wanglab/gogpt-training-data huggingface dataset:
Protein: (DL)-glycerol-3-phosphatase 2 (EC 3.1.3.21) (Glycerol-1-phosphatase 2) (Haloacid dehalogenase-like hydrolase domain-containing protein GPP2) (Q8VZP1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a glycerol-3-phosphatase with higher stereospecificity for L-glycerol-3-phosphate than DL-glycerol-3-phosphate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:17136424}.
Interaction partners:
- Glycerol kinase
- Aldo-keto reductase family 4 member C10
- 
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Alpha/beta-Hydrolases superfamily protein
- Haloacid dehalogenase-like hydrolase domain-containing protein At2g33255
- Haloacid dehalogenase-like hydrolase domain-containing protein Sgpp
- Haloacid dehalogenase-like hydrolase domain-containing protein At4g39970
- Gamma-glutamyl peptidase 2
Sequence:
MSNPAAVTAGRGSITHVIFDMDGLLLDTEKFYTEVQEIILARFNKKFDWSLKAKMMGRKAIEAARIFVEESGISDSLSAEDFLVERESMLQDLFPTSELMPGASRLIKHLHVKNIPICIATGTHTRHYDLKTQRHRELFSLMHHVVRGDDPEVKQGKPAPDGFLAAARRFKDGPVDSQKVLVFEDAPSGVLAAKNAGMNVVMVPDPRLDISHQDVADQIITSLVDFKPEEWGLPPFEDSN
Protein: Tudor-interacting repair regulator protein (NUDT16-like protein 1) (Protein syndesmos) (Q9BRJ7)
Organism: Homo sapiens (Human)
Function: Key regulator of TP53BP1 required to stabilize TP53BP1 and regulate its recruitment to chromatin. In absence of DNA damage, interacts with the tandem Tudor-like domain of TP53BP1, masking the region that binds histone H4 dimethylated at 'Lys-20' (H4K20me2), thereby preventing TP53BP1 recruitment to chromatin and maintaining TP53BP1 localization to the nucleus. Following DNA damage, ATM-induced phosphorylation of TP53BP1 and subsequent recruitment of RIF1 leads to dissociate NUDT16L1/TIRR from TP53BP1, unmasking the tandem Tudor-like domain and allowing recruitment of TP53BP1 to DNA double strand breaks (DSBs). Binds U8 snoRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:28241136}.
Interaction partners:
- TP53-binding protein 1
- Syndecan-4
Sequence:
MSTAAVPELKQISRVEAMRLGPGWSHSCHAMLYAANPGQLFGRIPMRFSVLMQMRFDGLLGFPGGFVDRRFWSLEDGLNRVLGLGLGCLRLTEADYLSSHLTEGPHRVVAHLYARQLTLEQLHAVEISAVHSRDHGLEVLGLVRVPLYTQKDRVGGFPNFLSNAFVSTAKCQLLFALKVLNMMPEEKLVEALAAATEKQKKALEKLLPASS
Protein: Glycosidase (EC 3.2.-.-) (A2QAC9)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MYFSKTAVALAAVLPLATAQTYTDCDPLNKTCPADTALSSTTFTTDFTTGSFSGWIATANNVTFTDEGANFVISEKGEAPTIETDFYFFFGKAEVVMKAASGTGICSSVVLESDDLDEIDWEALGGDTTQIETNYFGKGDTSSYDRATWATVSTPQETFHTYTVEWTESATTWSIDGTVVRTLAYSDAQSGTRYPQTPMRLKLGIWAAGDSSEPEGTIEWAGGETDYSDGPFTMTVKSVSITNYNPGSSYTYSDKTGDYTSIVVNNGTSSSSVSSTTGSTSSSTSSSTSSSSSSTSSSDSTSSSGSTSSSGSSTSSGSSTSASSAAAAGSSSALIGSGSSTSSGSSAAGSGAASASGSASASSSASASASPVYTGAATHVGASTSVLFAGLLAALL
Protein: Glutathione S-transferase P 10 (EC 2.5.1.18) (GST 5.4) (GST class-pi) (GSTP2-2) (Q9N4X8)
Organism: Caenorhabditis elegans
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Responsible for approximately one-third of 4-hydroxy-2-nonenal conjugation. May play a role in the detoxification of reactive oxygen species produced during pathogenic bacterial infection.
