wanglab/gogpt-training-data huggingface dataset:
Protein: Sister chromatid cohesion protein solo (Sisters on the loose) (B6JUP5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Isoform solo and SMC1 function as partners in mediating sister chromatid and centromere cohesion in meiosis. Not required for sister chromatid arm cohesion or for mitotic chromatid segregation.
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:20142422}. Note=Colocalizes with SMC1 to meiotic centromeres from early prophase I until both proteins disappear at anaphase II. Ord is required for stable centromere localization. {ECO:0000269|PubMed:20142422}.
Interaction partners:
- Sisters unbound
- Protein ORD
- ATP synthase subunit alpha, mitochondrial
- Stromalin-2
- Crossover suppressor on 2 of manheim
- ATP synthase subunit gamma, mitochondrial
- Cell division cycle 5, isoform A
- Structural maintenance of chromosomes protein
- ATP synthase subunit beta
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDAKELPPIPSSCDKDEVGAFIDQLDLSKYTTSLALIRKLRDYLLTAFKALVNQAWASLEKLAQEKRAQKAHQIRETTDMMNRLMEDMGRLIREGEHEEANGIGMGFQSIDADCRADLSQWRNLQQVVMPQSSEIRDGQTNRTSGTEGGRSGGLTDGDDLTEIQSAAYAVYHQVLDRGYQTGRRLYDDNQGALREDSIPTEDREHPENNQVDGSTYGVTRFLHWLSENFVTRHEIRAVRFGSPHMVFQSYDWPESPKQHISTVHQKGIFYSQPLIRTRIIATVASEPNNSSSGQLSSMVNLARHQRSQNQETPDGIYVSRYNATGDEETPCSATGVPGRVVALRASSTPNEHRSDPGLSFIPNLTYEDGTIPSLAAGGAASTPLAPSLPAEHSLGLEMDSNTLVVPADADETRLVGHPGSTVVRSRLGGPPASTPLLSFRPRLPVIDEEHHLRFTRVSRELQMSVAFPPEETTLSEQREWGSIFRPRDEMVNYAEGPPPRQTQRARRRSRTRRRRNRIASAASPQLTPERIVRREEAFQSSRHIAATFMSSLLQNAAGEVTTSSGLAVTRSVKEITTSVHITRNVLQEEVPPTTEATTTSLEVAQATGYSDSGACMQSAAFSQDLPVVAPLEISGNASSDQASFDQALALLPPINSTPIGQHPIAVFGPKTEIEIKPQKMDISNMMNTSVPPMPMEVDEVPLEVSNTLANMSDHAYVTDIQILPSLQLNSLNLVSTNITDNAVNIAPSTSTNDLQTPSDRRTSMQNQLYRVSMNDLAYISQHANVVRLMVDRQEELGAQVSSLGPFKENSQGALNFSTMPAVKVYDPRIIQNIQKDKMRVVHGLFGALIRQSQVDMHNAPFIRNRKDALMAYRFLLELKTANIISLSSDGRFFGLL
Protein: ESX-2 secretion system protein EccE2 (ESX conserved component E2) (Type VII secretion system protein EccE2) (T7SS protein EccE2) (P9WJE7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- ESX-2 secretion system protein EccA2
- Mycosin-2
- Probable conserved membrane protein
- ESX-2 secretion system protein eccD2
Sequence:
MTSKLTGFSPRSARRVAGVWTVFVLASAGWALGGQLGAVMAVVVGVALVFVQWWGQPAWSWAVLGLRGRRPVKWNDPITLANNRSGGGVRVQDGVAVVAVQLLGRAHRATTVTGSVTVESDNVIDVVELAPLLRHPLDLELDSISVVTFGSRTGTVGDYPRVYDAEIGTPPYAGRRETWLIMRLPVIGNTQALRWRTSVGAAAISVAQRVASSLRCQGLRAKLATATDLAELDRRLGSDAVAGSAQRWKAIRGEAGWMTTYAYPAEAISSRVLSQAWTLRADEVIQNVTVYPDATCTATITVRTPTPAPTPPSVILRRLNGEQAAAAAANMCGPRPHLRGQRRCPLPAQLVTEIGPSGVLIGKLSNGDRLMIPVTDAGELSRVFVAADDTIAKRIVIRVVGAGERVCVHTRDQERWASVRMPQLSIVGTPRPAPRTTVGVVEYVRRRKNGDDGKSEGSGVDVAISPTPRPASVITIARPGTSLSESDRHGFEVTIEQIDRATVKVGAAGQNWLVEMEMFRAENRYVSLEPVTMSIGR
