wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-induced protein 44 (Microtubule-associated protein 44) (Q8BV66)
Organism: Mus musculus (Mouse)
Function: This protein aggregates to form microtubular structures.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Antiviral innate immune response effector IFIT1
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Ubl carboxyl-terminal hydrolase 18
- 2'-5'-oligoadenylate synthase-like protein 2
- Interferon-induced protein with tetratricopeptide repeats 3
- Receptor-transporting protein 4
- Interferon-induced helicase C domain-containing protein 1
- Ubiquitin-like protein ISG15
- Antiviral innate immune response receptor RIG-I
- Interferon-induced protein with tetratricopeptide repeats 2
Sequence:
MAMRTRLTWQQEKCLQNYFGGKRFCLLYKASVQKFSHQNLLCTCENQGPTMIVVYSEKCVIGMYLKEGFQGKDVSITIFALQETGFSLCAKGPDSPYLLFHKRKTNDFSILLDEKAVIVSSAICKMLQLTARNNVIPIQECEAFRCEELLDERKTRGIAVLHSNLLQALRDYKPYGDLVQQTRVLLLGPIGAGKSSFVNSVKSVFKGSITHQILVGCDEDGISDKYRTYSIKAKDDSDPLPFILCDSLGLGENAGLHTDDVWHILKGHTPDRYQFDSMKPITSNHPNYTHDPLLKDRIHCVVFVFDINSFEMHSSELVAKIKKIRRDLIKHGILHLALLTHVDSLDLITKEDMTDIYNYSPVKSKLEAFHGVFGFALSDILVVSNYVSEWQLDPVKDMLILSALKEILYTANEFLEDLPLNK
Protein: Anti-sigma factor (Q9X914)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Interaction partners:
- Anti-sigma-B factor antagonist
- tRNA adenosine deaminase-associated protein
- Conserved integral membrane protein
- K
- Helicase
Sequence:
MATVELRFSALPEHVRTARLVAAAVARRAGVDEAVLDEVRLAVGEACTRAVGLHQHVGITAPVKVSLIEEEKQFSIEVGDEAPHAVPGVKTSGDAVDELEAEEDEMGLAVISGLVDDVEVSAGEDGGLIRMTWPTASAVLPPI
Protein: MAL-like protein (Protein BENE) (Q13021)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nephrocystin-1
- Tumor protein D54
- Caveolin-1
Sequence:
MASPDPPATSYAPSDVPSGVALFLTIPFAFFLPELIFGFLVWTMVAATHIVYPLLQGWVMYVSLTSFLISLMFLLSYLFGFYKRFESWRVLDSLYHGTTGILYMSAAVLQVHATIVSEKLLDPRIYYINSAASFFAFIATLLYILHAFSIYYH
Protein: Serine/threonine-protein phosphatase PP1-gamma (EC 3.1.3.16) (CeGLC-7-gamma) (Glc seven-like phosphatase 3) (O02658)
Organism: Caenorhabditis elegans
Function: Probable phosphatase which plays a redundant role with gsp-4 in spermatogenesis by regulating sister chromatid segregation during meiosis. In addition, involved in sperm motility by controlling the dynamic disassembly of major sperm proteins (MSP) in the spermatozoan pseudopodium.
Subcellular location: Chromosome {ECO:0000269|PubMed:16943775}. Cell projection, pseudopodium {ECO:0000269|PubMed:22042574}. Cytoplasm {ECO:0000269|PubMed:22042574}. Note=Co-localizes with MSP in oblong stripes in the cytoplasm of inactive sperm and in the pseudopodium in activated sperm. {ECO:0000269|PubMed:22042574}.