Interaction partners:
- Glutathione transferase omega-1
- Probable glutathione transferase omega-2
- Probable glutathione S-transferase 7
- Protein skinhead-1
- Glutamate--cysteine ligase
- Probable glutathione S-transferase 6
- Glutathione reductase, mitochondrial
- Glutathione S-transferase 4
- Probable glutathione S-transferase 5
- Glutathione S-transferase omega
Sequence:
MAVPQLYYFTIRGFGEYIRLLFLDNGIKFEDIRFDYEGNEWQEFKKGMLLGQLPCLKVDGQEIVQTGAIMRHLGRVHGLNGSNEQEATFLDMFFEGVRDVRMKYVRYIYYDEGTREDCVNKTIPEALVKLEELFKAHSGDFIIGNKISYADYILFEELDVYHVLDANILDKFPTLKSFWERMWKRPNLNAYLEKRKADKVWINAIEKGMN
Protein: Peptide ARACIN 1 (Phytocytokine ARACIN1) (Mature form of ARACIN1) (mARACIN1) (Precursor of Peptide ARACIN 1) (Q9FIW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation (By similarity). Inhibits the fungal growth of Alternaria brassicicola, Sclerotinia sclerotiorum, Fusarium graminearum, yeast (Saccharomyces) and Botrytis cinerea, thus being an antimicrobial peptide (AMP). Promotes resistance to A.brassicicola and B.cinerea.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:B3H7I1}. Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:B3H7I1}. Endoplasmic reticulum {ECO:0000269|PubMed:25593351}. Note=Observed in a reticular pattern and a perinuclear ring (PubMed:25593351). The precursor of ARACIN1 accumulates at the plasma membrane and is proteolytically cleaved to release the ARACIN1 in the apoplasm (By similarity). {ECO:0000250|UniProtKB:B3H7I1, ECO:0000269|PubMed:25593351}.
Interaction partners:
Sequence:
MAMKTSHVLLLCLMFVIGFVEARRSDTGPDISTPPSGSCGASIAEFNSSQILAKRAPPCRRPRLQNSEDVTHTTLP
Protein: Scygonadin (Q5D710)
Organism: Scylla serrata (Mud crab)
Function: Has antibacterial activity against the Gram-positive bacterium M.luteus with an IC(90) of 125ug/ml. Has weak antibacterial activity against the Gram-negative bacterium A.hydrophila.
Subcellular location: Secreted {ECO:0000269|Ref.2}.
Interaction partners:
Sequence:
MRSSLLLGLTVVVLLGVIVPPCMAGQALNKLMPKIVSAIIYMVGQPNAGVTFLGHQCLVESTRQPDGFYTAKMSCASWTHDNPIVGEGRSRVELEALKGSITNFVQTASNYKKFTIDEVEDWIASY
Protein: Myosin regulatory light polypeptide 9 (20 kDa myosin light chain) (LC20) (MLC-2C) (Myosin RLC) (Myosin regulatory light chain 2, smooth muscle isoform) (Myosin regulatory light chain 9) (Myosin regulatory light chain MRLC1) (P24844)
Organism: Homo sapiens (Human)
Function: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion. In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9CQ19}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9CQ19}. Note=Colocalizes with F-actin, MYH9 and PIEZO1 at the actomyosin cortex in myoblasts. {ECO:0000250|UniProtKB:Q9CQ19}.
