wanglab/gogpt-training-data huggingface dataset:
Protein: Aminopeptidase Y (EC 3.4.11.15) (P37302)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole. Note=Lysosome-like vacuoles.
Interaction partners:
- Vacuolar membrane protease
- Dipeptidyl aminopeptidase B
- Carboxypeptidase S
- Aminopeptidase 2, mitochondrial
- Cerevisin
Sequence:
MHFSLKQLAVAAFYATNLGSAYVIPQFFQEAFQQEEPIENYLPQLNDDDSSAVAANIPKPHIPYFMKPHVESEKLQDKIKVDDLNATAWDLYRLANYSTPDYGHPTRVIGSKGHNKTMEYILNVFDDMQDYYDVSLQEFEALSGKIISFNLSDAETGKSFANTTAFALSPPVDGFVGKLVEIPNLGCEEKDYASVVPPRHNEKQIALIERGKCPFGDKSNLAGKFGFTAVVIYDNEPKSKEGLHGTLGEPTKHTVATVGVPYKVGKKLIANIALNIDYSLYFAMDSYVEFIKTQNIIADTKHGDPDNIVALGAHSDSVEEGPGINDDGSGTISLLNVAKQLTHFKINNKVRFAWWAAEEEGLLGSNFYAYNLTKEENSKIRVFMDYDMMASPNYEYEIYDANNKENPKGSEELKNLYVDYYKAHHLNYTLVPFDGRSDYVGFINNGIPAGGIATGAEKNNVNNGKVLDRCYHQLCDDVSNLSWDAFITNTKLIAHSVATYADSFEGFPKRETQKHKEVDILNAQQPQFKYRADFLII
Protein: Nucleolar protein 58 (Nucleolar protein 5) (Q9Y2X3)
Organism: Homo sapiens (Human)
Function: Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:33367824, ECO:0000269|PubMed:34516797}. Nucleus, nucleoplasm {ECO:0000269|PubMed:33367824}. Note=Localizes to the nucleolus with a minor part present in the nucleoplasm. {ECO:0000269|PubMed:33367824}.
Interaction partners:
- HEAT repeat-containing protein 1
- U3 small nucleolar RNA-associated protein 4 homolog
- rRNA 2'-O-methyltransferase fibrillarin
- H/ACA ribonucleoprotein complex subunit DKC1
- WD repeat-containing protein 75
- U3 small nucleolar RNA-associated protein 15 homolog
- Nucleolar protein 56
- KRR1 small subunit processome component homolog
- Ribosome biogenesis protein BMS1 homolog
- Transducin beta-like protein 3
Sequence:
MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKFQDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKEKLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYRLKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISDNLTYCKCLQKVGDRKNYASAKLSELLPEEVEAEVKAAAEISMGTEVSEEDICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIAHAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQTSPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGVENRAKLEARLRTLEDRGIRKISGTGKALAKTEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEQVDKEDEITEKKAKKAKIKVKVEEEEEEKVAEEEETSVKKKKKRGKKKHIKEEPLSEEEPCTSTAIASPEKKKKKKKKRENED
Protein: Myrosinase 2 (EC 3.2.1.147) (Beta-glucosidase 37) (AtBGLU37) (Sinigrinase 2) (Thioglucosidase 2) (Q9C5C2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May degrade glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. These toxic degradation products can deter insect herbivores. Seems to function in abscisic acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. Functionally redundant with TGG1.
