSGVYECIYNTNPVAKGNVSIEVEPQVVAYKKSEHGNEGDVGVLTCKSPSYPPVDHWAWYKSGQTVPLESSAGIYNISRTGNKTELRILKLNIEQDMGDYSCNGTNMKGSGSATVNLRVRSRLAALWPFLGIVAEVLVLVTIIFIYEKRRKPDEVLDDDDGGSAPLKSNATNHKDKNVRQRNAN
Protein: Ribose-phosphate pyrophosphokinase A (EC 2.7.6.1) (Phosphoribosyl pyrophosphate synthase A) (Q54PA9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Transketolase
- Amidophosphoribosyltransferase
- Probable phosphoglucomutase-2
- Ribose-5-phosphate isomerase
- Ribokinase
- Uridine 5'-monophosphate synthase
- Phosphoglucomutase-1
- Nudix hydrolase domain-containing protein
- Ribose-phosphate pyrophosphokinase C
- Ribose-phosphate pyrophosphokinase B
Sequence:
MGDRIKILTGNAHRELASEISDDLNLALGKAHVGKFSNGETSVMISESIRDMDVYIIQPTCNPNVNDNLMELLIMADAIRRASAHRITAVIPCFGYARQDKKDKSRAPITGKLVANLIETAGIDRVITMDLHASQIQGFFNIPVDNLYAEPQIIKYIRKYIPGEKVIVSPDAGGVKRAKSISDKLDADLAIIHKERKKANEVSGMILVGDVKDKVALIVDDMADTCGTLVSACEMLISKGATKVYALVTHGVLSGDAIQKLNESSLTELVITNTIPHAEKAAKCPKIKTINIAHTLSEAIRRTHHGESISSLFSDTK
Protein: Negative elongation factor E (NELF-E) (RNA-binding protein RD) (P18615)
Organism: Homo sapiens (Human)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14701750}. Chromosome {ECO:0000269|PubMed:14701750}. Note=Localizes to chromatin (PubMed:14701750). Phosphorylation by the P-TEFb complex promotes its release from chromatin (PubMed:14701750). {ECO:0000269|PubMed:14701750}.
Interaction partners:
- Negative elongation factor A
- Negative elongation factor B
- Negative elongation factor C/D
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
- Cyclin-dependent kinase 9
- Cyclin-T1
- Cyclin-T2
Sequence:
MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESFVSSSDRLRELGPDGEEAEGPGAGDGPPRSFDWGYEERSGAHSSASPPRSRSRDRSHERNRDRDRDRERDRDRDRDRDRERDRDRDRDRDRDRERDRDRERDRDRDREGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGKSVWGSLAVQNSPKGCHRDKRTQIVYSDDVYKENLVDGF