Interaction partners:
- Major sperm protein
- Membrane transporter protein
- non-specific serine/threonine protein kinase
- PDZ domain-containing protein
- SPerm CHromatin enriched
- MFS domain-containing protein
- DUF389 domain membrane protein
- Expressed conserved protein
- Nematode Specific Peptide family
- non-specific serine/threonine protein kinase
Sequence:
MTAPMDVDNLMSRLLNVGMSGGRLTTSVNEQELQTCCAVAKSVFASQASLLEVEPPIIVCGDIHGQYSDLLRIFDKNGFPPDVNFLFLGDYVDRGRQNIETICLMLCFKIKYPENFFMLRGNHECPAINRVYGFYEECNRRYKSTRLWSIFQDTFNWMPLCGLIGSRILCMHGGLSPHLQTLDQLRQLPRPQDPPNPSIGIDLLWADPDQWVKGWQANTRGVSYVFGQDVVADVCSRLDIDLVARAHQVVQDGYEFFASKKMVTIFSAPHYCGQFDNSAATMKVDENMVCTFVMYKPTPKSMRRG
Protein: G patch domain and ankyrin repeat-containing protein 1 (Ankyrin repeat domain-containing protein 59) (G patch domain-containing protein 10) (HLA-B-associated transcript 4) (Protein G5) (O95872)
Organism: Homo sapiens (Human)
Interaction partners:
- Apolipoprotein M
- Protein PRRC2A
Sequence:
MSRPLLITFTPATDPSDLWKDGQQQPQPEKPESTLDGAAARAFYEALIGDESSAPDSQRSQTEPARERKRKKRRIMKAPAAEAVAEGASGRHGQGRSLEAEDKMTHRILRAAQEGDLPELRRLLEPHEAGGAGGNINARDAFWWTPLMCAARAGQGAAVSYLLGRGAAWVGVCELSGRDAAQLAEEAGFPEVARMVRESHGETRSPENRSPTPSLQYCENCDTHFQDSNHRTSTAHLLSLSQGPQPPNLPLGVPISSPGFKLLLRGGWEPGMGLGPRGEGRANPIPTVLKRDQEGLGYRSAPQPRVTHFPAWDTRAVAGRERPPRVATLSWREERRREEKDRAWERDLRTYMNLEF
Protein: Always early, isoform A (Always early, isoform B) (Q9VZW3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Lin-52, isoform A
- Chromatin assembly factor 1 p55 subunit
- RT06796p1
- LD06557p
- Transcription initiation factor TFIID subunit 8
- Protein lin-54 homolog
- Myb protein
- Wake-up-call, isoform A
Sequence:
MSVDPLSIDNFTIQSEICEENEFLANIGLLSTTTMSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRIKPGVASKRTENFTKKPSNISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGNSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (EC 6.2.1.5) (Succinyl-CoA synthetase beta chain) (SCS-beta) (O82662)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03219, ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022}.
Interaction partners:
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- AT3g59090/F17J16_140
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex 2, mitochondrial
Sequence:
MRGLVNKLVSRSLSISGKWQNQQLRRLNIHEYQGAELMGKYGVNVPKGVAASSLEEVKKAIQDVFPNESELVVKSQILAGGRGLGTFKSGLKGGVHIVKRDEAEEIAGKMLGQVLVTKQTGPQGKVVSKVYLCEKLSLVNEMYFSIILDRKSAGPLIIACKKGGTSIEDLAEKFPDMIIKVPIDVFAGITDEDAAKVVDGLAPKAADRKDSIEQVKKLYELFRKTDCTMLEINPLAETSTNQLVAADAKLNFDDNAAFRQKEVFAMRDPTQEDPREVAAAKVDLNYIGLDGEIGCMVNGAGLAMATMDIIKLHGGTPANFLDVGGNASEHQVVEAFKILTSDDKVKAILVNIFGGIMKCDVIASGIVNAAKEVALKVPVVVRLEGTNVEQGKRILKESGMKLITADDLDDAAEKAVKALAH
Protein: Cyclin-dependent kinase 8 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division protein kinase 8) (Mediator complex subunit CDK8) (Mediator of RNA polymerase II transcription subunit CDK8) (Protein kinase K35) (P49336)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Phosphorylates CCNH leading to down-regulation of the TFIIH complex and transcriptional repression. Recruited through interaction with MAML1 to hyperphosphorylate the intracellular domain of NOTCH, leading to its degradation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 17
- Cyclin-C
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 18
Sequence:
MDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPGNQDSSHTQGPPLKKVRVVPPTTTSGGLIMTSDYQRSNPHAAYPNPGPSTSQPQSSMGYSATSQQPPQYSHQTHRY
Protein: Ribonuclease H2 subunit A (RNase H2 subunit A) (EC 3.1.26.4) (Q54D13)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Participates in DNA replication (By similarity).
