wanglab/gogpt-training-data huggingface dataset:
Protein: Protein eva-1 (Enhancer of ventral-axon guidance defects of unc-40 mutants) (Q9XU98)
Organism: Caenorhabditis elegans
Function: Acts as a receptor for slt-1. Required for the guidance of the AVM pioneer axon to the ventral nerve cord. Acts as a unc-40 coreceptor to enhance the sensitivity of unc-40 to the madd-4 midline guidance cue to guide muscle arm extensions (muscle arms) and AVM mechanosensory axons towards the dorsoventral midline.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Slit homolog 1 protein
- Protein sax-3
- Teneurin-1
- Netrin receptor unc-5
- Netrin receptor unc-40
- E3 ubiquitin-protein ligase TRIM9
Sequence:
MNMHIVSPVLLLFWFGIIVTDGKLKSGFIGGSHHHEVNPIEGILRESLRSNRVQACDGERITLSCPRNTQISVQTGFYGRVVPENQLCPPQAGRKHSEANLDPLSMIHHSSTCDVIQAHTRISELCDKRRKCTVVVDSNTFEDDPCPTTSKYLQMAYGCIPMSFDEETFCTPKPTDPPRPEIRLECREGRRLAVYSAQMKTSPQCDPETEIRHECVSDVLPQVLRQCHAKEGCTLKSDGIKGHCRHGHLHVVYVCVNEEIFSEEAIKGELTSLETYLKEADAMQKQDDERFFKDVNDKTQWERVVDSEPAKDPDVHQIANDASYVTHDEYRMEKQDPPPITERVEPNLVGVGHDLLQVVQFFKENKEKAVMCIVLAVSMAAIVVLSACIITRLCSSNKDSSRSSRRSRSRRSLETSKLVSSNYGGSITPQHMMQDIEDEQFLRFSMGSAATSNPHYSHYDF
Protein: Cytokine-inducible SH2-containing protein (CIS) (CIS-1) (Protein G18) (Suppressor of cytokine signaling) (SOCS) (Q9NSE2)
Organism: Homo sapiens (Human)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Interaction partners:
- Cullin-5
- Elongin-B
- Elongin-C
- RING-box protein 2
- Signal transducer and activator of transcription 3
- Signal transducer and activator of transcription 5B
- Signal transducer and activator of transcription 1-alpha/beta
- Signal transducer and activator of transcription 5A
- Tyrosine-protein kinase JAK2
- Cullin-2
Sequence:
MVLCVQGPRPLLAVERTGQRPLWAPSLELPKPVMQPLPAGAFLEEVAEGTPAQTESEPKVLDPEEDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCTADTRSDSPDPAPTPALPMPKEDAPSDPALPAPPPATAVHLKLVQPFVRRSSARSLQHLCRLVINRLVADVDCLPLPRRMADYLRQYPFQL
Protein: Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) (P0A3J0)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Function: Acts as a chaperone.
Interaction partners:
Sequence:
MSKIIGIDLGTTNSAVAVLEGTESKIIPNPEGNRTTPSVVAFKNGEIIVGDAAKRQAVTNPETIISIKSKMGTSEKVSANGKEYTPQEISAMILQNLKATAEAYLGEKVEKAVITVPAYFNDAQRQATKDAGKIAGLEVERIVNEPTAAALAYGLDKTDKDEKILVFDLGGGTFDVSILELGDGVFDVLATAGNNKLGGDDFDQKIIDWMVAEFKKENGIDLAQDKMALQRLKDAAEKAKKDLSGVTTTQISLPFITAGAAGPLHLEMALTRAKFDELTHDLVEATRQPVRQALSDAGLSTSDIDEVLLVGGSTRIPAVVELVRHETNKEPNKSVNPDEVVAMGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQPAVDIHVLQGERPMAADNKTLGRFQLTDIPAAPRGIPQIEVTFDIDKNGIVSVKAKDLGTQKEQTIVIKSNSGLSDEEIDKMMKDAEANADADAKRKEEVDTRNEADALVFQTEKTLKDLEGKVEEAEVKKAEEAKEELKKALEGEDIDDIKAKSEALSEIAQNLAVKLYEQANAAQGEAGQATDAQEAPKDDNTFDGDFEESK