Protein: Oxidized purine nucleoside triphosphate hydrolase (EC 3.6.1.56) (2-hydroxy-dATP diphosphatase) (7,8-dihydro-8-oxoguanine triphosphatase) (8-oxo-dGTPase) (Methylated purine nucleoside triphosphate hydrolase) (EC 3.6.1.-) (Nucleoside diphosphate-linked moiety X motif 1) (Nudix motif 1) (P53368)
Organism: Mus musculus (Mouse)
Function: Oxidized purine nucleoside triphosphate hydrolase which is a prominent sanitizer of the oxidized nucleotide pool. Catalyzes the hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP (By similarity). Has also a significant hydrolase activity toward 2-oxo-ATP, 8-oxo-dGTP and 8-oxo-dATP. Through the hydrolysis of oxidized purine nucleoside triphosphates, prevents their incorporation into DNA and the subsequent transversions A:T to C:G and G:C to T:A. Also catalyzes the hydrolysis of methylated purine nucleoside triphosphate preventing their integration into DNA. Through this antimutagenic activity protects cells from oxidative stress.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus {ECO:0000250|UniProtKB:P53369}. Nucleus membrane {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:P53369}.
Interaction partners:
- N-glycosylase/DNA lyase
- Adenine DNA glycosylase
- ADP-sugar pyrophosphatase
- Nucleotide triphosphate diphosphatase NUDT15
- 8-oxo-dGDP phosphatase NUDT18
- Uridine diphosphate glucose pyrophosphatase NUDT14
Sequence:
MSTSRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGAKRELLEESGLSVDTLHKVGHISFEFVGSPELMDVHIFSADHVHGTPTESEEMRPQWFQLDQIPFADLWPDDSYWFPLLLQKKKFCGHFKFQDQDTILSYSLREVDSF
Protein: Cruzioseptin-4 (CZS-4) (A0A193H2U2)
Organism: Cruziohyla calcarifer (Splendid leaf frog) (Agalychnis calcarifer)
Function: Has antimicrobial activity.
Subcellular location: Secreted {ECO:0000269|PubMed:27321580}.
Interaction partners:
Sequence:
KRGFLDVIKHVGKAALSVVSHLINEGEH
Protein: Leucine aminopeptidase 3, chloroplastic (EC 3.4.11.1) (Leucyl aminopeptidase 3) (AtLAP3) (Proline aminopeptidase 3) (EC 3.4.11.5) (Prolyl aminopeptidase 3) (Q8RX72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (By similarity). Possesses Cys-Gly dipeptidase activity.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Gamma-glutamylcyclotransferase 2-2
- Gamma-glutamylcyclotransferase 2-3
- Puromycin-sensitive aminopeptidase
- Glutathione hydrolase 1
- Glutathione hydrolase 3
- Glutathione hydrolase 2
- Putative inactive glutathione hydrolase 4
- Glutathione synthetase, chloroplastic
- Leucine aminopeptidase 1
- Glutamate--cysteine ligase, chloroplastic
Sequence:
MAVTLVTSCASSSRFHFRSFSSSPSSLSSCFVRFQLLSRLRVSFAITPLYCSSKATAHTIAHATLGLTQANSVDHPKISFSGKEIDVTEWKGDILAVGVTEKDMAKDANSKFENPILKKLDAHLGGLLADVSAEEDFSGKPGQSTVLRLPGLGSKRVGLIGLGKSASTPSAFQSLGEAVAAAAKASQASSVAVVLASSESFSDESKLSSASDIASGTVLGLFEDSRYKSESKKPSLKSVVFIGFGTGPELENKLKYAEHVSYGVIFTKELVNSPANVLSPAVLAEEASNLASMYSNVMTANILKEEQCKELKMGSYLAVAAASANPPHFIHLIYKPSSGPVKTKLALVGKGLTFDSGGYNIKIGPELIIELMKIDVGGSAAVLGAAKAIGEIKPPGVEVHFIVAACENMISGTGMRPGDVITASNGKTIEVNDTDSEGRLTLADALVYACNQGVDKIVDIATLTGEIIVALGPSMAGMYTASDELAKEVIAASQRSGEKLWRMPMEESYWEMMKSGVADMVNFGGRAGGSITAALFLKRFVSENVEWLHIDMAGRVWNEKKKAATGFGVATLVEWVQNNSS