Interaction partners:
- Ribonuclease H2 subunit B
- Proliferating cell nuclear antigen
- CLPTM1-like membrane protein cnrB
- DNA primase
- DNA polymerase epsilon catalytic subunit A
- DNA helicase
- RNase H type-1 domain-containing protein
- Proteasome subunit beta type-2
- DNA topoisomerase 1
Sequence:
MDNKIIYLTELDSSVDKSEPFVMGIDEAGRGPVMGPMVYGCCYAPISKSTTLKSMKFNDSKKLTEQQRDQLFDKMGESNKILAYETDVITAEILSEKMLYKKPISLNVISHESAIGLIRSVLKKGVNVQELYLDTVGPPDKYQLMLKKLFPEIGKIIVSKKADSLYPIVSAASIAAKVVRDFEITNKNFDYLNIYDQDEQLSTDFGSGYPSDPLSKKWLVKNRDKVFGYPNFIRFSWKTTETAMRGACFGVDWVLENDKLKQHFQENQNDKKRFMFFKENNIENCINDF
Protein: Cinnamyl alcohol dehydrogenase 3 (AtCAD3) (EC 1.1.1.195) (Q9SJ10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Interaction partners:
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Aldehyde dehydrogenase family 2 member C4
- Flavone 3'-O-methyltransferase 1
- F5F19.5 protein
- Cytochrome P450 84A1
Sequence:
MVDQNRAFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRSSDGTRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHALLPLFSLLKVSGKLVALGLLEKPLDLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSDINSAMDRLVKSDVRYRFVIDVANSLLPESSAEILTEHVDHGVSITSRF
Protein: GRAM domain-containing protein (Q55FU7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- EGF-like domain-containing protein
- Transmembrane protein
- Winged helix repair factor 1
- EGF-like domain-containing protein
- EGF-like domain-containing protein
- C2 domain-containing protein DDB_G0290753
- Transmembrane protein
- von Willebrand factor A domain-containing protein DDB_G0292028
- Purple acid phosphatase N-terminal domain-containing protein
- WW domain-containing protein
Sequence:
MASLPNNSSGSVMISPNQGPISHDSNNFSSSSPISSPYLIQNGGPQSPTVFSPIGSTSPKTHNTLNNSNNNNNNNGHFSPPTTSSSDNDHSINKLKTRSHSSEDLKSISSDEKKKKLFVTPKLIAPSKKNGSSSSDEPPVSKTIEGRMKSEPFTKKFKLPSTEILLHDYSAALFRQILLHGRIYLFTNHICFESKIFGIKTSEVIPIKDVIQIKKKSRFTVGIEIITSENVKYSFASFVSRDKTYKDLLEVWKDVTGETHEDASSLSIDDDIEDEISNNELDNHNNNQQQQINNNNNNNVNNVQQQQQQQQQQQNGNYNSNINNEPQQQLHQSQQQPSQQQTPLTSSIVKEDMTNINNNSGNSVNNTLTNSQIKNIQQQQQQQQQQQQQQQQQQQQQQQQQQNQQNNNSDGSGSNDSSTTAIPVVGIVAASTITSSSSSTTMTSSSTTTTTTQPLTTIKEIEKDPLDEIYGGVEQYLSKDQQPQSILESQSSDFQEILSDNFNVSVVNFYRALYSDRCNFVHSYHVKRGDMNVNVKPWTFRERFGTIREVEYVAPVSSPIGPDKTRIQETQRYQLTRKKLIVETDTIMLDIPYGDHFRIEAKWEVTETSQDTCRLSISLTVRFVKKTWFKSKIETTTVKETKTSFDKWVQLAKVEVQKMLQVKPLPSASSSTATNTTNNNKVVNHHNGAGSLTPTILIPSLNKSMDKNEMVARLKQDDERLESPKPHHTRSRSRQHLISSSSQVNSTSPPPNPMISSNNNNNNSNNSIGNIVNSTSNSSNSLQSQISPPILPNSPFNLTNNGADNNTNSTNISSDSIKSTFEKKNNNLEKVSDESGKFILKTPFGVLSFGSSQLSILVICSLLFILYSYMFMKILTLSSKIDTMESIFKDLINKNLNK
Protein: Aquaporin-9 (Q7Z138)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGVFQDKVASILRIEDQQFTRELLAECIGTFFLLLIGNAANIQAAVAVGGNSTSCHIAWGIGFMFAVYLAASVSGGHLNPAISVAQSILGNLPPWKIIPYAIAQVIGAFLGAAVAYFGHHDDLWKLDGGIRQVTGGQATAGLFTTFPPDHMSVWGSLLDQIIGTAMLSGLVCLITDKRHQIPTGVVPVLAGSIMSMVAMTFGANGGFAINPARDFGPRVFCLCAGYGWEVFSAHGYYFWIPIVGALIGSIIGAWIYKIFVGLHGMNESLDIQPAKGFNEMQRNSEGILIGYDNTLSRARGGEIAAPRTYTPSYQVFESSRTQITTADRRY
Protein: Brevinin-1OKa (C0HL08)
Organism: Nidirana okinavana (Kampira Falls frog) (Babina okinavana)
Function: Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=12.5 uM) and against Gram-positive bacterium S.aureus (MIC=12.5 uM).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P86027}.
Interaction partners:
Sequence:
FFGSMIGALAKGLPSLISLIKK
Protein: Immunoglobulin kappa variable 3-15 (Ig kappa chain V-III region CLL) (Ig kappa chain V-III region POM) (P01624)
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:
MEAPAQLLFLLLLWLPDTTGEIVMTQSPATLSVSPGERATLSCRASQSVSSNLAWYQQKPGQAPRLLIYGASTRATGIPARFSGSGSGTEFTLTISSLQSEDFAVYYCQQYNNWP
Protein: Pyruvate dehydrogenase E1 component subunit beta (EC 1.2.4.1) (Q57ZD2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- pyruvate dehydrogenase
- 2-oxoisovalerate dehydrogenase subunit alpha
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase, putative
- Dihydrolipoyl dehydrogenase
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Acetyl-coenzyme A synthetase
Sequence:
MRRFATTFSASSAALGSRTVTSLTVRDALNSAIDEELSRDKTVFVLGEEVGQYQGAYKVTRGLVDKYGTSRVIDTPITEHGFAGMAVGAAMNGMRPVCEFMTMNFAMQAIDQIVNSAGKGLYMSAGQLKCPIVFRGPNGASAGVGAQHSQCFAAWYASIPGLKVFSPYSSEDARGMLKAAIRDDNPVVMLEHELMYGETFKVSDEAMGEDFVIPFGKAKIERPGKDITMIGFSRGVSLCLKAAEQLAKSGIEAEVINLRSLRPLDRATIIQSVKKTGRAMTVDESFPICNIGAEICAIVMESEAFDYLDAPMERVSCADCPTPYSKNLEVASQPQVSDVLDVARRILS