Protein: AT28817p (Q8IH89)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCEVCADFQNLLELYEVRVASSDLKFQLLLKSEIETTFNYIQSWPQRQCMCLYRDTKNYDRFNLVVQSLICLTVQHLKHIDHLIDNYKRLTASAAQVVAQAQQQREQQRDEASAQAEAKESSAPAEEPKKEEPSGSAGEEAQGSGDGPAKKPPVGPCTPPPPQTANPQHKSHLQYTEEPWILPEVEKLLVLVSKVFLLNFPLYIAHKHGMHSRLDDLQAEEAHHLALICDLHDNDLPIYLLRNVSLFCNSGGFGAMSLCFEHPDLPVSTAHSMTAAVSNVKLWLNYHCNTQLFVPLRSRILQYMCKLSDQSLRSAATRAMADFVWSSMRDPLDVAVNFDTEGLALAFKYFTSTTLTMRLAGMSYDVDILN
Protein: Cytohesin 4 (B1AHH4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLCHPEPAELSSGETEELQRIKWHRKQLLEDIQKLKDEIADVFAQIDCFESAEESRMAQKEKELCIGRKKFNMDPAKGIQYFIEHKLLTPDVQDIARFLYKGEGLNKTAIGTYLGE
Protein: Nuclear receptor subfamily 6 group A member 1 (Germ cell nuclear factor) (GCNF) (mGCNF) (Retinoid receptor-related testis-specific receptor) (RTR) (Q64249)
Organism: Mus musculus (Mouse)
Function: Orphan nuclear receptor. Binds to a response element containing the sequence 5'-TCAAGGTCA-3'. May be involved in the regulation of gene expression in germ cell development during gametogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear receptor corepressor 1
- DNA
- DNA
- Nuclear receptor corepressor 2
Sequence:
MERDERPPSGGGGGGGSAGFLEPPAALPPPPRNGFCQDELAELDPGTNGETDSLTLGQGHIPVSVPDDRAEQRTCLICGDRATGLHYGIISCEGCKGFFKRSICNKRVYRCSRDKNCVMSRKQRNRCQYCRLLKCLQMGMNRKAIREDGMPGGRNKSIGPVQISEEEIERIMSGQEFEEEANHWSNHGDSDHSSPGNRASESNQPSPGSTLSSSRSVELNGFMAFRDQYMGMSVPPHYQYIPHLFSYSGHSPLLPPQARSLDPQSYSLIHQLMSAEDLEPLGTPMLIEDGYAVTQAELFALLCRLADELLFRQIAWIKKLPFFCELSIKDYTCLLSSTWQELILLSSLTVYSKQIFGELADVTAKYSPSDEELHRFSDEGMEVIERLIYLYHKFHQLKVSNEEYACMKAINFLNQDIRGLTSASQLEQLNKRYWYICQDFTEYKYTHQPNRFPDLMMCLPEIRYIAGKMVNVPLEQLPLLFKVVLHSCKTSTVKE
Protein: HAUS augmin-like complex subunit 2 (Centrosomal protein of 27 kDa) (Cep27) (Q9NVX0)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 1
- HAUS augmin-like complex subunit 3
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 7
- HAUS augmin-like complex subunit 6
- HAUS augmin-like complex subunit 5
- HAUS augmin-like complex subunit 4
- Tubulin gamma-1 chain
- Centrosomal protein of 290 kDa
- Zinc finger protein 223
Sequence:
MAAANPWDPASAPNGAGLVLGHFIASGMVNQEMLNMSKKTVSCFVNFTRLQQITNIQAEIYQKNLEIELLKLEKDTADVVHPFFLAQKCHTLQSMNNHLEAVLKEKRSLRQRLLKPMCQENLPIEAVYHRYMVHLLELAVTFIERLETHLETIRNIPHLAANLKKMNQALAKMDILVTETEELAENILKWRKQQNEVSSCIPKILAEESYLYKHDIIMPPLPFTSKVHVQTINAK
Protein: Alpha-1-antiproteinase (Alpha-1-antitrypsin) (Alpha-1-proteinase inhibitor) (Serpin A1) (P17475)
Organism: Rattus norvegicus (Rat)
Function: Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin.