Interaction partners:
- Cytosolic sulfotransferase 16
- Nitrilase 1
- Inactive GDSL esterase/lipase-like protein 25
- Indoleacetaldoxime dehydratase
- Cytochrome P450 71A12
- Nitrilase 3
- Nitrilase 2
- Cytochrome P450 71A18
- N-
- Transcription factor MYB28
Sequence:
MQHNTYIYILTMKLLGFALAILLVVATCKPEEEITCEENVPFTCSQTDRFNKQDFESDFIFGVASSAYQIEGGRGRGLNVWDGFTHRYPEKGGADLGNGDTTCDSYRTWQKDLDVMEELGVKGYRFSFAWSRILPKGKRSRGINEDGINYYSGLIDGLIARNITPFVTLFHWDLPQSLQDEYEGFLDRTIIDDFKDYADLCFERFGDRVKHWITINQLFTVPTRGYALGTDAPGRCSQWVDKRCYGGDSSTEPYIVAHNQLLAHATVVDLYRTRYKYQGGKIGPVMITRWFLPYDDTLESKQATWRAKEFFLGWFMEPLTKGKYPYIMRKLVGNRLPKFNSTEARLLKGSYDFLGLNYYVTQYAHALDPSPPEKLTAMTDSLANLTSLDANGQPPGPPFSKGSYYHPRGMLNVMEHFKTKYGDPLIYVTENGFSTSGGPIPFTEAFHDYNRIDYLCSHLCFLRKAIKEKRVNVKGYFVWSLGDNYEFCNGYTVRFGLSYVDFNNVTADRDLKASGLWYQSFLRDTTKNQDILRSSLPFKNGDRKSLT
Protein: Growth hormone (A0FJ27)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELGDVTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Kinesin-like protein KIF2C (Kinesin-like protein 6) (Mitotic centromere-associated kinesin) (MCAK) (P70096)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells (By similarity). Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. Plays a role in chromosome congression and is required for the lateral to end-on conversion of the chromosome-microtubule attachment (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19543227}. Nucleus {ECO:0000269|PubMed:7822426}. Chromosome, centromere {ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:7822426}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14960279, ECO:0000269|PubMed:7822426}. Note=Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, through interaction with MTUS2/TIP150 and MAPRE1 (PubMed:19543227). Association with microtubule plus ends is also mediated by interaction with KIF18B (By similarity). Centromeric localization requires the presence of BUB1 and SGO2 (By similarity). {ECO:0000250|UniProtKB:Q99661, ECO:0000269|PubMed:19543227}.
Interaction partners:
Sequence:
MESLPARLFPGLSIKIQRSNGLIHSANISTVNVEKSCVSVEWIEGGNTKGKEIDFDDVAAINPELLQLLPLHPKDNLPLQENVTVPKQKRRSVNSKIPAPKEGLRSRSTRMSTVPEVRIATQENEMEVELPVATNSRKQFSVATGLPRPSCPAMTELPLSMVSEEAEEQVHPTRSTSSANPARRKSCIVKEMEKMKNKREEKRAQNSEIRIKRAQEYDSSFPNWEFARMIKEFRVTIECHPLTLTDPTEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLFVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNTSKGIYAMASRDVFLLKSQPRYRNLNLEVYVTFFEIYNGKVFDLLNKKAKLRVLEDSKQQVQVVGLQEYLVNCADDVIKMLNMGSACRTSGQTFANSNSSRSHACFQILLRAKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGLSGEQPIQMETEEMEASSNGTSLAVNFKEEEELSSQMSSFNEAMSQIRELEERAMEELREIIQQGPGWLELSEMTDQPDYDLETFVNKAESALTQQTKHFSALREVIKALRVAMQLEEQASKQMNSKKRHQ
Protein: NF-kappa-B inhibitor delta (I-kappa-B-delta) (IkB-delta) (IkappaBdelta) (IkappaBNS) (Q2TB02)
Organism: Mus musculus (Mouse)
Function: Regulates the expression of IL-2, IL-6, and other cytokines through regulation on NF-kappa-B activity. Functions in the regulation of inflammatory responses. Involved in the induction of T helper 17 cells (Th17) differentiation upon recognition of antigen by T cell antigen receptor (TCR). According to PubMed:11931770, it may also regulate TCR-induced negative selection of thymocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:11931770}.
Interaction partners:
- Proto-oncogene c-Rel
- NF-kappa-B inhibitor beta
- Transcription factor RelB
- Transcription factor p65
- Nuclear factor NF-kappa-B p100 subunit
- Nuclear factor NF-kappa-B p105 subunit
Sequence:
MEDSLDTRLYPEPSLSQVGSWRVSSLPSGSPQLPSPTGPSLETARAHILALGPQQLLAQDEEGDTLLHLFAARGLRWAAYAAAEVLQMYRQLDIREHKGKTPLLVAAAANQPLIVEDLLSLGAEPNATDHQGRSVLHVAATYGLPGVLSAVFKSGIQVDLEARDFEGLTPLHTAVLALNAAMLPASVCPRMQNSQARDRLTCVQMLLQMGASHTSQEIKSNKTILHLAVQAANPTLVQLLLGLPRGDLRAFVNMKAHGNTALHMAAALPPGPPQEAIVRHLLAAGADPTLRNLENEQPVHLLRPGPGPEGLRQLLKRSRTAPPGLSS
Protein: Coatomer subunit beta' (Beta'-coat protein) (Beta'-COP) (p102) (P35606)
Organism: Homo sapiens (Human)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi. {ECO:0000250}.