Protein: Dementin, isoform H (E1JJ71)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDTTPNAAPNPNQNRDFVTLKPLRPSRGSSSNLRASRSPSASRSTEQMSRERASEAAAATQTAAATAGGATAHSAGGTAGGSAAATTTAGGATSGSGTASANTNSNSSASSSTVAAAQAAVYSGGNTVTGSLGSAGVVARGFRSHSPTHRRRSRERQRRTHGSDQGGLLAYSGLVGVNDMTDFLGPQQGGGGGGGGGGGGGGGGGSAGTGSGLEDSRLSGNEDYYSSFVSDEFDSSKKVHRRCHERSSSVQAIDRLNTKIQCTKESIRQEQTARDDNVNEYLKLAASADKQQLQRIKAVFEKKNQKSAHNISQLQKKLDNYTKRAKDLQNHQFQTKSQHRQPREVLRDVGQGLRNVGGNIRDGITGFSGSVMSKPREFAHLIKNKFGSADNINQMSEAELQGMQSANADVLGSERLQQVPGAGTSTGSGGGGQNNNTGGAGSGTGKFNSDNGSECSSVTSESIPGGSGKSQSGASQYHIVLKTLLTELAERKAENEKLKERIERLETGQKEFNNLTATLESERYRAEGLEEQINDLTELHQNEIENLKQTIADMEEKVQYQSDERLRDVNEVLENCQTRISKMEHMSQQQYVTVEGIDNSNARALVVKLINVVLTILQVVLLLVATAAGIIMPFLKTRVRVLTTFLSICFVIFVIRQWPDVQDIGSGLVRHLKQSLVVK
Protein: UVR domain-containing protein (Q9JK28)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
ILEFLHRLDVENSSDVAVSVLHSLFSMTPLSELVGICKNDDGRKLIPVETLTPEIALYWCTLCEYLKSKGDEGEEFLEQILPEPAVYAEYLLSYIQGFPVVNEEQKGDFTFIGDLMKREFIGQQLILIMKSLDTSEEGGRKRLLAILQETLILPTTPISLVSLIVERLLHIIRDDNERIQIVTEIISEIRAPIVNVVVDPSDTRKKELKMAEIKVKLIEAKEALENCIAVQDFDQASKLKEEIKILEDAKINLLKETEQLEIKEVHTGKGTMRKHYRSVLFCVTNC
Protein: CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A) (ssDNase Cas10) (EC 3.1.-.-) (Cyclic oligoadenylate synthase) (EC 2.7.7.-) (ToCsm1) (B6YWB8)
Organism: Thermococcus onnurineus (strain NA1)
Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities.
Interaction partners:
- CRISPR system Cms endoribonuclease Csm3
- CRISPR system Cms protein Csm4
- CRISPR system Cms protein Csm5
- CRISPR system Cms protein Csm2
- CRISPR associated protein Cas6 C-terminal domain-containing protein
- CRISPR system endoribonuclease Csx1 CARF domain-containing protein
- CRISPR-associated endoribonuclease Cas2
Sequence:
MEIDELTALGGLLHDIGKPVQRAGLYSGDHSTQGARFLRDLAENTGRAEYELLSLFSEFHHKGHMKNDELMIRRIKELSPERFGLTMEDVLNALWIVYEADNLASGEREEGQPQASRPLYSVFNPGKAYPWAELDFEKELPVPGDVFSIRSQDYRELVKRLWEELSKAKLRSDRLLPVLEKYLTFVSSVTSEGNIISLYDHMRMTSAIALAMLRAGCTAEDVRSGRCRKEKRFLLIEGDFSGIQDFIYRVSGKGTLKYLRARSAYLELIGWDVVLEILSRLGLTRANVVFNAGGHFMIIAQNTPDAVKELEEIRAKAVEWLYREFESDLYLAIEWEPVSGREFGREGGKNLFAEARKRLKHKLTVRKLKRFGEIKGLFEHGHTERLAECPVCGRELPEGKLEPSASDPETKVCPTCNRLVSLGGNLPKLLGFGRTAKNDAGVLVEGPFSGFVPYLQGGRPVGEQILVKNTLNPGEIPESAQFVPYFVADYFKKDPKGGVATFEELSMASTGTRRLGVMKGDVDRLGEFFSSMDSPSKLATASRFMDYFFKGYIGAIIEGKFGYIIGDVPSLRDWPEEPDIVVVYAGGDDFFIVGAWDQIFELAFRVRRAFNAYTGGKLTLSVGLGYFDERTPIYRMADVVSERLDTAKDEGRNRVFVVGRSRPLDGKHKLSYEWNHYEELWRTYAPRIYAGNGRLKGKLESKKGLLWKLLEIRELYVRDPNDVRWAYLTAYLLGRHGLSDLFPELVGIDTKAVERKEPQPVYWVDGVLKIVLMAVRR