Protein: Chromaffin granule amine transporter (Solute carrier family 18 member 1) (Vesicular amine transporter 1) (VAT1) (Q8R090)
Organism: Mus musculus (Mouse)
Function: Electrogenic antiporter that exchanges one cationic monoamine with two intravesicular protons across the membrane of secretory and synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to accumulate high concentrations of monoamines inside the vesicles prior to their release via exocytosis. Transports catecholamines and indolamines with higher affinity for serotonin. Regulates the transvesicular monoaminergic gradient that determines the quantal size. Mediates presynaptic monoaminergic vesicle transport in the amygdala and prefrontal brain regions related with emotion processing in response to environmental stimuli (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P54219}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:23201251}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vesicular inhibitory amino acid transporter
- Vesicular glutamate transporter 2
- Vesicular glutamate transporter 1
- Vesicular glutamate transporter 3
- Alpha-synuclein
- Vesicular acetylcholine transporter
- Synaptic vesicular amine transporter
Sequence:
MFQVVLGAPQRLLKEGRQSRKLVLVVVFVALLLDNMLLTVVVPIVPTFLYATEFKDINSSLLRGPSVSSQQALTSPAFSTTFSFFDNTTMTVEEHVPFRVAWINGTIPPPVTEAGSVPKNNCLQGIEFLEEENVRIGILFASKALMQLLVNPFVGPLTNRIGYHIPMFVGFMIMFLSTLMFAFSGTYALLFVARTLQGIGSSFSSVAGLGMLASVYTDNYERGRAMGIALGGLALGLLVGAPFGSVMYEFVGKSSPFLILAFLALLDGALQFCILWPSKVSPESAMGTPLLTLLKDPYILVAAGSICLANMGVAILEPTLPIWMMQTMCSPEWQLGLAFLPASVAYLIGTNLFGVLANKMGRWLCSLVGMVAVGISLLCVPLAHNIFGLIGPNAGLGFAIGMVDSSLMPIMGYLVDLRHTSVYGSVYAIADVAFCVGFAIGPSTGGVIVPVIGFPWLMVIIGTINIIYAPLCCFLQNPPAKEEELAILNQECPTETQMYTIQRPTKEFPLGENSDDPGSEE
Protein: Proliferating cell nuclear antigen 2 (PCNA 2) (Q9ZW35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 (By similarity). May be involved in UV resistance.
Subcellular location: Nucleus.
Interaction partners:
- DNA polymerase eta
- Replication factor C subunit 3
- Replication factor C subunit 2
- DNA polymerase delta small subunit
- DNA ligase 6
- Replication factor C subunit 5
- Flap endonuclease 1
- DNA repair protein REV1
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein MSH2
Sequence:
MLELRLVQGSLLKKVLEAVKDLVNDANFDCSTTGFSLQAMDSSHVALVSLLLRSEGFEHYRCDRNLSMGMNLGNMSKMLKCAGNDDIITIKADDGSDTVTFMFESPTQDKIADFEMKLMDIDSEHLGIPDAEYHSIVRMPSGEFSRICKDLSSIGDTVVISVTKEGVKFSTAGDIGTANIVLRQNTTVDKPEDAIVIEMNEPVSLSFALRYMNSFTKATPLSETVTISLSSELPVVVEYKVAEMGYIRYYLAPKIEEEEDTKPE
Protein: Cell division control protein 13 (P32797)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.