Interaction partners:
- Myosin-10
- Myosin-9
- Protein phosphatase 1 regulatory subunit 12C
- Myosin light chain kinase, smooth muscle
- Myosin light chain kinase 2, skeletal/cardiac muscle
- Myosin-11
- Myosin light polypeptide 6
- Protein phosphatase 1 regulatory subunit 12A
- Myosin light chain 6B
- Actin, gamma-enteric smooth muscle
Sequence:
MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD
Protein: Protein disulfide-isomerase 1 (PDI 1) (EC 5.3.4.1) (Prolyl 4-hydroxylase subunit beta-1) (Q17967)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Endoplasmic reticulum oxidoreductin-1
- Heat shock 70 kDa protein C
- Endoplasmic reticulum chaperone BiP homolog
- Calreticulin
- Thioredoxin domain-containing protein
Sequence:
MSLSVSFIFLLVASIGAVVADSENVLVLTESNFEETINGNEFVLVKFYAPWCVHCKSLAPKYDEAADLLKEEGSDIKLAKVDATENQALASKFEVRGYPTILYFKSGKPTKYTGGRATAQIVDWVKKKSGPTVTTVESVEQLEELKGKTRVVVLGYFKDAKSDAATIYNEVADSVDDAFFAVAGSAEVAAAASLNEDGVALIRTDGDDSETSTIAEAEITNTIALKQWLHAYKLSAVTEFTHESAQEIVGGDLKKFHFLIIRKSDSSFDETIAKFTEVAKKFRAKIVFVLLDVDVEENARILEFLGVDAKNTPANRIVSLADQVEKFKPQEGEDFEAFTNSYLEGKSAQDLKAQDLPEDWNALPVKVLVASNFNEIALDETKTVFVKFYAPWCGHCKQLVPVWDELAEKYESNPNVVIAKLDATLNELADVKVNSFPTLKLWPAGSSTPVDYDGDRNLEKFEEFVNKYAGSASESETASQDHEEL
Protein: Probable tubulin--tyrosine ligase PBY1 (EC 6.3.2.25) (P-body-associated protein 1) (P38254)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable P-body-associated tubulin--tyrosine ligase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Cytoplasm, P-body {ECO:0000269|PubMed:17307817}.
Interaction partners:
- Enhancer of mRNA-decapping protein 3
- mRNA-decapping enzyme subunit 1
- m7GpppN-mRNA hydrolase
- ATP-dependent RNA helicase DHH1
- LSM complex subunit LSM4
Sequence:
MRVLITNDDGPLSDQFSPYIRPFIQHIKRNYPEWKITVCVPHVQKSWVGKAHLAGKNLTAQFIYSKVDAEDNTFWGPFIQPQIRSENSKLPYVLNAEIPKDTIEWILIDGTPASCANIGLHLLSNEPFDLVLSGPNVGRNTSAAYITSSGTVGGAMESVITGNTKAIAISWAYFNGLKNVSPLLMEKASKRSLDVIKHLVKNWDPKTDLYSINIPLVESLSDDTKVYYAPIWENRWIPIFNGPHINLENSFAEIEDGNESSSISFNWAPKFGAHKDSIHYMDEYKDRTVLTDAEVIESEMISVTPMKATFKGVNHLLGELKLTEEENNLSKTNNLIVVSIDPMEYIYKPLTHALKKYLPQVEIVSNLPEFDNGGCEKEMKVFHYGDYEQLDMDKLMELPNNYFTNSYIYRKALIRKHFLSHTIQTYTAKNPESILKKAYLESFTIDLDYAEFLDDALDENWELRQELENESQDKWWIVKPSMSDKGQGIRVFKTIEDLQAIFDSFDDEDSEAEESGNDDDADDVNGEFMDNNKVNISQLRHFIIQEYLTNPLLLASMDNRKFHIRCYVVCRGDLQVFVYDRMLALFAAKPFVPLDPYAYSVTDLKDLECHLTNTCLQSKKKDKDSSVLEFDSIEEIPNERKSNIKEQIHSITNDVFLAAVNVNRLNFQPLPNAFETYGVDFLIDSNYEVKLLEINAFPDFKQTGKDLKNLIDELFDDTVKYCVTPIFNENRNKTDDETDPNFVKVIDYTSNGW
Protein: Enhancer of split m4 protein (E(spl)m4) (P13095)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of the Notch signaling pathway.