Subcellular location: Secreted.
Interaction partners:
- Albumin
- Vitamin K-dependent protein C
- Haptoglobin
- Alpha-2-HS-glycoprotein
- Alpha-1-acid glycoprotein
- Hemopexin
- Ceruloplasmin
- Beta-2-glycoprotein 1
- Fibrinogen gamma chain
- Inter-alpha-trypsin inhibitor heavy chain 4
Sequence:
MAPSISRGLLLLAALCCLAPSFLAEDAQETDTSQQDQSPTYRKISSNLADFAFSLYRELVHQSNTSNIFFSPMSITTAFAMLSLGSKGDTRKQILEGLEFNLTQIPEADIHKAFHHLLQTLNRPDSELQLNTGNGLFVNKNLKLVEKFLEEVKNNYHSEAFSVNFADSEEAKKVINDYVEKGTQGKIVDLMKQLDEDTVFALVNYIFFKGKWKRPFNPEHTRDADFHVDKSTTVKVPMMNRLGMFDMHYCSTLSSWVLMMDYLGNATAIFLLPDDGKMQHLEQTLTKDLISRFLLNRQTRSAILYFPKLSISGTYNLKTLLSSLGITRVFNNDADLSGITEDAPLKLSQAVHKAVLTLDERGTEAAGATVVEAVPMSLPPQVKFDHPFIFMIVESETQSPLFVGKVIDPTR
Protein: Cell division protein FtsX (A5U7B6)
Organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16416128}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:16416128}.
Interaction partners:
Sequence:
MRFGFLLNEVLTGFRRNVTMTIAMILTTAISVGLFGGGMLVVRLADSSRAIYLDRVESQVFLTEDVSANDSSCDTTACKALREKIETRSDVKAVRFLNRQQAYDDAIRKFPQFKDVAGKDSFPASFIVKLENPEQHKDFDTAMKGQPGVLDVLNQKELIDRLFAVLDGLSNAAFAVALVQAIGAILLIANMVQVAAYTRRTEIGIMRLVGASRWYTQLPFLVEAMLAATMGVGIAVAGLMVVRALFLENALNQFYQANLIAKVDYADILFITPWLLLLGVAMSGLTAYLTLRLYVRR
Protein: G-protein regulator 1 (Q95QJ7)
Organism: Caenorhabditis elegans
Function: In the 1-cell embryo, probably together with gpr-2, controls nuclear rotation and spindle elongation during mitosis. Complex of gpr-1 and gpr-2, in association with lin-5, activates G-protein signaling to affect mitotic spindle force. Polarity determinants (par genes) may regulate lin-5/gpr-1/gpr-2/goa-1 locally to create the asymmetric forces that drive spindle movement.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12730122}. Note=Located to the spindle and cell cortex when in complex with lin-5 and gpr-2 (PubMed:12730122). During early embryogenesis, cortical localization changes with the cell cycle. In one-cell embryo, uniform cortical localization from prophase to metaphase and posterior enrichment during anaphase. In the 2-cell embryo, uniform cortical localization in AB blastomere and posterior cortical enrichment in P1 blastomere during interphase. In P1, uniform cortical localization from prophase to early anaphase and then posterior cortical enrichment during late anaphase and telophase (PubMed:12730122, PubMed:14534135). Cortical localization and asymmetrical distribution is regulated by the csnk-1-mediated regulation of pkk-1 (PubMed:18694560). Enriched at the contact site between EMS and P2 from prophase to prometaphase (PubMed:14534135). {ECO:0000269|PubMed:12730122, ECO:0000269|PubMed:14534135, ECO:0000269|PubMed:18694560}.