Protein: Ubiquitin-conjugating enzyme E2 (Q84K64)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Ubiquitin-conjugating enzyme E2 variant 1A-like
- Ubiquitin-conjugating enzyme E2 variant 1A-like
- Ubiquitin-conjugating enzyme E2 variant 1A-like
- Ubiquitin-conjugating enzyme E2 variant 1C-like
- Ubiquitin-conjugating enzyme E2 variant 1A-like
- Ubiquitin-conjugating enzyme E2 variant 1A-like
- Ubiquitin-conjugating enzyme E2 variant 1D-like
- E1 ubiquitin-activating enzyme
- E1 ubiquitin-activating enzyme
- E1 ubiquitin-activating enzyme
Sequence:
MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATLMGPSDSPYAGGVFLVSIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRAKYEATACGWTQKYAMG
Protein: Metastasis associated 1 family, member 2 (F7F888)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILNQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKFQAEIPDRLAEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQVKKRLKAAEADSKLKQVYIPTYTKPNPNQIISVGSKPGMNGAGFQKGLTCESCHTTQSAQWYAWGPPNMQCRLCASCWIYWKKYGGLKTPTQLEGAARGTTEPHSRGHLSRPEAQSLSPYTTSANRAKLLAKNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLARLPLAAIVKDLVAQAPLKPKTPRGTKTPINRNQLTQNRGLGGIMVKRSYETMAGAGVPFSANGRPLASGIRSSSQPAAKRQKLNPADAPNPVVFVATKDTRALRKALTHLEMRRAARRPNLPLKVKTALMTVRPPVPLPASSHPASTNEPIVLED
Protein: Leucine-rich repeat neuronal protein 1 (Neuronal leucine-rich repeat protein 1) (NLRR-1) (Q6UXK5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MARMSFVIAACQLVLGLLMTSLTESSIQNSECPQLCVCEIRPWFTPQSTYREATTVDCNDLRLTRIPSNLSSDTQVLLLQSNNIAKTVDELQQLFNLTELDFSQNNFTNIKEVGLANLTQLTTLHLEENQITEMTDYCLQDLSNLQELYINHNQISTISAHAFAGLKNLLRLHLNSNKLKVIDSRWFDSTPNLEILMIGENPVIGILDMNFKPLANLRSLVLAGMYLTDIPGNALVGLDSLESLSFYDNKLVKVPQLALQKVPNLKFLDLNKNPIHKIQEGDFKNMLRLKELGINNMGELVSVDRYALDNLPELTKLEATNNPKLSYIHRLAFRSVPALESLMLNNNALNAIYQKTVESLPNLREISIHSNPLRCDCVIHWINSNKTNIRFMEPLSMFCAMPPEYKGHQVKEVLIQDSSEQCLPMISHDSFPNRLNVDIGTTVFLDCRAMAEPEPEIYWVTPIGNKITVETLSDKYKLSSEGTLEISNIQIEDSGRYTCVAQNVQGADTRVATIKVNGTLLDGTQVLKIYVKQTESHSILVSWKVNSNVMTSNLKWSSATMKIDNPHITYTARVPVDVHEYNLTHLQPSTDYEVCLTVSNIHQQTQKSCVNVTTKNAAFAVDISDQETSTALAAVMGSMFAVISLASIAVYFAKRFKRKNYHHSLKKYMQKTSSIPLNELYPPLINLWEGDSEKDKDGSADTKPTQVDTSRSYYMW