Subcellular location: Chromosome, telomere.
Interaction partners:
- DNA polymerase alpha catalytic subunit A
- Telomere elongation protein EST1
- Telomere length regulation protein TEN1
- Protein STN1
- Telomere replication protein EST3
- ATP-dependent DNA helicase II subunit 1
- ATP-dependent DNA helicase II subunit 2
- Telomerase reverse transcriptase
- Protein RIF2
- Exodeoxyribonuclease 1
Sequence:
MDTLEEPECPPHKNRIFVSSSKDFEGYPSKAIVPVQFVALLTSIHLTETKCLLGFSNFERRGDQSQEDQYLIKLKFKDRGSERLARITISLLCQYFDIELPDLDSDSGASPTVILRDIHLERLCFSSCKALYVSKHGNYTLFLEDIKPLDLVSVISTISTKSTNSSKHSSSELISECDLNNSLVDIFNNLIEMNRDEKNRFKFVKLIHYDIELKKFVQDQQKVLSQKSKAAAINPFFVPNRLGIPYIESQNEFNSQLMTLNVDEPTTDISNMGEEMHDSADPIEDSDSSTTSSTGKYFSSKSYIQSQTPERKTSVPNNWHDDDSGSKRKRKLSFHSPNASSIRKAISYEQLSLASVGSVERLEGKIVGMNPPQFASINEFKYCTLKLYFTQLLPNVPDKVLVPGVNCIEIVIPTRERICELFGVLNCQSDKISDILLLEKPDRISVEVERILWDNDKTASPGMAVWSLKNISTDTQAQAQVQVPAQSSASIDPSRTRMSKMARKDPTIEFCQLGLDTFETKYITMFGMLVSCSFDKPAFISFVFSDFTKNDIVQNYLYDRYLIDYENKLELNEGFKAIMYKNQFETFDSKLRKIFNNGLRDLQNGRDENLSQYGIVCKMNIKVKMYNGKLNAIVRECEPVPHSQISSIASPSQCEHLRLFYQRAFKRIGESAISRYFEEYRRFFPIHRNGSHLAKLRFDEVKHEPKKSPTTPALAEHIPDLNADVSSFDVKFTDISSLLDSSARLPRPQQTHKSNTLYSCEGRIIAIEYHASDLCFHITNELPLLQTRGLAPERVLQLHIITSKNFAYFFNRSSAYLQRQPLEEKYTQLAQFLGHSFKFNITSSLTLFPDTTVALQIWCPIECTFRELQQQLAHPKVAAAPDSGSLDCAINATVNPLRLLAAQNGVTVKKEEDNDDDAGAVPTS
Protein: Gamma-tubulin complex component gfh1 (Gcp4 homolog 1) (Q9P7R5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for proper anchoring of astral microtubules at the spindle pole bodies (SPBs), during anaphase, ensuring correct cell polarity.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:16823372}. Note=Localizes at the microtubule organizing center (MTOC).