Interaction partners:
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit alpha
- Coatomer subunit epsilon
- Coatomer subunit gamma-1
- Coatomer subunit zeta-1
- Coatomer subunit gamma-2
- Coatomer subunit zeta-2
- Bifunctional glutamate/proline--tRNA ligase
- ADP-ribosylation factor GTPase-activating protein 2
Sequence:
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLSKVNQKAAESLADPTEYENLFPGLKEAFVVEEWVKETHADLWPAKQYPLVTPNEERNVMEEGKDFQPSRSTAQQELDGKPASPTPVIVASHTANKEEKSLLELEVDLDNLELEDIDTTDINLDEDILDD
Protein: Protein BRI1-5 ENHANCED 1 (EC 1.1.1.-) (O22133)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Element of the brassinosteroid metabolic pathway that regulates typhasterol (TY), castasterone (CS) and brassinolide (BL) levels. Involved in the control of organ elongation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17521414}.
Interaction partners:
- Nucleotide binding protein
- 11-beta-hydroxysteroid dehydrogenase-like 2
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- rRNA biogenesis protein RRP36
- Cytochrome P450 709B2
- At1g19540
- At5g56840
- Protein RESPONSE TO LOW SULFUR 3
- Cytochrome P450 76C1
- Protein LOW PHOTOSYNTHETIC EFFICIENCY 1
Sequence:
MVREEQEEDDNNNNNNGGGERKLLVADETVPSLLDETGLVCVTGGSGFVASWLIMRLLQRGYSVRATVRTNSEGNKKDISYLTELPFASERLQIFTADLNEPESFKPAIEGCKAVFHVAHPMDPNSNETEETVTKRTVQGLMGILKSCLDAKTVKRFFYTSSAVTVFYSGGNGGGGGEVDESVWSDVEVFRNQKEKRVSSSYVVSKMAAETAALEFGGKNGLEVVTLVIPLVVGPFISSSLPSSVFISLAMLFGNYKEKYLFDTYNMVHIDDVARAMIFLLEKPVAKGRYICSSVEMKIDEVFEFLSTKFPQFQLPSIDLNKYKVEKRMGLSSKKLKSAGFEFKYGAEEIFSGAIRSCQARGFL
Protein: Heat stress transcription factor A-1b (AtHsfA1b) (AtHsf-18) (Heat shock factor protein 3) (HSF 3) (Heat shock transcription factor 3) (HSTF 3) (O81821)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Heat shock protein 90-1
- Heat shock 70 kDa protein 4
- L-ascorbate peroxidase 2, cytosolic
- Heat shock factor-binding protein
- Dehydration-responsive element-binding protein 2A
- Chaperone protein ClpB1
- Multiprotein-bridging factor 1c
- 18.1 kDa class I heat shock protein
- 22.0 kDa heat shock protein
- Heat shock protein 21, chloroplastic
Sequence:
MESVPESVPSPNSNTPSIPPPVNSVPPFLSKTYDMVDDPLTNEVVSWSSGNNSFVVWSAPEFSKVLLPKYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGRKQLLKSIVRRKPSHVQQNQQQTQVQSSSVGACVEVGKFGIEEEVERLKRDKNVLMQELVRLRQQQQATENQLQNVGQKVQVMEQRQQQMMSFLAKAVQSPGFLNQLVQQNNNDGNRQIPGSNKKRRLPVDEQENRGDNVANGLNRQIVRYQPSINEAAQNMLRQFLNTSTSPRYESVSNNPDSFLLGDVPSSTSVDNGNPSSRVSGVTLAEFSPNTVQSATNQVPEASLAHHPQAGLVQPNIGQSPAQGAAPADSWSPEFDLVGCETDSGECFDPIMAVLDESEGDAISPEGEGKMNELLEGVPKLPGIQDPFWEQFFSVELPAIADTDDILSGSVENNDLVLEQEPNEWTRNEQQMKYLTEQMGLLSSEAQRK
Protein: Sodium-dependent noradrenaline transporter (Norepinephrine transporter) (NET) (Solute carrier family 6 member 2) (P51143)
Organism: Bos taurus (Bovine)
Function: Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline). Can also mediate sodium- and chloride-dependent transport of dopamine (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P23975}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Synaptic vesicular amine transporter
- SEC24 homolog D, COPII coat complex component
- Dopamine beta-hydroxylase
- Tyrosine 3-monooxygenase
- Amine oxidase [flavin-containing] A
Sequence:
MLLARMNPQVQPENGGAGPGSEQPPRKRKEVLVVKERNGVQCLLASRDGDEQPRETWGKKIDFLLSVVGFAVDLANVWRFPYLCYKNGGGAFLIPYTLFLIIAGMPLFYMELALGQYNREGAATVWKICPFFKGVGYAVILIALYVGFYYNVIIAWSLYYLFSSFTPTLPWTDCGHAWNSPNCTDPKLLNSSVLGNHTKYSKYKFTPAAEFYERGVLHLHESSGIHDIGLPQWQLLLCLIIVVIVLFFSLWKGVKTSGKVVWITATLPYLVLFVLLVHGITLPGASNGINAYLHIDFYRLKEATVWIDAATQIFFSLGAGFGVLIAFASYNKFDNNCYRDALLTSTINCVTSFISGFAIFSILGYMAHEHKVNIEDVATEGAGLVFILYPEAISTLSGSTFWAIVFFIMLLALGIDSSMGGMEAVITGLADDFQVLKRHRKLFTFAVSFGTFLLALFCITKGGIYVLTLLDTFAAGTSILFAVLMEAIGVSWFYGVDRFSNDIQQMMGFKPGLYWRLCWKFVSPAFLLFVVIVSIINFKPLTYDDYIFPLWANWVGWGIAGSSMVLVPAYIVYKFFSTRGSIRERLAYGITPASEHHLVAQRDIRQFQLQHWLAI
Protein: UDP-glucuronosyltransferase 2B10 (UDPGT 2B10) (EC 2.4.1.17) (P36537)
Organism: Homo sapiens (Human)
Function: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Subcellular location: Microsome membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 3A4)
- UDP-galactose translocator
- Cytochrome P450 2A6
- Cytochrome P450 2D6
- Cytochrome P450 1A1
- Cytochrome P450 3A5
- Cytochrome P450 2E1
- Aldehyde oxidase
- Beta-glucuronidase
- Cytochrome P450 2A13
Sequence:
MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSASILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAINDIIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFERHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLGRPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQNDLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMSSTDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD
Protein: ATP-sensitive inward rectifier potassium channel 8 (Inward rectifier K(+) channel Kir6.1) (Potassium channel, inwardly rectifying subfamily J member 8) (uKATP-1) (Q15842)
Organism: Homo sapiens (Human)
Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by external barium (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP-binding cassette sub-family C member 9
- ATP-binding cassette sub-family C member 8
- ATP-sensitive inward rectifier potassium channel 11
- Protein kinase C epsilon type
- A-type voltage-gated potassium channel KCND3
- Potassium voltage-gated channel subfamily E member 3
- Sodium channel regulatory subunit beta-3
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Potassium voltage-gated channel subfamily E regulatory beta subunit 5
- Sodium channel regulatory subunit beta-1
Sequence:
MLARKSIIPEEYVLARIAAENLRKPRIRDRLPKARFIAKSGACNLAHKNIREQGRFLQDIFTTLVDLKWRHTLVIFTMSFLCSWLLFAIMWWLVAFAHGDIYAYMEKSGMEKSGLESTVCVTNVRSFTSAFLFSIEVQVTIGFGGRMMTEECPLAITVLILQNIVGLIINAVMLGCIFMKTAQAHRRAETLIFSRHAVIAVRNGKLCFMFRVGDLRKSMIISASVRIQVVKKTTTPEGEVVPIHQLDIPVDNPIESNNIFLVAPLIICHVIDKRSPLYDISATDLANQDLEVIVILEGVVETTGITTQARTSYIAEEIQWGHRFVSIVTEEEGVYSVDYSKFGNTVKVAAPRCSARELDEKPSILIQTLQKSELSHQNSLRKRNSMRRNNSMRRNNSIRRNNSSLMVPKVQFMTPEGNQNTSES
Protein: COP9 signalosome complex subunit 4 (A0A0S2Z5H7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000256|ARBA:ARBA00004234}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGAEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEIYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
Protein: Delta(14)-sterol reductase TM7SF2 (Delta-14-SR) (EC 1.3.1.70) (3-beta-hydroxysterol Delta (14)-reductase) (C-14 sterol reductase) (Sterol C14-reductase) (Transmembrane 7 superfamily member 2) (E9PRQ1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Microsome membrane {ECO:0000256|RuleBase:RU369120}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369120}.