Interaction partners:
- Spindle apparatus protein lin-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein alpha-16 subunit
- Protein let-99
- G-protein regulator 2
- Tetratricopeptide repeat protein 28
- Epimerase domain-containing protein
- Probable delta-1-pyrroline-5-carboxylate synthase
- RING-type domain-containing protein
- Protein regulator of cytokinesis 1
Sequence:
MDVSYYDGPKDEVAEAMLKSAVTAMRLGQYEDGKGRLEEIMEFGTSNFQLLGTIYMYYGRVCRHLNHDAKALEFFEHELNMFKLIFNYPEACDSTRRIVEQALKMGKFPKARRFAEDLIDYTSNKKNGEKYIGQARILFASVCLEGCERDVESNQDEKKKLLSICAEQIAAVKLFNENNTEGAVSETKIMLLEAKCLSLDEKYEESRRKYQECIDFAIKTDQFEAVHIAYYDKALYAETDLLFFIIRDLRSALFYATKFGKERDVVKYKSKLSEEMLRNGEFHEAYLYGLEALVSIRKLGLNEYIGDVLLTIAKCLIALGKRRQAAYFIILGSVLTINQNSFKLFYEQIDVAMNQERSETATDQDVCLAIDSSPDPTSSNDMINKFVVELEHATNVETWEMIVNGIIDDQKKPVAIEKKENEEPVDMMDLIFSMSSRMDDQRTELPAARFIPPRPVSSASKKTTKSHRILPGLRANWTKVQSMKFDGHTMNRILKRSKKSKSSLDSTNSMQGDDTRSDDVTMTSK
Protein: Desmocollin-2 (Epithelial type 2 desmocollin) (P55292)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q02487}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q02487}. Cell junction, desmosome {ECO:0000269|PubMed:38395410}.
Interaction partners:
- Desmoglein-2
- Plakophilin-2
- Junction plakoglobin
- Desmoplakin
- Plakophilin-3
- Plakophilin-1
- Desmoglein-3
- Plakophilin-4
- Transmembrane protein 43
- p53 apoptosis effector related to PMP-22
Sequence:
MAAVGSMRSGSPAFGLGHLLTLAILALASDACKEVVLQVPSELPAEKFVGRVNLMDCLKSADIVHLSDPDFQVLEDGSVYTTSSVVLSSGQRSFTIWLFSTDSQEEREISVHLEGPVEVLNKRPHTEKVLSRAKRRWAPIPCSMLENSLGPFPLFLQQIQSDTAQNYTIYYSIRGPGVDKEPLNLFYVERDTGNLYCTGRVDREQYESFELTAFATTPDGYTPEYPLPLLIKIEDENDNYPIFTQKLYSFTVQENSRIGSIVGEVCATDLDEPDTMHTRLRYSILEQSPSPPMLFTMHPSTGVITTTSAQLDRELIDKYQLLIKVQDMDGQYFGLHTTAKCIITIEDVNDNLPTFTRTTYVTSVEENTVNVEILRLTVQDKDLVNSPNWRANYTILKGNENGNFKIVTDPKTNEGILCVIKPLDYEERQQVTLQIGVVNEAPYTREASSKSPMSTATVTVTVTNQDEGPECIPPMQTVRIQENVPVGTRNDGYKAYDPETRSSSGIRYRKLSDPRGWVTVNEDSGSITIFRALDREAETVRNGIYNITVLALDADGRSCTGTLGIILEDVNDNGPFIPKQTVVICKATMSSAEIVAVDLDDPVNGPPFDFSLESSDSEVQRMWRLTRINDTAARLSYQNDPSFGSYAVPIRVTDRLGLSSVTTLNVLVCDCITESDCTLRSGERTGYADVRLGPWAILAILLGIALLFCILFTLVCSVSRASKQQKILPDDLAQQNLIVSNTEAPGDDKVYSTNGLTTQTMGASGQTAFTTMGTGVKSGGQETIEMVKGGQQTLDSRRGAGYHHHTLDPCRGGHVEVDNYRHTYSEWYNFIQPRLGDKVQFCHTDDNQKLAQDYVLTYNYEGKGSAAGSVGCCSDLQEEDGLEFLDHLEPKFRTLAEVCAKR
Protein: Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase) (Q8MK44)
Organism: Bos taurus (Bovine)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats. In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (By similarity). Also present in female mammary glands, where it produces fat in the milk. May be involved in VLDL (very low density lipoprotein) assembly (By similarity). In contrast to DGAT2 it is not essential for survival (By similarity). Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders (By similarity). Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z2A7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75907}.