Interaction partners:
- Gamma-tubulin complex subunit mod21
- Spindle pole body component alp16
- Spindle pole body component alp4
- Tubulin gamma chain
- Spindle pole body component alp6
- Mitotic-spindle organizing protein 1
- Gamma tubulin complex adapter mto1
- Gamma tubulin complex adapter mto2
- Myosin type-2 heavy chain 2
Sequence:
MLHEIILLLAGNTSGLFIEKNGQILLHPSVQPLHPGERELINDIVSLASKRKRIERYIEIFDEDLIQQNQFLLKALRLLLSKKLFLYDESLANLERMIISSDPYFVGSGKFVSLAQLEAHLADWKETLSSLLVLQGNISQCLSVASTFQKLHNMYMGSTHLNFKKLVLECECAFQKTWLDELVQYLVNDSGDDSFKCSFLCGDTKDFVSCSNNVPFLTQDIVNCLVSIRTCMLNAKKCFTDAFCEILRCFYRLVYEMPLPLTKSSVTKLADEMFTLVSEKIIFQLASFHQIFDLVKMLEMVMLLENVEFLPTLSEMFRDVRGEYCSSNDVQGVVIDDILPVVLRKTISLLDLATEYGECVSFLKLVSIFDEEDEMIRSENRKIDVEGLNMQLLLCLKWPFNLFMDKNALNVYSDLWILLGSLHLSITKIKSLFYERKEYTAKGISQPWTQLWVTLWFLSSLQYYAYECVIKPSYCKLRESLTELYRTQKLRMQDCSQLHALTLTYAKKMLFFYDDDLHISLNSIYHELSLFRSQEVSKVDCQLAAHVSHSIECIRQKENDPSYDREIINALIVQLNL
Protein: Protein pat-12 (Paralyzed arrest at two-fold 12 protein) (Q95QA6)
Organism: Caenorhabditis elegans
Function: Required for embryonic morphology and development. Plays both a functional and a structural role in the maintenance and probably biogenesis of fibrous organelles, a hemidesomosome-like junction structure, which ensures muscle stability and muscle connection to the external cuticle.
Subcellular location: [Isoform a]: Apical cell membrane {ECO:0000269|PubMed:21130760}; Peripheral membrane protein {ECO:0000303|PubMed:21130760}. Basal cell membrane {ECO:0000269|PubMed:21130760}; Peripheral membrane protein {ECO:0000303|PubMed:21130760}. Cytoplasm {ECO:0000269|PubMed:21130760}. Cell junction, hemidesmosome {ECO:0000269|PubMed:21130760}. Note=Co=localizes with cytoplasmic intermediate filaments. {ECO:0000269|PubMed:21130760}.; SUBCELLULAR LOCATION: [Isoform e]: Cell membrane {ECO:0000269|PubMed:21130760}.; SUBCELLULAR LOCATION: [Isoform i]: Cell membrane {ECO:0000269|PubMed:21130760}.; SUBCELLULAR LOCATION: [Isoform j]: Basal cell membrane {ECO:0000269|PubMed:21130760}. Apical cell membrane {ECO:0000269|PubMed:21130760}. Cytoplasm {ECO:0000269|PubMed:21130760}. Cell junction, hemidesmosome {ECO:0000269|PubMed:21130760}.; SUBCELLULAR LOCATION: [Isoform k]: Cell junction, hemidesmosome {ECO:0000269|PubMed:21130760}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21130760}. Note=Co-localizes with actin. {ECO:0000269|PubMed:21130760}.
Interaction partners:
Sequence:
MTSHIATETSVNRWSTEPVVREEGRPPGPEDFPSTKQGREQDGNVIGITPNYKIGEQKPNSELNLGKTGSLPRGSGDYKMTYRQEDYKQTIIDPKVITNANMPYISTRIPDPRRNLAGDFPSEHSKSKIKLDPLEQRRFRSSESRPITTSNYLAESVDRHREMEASRLREYLKAKENEANQPWNKPGWPGPKKNDESLRELETMKQRIETLKRDANKGPVNAELDELSKRAEELRKRDGWSKYKLVESDIYKTDPDPMPANIKDQVRDLLESRNSVETTTTQRDHDKSGYVTDVSTATWNFSTVDYSPRSVVSMNGASHDILKDDKPRSIMKRNDLVRREQMLYPTVDTQVVKSVVKKPTVTETVQRFEETRRTEEVERRVQRREKKERRSRHHSSSRHHSGWEGHTGGYQGHRSSSLSRGGHGGGGQETYYRQETTRRQQHNNYDDNFNRGIAHARYGSLSDSLRRGELQYVPNGEVRQSFYRDGSNGGQRMHKSYSTRDVFTGDGYDDRRSVSSFRRGSQQQVSPFVEFPPTLPRRGGGGDYRREEDAYFRPVSKSRSYADWDDAGRAGMGREVRRYDDDMSRLEAEFRDSLLMPMPAGNMNERDHRTEQLPGGYETFNKERHANSGRRSGRDGKPVDFNEATQEYNYKREQTLNDDRRRR
Protein: Nucleolar GTP-binding protein 1 (Q9U6A9)
Organism: Trypanosoma brucei brucei
Function: Involved in the biogenesis of the 60S ribosomal subunit.
