wanglab/gogpt-training-data huggingface dataset:
Protein: Glutathione peroxidase-like peroxiredoxin GPX5 (EC 1.11.1.24) (CrGPX5) (Glutathione peroxidase GPX5) (EC 1.11.1.9) (Glutathione peroxidase homolog) (O22448)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Has thioredoxin peroxidase activity. May also have glutathione peroxidase activity, although this activity is controversial. Protects cells against reactive oxygen species, which may include photooxidative stress, hydrogen peroxide and organic hydroperoxides.
Subcellular location: Cytoplasm {ECO:0000269|Ref.10}. Note=Localizes to the cytoplasm in nitrogen-replete and nitrogen-deplete conditions. {ECO:0000269|Ref.10}.
Interaction partners:
- glutathione-disulfide reductase
- L-ascorbate peroxidase
- Uncharacterized protein
- BZIP domain-containing protein
- Catalase
- Endoplasmic reticulum oxidoreductin 1
Sequence:
MANPEFYGLSTTTLSGQPFPFKDLEGKAVLIVNVASKCGFTPQYKGLEELYQQYKDRGLVILGFPCNQFGGQEPGDASAIGEFCQRNFGVTFPIMEKSDVNGNDANPVFKYLKSQKKQFMMEMIKWNFEKFLVDKSGQVVARFSSMATPASLAPEIEKVLNA
Protein: NK6 homeobox 2 (D3Z4R4)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Myelin-associated oligodendrocyte basic protein
- Oligodendrocyte transcription factor 2
- Oligodendrocyte transcription factor 1
- Transcription factor SOX-10
Sequence:
MDANRPGAFVLSSAPLAALHNMAEMKTSLFPYALQGPAGFKTPALGSLGAQLPLGTPHGISDILGRPVGAAGGGLLGSLPRLNGLASSAGVYFGPAAAVARGYPKPLAELPGRPPIFWPGVVQGSPWRDPRLAGSAQAGGVLDKDGKKKHSRPTFSGQQIFALEKTFEQTKYLAGPERARLAYSLGMTESQVKVWFQNRRTKWRKRHAAEMASAKKKQDSDAEKLKVGGSDAEDDDEYNRPLDPNSDDEKITRLLKKHKPSNLALVSPCGGSAGDAL
Protein: Ubiquitin carboxyl-terminal hydrolase 53 (EC 3.4.19.12) (Ubiquitin-specific peptidase 53) (Q70EK8)
Organism: Homo sapiens (Human)
Function: Tight junction-associated protein that is involved in the survival of auditory hair cells and hearing. Maybe by modulating the barrier properties and mechanical stability of tight junctions. Has no peptidase activity.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:32124521}.
Interaction partners:
- Tight junction protein 2
Sequence:
MAWVKFLRKPGGNLGKVYQPGSMLSLAPTKGLLNEPGQNSCFLNSAVQVLWQLDIFRRSLRVLTGHVCQGDACIFCALKTIFAQFQHSREKALPSDNIRHALAESFKDEQRFQLGLMDDAAECFENMLERIHFHIVPSRDADMCTSKSCITHQKFAMTLYEQCVCRSCGASSDPLPFTEFVRYISTTALCNEVERMLERHERFKPEMFAELLQAANTTDDYRKCPSNCGQKIKIRRVLMNCPEIVTIGLVWDSEHSDLTEAVVRNLATHLYLPGLFYRVTDENAKNSELNLVGMICYTSQHYCAFAFHTKSSKWVFFDDANVKEIGTRWKDVVSKCIRCHFQPLLLFYANPDGTAVSTEDALRQVISWSHYKSVAENMGCEKPVIHKSDNLKENGFGDQAKQRENQKFPTDNISSSNRSHSHTGVGKGPAKLSHIDQREKIKDISRECALKAIEQKNLLSSQRKDLEKGQRKDLGRHRDLVDEDLSHFQSGSPPAPNGFKQHGNPHLYHSQGKGSYKHDRVVPQSRASAQIISSSKSQILAPGEKITGKVKSDNGTGYDTDSSQDSRDRGNSCDSSSKSRNRGWKPMRETLNVDSIFSESEKRQHSPRHKPNISNKPKSSKDPSFSNWPKENPKQKGLMTIYEDEMKQEIGSRSSLESNGKGAEKNKGLVEGKVHGDNWQMQRTESGYESSDHISNGSTNLDSPVIDGNGTVMDISGVKETVCFSDQITTSNLNKERGDCTSLQSQHHLEGFRKELRNLEAGYKSHEFHPESHLQIKNHLIKRSHVHEDNGKLFPSSSLQIPKDHNAREHIHQSDEQKLEKPNECKFSEWLNIENSERTGLPFHVDNSASGKRVNSNEPSSLWSSHLRTVGLKPETAPLIQQQNIMDQCYFENSLSTECIIRSASRSDGCQMPKLFCQNLPPPLPPKKYAITSVPQSEKSESTPDVKLTEVFKATSHLPKHSLSTASEPSLEVSTHMNDERHKETFQVRECFGNTPNCPSSSSTNDFQANSGAIDAFCQPELDSISTCPNETVSLTTYFSVDSCMTDTYRLKYHQRPKLSFPESSGFCNNSLS
Protein: Energy-dependent translational throttle protein EttA (EC 3.6.1.-) (Translational regulatory factor EttA) (P0A9W3)
Organism: Escherichia coli (strain K12)
Function: A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. Stimulates dipeptide bond synthesis in the presence of ATP (cell in high energy state), but inhibits dipeptide synthesis in the presence of ADP (cell in low energy state), and thus may control translation in response to changing ATP levels (including during stationary phase). Following ATP hydrolysis is probably released allowing the ribosome to enter the elongation phase. ATPase activity is stimulated in the presence of ribosomes. Its specificity for the IC may be conferred by its recognition of features unique to tRNA(fMet).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00847, ECO:0000269|PubMed:24389466}. Note=Associates with ribosomes and polysomes. {ECO:0000255|HAMAP-Rule:MF_00847}.
