wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (EC 2.4.3.7) (GalNAc alpha-2,6-sialyltransferase III) (ST6GalNAc III) (ST6GalNAcIII) (STY) (Sialyltransferase 7C) (SIAT7-C) (Q64686)
Organism: Rattus norvegicus (Rat)
Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b. GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- ST3 beta-galactoside alpha-2,3-sialyltransferase 1
Sequence:
MACILKRKPALAVSFIALCILLLAMRLANDVTFPLLLNCFGQPKTKWIPLSYTLRQPLQTHYGYINVRTQEPLQLNCNHCAVVSNSGQMVGQKVGEEIDRASCIWRMNNAPTKGFEEDVGYMTMVRVVSHTSVPLLLKNPDYFFKEASTTIYVIWGPFRNMRKDGNGIVYNMLKKTVDAYPDAQIYVTTEQRMTYCDGVFKDETGKDRVQSGSYLSTGWFTFILAMDACYSIHVYGMINETYCTTEGYRKVPYHYYEQGKDECNEYLLHEHAPYGGHRFITEKKVFAKWAKKHRIVFTHPNWTVS
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FUJ4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- SWR1-complex protein 4
- Candida glabrata strain CBS138 chromosome F complete sequence
- RuvB-like helicase 1
- RuvB-like helicase 2
- Histone H2A
- Candida glabrata strain CBS138 chromosome J complete sequence
- Actin-like protein ARP6
- Candida glabrata strain CBS138 chromosome K complete sequence
- High osmolarity signaling protein SHO1
- Candida glabrata strain CBS138 chromosome A complete sequence
Sequence:
MRKLLLLVRSLLLVAVTATTSANDTPVPNPISEDISSVLSASIQPEIPSAQPSVQSEIQSIPSVQSEIQSVPSVQSEIQSVQPSEVQPSPVANSIESNTNTNTNTNTYPDAGSSIQPNSVSNSIVSQPSDDINTDDLNFLDDGSSQQGPSSILSINPSVQPSSIDYHSSSKINVESSSSVIPVFAPSEARAPAKPPAFEISSSASSVQVSSQQQQPSIQPSSVEPVQSNSPSPSSVVPSPSSVIPLVPPEVQVSPSSAAPLIPPEVQVSPSSVLPSSSISQLGPSILVSPPVSSPPTSSIPSQQISSQEINFSEFSGSFNVPSWLLSSNAPSSSFSEQLSPSSLDYSQAIHSRVADSSTTTLPLIVPPTTTTTPTLVSESSTLSNFLKPSADREFSVHFPVLSPSSIENEPPSSIQSVASSTILSQAAPLSPAQAASIPSSILEPTGSSVASEYISSNSLSQIPVEAVDAKQAPSSSSLSSILSNTDNIEAISSNLEQATPSRPVDNNATPTANSGTVLDSASQINSQSISRDDASYAEIAQSSVNVQNSASNFANSVPSADSSNTIPQPEDNTPTTSTVSEFTASNVDVSSVHIASKDADSSPNSVSNHDALNSVAPSVDVDIVSSNSIPTQVLTEPSSAVPPNVGFDISSDINIPSENIESDSNLVVTSTSRPSQGTFQNNPTNSRTITNQIPSSASPPPATPTGPKTLSSDENWLPSGIIFQSDFATTVSSSFNPTATKSLPQFIAPPKMTVKSPNTTLVTIGLKQGLNYQFLIDNPLSSAQIFNFLPSVLTYPFSSYAPNDFPINSLIDDNALAFLDSNLFNASTISVHGIVPLLIPGHEFFVSVVEVYFPNDLLDSLSALIKDRNSSLYSNPNDSLSALARLIDPSIPLTGLISGSSIESTSNSDADYNSDQSGNTRQSRKGKGLPSNLSIVGSLDNYDKNPEKEEHKNRVISIVLPTVLPLGLLFIWCLFFILMSRTQRRRKGNATIEKSNIKVDNTSGYHDNGRSNYKDNVYDGILDEKHYSSSEGVSNGSTMAGLAYAFNNFVGGPNMYSSYDTGALADSTLYSSSNQLQIPRENSSPWPAQYITAPSRKSQHSTEEVSPITLVPRIDSDVYNLQKQEMMAESVSGTFSLGSDIFIDDDEDENVKDLQIEDVDEFDEELYKRLSKFTDYRDVNNISL
Protein: Thiamine-repressible acid phosphatase pho4 (EC 3.1.3.2) (Q01682)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May dephosphorylate thiamine phosphates.