Subcellular location: Nucleus, nucleolus.
Interaction partners:
Sequence:
MSTIYNFKTVTVVPSYKDFIDIVLSKTQRKTPTVVHKGYHISRIRQFYMRKVKFTQKTINEKLTHILTEFPRMDDIHPFYGDLMHVLYDRDHYKVALGQVGAVRHMVDNVGRDYVRLLKYGDSLYRCKQLKRAALGRMATACKKLTSALVYLEKVRQHMSRLPSIDPNARTLLITGFPNVGKSSFMNKVTRADVEVQPYAFTTKSLFVGHTDFKYASWQVIDTPGILDHSLEERNVIEMQAITALAHLRACILFFMDLSTQCGHSIAQQVSLFKSIGPLFTGKPVIVVFNKSDLCTFDDITAEEQSLVMTAIEECGAKWITTSTLTDAGVGDLKTLACETLLAHRSEQKEGSGRFQAIQNRLYCAVPQKRDNVERPAYVPPSVEEIRQRLASGEPVRERRKTERDYEWENGGPGQYQPNERKTWDLENPEWVDDIIPDIMDGHNIYDNVDPDIHERLMELEAEEDARLQELELEASKKRPQYELHDSTVEAVRFIRDKIKVIKMERAMKNPSLRRTRRQSVAIEKFNKRTGSQVDRSATPGCSSETTNSSAKRGRSLSAAQEAVMRDRSSSHMSTKTTRGISSHSATRDRSLSVNRGEGYRDVNEKLRAVKLSKVVARPRNLQAKKGEGDRAIPNLRPKHLFTGKVKSNGRRDRR
Protein: Antimicrobial peptide 4 (XT-4) (P84384)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Has very strong antimicrobial activity against Gram-positive bacterium S.aureus and yeast C.albicans, and very weak activity against Gram-negative bacterium E.coli. Has strong hemolytic activity against human red blood cells.
Subcellular location: Secreted {ECO:0000269|PubMed:11738090}.
Interaction partners:
Sequence:
GVFLDALKKFAKGGMNAVLNPK
Protein: Autophagy-related protein (A8MS84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIFACLKFAETNRIAMAKSSFKISNPLEARMSESSRIREKYPDRIPVIVEKAGQSDVPDIDKKKYLVPADLTVGQFVYVVRKRIKLGAEKAIFVFVKNTLPPTAALMSAIYEEHKDEDGFLYMTYSGENTFGSLTVA
Protein: Endosome-lysosome associated apoptosis and autophagy regulator 1 (E9PLQ2)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00046288}.
Interaction partners:
Sequence:
MAEPGHSHHLSARVRGRTERRIPRLWRLLLWAGTAFQVTQGTGPELHACKESEYHYEYTACDSTGSRWRVAVPHTPGLCTSLPDPIKGTECSFSCNAGEFLDMKDQSCKPCAEGRYSLGTGIRFDEWDELPHGFASLSANMELDDSAAESTGNCTSSKWVPRGDYIASNTDECTATLMYAVNLKQSGTVNFEYYYPDSSIIFEFF
Protein: Meiotically up-regulated gene 113 protein (Q10180)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Note=Localizes to the barrier septum and cell tip.