Interaction partners:
- 2-acylglycerol O-acyltransferase 1
- phosphatidate phosphatase
- Acyltransferase
- phosphatidate phosphatase
- phosphatidate phosphatase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Phospholipid phosphatase 2
- Retinol dehydrogenase 12
- Short chain dehydrogenase/reductase family 16C member 5
- Phospholipid phosphatase 3
Sequence:
MGDRGGAGGSRRRRTGSRPSIQGGSGPAAAEEEVRDVGAGGDAPVRDTDKDGDVDVGSGHWDLRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQVVSLFLKDPYSWPALCLVIVANIFAVAAFQVEKRLAVGALTEQAGLLLHGVNLATILCFPAAVAFLLESITPVGSVLALMVYTILFLKLFSYRDVNLWCRERRAGAKAKAALAGKKANGGAAQRTVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRLLEMLFLTQLQVGLIQQWMVPAIQNSMKPFKDMDYSRIVERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESITYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWAARTAVFLASAFFHEYLVSIPLRMFRLWAFTGMMAQIPLAWIVGRFFRGNYGNAAVWLSLIIGQPVAVLMYVHDYYVLNREAPAAGT
Protein: Uncharacterized protein (Q384L7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALEGSTPEAFSLYALPTFRITNSWAQQTRTGLFQPPELSTSPARFDSGDCSSSNGANSAPFAASRNECYLVSRCNFGPDGELLLRKGDRSLESIMNMIINEIGKEQDAFATQREGNLVLERELRQVQQGRRDAELELHKTEALLFCVKSIVKEQQNLLNELRHV
Protein: BUB3-interacting and GLEBS motif-containing protein ZNF207 (BuGZ) (hBuGZ) (Zinc finger protein 207) (O43670)
Organism: Homo sapiens (Human)
Function: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly. ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks. Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3. According to another report, the stabilization is independent of the proteasome.
Subcellular location: Nucleus {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26388440}. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding. {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}.
Interaction partners:
- Mitotic checkpoint protein BUB3
- Heterogeneous nuclear ribonucleoprotein M
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 3
- Serine/arginine-rich splicing factor 3
- Heterogeneous nuclear ribonucleoprotein U-like protein 1
- Far upstream element-binding protein 1
Sequence:
MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQAPIGNPPVGPIGGMMPPQPGIPQQQGMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY
Protein: CTP synthase (EC 6.3.4.2) (UTP--ammonia ligase) (O64753)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Alkaline-phosphatase-like family protein
- GMP synthase
- Nucleoside diphosphate kinase IV, chloroplastic/mitochondrial
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase 1
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase B
- Aspartate--tRNA ligase, chloroplastic/mitochondrial
- Protein trichome birefringence-like 21
- UMP kinase
Sequence:
MKYVLVTGGVVSGLGKGITASSVGVLLQSCGLRVTCIKIDPYLNYDAGTISPYEHGEVFVLDDGSEVDLDLGNYERFLDTTLTRDNNITYGKIQRYVMEKERKGDYLGETVQIVPHVTDTIREWVERVAMIPVDGKEGPPDVCIIELGGTIGDNESRPFADALSQLSYSVGRENFCLIHVTLVPVLSVVGEQKTKPTQHSIKDLRGFGLTPNIIACRSTKALEENVKAKLSRFCYVPIQNIFSLCDVPNIWHIPLLLKEQKAHEAISKVLNLSGIAKEPSLEKWASMVEISDGLNVPVRIAIVGKYTDLSDAYLSVLKALLHASVAFHKKLEVDMVPSCDLEKTKKQEDSRAYEAAWKLLKDANGVLLPGGFGDRGVEGMILAAKYARENNIPFLGICLGMQIAVIEFARSLLCLPDANSTEFEPETKHPCIIFMPEGSITHMGGTMRLGSRRAYFHDKESKSARLYGNKEFVDERHRHRYEVNPDMVASLEQAGLSFAAKDETGERMEIVELPSHPFFIGAQFHPEYKSRPRKVSPLFLGLIAASCGELDAVLNPVSIHQHNQTMFLEKKQHIGWSKKCFGDKNQQEEISETSFPM
Protein: E3 ubiquitin-protein ligase SHPRH (EC 2.3.2.27) (EC 3.6.4.-) (RING-type E3 ubiquitin transferase SHPRH) (SNF2, histone-linker, PHD and RING finger domain-containing helicase) (Q149N8)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase involved in DNA repair. Upon genotoxic stress, accepts ubiquitin from the UBE2N-UBE2V2 E2 complex and transfers it to 'Lys-164' of PCNA which had been monoubiquitinated by UBE2A/B-RAD18, promoting the formation of non-canonical poly-ubiquitin chains linked through 'Lys-63'.