Subcellular location: Secreted, cell wall.
Interaction partners:
- Probable thiamine biosynthetic bifunctional enzyme
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 1
- Acid phosphatase
- 4-nitrophenylphosphatase
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2
- Alkaline phosphatase
- Putative hydroxymethylpyrimidine/phosphomethylpyrimidine kinase C18B5.05c
- Thiamine-repressible acid phosphatase SPBC21H7.03c
- Riboflavin synthase
- Probable FAD synthase
Sequence:
MKLSGISLWLLAASIVHAGKSQFEAFENEFYFKDHLGTISVYHEPYFNGPTTSFPESCAIKQVHLLQRHGSRNPTGDDTATDVSSAQYIDIFQNKLLNGSIPVNFSYPENPLYFVKHWTPVIKAENADQLSSSGRIELFDLGRQVFERYYELFDTDVYDINTAAQERVVDSAEWFSYGMFGDDMQNKTNFIVLPEDDSAGANSLAMYYSCPVYEDNNIDENTTEAAHTSWRNVFLKPIANRLNKYFDSGYNLTVSDVRSLYYICVYEIALRDNSDFCSLFTPSEFLNFEYDSDLDYAYWGGPASEWASTLGGAYVNNLANNLRKGVNNASDRKVFLAFTHDSQIIPVEAALGFFPDITPEHPLPTDKNIFTYSLKTSSFVPFAGNLITELFLCSDNKYYVRHLVNQQVYPLTDCGYGPSGASDGLCELSAYLNSSVRVNSTSNGIANFNSQCQAHSTNVTVYY
Protein: VIP36-like protein (Lectin mannose-binding 2-like) (LMAN2-like protein) (Q9H0V9)
Organism: Homo sapiens (Human)
Function: May be involved in the regulation of export from the endoplasmic reticulum of a subset of glycoproteins. May function as a regulator of ERGIC-53.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Predominantly found in the endoplasmic reticulum. Partly found in the Golgi.
Interaction partners:
- Multiple coagulation factor deficiency protein 2
- Dolichol kinase
- Protein ERGIC-53
Sequence:
MAATLGPLGSWQQWRRCLSARDGSRMLLLLLLLGSGQGPQQVGAGQTFEYLKREHSLSKPYQGVGTGSSSLWNLMGNAMVMTQYIRLTPDMQSKQGALWNRVPCFLRDWELQVHFKIHGQGKKNLHGDGLAIWYTKDRMQPGPVFGNMDKFVGLGVFVDTYPNEEKQQERVFPYISAMVNNGSLSYDHERDGRPTELGGCTAIVRNLHYDTFLVIRYVKRHLTIMMDIDGKHEWRDCIEVPGVRLPRGYYFGTSSITGDLSDNHDVISLKLFELTVERTPEEEKLHRDVFLPSVDNMKLPEMTAPLPPLSGLALFLIVFFSLVFSVFAIVIGIILYNKWQEQSRKRFY
Protein: Zinc finger protein 101 (Zinc finger protein HZF12) (Q8IZC7)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDSVAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLASVGIQWKDQDIENLYQNLGIKLRSLVERLCGRKEGNEHRETFSQIPDCHLNKKSQTGVKPCKCSVCGKVFLRHSFLDRHMRAHAGHKRSECGGEWRETPRKQKQHGKASISPSSGARRTVTPTRKRPYECKVCGKAFNSPNLFQIHQRTHTGKRSYKCREIVRAFTVSSFFRKHGKMHTGEKRYECKYCGKPIDYPSLFQIHVRTHTGEKPYKCKQCGKAFISAGYLRTHEIRSHALEKSHQCQECGKKLSCSSSLHRHERTHSGGKLYECQKCAKVFRCPTSLQAHERAHTGERPYECNKCGKTFNYPSCFRRHKKTHSGEKPYECTRCGKAFGWCSSLRRHEMTHTGEKPFDCKQCGKVFTFSNYLRLHERTHLAGRSQCFGRRQGDHLSPGV
Protein: Uncharacterized protein C19F5.03 (EC 3.1.3.-) (O60162)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphoinositide 3-phosphatase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1
- Phosphatidylinositol 4-kinase pik1
- Phosphatidylinositol 4-kinase stt4
- Phosphatidylinositol 4-kinase lsb6
- Inositol-1,4,5-trisphosphate 5-phosphatase 2
- Inositol-1,4,5-trisphosphate 5-phosphatase 1
- Phosphatidylinositol 4-phosphate 5-kinase its3
- Uncharacterized protein C3C7.01c
- Phosphatidylinositol 3-kinase pik3
Sequence:
MVQFEANEKQFKLRREDCCLTIDRESGAVSFEPDELKPVARSKENSVTLFGSIKLKKDKYLILATEKSSAAQILGHKIYRVHKFEVIPYRNLLADDQDELDLYNLLQNHLKTGPFYFSYTWDLTNSLQRSCTDEGKASPILRSDKRFFWNEFASKDFIDLIGAHSEVSLFITPMIYGFITSASTIVKGRTITLALISRRSKQRAGTRYFTRGLDENGNPANFNETEQITIVSDEKSEVTYSHVQTRGSVPAFWAEVNNLRYKPLMVANSASMAAAAAKKHFDEQISIYGDQVVVNLVNCKGHELPIKQLYENVIRRLDNPHIHYHYFDFHKECSHMRWDRVSLLLNEIQPELEEQGYTTLDTQKYRVLSRQNGVVRSNCMDCLDRTNVVQSCIGRWVLTNQLRKCGIIGATHPLRSVIPLDNIFCNIWSDNADYISLSYSGTGALKTDFTRTGIRTRKGAFNDFVNSAKRYILNNFYDGARQDAYDLVLGQFRPDVNFRYRLDLRPLTIRCVPYILLACLILFFMTLFSRSSSTILPPSILLILTFLGIVASLYYCFAHGLQFINWPRLLLPSFLRSDMTPEGRVFVINRQLASKHKV
Protein: Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPI-HBP1) (GPI-anchored HDL-binding protein 1) (High density lipoprotein-binding protein 1) (Q8IV16)
Organism: Homo sapiens (Human)
Function: Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (By similarity). Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (By similarity). Protects LPL against loss of activity, and against ANGPTL4-mediated unfolding. Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis. Binds chylomicrons and phospholipid particles that contain APOA5. Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. Cell membrane {ECO:0000269|PubMed:19304573}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}.
Interaction partners:
- Lipoprotein lipase
- Angiopoietin-related protein 4
- Apolipoprotein C-II
- Lipase maturation factor 1
- Angiopoietin-related protein 3
- Angiopoietin-like protein 8
- Apolipoprotein A-V
- Apolipoprotein C-III
- Proprotein convertase subtilisin/kexin type 5
- Hepatic triacylglycerol lipase
Sequence:
MKALGAVLLALLLFGRPGRGQTQQEEEEEDEDHGPDDYDEEDEDEVEEEETNRLPGGRSRVLLRCYTCKSLPRDERCNLTQNCSHGQTCTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQVTMTCCQSSLCNVPPWQSSRVQDPTGKGAGGPRGSSETVGAALLLNLLAGLGAMGARRP
Protein: UBX domain-containing protein 2 (Secretion lowering protein 1) (Q04228)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Integral endoplasmic reticulum membrane protein that coordinates the assembly of the ER-associated protein degradation (ERAD) machinery at the ER membrane. Mediates binding of CDC48 to the E3 ubiquitin ligases SSM4/DOA10 and HRD1, and to ERAD substrates. Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Also a component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cell division control protein 48
- Ubiquitin fusion degradation protein 1
- Protein OS-9 homolog
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Nuclear protein localization protein 4
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- Ubiquitin-conjugating enzyme E2 7
- DER1-like family member protein 1
- Degradation in the endoplasmic reticulum protein 1
Sequence:
MPVVNHEDSEFHLSHTEEDKLNEFQVITNFPPEDLPDVVRLLRNHGWQLEPALSRYFDGEWKGEPDQMGEPTQTSTPMAETLVPPALGPRPLLFTASLPVVRPLPANFRNDFRTIGLNGRSNTVWSMFESFSYDGNPFLFILLLIPRIINRLSATIFTFFCTLLSLHSISGGGNSGKPKISKVPKAPTRETHIPLAEILGDTKDKDAFCELKSFKPDISFNEALRIAKEEFKFMLLILVGDTYDTDTDTVDVNSKLLLEKILLNKKTLQYLRKIDNDLIIYLKCVHELEPWLVARQLGVRNTPEIFLIANVANKASHSETLPSQRLSILGKLKVNSLNRFLQSLTNVVEKYTPELVVNKTEMHELRMSREIKKLQEDAYKKSLEMDRIKAIEKEKSLKHAQDLKLNSTARQLKWLKACIDEIQPFETTGKQATLQFRTSSGKRFVKKFPSMTTLYQIYQSIGCHIYLAVYSSDPAEWSNALQDKIRQLSADDDMLCFKEGQLETATATTIEELGHIINNELTSFDLERGKLEFDFELVSPFPKYTVHPNEHMSVDQVPQLWPNGSLLVEALDEEDEEDEENEEQ
Protein: Proliferating cell nuclear antigen (PCNA) (Cyclin) (P18248)
Organism: Xenopus laevis (African clawed frog)
Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular location: Nucleus {ECO:0000269|PubMed:1697269}.
Interaction partners:
Sequence:
MFEARLVQGSILKKVLEALKDLIDEACWDITSSGISLQSMDSSHVSLVQLTLRSDGFDTYRCDRNQSIGVKMSSMSKILKCAASDDIITLRAEDNADTVTMVFESPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVIKMPSGEFARICRDLSQIGDAVVISCAKDGVKFSASGELGTGNVKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSPTVILSMSADIPLVVEYKIADMEHVKYYLAPKIEDEEAS
Protein: Uncharacterized HTH-type transcriptional regulator YfeR (P0ACR7)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MNYSLKQLKVFVTVAQEKSFSRAGERIGLSQSAVSHSVKELENHTGVRLLDRTTREVVLTDAGQQLALRLERLLDELNSTLRDTGRMGQQLSGKVRVAASQTISAHLIPQCIAESHRRYPDIQFVLHDRPQQWVMESIRQGDVDFGIVIDPGPVGDLQCEAILSEPFFLLCHRDSALAVEDYVPWQALQGAKLVLQDYASGSRPLIDAALARNGIQANIVQEIGHPATLFPMVAAGIGISILPALALPLPEGSPLVVKRITPVVERQLMLVRRKNRSLSTAAEALWDVVRDQGNALMAGREGDPLYQI
Protein: Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2) (Q61539)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcriptional activity. Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryonic and trophoblast stem cells through different signaling pathways including FGF signaling pathway and Wnt signaling pathways. Upon FGF signaling pathway activation, interacts with KDM1A by directly binding to enhancer site of ELF5 and EOMES and activating their transcription leading to self-renewal of trophoblast stem cells. Also regulates expression of multiple rod-specific genes and is required for survival of this cell type. Plays a role as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1. Plays a role as transcription factor repressor of NFE2L2 transcriptional activity and ESR1 transcriptional activity (By similarity). During mitosis remains bound to a subset of interphase target genes, including pluripotency regulators, through the canonical ESRRB recognition (ERRE) sequence, leading to their transcriptional activation in early G1 phase. Can coassemble on structured DNA elements with other transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation. This mechanism, in the case of SOX2 corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition through positive regulation of NR0B1 that inhibits the EpiSC transcriptional program. Also plays a role inner ear development by controlling expression of ion channels and transporters and in early placentation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18472334}. Cytoplasm {ECO:0000269|PubMed:18472334}. Chromosome {ECO:0000269|PubMed:27723719}.