Protein: Zinc finger protein 883 (P0CG24)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESEKIYMTANPYLCTECGKGYTCLASLTQHQKTHIGEKPYECKICGKSFTRNSNLVQHQRIHTGEKPYECNECGKAFSQSTNLIQHQRVHTGEKPYECNECEKTFSHRSSLRNHERIHTGEKPYPCNECGKAFSHISALTQHHRIHTGKKPYECTECGKTFSRSTHLIEHQGIHSEEKSYQCKQCRKVFCHSTSLIRHQRTHTGEKPYECNECGKAFSHTPAFIQHQRIHTGEKPYECNACGKAFNRSAHLTEHQRTHTGEKPYVCKECGKTFSRSTHLTEHLKIHSCVKPYQCNECQKLFCYRTSLIRHQRTHTGEKPYQCNECGKSFSLSSALTKHKRIHTRERPYQCTKCGDVFCHSTSLIRHQKTHFRKETLAE
Protein: Galactoside permease (LacY) (D0UXZ4)
Organism: Escherichia coli
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
Sequence:
TGEQGTRVFGYVTTMGELLNASIMFFAPLIINRIGGKNALLLAGTIMSVRIIGSSFATSALEVVILKTLHMFEVPFLLVGCFKYITSQFEVRFSA
Protein: Long chain base biosynthesis protein 1 (AtLCB1) (EC 2.3.1.50) (Protein EMBRYO DEFECTIVE 2779) (Protein FUMONISIN B1 RESISTANT 11) (Q94IB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine palmitoyltransferase (SPT). The heterodimer formed with LCB2 constitutes the catalytic core. Involved in the regulation of the programmed cell death (PCD) signaling pathway. Plays an important role during male gametogenesis and embryogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17194770}; Single-pass membrane protein {ECO:0000269|PubMed:17194770}.
Interaction partners:
- 3-dehydrosphinganine reductase TSC10A
- 3-dehydrosphinganine reductase TSC10B
- Long chain base biosynthesis protein 2a
- Long chain base biosynthesis protein 2b
- serine C-palmitoyltransferase
- At5g42000
- ORMDL family protein
- Ceramide kinase
- Alkaline ceramidase
- Sphingosine-1-phosphate lyase
Sequence:
MASNLVEMFNAALNWVTMILESPSARVVLFGVPIRGHFFVEGLLGVVIIILLTRKSYKPPKRPLTEQEIDELCDEWVPEPLIPPITEDMKHEPPVLESAAGPHTTVNGKDVVNFASANYLGLIGHEKLLESCTSALEKYGVGSCGPRGFYGTIDVHLDCETRISKFLGTPDSILYSYGLSTMFSTIPCFCKKGDVIVADEGVHWGIQNGLQLSRSTIVYFKHNDMESLRITLEKIMTKYKRSKNLRRYIVAEAVYQNSGQIAPLDEIVKLKEKYRFRVILDESNSFGVLGRSGRGLAEHHSVPIEKIDVVTAAMGHALATEGGFCTGNARIIDYQRLSSSGYVFSASLPPYLASAAITAIDVIDQNPDMLVKLKQNVALLWKGLSDIKGMSLTSNRESPIVFLKLEKSSGSAKDDLLLLEKMADRALKEDSLLVVSSKRSFLDKCRLPVGIKLYVSAGHSESDLLKASESLKRLASELLLKS