Interaction partners:
Sequence:
MFHLLLAARSGPARLLGPPASLPGLEVLWSPRALLLWLAWLGLQAALYLLPARKVAEGQELKDKSRLRYPINGFQALVLTALLVGLGMSAGLPLGALPEMLLPLAFVATLTAFIFSLFLYMKAQVAPVSALAPGGNSGNPIYDFFLGRELNPRICFFDFKYFCELRPGLIGWVLINLALLMKEAELRGSPSLAMWLVNGFQLLYVGDALWHEEAVLTTMDITH
Protein: Internalin A (P0DJM0)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Mediates the entry of L.monocytogenes into host intestinal epithelial cells; transformation with inlA alone allows L.innocua (a non-invasive species) to be taken up by host cells. Binds to human receptor cadherin-1 (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin-2 function as receptors. Mouse cadherin-1 is not a receptor, however mutating a single surface-exposed residue (Glu-172 to Pro in mouse) allows cadherin-1 to act as a receptor for InlA.
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:10736172, ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:20176794, ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:10736172, ECO:0000269|PubMed:11929538}. Secreted {ECO:0000269|PubMed:11854224, ECO:0000269|PubMed:20176794}. Note=In the absence of SrtA in exponential phase some protein is still anchored to the cell wall and a very small amount is secreted while overall protein levels are the same in the srtA mutant; in stationary phase almost no protein accumulates (PubMed:22837151). During exponential growth detected on the cell surface as a series of dots in a helical pattern, it is excluded from the septum; if expression is increased it accumulates at cell poles (PubMed:21725001). The helical pattern of InlA does not overlap with that of InlH, InlJ or Hbp2 (SvpA) (PubMed:21725001). In stationary phase colocalizes with InlH at cell poles and at the septum, the location shift requires SigB (PubMed:21725001). {ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151}.
Interaction partners:
- Internalin B
- Zinc metalloproteinase
- Actin assembly-inducing protein
- Phospholipase C
- Listeriolysin O
- Lmo2387 protein
- Lmo0514 protein
- Uncharacterized protein Lmo0206
- Putative peptidoglycan bound protein
Sequence:
MRKKRYVWLKSILVAILVFGSGVWINTSNGTNAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVEYLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLSFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISPISNLKNLTYLTLYFNNISDISPVSSLTKLQRLFFYNNKVSDVSSLANLTNINWLSAGHNQISDLTPLANLTRITQLGLNDQAWTNAPVNYKANVSIPNTVKNVTGALIAPATISDGGSYTEPDITWNLPSYTNEVSYTFSQPVTIGKGTTTFSGTVTQPLKAIFNVKFHVDGKETTKEVEAGNLLTEPAKPVKEGHTFVGWFDAQTGGTKWNFSTDKMPTNDINLYAQFSINSYTATFDNDGVTTSQTVDYQGLLQEPTAPTKEGYTFKGWYDAKTGGDKWDFATSKMPAKNITLYAQYSANSYTATFDVDGKSTTQAVDYQGLLKEPKAPTKAGYTFKGWYDEKTDGKKWDFATDKMPANDITLYAQFTKNPVAPPTTGGNTPPTTNNGGNTTPPSANIPGSDTSNTSTGNSASTTSTMNAYDPYNSKEASLPTTGDSDNALYLLLGLLAVGTAMALTKKARASK