Interaction partners:
- Homeobox protein NANOG
- Transcription factor CP2-like protein 1
- Nuclear receptor subfamily 0 group B member 1
- POU domain, class 5, transcription factor 1
- Sal-like protein 4
- Transcription factor SOX-2
- Krueppel-like factor 5
- T-box transcription factor TBX3
- Zinc finger protein 42
- Krueppel-like factor 4
Sequence:
MSSEDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGIALSTHANGLDSPPMFAGAGLGGNPCRKSYEDCTSGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYNCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSENSPYLNLPISPPAKKPLTKIVSNLLGVEQDKLYAMPPNDIPEGDIKALTTLCELADRELVFLINWAKHIPGFPSLTLGDQMSLLQSAWMEILILGIVYRSLPYDDKLAYAEDYIMDEEHSRLVGLLDLYRAILQLVRRYKKLKVEKEEFMILKALALANSDSMYIENLEAVQKLQDLLHEALQDYELSQRHEEPRRAGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV
Protein: Isoaspartyl peptidase/L-asparaginase (EC 3.4.19.5) (EC 3.5.1.1) (Asparaginase-like protein 1) (Beta-aspartyl-peptidase) (Isoaspartyl dipeptidase) (L-asparagine amidohydrolase) [Cleaved into: Isoaspartyl peptidase/L-asparaginase alpha chain; Isoaspartyl peptidase/L-asparaginase beta chain] (Q7L266)
Organism: Homo sapiens (Human)
Function: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:27106100}. Note=Midpiece of sperm tail.
Interaction partners:
- Asparagine synthetase
- 60 kDa lysophospholipase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Putative aspartate aminotransferase, cytoplasmic 2
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- Argininosuccinate synthase
- L-amino-acid oxidase
- Aspartoacylase
Sequence:
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
Protein: Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1 (JC7) (Q80XU3)
Organism: Mus musculus (Mouse)
Function: Chromatin-associated protein involved in DNA repair by promoting homologous recombination (HR). Binds double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures, but with less affinity than RAD51AP1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H1E3}. Chromosome {ECO:0000250|UniProtKB:Q9H1E3}.
Interaction partners:
- Ras-related protein Rab-7L1
- Solute carrier family 41 member 1
- N-fatty-acyl-amino acid synthase/hydrolase PM20D1
Sequence:
MSRPVRNRKVVDYSQFQESDDADEDYGRDSGPPAKKIRSSPREAKNKRRSGKNSQEDSEDSEEKDVKTKKDDSHSAEDSEDEKDDHKNVRQQRQAASKAASKQREMLLEDVGSEEEPEEDDEAPFQEKDSGSDEDFLMEDDDDSDYGSSKKKNKKMVKKSKPERKEKKMPKPRLKATVTPSPVKGKAKVGRPTASKKSKEKTPSPKEEDEEAESPPEKKSGDEGSEDEASSGED
Protein: Replication-associated protein (Rep) (EC 2.7.7.-) (EC 3.1.21.-) (Q67622)
Organism: Wheat dwarf virus (isolate Sweden) (WDV)
Function: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities. Acts as an inhibitor of C-sense gene transcription (By similarity).
Subcellular location: Host nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MASSSAPRFRVYSKYLFLTYPECTLEPQYALDSLRTLLNKYEPLYIAAVRELHEDGSPHLHVLVQNKLRASITNPNALNLRMDTSPFSIFHPNIQAAKDCNQVRDYITKEVDSDVNTAEWGTFVAVSTPGRKDRDADMKQIIESSSSREEFLSMVCNRFPFEWSIRLKDFEYTARHLFPDPVATYTPEFPTESLICHETIESWKNEHLYSESPGRHKSIYICGPTRTGKTSWARSLGTHNYYNSLVDFTTYDVNAKYNIIDDIPFKFTPNWKCFVGAQRDFTVNPKYGKRKVIRGGIPCIILVNPDEDWLKDMTPEQSDYMYSNTVVHYMYEGETFINYSFASGEDVTASQ
Protein: Submaxillary gland androgen-regulated protein 3B (Proline-rich peptide P-B) (Proline-rich protein 3) [Cleaved into: Peptide P-A; Peptide D1A] (P02814)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Statherin
- Mucin-7
Sequence:
MKSLTWILGLWALAACFTPGESQRGPRGPYPPGPLAPPQPFGPGFVPPPPPPPYGPGRIPPPPPAPYGPGIFPPPPPQP
Protein: Protein rolling stone (O44252)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a central role in the fusion process during myogenesis, within the somatic mesoderm.