Interaction partners:
- Uncharacterized protein C56F8.02
- Uncharacterized protein C1494.08c
- Uncharacterized protein C14G10.04
- Uncharacterized protein C16C6.04
- Uncharacterized protein C9G1.07
- Ceramide-binding protein svf1
- U6 snRNA phosphodiesterase 1
Sequence:
MKMPNTLHSVSISTDFPSPNVESEAADVNEYSSTSKFETLGNQSSTNLGFSNSLQDKWDCWKRDLWSIWWSLSRKATRFYRWLSRSLKWRPVTYETVYPQTYETQMSEPREVTTIVKDLNNGDSFVLNVTEPVDPEFLRANIPPVHRKHLPPRLSLVASPGTIPTRGVVVLEDWINPLLSERCKLLLQSELCNQDSYDCPGYICVYRFEQKNNPSVVLGDSTLIQISRVSDLQRHLREYPKNCAFSRSVLEIFPDPGKTSKPCQVSFKVERLVHKELNEYLSWMQPFTCDSCGSLHENWLQIDSKQWDQIRGVILRWVEYSRVIYA
Protein: Embryo-specific protein ATS3A (Protein ARABIDOPSIS THALIANA SEED 3A) (Q681K2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role during embryo development.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Ricin B-like lectin EULS3
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Selenium binding protein
- At2g39980/T28M21.14
- Selenium-binding protein 2
- Expressed protein
Sequence:
MLRLAIPLFLFALCSFTLFSSARSFITTKPLPIDSFIPKPKLENAAACSYTVIIKTSCSSVSYTRDKISISFGDVYGNEVYVKRLDDPSSRTFEKCSSDTYKISGPCMRDVCYLYLLRQGSDGWKPENVKIYGSSIRSVTFYYNLFLPNSVWYGFNVCNGIGNTKSSQPISTTSSVAAM
Protein: Tricyclic peptide MS-271 (Class I lasso peptide) (P85078)
Organism: Streptomyces sp
Function: Inhibits chicken myosin light chain kinase with an IC(50) of 8 M. Does not inhibit bovine cAMP-dependent protein kinase or rat protein kinase C. Antibacterial activity against the Gram-positive bacteria B.subtilis, E.faecium and S.aureus. No antibacterial activity against the Gram-negative bacteria E.coli, K.pneumoniae, P.aeruginosa, P.vulgaris, S.sonnei and S.typhosa. No antifungal activity against C.albicans.
Interaction partners:
Sequence:
CLGVGSCNDFAGCGYAIVCFW
Protein: Uncharacterized protein (Q381K7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKGKAVKERCFKEAQKVKVAKLVGRYRELVGRLQLPVIDLSFYDSCFVEPLLRHPKDRRLEDALTTLCDYLEKHRCRTVEVLELCERRDQLVEWLLTCCEKFEESVIRPRLLRVIAHEVAPIDDNERHFFHFFRGALTAHQFLTGQLVEGIFHWREQLTRPFAFNVSDENYIYRILEDCELLDASSLGKALKLRLSDHPLGAHQVTTSDLCDHIVGRGFQIPSGDHRYGCLTGDPRGCSNALVAVGECWRPSAVQQRHRTCNDRASGNQVYLVLGEAIIKGEHLLQSRLLDELRALADNNRFLPMLSTPTLVTLGDLGLPLAEPSTKEWLQFVVRPGVGSALPCNPSTGDGNDTHGSRESPSQTVTTSSSSTSTSTLSESQLYPGTEPSSTAASSVTQ
Protein: Regulator of G-protein signaling 20 (RGS20) (Gz-selective GTPase-activating protein) (G(z)GAP) (Gz-GAP) (Regulator of G-protein signaling Z1) (Regulator of Gz-selective protein signaling 1) (O76081)
Organism: Homo sapiens (Human)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity).