Interaction partners:
- E3 ubiquitin-protein ligase RAD18
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin-conjugating enzyme E2 N
- Proliferating cell nuclear antigen
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- DNA repair protein RAD52 homolog
- Zinc finger protein 609
- DNA polymerase zeta catalytic subunit
- Helicase-like transcription factor
Sequence:
MSSRRKRAPPVRVDEEKRQQLHWNMHEDRRNEPIIISDDDEQPCPGSDTSSAHYIILSDSLKEEVAHRDKKRCSKVVSFSKPIEKEETVGIFSPLSVKLNIVISPYHFDNSWKAFLGELTLQLLPAQSLIENFSERSITLMSSESSNQFLIYVHSKGEDVEKQKKEPMSICDKGILVESSFSGEMLEDLGWLQKKRRIKLYQKPEGNHIIKVGIYLLEAGLAKLDFLSDANSRMKKFNQLMKKVMEKLHNSIIPDVLEEDEDDPESEPEGQDIDELYHFVKQTHQQETQSIQVDVQHPALIPVLRPYQREAVNWMLQQECFRSSPATESALHFLWREIVTSEGLKLYYNPYTGCIIREYPNSGPQLLGGILADEMGLGKTVEVLALILTHTRQDVKQDALTLPEGKVVNYFIPSHYFGGKLKKTEIQNIEFEPKEKVQCPPTRVMILTAVKEMNGKKGVSILSIYKYVSSIYRYDVQRNRSLLKRMLKCLIFEGLVKQIKGHGFSGTFTLGKNYKEEDICDKTKKQAVGSPRKIQKETRKSGNKDTDSEYLPSDTSDDDDDPYYYYYKSRRNRSKLRKKLVPSTKKGKSQPFINPDSQGHCPATSDSGITDVAMSKSTCISEFNQEHETEDCAESLNHADSDVPPSNTMSPFNTSDYRFECICGELDQIDRKPRVQCLKCHLWQHAKCVNYDEKNLKIKPFYCPHCLVAMEPVSTRATLIISPSSICHQWVDEINRHVRSSSLRVLVYQGVKKDGFLQPHFLAEQDIVIITYDVLRSELNYVDIPHSNSEDGRRLRNQKRYMAIPSPLVAVEWWRICLDEAQMVECPTVKAAEMAQRLSGINRWCISGTPVQRGLEDLFGLVVFLGIEPYCVKHWWVRLLYRPYCKKNPQHLYSFIAKILWRSAKKDVIDQIQIPPQTEEIHWLHFSPVERHFYHRQHEVCCQDVVVKLRKISDWALKLSSLDRRTVTSILYPLLRLRQACCHPQAVRGEFLPLQKSTMTMEELLTSLQKKCGTECEEAHRQLVCALNGLAGIHIIKGEYALAAELYREVLRSSEEHKGKLKTDSLQRLHATHNLMELLIARHPGIPPTLRDGRLEEEAKQLREHYMSKCNTEVAEAQQALYPVQQTIHELQRKIHSNSPWWLNVIHRAIEFTIDEELVQRVRNEITSNYKQQTGKLSMSEKFRDCRGLQFLLTTQMEELNKCQKLVREAVKNLEGPPSRNVIESATVCHLRPARLPLNCCVFCKADELFTEYESKLFSNTVKGQTAIFEEMIEDEEGLVDDRAPTTTRGLWAISETERSMKAILSFAKSHRFDVEFVDEGSTSMDLFEAWKKEYKLLHEYWMALRNRVSAVDELAMATERLRVRDPREPKPNPPVLHIIEPHEVEQNRIKLLNDKAVATSQLQKKLGQLLYLTNLEKSQDKTSGGVNPEPCPICARQLGKQWAVLTCGHCFCNECISIIIEQYSVGSHRSSIKCAICRQTTSHKEISYVFTSEKANQEEDIPVKGSHSTKVEAVVRTLMKIQLRDPGAKALVFSTWQDVLDIISKALTDNNMEFAQISRVKTFQENLSAFKRDPQINILLLPLHTGSNGLTIIEATHVLLVEPILNPAHELQAIGRVHRIGQTKPTIVHRFLIKATIEERMQAMLKTAERSHTNSSAKHSEASVLTVADLADLFTKETEELE
Protein: Small ribosomal subunit protein uS10z/uS10x (40S ribosomal protein S20-1) (P49200)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS19x
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS15z
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein uS15y