Interaction partners:
- Bearded
- Enhancer of split m8 protein
- Enhancer of split mgamma protein
- ABC-type xenobiotic transporter
- Enhancer of split m5 protein
- Enhancer of split m7 protein
- Defective proboscis extension response 10, isoform A
- Defective proboscis extension response 6, isoform F
- BARBU
- Ocho, isoform B
Sequence:
MCQNKINTNNTMTIKSNKKLSYSVKKLLQKIFKQQQRVEEEQNLKNALKANSLESLESMENSRNADLESASICASLESCENEANERLSQSCEIEDYDFEQLPTVPVHFVRTAHGTFFWTAVSDLPADNDLVEPLYCSTSNAIAIPQDRWVQA
Protein: SPG11 vesicle trafficking associated, spatacsin (H0YN34)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAEEGVASAASAGGSWGTAAMGRVLPMLLVPVPAEAMGQLGSRAQLRTQPEALGSLTAAGSLQVLSLTPGSRGGGRCCLEGPFWHFLWEDSRNSSTPTEKPKLLALGENYELLIYEFNLKDGRCDATILYSCSREALQKLIDDQDISISLLSLRILSFHNNTSLLFINKCVILHIIFPERDAAIRVLNCFTLPLPAQAVDMIIDTQLCRGILFVLSSLGWIYIFDVVDGTYVAHVDLALHKEDMCNEQQQEPAKISSFTSLKVSQDLDVAVIVSSSNSAVALNLNLYFRQHPGHLLCERILEDLPIQGPKGVDEDDPVNSAYNMKLAKFSFQIDRSWKAQLSSLNETIKNSKLEVSCCAPWFQDILHLESPESGNHSTSVQSWAFIPQDIMHGQYNVLQKDHAKTSDPGRSWKIMHISEQEEPIELKCVSVTGFTALFTWEVERMGYTITLWDLETQGMQCFSLGTKCIPVDSSGDQQLCFVLTENGLSLILFGLTQEEFLNRLMIHGSASTVDTLCHLNGWGRCSIPIHALEAGIENRQLDTVNFFLKSKENLFNPSSKSSVSDQFDHLSSHLYLRNVEELIPALDLLCSAIRESYSEPQSKHFSEQLLNLTLSFLNNQIKELFIHTEELDEHLQKGVNILTSYINELRTFMIKFPWKLTDAIDEYDVHENVPKVKESNIWKKLSFEEVIASAILNNKIPEAQTFFRIDSHSAQKLEELIGIGLNLVFDNLKKNNIKEASELLKNMGFDVKGQLLKICFYTTNKNIRDFLVGKGETT
Protein: Skp1-related protein (G5EDY3)
Organism: Caenorhabditis elegans
Interaction partners:
- Skp1-related protein
- Cullin-1
- Cullin-6
- RING-box protein 1
- F-box/WD repeat-containing protein lin-23
- Delta-like protein
- DUF38 domain-containing protein
- Tyrosine-protein phosphatase domain-containing protein
- C-type lectin domain-containing protein
- Uncharacterized protein
Sequence:
MSAEAAAVEVQANEAPIVAPIMYKVESSDGQVYEISDEAVKQSNTLSNLISTCVANDVASMDPIPITNVTGNIMKMVIEWCEKHKGETLPVEDDSVPKNITVPEWDTNFLKIDNDVLFDLIVASNFLDVPGLMSYACKMVANMAIGKSPDEMRVLFAIPTDEEDEAAEKAAKEKAEAEKKAITEKDAAEPSTSK
Protein: T3SS structure protein SepQ (B7UMA3)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Interaction partners:
Sequence:
MKPLSSQLNMKINDFYLPLLPVIGTGRLYITSEGHACHAYFREVSGHGIRFTLTYSGYEGRFWISEEQFIQWCQELFPYSESRLIPEDMIKLMILWVMQTALPEGDVSVDDVQFTMLNKDVYPVIENNNGENRLNVIILETTVQSLQHLINDNWQFVPHSNALFFDGYIVPGWTDYPVTELRVGDSLRLYHVDDSQERRCWIVINNPLATVKLSDNNLSVTDVLAADPLCTISSETVMNRIYCVIGTVHIDIHMLRNVQKDDIIDSTGYHLFGGCQLVRNNTTIAYGSIIKINEDFYFTISVVCD