Protein: Platelet-derived growth factor receptor-like protein (PDGFR-like protein) (PDGF receptor beta-like tumor suppressor) (Q15198)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
Sequence:
MKVWLLLGLLLVHEALEDVTGQHLPKNKRPKEPGENRIKPTNKKVKPKIPKMKDRDSANSAPKTQSIMMQVLDKGRFQKPAATLSLLAGQTVELRCKGSRIGWSYPAYLDTFKDSRLSVKQNERYGQLTLVNSTSADTGEFSCWVQLCSGYICRKDEAKTGSTYIFFTEKGELFVPSPSYFDVVYLNPDRQAVVPCRVTVLSAKVTLHREFPAKEIPANGTDIVYDMKRGFVYLQPHSEHQGVVYCRAEAGGRSQISVKYQLLYVAVPSGPPSTTILASSNKVKSGDDISVLCTVLGEPDVEVEFTWIFPGQKDERPVTIQDTWRLIHRGLGHTTRISQSVITVEDFETIDAGYYICTAQNLQGQTTVATTVEFS
Protein: Large ribosomal subunit protein bL19m (39S ribosomal protein L19, mitochondrial) (L19mt) (MRP-L19) (Q2HJI0)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P49406}.
Interaction partners:
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS4
- Ribosomal protein
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL27m
Sequence:
MAASIARGCQAAKGLGPSFRSARALLPVSTSVASRVLAGPGRRQITGPSEPGVFQPPPKPVIVDKRGPQRRESRFLSPEFIPPRGRTNPLKFQIERKDMLERRKILHIPEFYVGSILRVTTADPYANGKTSQFLGICIQRSGKGLGATFILRNTIEGQGVEICFELYNPRIQEIQVVKLEKRLDDSLLYLRDALPEYSTFDMNMKPVAQEPSREVPINQLKVKMKPKPWSKRWERPKFNVKGIRFDLCLTEEQMKEAQKWSQPWLEFDMMREYDTSKIETAIWNEIEASKSS
Protein: Exocyst complex component EXO70A3 (AtExo70a3) (Exocyst subunit Exo70 family protein A3) (F4KG58)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in PIN4 exocytosis and gravitropic responses in columella cells. By monitoring PIN4 distribution in columella cells, modulates auxin repartition and subsequently regulates the root system architecture (RSA), thus being a component of the auxin-dependent root directional growth (ARD).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Exocyst complex component EXO84C
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5A
- Exocyst complex component SEC5B
- Exocyst complex component EXO84A
- Exocyst complex component EXO84B
- Exocyst complex component SEC10a
- Exocyst complex component SEC3B
- Exocyst complex component SEC3A
Sequence:
MSNVLDKTNLHELSIAPKISTHDEKLYECTKCGIFFHRDSVESATEINPHENLGEVRAVEDKPNNESIKVDERGTCNFHFIDEHHGKVDGINTEYDASKFKQILENYSKLTEPNQLFECLPSNLRPPSDDEGSDGKSHDPQSNGLGKTDYTVPTIIPPTVLPVLHDLAQQMVKAGHQQELFKTYRDIRRAVLAQSLEKLGVERHSKYDVERMNQDVFEAKIMNWIHYIRISVKLLFAAEKEICHQILDGVEPFRDQSFAEITTISFGMLLSFGYAIAISRRSPEKVFVILDMYEIMIELQPEFELIFGSKPCTEMKEDALNLTKLLAQTVKETIADFEVAIEMDATETVVMDGSVHALTSYVARYVKFLFDYEPTLRQLFQEFNSNDPDTKLKSVMTGIMRALRNNLDGKSRQFEDAALTQLFLMNNVYYIVRNFRREEAKNFLGDDLVQTHRRIVQQHAKQYQTISWNKILQCITVQSSKSGLIKNESIKKTLVKEKFKTFNSQFEELHQRQCQWSVSDVELRESLRLAIAEVLLPAYGSFLKRFGPMIESGKNSQKYIRFTPEDLERMLNDFFQGKNLDVSPKR