Subcellular location: Membrane {ECO:0000269|PubMed:9230076}; Multi-pass membrane protein {ECO:0000269|PubMed:9230076}. Note=Enriched in the embryonic membrane fraction.
Interaction partners:
Sequence:
MQLFDDFCKSFNKELQRANFGFAYNRVHLFYRSQWQKDEINTIYLLYRWIWALFFLGVYIMCVIVQFCDGKFFIYMTNWGFGLCTITMLISAVQVTCWHFDVRSTRSLVQESGHKAETSRGLKIYWWLYNMTLSLALIISTVYWVFLHGKMNKPMRFPAISIITHGMNSVMMLIDFLVIAFPLRILHMVYGMSLAIFFFLFTLIYHLCGGTDEFGNHYVYPILDWNNPNRCMVTFVGIFLLIMCYWVLLFGLYKLKRMFNRAFSVVWSPHAVGLI
Protein: Light-harvesting complex stress-related protein 3.2, chloroplastic (Chlorophyll a-b binding protein LHCSR3.2) (P0DO18)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage. NPQ includes dissipating excess light energy to heat (qE) and the reversible coupling of LHCII to photosystems (state transitions or qT), which are considered separate NPQ mechanisms. Is responsible for most of the excess light energy to heat dissipation (qE), also known as energy-dependent chlorophyll fluorescence quenching activity of chlorophyll excited states. Involved in a de-coupling and re-coupling of energy transfer to photosystem II (PSII) during qT. Binds chlorophyll a and b. Is able to sense luminal acidification of the thylakoid membranes, which occurs along with elevated electron flow caused by excess light. Establishes interactions with photosystem II (PSII) antenna components upon lumen acidification, and protonation of lumen-exposed, negatively charged residues both in LHCSR3 and in PSII antenna components. Mediates excitation energy transfer from light-harvesting complex II (LHCII) to photosystem I (PSI), rather than photosystem II (PSII), at low pH, which mimics the acidified lumen of the thylakoid membranes in high light-exposed chloroplasts. Activates PSI-dependent fluorescence quenching in addition to dissipating excitation energy in LHCII to avoid photooxidative stress under excess light. Contributes with PGRL1 to the regulation of electron flow upstream of photosystem I (PSI), and limits the accumulation of electrons on the PSI acceptor side, thus avoiding PSI photoinhibition.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem II protein PSBS1
- Chlorophyll a-b binding protein
- Photosystem II protein PSBS2
- Uncharacterized protein
- Phototropin
- Chlorophyll a-b binding protein
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosystem II protein D1
Sequence:
MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL
Protein: RNA lariat debranching enzyme (A0A1D8PPT8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Karyopherin
- RNA helicase
Sequence:
MSNTLKIAIEGCCHGELNDIYNSIPDIESLDLLLICGDFQSLRNKCDLQSLNVPLKYQRMADFHEYYSGKRKAPVLTIFIGGNHECSSYLQELKYGGWVAPNIYYLGEFGSIWYKGLQITGWSGIFNYHTFIANNIEMEKLPFDSRTIRSVYHQKLANFLKMYMMNHDMDIVLSHDWPVGIEKYGNVKRLLKLKPFFRDDIQRGQLGSPLNKFLIHYLRPRYWFSGHLHVKFEARIVDLVRSTDKKKSATTVDLITESNKEEISLDMDDEEEEEGGNVREVSFEEKFYFKQHSNPAKRPKNDLTPERDVCEHATEFLALDKCGKRRQFLDIKTIEVHNTSHPSFINAGKLYYSKRSIAINKVVEKYLNDNRQDFTELNTKQILSNPQQFPLVNELMPIIENDFKSMQKNITDEDFFMVPENFQTIAPTDDEHTESKLKYYPNNQTSEYCEKFGIPKLVLSKESDQ