Protein: tRNA pseudouridine synthase B (EC 5.4.99.25) (MTB-TRUB) (tRNA pseudouridine(55) synthase) (Psi55 synthase) (tRNA pseudouridylate synthase) (tRNA-uridine isomerase) (P9WHP7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Interaction partners:
- Ribosome-binding factor A
- Translation initiation factor IF-2
- Riboflavin biosynthesis protein
- GMP synthase
- Putative methyltransferase Rv1407
- 4'-phosphopantetheinyl transferase PptT
- Small ribosomal subunit protein uS15
- [Acyl-carrier-protein] phosphodiesterase PptH
- propanoyl-CoA C-acyltransferase
- tRNA pseudouridine synthase A
Sequence:
MSATGPGIVVIDKPAGMTSHDVVGRCRRIFATRRVGHAGTLDPMATGVLVIGIERATKILGLLTAAPKSYAATIRLGQTTSTEDAEGQVLQSVPAKHLTIEAIDAAMERLRGEIRQVPSSVSAIKVGGRRAYRLARQGRSVQLEARPIRIDRFELLAARRRDQLIDIDVEIDCSSGTYIRALARDLGDALGVGGHVTALRRTRVGRFELDQARSLDDLAERPALSLSLDEACLLMFARRDLTAAEASAAANGRSLPAVGIDGVYAACDADGRVIALLRDEGSRTRSVAVLRPATMHPG
Protein: Myosin phosphatase Rho interacting protein (H0Y2S9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XQEAELGEPDPEQKRSRARERRREGRSKTFDWAEFRPIQQALAQERVGGVGPADTHEPLRPEAEPGELERERARRREERRKRFGMLDATDGPGTEDAALRMEVDRSPGLPMSDLKTHNVHVEIEQRWHQVETTPLREEKQVPIAPVHLSSEDGGDRLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQTEVAASPSGAWQRLHRVNQDLQSELEAQCQRQELITHQIQTLKRSYGEAKDTIRHHEAEIRSLQARLSNAAAELAIKEQALAKLKGDLKREQGRVREQLEERQHSEAALSSQLRASEQKLKSAEALLLEKTQELRGLETQQALQRDRQKEVQRLQERIADLSQQLGASEQAQRLMEEKLQRNYELLLESCEKEKQALLQNLKEVEDKASAYEDQLQGQAQQVETLQKEKLSATFEGSEQVHQLEEQLEAREASVRRLAEHVQSLCDERDLLRQRFQELTERVATSDEDVAELREKLRRREADNQSLEHSYQRVSSQLQSMHTLLREKEEELERIKEAHEKVLEKKEQDLNEALVKMVALGSSLEETEIKLQAKEEILRKFASESPKDMEEPRSTPEETERDGTLLPGQPVQATRAPLGLPHTRLEDEDEDLGAPPGEEYGDGSPSREDSMVPPKSVEVLDREGHQQGTAKLDQGAPGVKRQRIRFSTIQCQRYIHPEGSEKTWTSSTSSDTSQDRSPSEESMSSEPAPSVLPATGDSDTYLSIIHSLETKLYVTEEKLKDVTVRLESQQGQSREALLALHHQWAGTEAQLREQLRASLLQVGALASQLEQERQERARRVEGHVGELGDFQVKNSQALMCLENCREQLRSLPRASQEDEQDARAASLASVESALVSAIQALQHWPAPAHGGARAQLETGGTEENGKPASLQQCSQSELTEQEQVRLLSDQIALEASLISQIADSLKNTTSDVSRMLHEISWSGQPPMESAGAPVDTWARKVLVDGEFWSQVESLRKHLGTLGGEAVGASGDGQQSIPQGLAPILANATWVRAELSFATQSVRESFHRRLQSIQETLRGTQTALRQHKCLLREILGAYQTPDFERVMQQVLEALRLPAGHEDGVQLSWDLSPLGEVLGRDSDSSQEPFDVSDQSPGAFVAIQEELAQQLKEKASLLEEIAAALPSLPPVESLRDCQKLLQVSQSLSYNTCLGGLGQYSSLLVQDAIIQAQVCYASCRIRLEYEKELQLCKESWQTREPSCSEQAQAARALREEYEELLRKQKSEYLDVIAIVERENAELKAKAAQLDHQQQCLEDAESKHSMSMFTLRGRYEEEIRCVVEQLTRTESTLQAERSRVLSQLDASVRDRQDMERHHGEQIQTLEDRFQLKVRELQTIHEEELRTLQEHYSQSLRCLQDTLCLHQGPHPKALPAPAPNWQATQGEADSMTGLRERIQELEAQMDVMREELGHKDLEGDAATLREKYQRDLESLKATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSVNSDVEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEATGSPLAQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPDSATVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSLKEGLTVQERLKLFESRDLKKD
Protein: Putative zinc metalloprotease PA3649 (EC 3.4.24.-) (Q9HXY3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Outer membrane protein assembly factor BamA
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- Elastase
- Phosphatidate cytidylyltransferase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Serralysin
- Uridylate kinase
- Ribosome-recycling factor
- Protease LasA
- Skp-like protein
Sequence:
MSALYMIVGTLVALGVLVTFHEFGHFWVARRCGVKVLRFSVGFGTPLVRWHDRHGTEFVVAAIPLGGYVKMLDEREAEVPAHLLEQSFNRKTVRQRIAIVAAGPIANFLLAILFFWVVALLGSQQVRPVIGSVAPESLAAQAGLEAGQELLAVDGEPVTGWNGVNLQLVRRLGESGTLEVRVQEKGSNVDSTHQVRLDGWLKGEDNPDPIASLGIRPWRPALPPVLAELDPKGPAQAAGLKLGDRLQSIDGIAVDDWQQVVDSVRARPGQRVQLKVLRDGEVLDVALELAVRGEGKARSGYMGAGVAGTEWPAEMLREVSYGPLEAVGQALSRTWTMSLLTLDSIKKMLLGELSVKNLSGPITIAKVAGASAQSGVGDFLNFLAYLSISLGVLNLLPIPVLDGGHLLFYLVEWVRGRPLSERVQAWGMQIGISLVVGVMLLALVNDLSRL
Protein: Ras-related protein RABA1e (AtRABA1e) (O49513)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Vesicle transport v-SNARE 12
- Syntaxin-32
- V-type proton ATPase subunit a1
- Kinesin-like protein KIN-14E
- Vesicle-associated membrane protein 711
- Novel plant SNARE 12
- Trafficking protein particle complex II-specific subunit 120 homolog
- Syntaxin-61
- Membrin-12
Sequence:
MGAYRADDDYDYLFKLVLIGDSGVGKSNLLSRFTRNEFSIESKSTIGVEFATRSVHVDEKIIKAQLWDTAGQERYRAITSAYYRGAVGALLVYDITRHITFENVERWLKELRDHTDANVVIMLVGNKADLRHLRAVPTEEARSFSERENMFFMETSALDATNVEQAFTHVLTQIYRVMSRKALDGTGDPMSLPKGQTIDIGNKDDVTAVKSSGCCSG
Protein: Methylcytosine dioxygenase TET (EC 1.14.11.80) (E7F958)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
- G/T mismatch-specific thymine DNA glycosylase
- G/T mismatch-specific thymine DNA glycosylase
- DNA
- ASXL transcriptional regulator 1.
- Isocitrate dehydrogenase
- DNA
- E3 ubiquitin-protein ligase UHRF1
- Isocitrate dehydrogenase
- Histone-lysine N-methyltransferase EZH2
- O-linked N-acetylglucosamine
Sequence:
METEKTSNETEKSHILAKISATQQTDFLTKHQNGDQSPEVLSQQKVPANLQGIFDQSMFGMKGQMKHALSEQALLDFHQTKTLVNGNENPRIWDKSEAGMENRLEVFPKHNKAGDLTHAKINCNFTNGDLFSLSRNKQVQMPNGATTSPPSVKGTTGDLLEKTLSQYYPEHVSIAPQTNSSQVDQVTSNLPDQATSSPSFTSGFPISPQISASETLVKAPPEVQNSNGYNPELAVNGYSSFAAEQKKPAYSLSDLPELSQKDSESNVPSQTVVNGSSQIQEDREALPNDSECVNMFSKSNQNLSHGSYTLPPVTAGSPSQTSQTGQYNPQIKVPQKKTTDENLHGNRDFSLLQQQTHEPQAVESKLIPQACTSPSQNRNNDQDNKSKLGLEKTLSKGTDPSSQMEWIDLNSTSASTPSTEHSQMWDLFLPQTNIQQHTVPQSQSQCINSIPPNNFQSHNFSNSSFPSHEIEAQENKNMLPPTRFPHSAAPESQQRNSGMHNHINMQFNNPQHMSQKLCKNDQDQILSPSFLSQLPPTETHQQATSTFSNQLPQDRQNMQASPLSRDASRSQEVEPLLKKLKTEDYLHSEFQMLPACIKTPAQVQISSKAIRENFGFQDSSKSNTPSLFKEVEALTERKLQQNTECSQNISTGQQIYQQPLQHRIYNHSEFSQSLISQSQHSQASDGLQIPVRTLTKAEFHESFAQIQRESLSSNGAQMDVQRHAALRMHLLQRQERQSPNNIRQMMPAIKSENCSGFEISAQPMEVQRQHEDHTKVLKAVVKQEHPPSSCDENQQRSILATMEQQLKQYQLSPVFEKKSLVIKSPNKVKVEMAGAVTVISTNAEGNAKEQCKQQHFTPPKKIEPGLQSFLESPMKLLNTPIKNLMDTPLKTQYEIPSCHCVEQISERDEGPYYTHLGSASNVAGIRKIMEERSGMTGSAIRIEKVLYTGKEGKSGLGCPIAKWVIRRANEDEKILVLVRERAGHSCETSCVVVVILIWEGIPTSLADRLYMELSDTLTKHGALTNRRCALNEERTCACQGLEADACGASFSFGCSWSMYYNGCKFARSKVPRKFKLLADDPKEEEKIEQNLQGLATYIAPVYKKMAPDAYSNQVEHENRAPDCRLGLKEGRPFSGVTACLDFCAHAHRDLHNMQGGSTVVCTLTREDNREIGKIPEDEQLHVLPLYKPSSTDEFGSAEAQLEKTKTGAIQVLSSFRRQVRMLPEPAKSCRQRKLDAKRANKPNNNTPNSKTDNTQQAKQKQTAYENPTVTGRGNMRTNLDSGHLPQAHAGHQPQQQFPQQTHPNPSYASPPFTRFPNASKPSTPHPQTPSVDPYASPLHAPNSYINASNAPSPYSRSLAPSPLYNGYQCNGGIPMDNYHPYHSSNLKHPDMFHPQRNPLYSEQQYNAPQHYGVNYPPHYGEAMATNGYGNCNMRPGIHSMGHYPGFDSNMSTNAFARPPSAHLHLDYAAAGNAYPKPHISQNPHMFSPNLNTLSMQSHKDLGISMHEANGISQGFPPLGKECFNFNQPSSLKLPNENAHNPAVNPTQLPQVSEKKEEDVWSDSEHNFLDPEIGGVAVAPSHGSIIIECAKRELHATTPVKKPDRNHPTRISLVFYQHKNLNEAKHGLSLWEAKMAEKAREKEEDAEKHGAENTSSKSGGKKAKREHSEHSEPSEPPYKQFLLMLTERSMSCTTNTYVSTSPYAFTKVTGPYNNFM
Protein: POU domain protein (A0A8I5ZSA9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MVHSSMGAPEIRMSKPLEAEKQSLDSPSEHTDTERNGPDINHQNPQNKASPFSVSPTGPSTKDIQQLLQLQQLVLVPGHHLQPPAQFLLPQAQQSQPGLLPTPNLFQLPQQTQGALLTSQPRAGLPTQAMTRPTLPDPHLSHPQPSKCLEPPSHPEEPSDLEELEQFARTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAETMSVDSSLPSPNQLSSPSLGFDGLPGRRRKKRTSIETNVRFALEKSFLANQKPTSEEILLIAEQLHMEKEVIRVWFCNRRQKEKRINPCSAAPMLPSPGKPTSYSPHLVTPQGGAGTLPLSQASSSLSTTVTTLSSAVGTLHPSRTAGGGGGGGGAAPPLNSIPSVTPPPPATTNSTNPSPQGSHSAIGLTGLNPSAGPGLWWNPAPYQP
Protein: Stearoyl-CoA desaturase (hSCD1) (EC 1.14.19.1) (Acyl-CoA desaturase) (Delta(9)-desaturase) (Delta-9 desaturase) (Fatty acid desaturase) (O00767)
Organism: Homo sapiens (Human)
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein {ECO:0000269|PubMed:18765284, ECO:0000305}.