- Small ribosomal subunit protein uS4y
- Small ribosomal subunit protein eS21y
- Small ribosomal subunit protein eS17x
- Small ribosomal subunit protein eS24y
Sequence:
MATAYQPMKPGKAGLEEPLEQIHKIRITLSSKNVKNLEKVCTDLVRGAKDKRLRVKGPVRMPTKVLKITTRKAPCGEGTNTWDRFELRVHKRVIDLFSSPDVVKQITSITIEPGVEVEVTIADS
Protein: L-Ala-D/L-amino acid epimerase (EC 5.1.1.-) (L-Ala-L-Xxx epimerase) (A5FHW9)
Organism: Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae)
Function: Catalyzes the epimerization of D-Ala-D-Ala to D-Ala-L-Ala. Has broad substrate specificity and catalyzes the epimerization of a variety of dipeptides containing an N-terminal Ala followed by Ser, Thr, Val, Met, His, Phe or Trp (in vitro).
Interaction partners:
- Aminotransferase, class I and II
Sequence:
MKLILREYNLKLKHTFTISRESIDFQPSLIVELQSEGFSGFGEATSNPYYNITVPMMMQDLEKIRSIIEDTENETPDVFWAKIHPYLKNDMFALCALDLAYNDLYARKKGKKLYELWNYTTERNPMTDYTIGIASIDKMVSKMQELPWPIYKIKLGTKEDIEIVKELRKHTNAVFRIDANCGWGVEETINNSVELKKLGVEFLEQPMKADNWEGHKEVFKHSVLPVIADESCIIEEDVAKCFNHFHGVNVKLVKCGGLTPGKRMIEEAKKLGLRTMVGCMTESTVGISAIAHLLPQLDYVDMDGALLLAEDIATGVTIKDGVVSYSNLNGTGVTLL
Protein: Signal peptide peptidase (AtSPP) (EC 3.4.23.-) (Intramembrane protease) (IMP) (IMPAS) (O81062)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane (By similarity). Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm (By similarity). Plays a critical role in the development and function of the reproductive tissues, especially in pollen development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18067581, ECO:0000269|PubMed:19168645}; Multi-pass membrane protein {ECO:0000269|PubMed:18067581, ECO:0000269|PubMed:19168645}.
Interaction partners:
- Transmembrane protein
- RHOMBOID-like protein 10, chloroplastic
- Nicastrin
- Presenilin-like protein At2g29900
- Solanesyl diphosphate synthase 2, chloroplastic
- At5g11810
- Solanesyl diphosphate synthase 1, chloroplastic
- Rhomboid-like protein 11, chloroplastic
- Protein RALF-like 22
- Probable inositol transporter 3
Sequence:
MKNCERFANLALAGLTLAPLVVRVNPNLNVILTACITVYVGCFRSVKDTPPTETMSKEHAMRFPLVGSAMLLSLFLLFKFLSKDLVNAVLTAYFFVLGIVALSATLLPAIRRFLPNPWNDNLIVWRFPYFKSLEVEFTKSQVVAGIPGTFFCAWYAWKKHWLANNILGLSFCIQGIEMLSLGSFKTGAILLAGLFFYDIFWVFFTPVMVSVAKSFDAPIKLLFPTGDALRPYSMLGLGDIVIPGIFVALALRFDVSRRRQPQYFTSAFIGYAVGVILTIVVMNWFQAAQPALLYIVPAVIGFLASHCIWNGDIKPLLAFDESKTEEATTDESKTSEEVNKAHDE