Subcellular location: Membrane; Lipid-anchor. Nucleus. Cytoplasm. Note=Shuttles between the cytoplasm/cell membrane and the nucleus. Anchored to the membrane through palmitoylation. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rho guanine nucleotide exchange factor 1
- Guanine nucleotide-binding protein G
- Rho guanine nucleotide exchange factor 11
- Regulator of G-protein signaling protein-like
- Beta-adrenergic receptor kinase 1
Sequence:
MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVEPSQHIFDDAQLQIYTLMHRDSYPRFMNSAVYKDLLQSLSEKSIEA
Protein: TATA-binding protein-associated factor 172 (EC 3.6.4.-) (ATP-dependent helicase BTAF1) (B-TFIID transcription factor-associated 170 kDa subunit) (TAF(II)170) (TBP-associated factor 172) (TAF-172) (O14981)
Organism: Homo sapiens (Human)
Function: Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner.
Subcellular location: Nucleus.
Interaction partners:
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 2
- Dr1-associated corepressor
- Protein Dr1
- TATA box-binding protein-like 2
- TATA box-binding protein-like 1
- Cilia- and flagella-associated protein HOATZ
- Transcription initiation factor IIB
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
Sequence:
MAVSRLDRLFILLDTGTTPVTRKAAAQQLGEVVKLHPHELNNLLSKVLIYLRSANWDTRIAAGQAVEAIVKNVPEWNPVPRTRQEPTSESSMEDSPTTERLNFDRFDICRLLQHGASLLGSAGAEFEVQDEKSGEVDPKERIARQRKLLQKKLGLNMGEAIGMSTEELFNDEDLDYTPTSASFVNKQPTLQAAELIDSEFRAGMSNRQKNKAKRMAKLFAKQRSRDAVETNEKSNDSTDGEPEEKRRKIANVVINQSANDSKVLIDNIPDSSSLIEETNEWPLESFCEELCNDLFNPSWEVRHGAGTGLREILKAHGKSGGKMGDSTLEEMIQQHQEWLEDLVIRLLCVFALDRFGDFVSDEVVAPVRETCAQTLGVVLKHMNETGVHKTVDVLLKLLTQEQWEVRHGGLLGIKYALAVRQDVINTLLPKVLTRIIEGLQDLDDDVRAVAAASLVPVVESLVYLQTQKVPFIINTLWDALLELDDLTASTNSIMTLLSSLLTYPQVQQCSIQQSLTVLVPRVWPFLHHTISSVRRAALETLFTLLSTQDQNSSSWLIPILPDMLRHIFQFCVLESSQEILDLIHKVWMELLSKASVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLEVKARAKEKTGGKVRQGQSQNKEVLQEYIAGADTIMEDPATRDFVVMRARMMAAKLLGALCCCICDPGVNVVTQEIKPAESLGQLLLFHLNSKSALQRISVALVICEWAALQKECKAVTLAVQPRLLDILSEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNNNVLTIDQASDLVTTVFNEATSSFDLNPQVLQQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTRTPCPNSKIIKNLCSSLCVDPYLTPCVTCPVPTQSGQENSKGSTSEKDGMHHTVTKHRGIITLYRHQKAAFAITSRRGPTPKAVKAQIADLPAGSSGNILVELDEAQKPYLVQRRGAEFALTTIVKHFGGEMAVKLPHLWDAMVGPLRNTIDINNFDGKSLLDKGDSPAQELVNSLQVFETAAASMDSELHPLLVQHLPHLYMCLQYPSTAVRHMAARCVGVMSKIATMETMNIFLEKVLPWLGAIDDSVKQEGAIEALACVMEQLDVGIVPYIVLLVVPVLGRMSDQTDSVRFMATQCFATLIRLMPLEAGIPDPPNMSAELIQLKAKERHFLEQLLDGKKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYARSKLAECMPLPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRAKCDVDETVSSATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLTPQHPEFKTTAEKLAVQNSSLHDIQHAPKLSALKQLLLDCGLGNGSTSESGTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQENSSLQSMGTDQLLDLFTLDKDGKAEKADTSTSGKASMKSILENLSDLWDQEQYDSEYSLENFMHSLK