Interaction partners:
- Cytochrome b5 type B
- Very long chain fatty acid elongase 6
- Cytochrome b5
- Sterol regulatory element-binding protein 1
- Acyl-CoA 6-desaturase
- Very-long-chain 3-oxoacyl-CoA reductase
- Fatty acid synthase
- Acyl-CoA
- Stearoyl-CoA desaturase 5
- Acetyl-CoA carboxylase 1
Sequence:
MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG
Protein: C2H2-type domain-containing protein (Q38BY1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein IFT88, putative
- Intraflagellar transport protein 57/55
- Intraflagellar transport protein 22
- Uncharacterized protein
- Intraflagellar transport protein 80
- Ankyrin repeat protein
- Intraflagellar transport protein 56 homolog
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein A1
Sequence:
MRQNPPKEPSEEEVLQYIVDNVNKLLSRHYSLVEFDAIQGTDLLQILADIFGTLSPAQQIDMGVAPTDEAAASMLEFLTKTLGYRVPPMLADSFPTSFSRAEPTVIYPTLYWVLSNMQQNEKRVYLARFLQRLEIPEAMLAQDEDVRALYQQYVNLRGMFVNTHRRVDALRTAHADPADARRAVTVLEEECDRLRGYIQVAEKKLAGVPDKEALLNACKSLRAALEEESRLAEKGVELQQQLISSRQRSTEMHNRLQNLRRDAADGRVDVIVRRLRDEIQTNKMIIEEQLPKELQQKQRENAEFDRLISEPLDMQALTTENQQLDEALKKLHQQVKERQKPGEDGSTIATIKQQVERVAKRKVEVMEQLTGLQADNSRTLNDIRERENRIEQLREAHHMLKDDDFREFSKQVLAKKAATESMRTHLSEQRVEYGVLNFTENVLRSQFTSLDAEIGDLEGKLGLQGYSRTVETLSKLTHEKDAIEGLKGKTLEELSRVVQDFTMAIRERRTKLAPLINELRSVRQTVAEVDQEWAEKKTQYEYQESVLMEDITKIEREVQSLHEETSTDESVYHRLQAQHLLLKAHVDRIEAEKDFAEIVRRGAEAADAAEKEGVVSGSGSLKCAHCAKACANKGWLLYHLCREHGLTVMAEKAFESAIEDLQIRLRDLQQKQRDIQENYEQNVQQVEWFGNLKRVLEAKLRTLHNEGSRCRNALDSDIKEIMGSAGAGGANVDMLVLPGD
Protein: No mechanoreceptor potential B, isoform C (Q9V9R6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSQITANGTQRLPEPVSEHEAVPPPPPTAAGRPRPPTSQLFSRGNLASSRATGGDKSGLARPSTAVRAVGYAANCESAHQRFEQFFLEKAKQQTLSSRAAVDAIKDVNPQMKYKNLEEKIVKLLESSIVLAWQGSPNKLLNLDTKLAEALSKAKEAFSLDRTLHQFRDQHGENVYHNFDLTYAVFFNLAEQYERSEMHIEALNTYSIMAKNKMFPHVNQLKLNMGNIYYSMGIYQKAVKMYRMALDSVPKSLSQLRLKIRENIGILFIRMGSYSDAASSFEFIMTERANIRSSIHLLLCYFALGDVEKVKLAFRRLCDVQTEAIESDMESETNIIKLQQQAEPIQQIGETDGYQSLNNEPVTGSVIKAEGGGKLNETVKFAATVKHRYVVQALKKDELAVYRNERRNAVKRSITMIVDLISPFIEDNYNDGYNWCIEIIKTSNLAWLANELELNKALVYLRQNDVHQAIETLQMYDRKSEGSMTASALTNLSFIYISLGNLEMASHCVNQLHEIGSLKNNAPGLINAGIVELGSHNLILASERFEGALQLQPMNFEARYNLGLVALAQNDYELAEERFELLKEQLMLPSSVQHSHVFYQLAKLQERRLESGLISNFTPGAALQAYLQVVGISASDIDSRLFEKVGSLYEQIQDHQEANQYYNEAYRINMSDIGIASSIGSYYIKLQATERALFYYERAVLADPNDPNLMLRIASCFRNSYLPTKQYLGLFQKIHARFPDNLTCIRALMQVTKSLELGDLYERYASEYTRLQSQQQERQSEQRYQQQRFPSAAKFSNRLRFLQFDPLGPPAERPKTGRPLQSRDDVDDDAEMNPESLLPI