Interaction partners:
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein bL33
Sequence:
MAQFVYTMHRVGKVVPPKRHILKNISLSFFPGAKIGVLGLNGAGKSTLLRIMAGIDKDIEGEARPQPDIKIGYLPQEPQLNPEHTVRESIEEAVSEVVNALKRLDEVYALYADPDADFDKLAAEQGRLEEIIQAHDGHNLNVQLERAADALRLPDWDAKIANLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLERFLHDFEGTVVAITHDRYFLDNVAGWILELDRGEGIPWEGNYSSWLEQKDQRLAQEASQEAARRKSIEKELEWVRQGTKGRQSKGKARLARFEELNSTEYQKRNETNELFIPPGPRLGDKVLEVSNLRKSYGDRLLIDDLSFSIPKGAIVGIIGPNGAGKSTLFRMISGQEQPDSGTITLGETVKLASVDQFRDSMDNSKTVWEEVSGGLDIMKIGNTEMPSRAYVGRFNFKGVDQGKRVGELSGGERGRLHLAKLLQVGGNMLLLDEPTNDLDIETLRALENALLEFPGCAMVISHDRWFLDRIATHILDYQDEGKVEFFEGNFTEYEEYKKRTLGADALEPKRIKYKRIAK
Protein: RNA polymerase II-associated factor 1 homolog (P90783)
Organism: Caenorhabditis elegans
Function: Component of the PAF1 complex which is a multifunctional complex involved in transcription initiation via genetic interactions with TATA-binding proteins, elongation and transcription-coupled histone modification.
Subcellular location: Nucleus {ECO:0000269|PubMed:24721716, ECO:0000305}. Note=Nuclear localization depends on PAF1 complex components ctr-9, leo-1 and cdc-73. {ECO:0000269|PubMed:24721716, ECO:0000303|PubMed:24721716}.
Interaction partners:
- RNA polymerase-associated protein LEO1
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein CTR9
- Cell division cycle protein 73
- WD_REPEATS_REGION domain-containing protein
- Transcription elongation factor SPT5
- FACT complex subunit spt-16
- DNA-directed RNA polymerase II subunit RPB1
- Transcription elongation factor SPT4
- FACT complex subunit ssrp1-B
Sequence:
MPQESSDAKRIEPPRKVDFMLKPRFTNTVPDVPFDAKFMTCPFVPLGRFVEFQPAAIYRDYKHAVICDDDMGLNVDLIDLKKYDEDPIETEIDEKDNILLEDDGAAKLIAKRSQQHSKLVPWMRKTEYISTEFNRFGVTADRQETKLGYNLKKNQQVEDMYRDKQSQIDAINKTFEDVRKPVKEHYSKKGVKAVEESFVFPDFDHWKHLFAHVQFDGDTITTEFEEEDERQQARESSVIKAMEFEDQKFAAVFVPTIGCLTSFMDDLELERPFDEDMKYEFLLSREYTFKMEHLPPRDRDVFIMYHRNNVFQYNEVDCNVKMTRKPKMALSRKSKLTLTYRNPSELEQKDMNKREAELYEQPKTRKQEILEKIQEKKEEGGDSSDQSSDSDDDKPQKSRSDSSSDVSSDDDSPRKKEPTVDSDSD
Protein: Beta-toxin KAaH1 (Peptide AaF1CA8) (Q4LCT0)
Organism: Androctonus australis (Sahara scorpion)
Function: Inhibits the vertebrate potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3 in vitro with an IC(50) of 5.3 nM and 50.0 nM respectively.
Subcellular location: Secreted {ECO:0000269|PubMed:15656785}.
Interaction partners:
Sequence:
MMKLMLFSIIVILFSLIGSIHGADVPGNYPLDSSDDTYLCAPLGENPFCIKICRKHGVKYGYCYAFQCWCEYLEDKNVKI
Protein: Kinesin-related protein (A4GU96)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAAEGMLSFSVASVVEDVLQQHGNRSKDLDLESRKAEEDASRRYEAAGWLRKMVGVVAAKDLPAEPSEEEFRLGLRSGIILCNVLNRVQPGAVPKVVESPCDAALIPDGAALSAFQYFENIRNFLVAGQGLGLPTFEASDLEQGGKSARVVNCVLALKSYNEWRLSGGNGVWKFGGNFKPATPTLGKSFVRKNSEPFTNSLQRTSSMNEKLLSGHSNEIDPNKMASSGSLSMLVRALLTDKKPEEVPTLVESVLSKVVEEFENRIASQSEVMKTTSKDITPSNFRKPVLKQTLGDKKIEEKNIEVMKKEDCFQKNLINEEELKGQLQKQQMIFDQQQRNIKELKHAINSTKAGMQFIQMKFHEEFNSLGMHIHGLAHAASGYHRVLEENRKLYNQVQDLKGSIRVYCRVRPFLSGSSYLSTVDHIEEGNIIINTPSKYGKGRKSFTFNKVFGQSATQAEVFSDMQPLIRSVLDGYNVCIFAYGQTGSGKTYTMTGPKDLTEKSQGVNYRALGDLFLLAEQRKDTFCYDVAVQMIEIYNEQVRDLLVTDGSNKRLEIRNSSQTGLNVPDANLMPVSSTSDVIDLMNLGQRNRAVGATALNDRSSRSHSCLTVHVQGRDLTSGTTLRGCMHLVDLAGSERVDKSEVTGDRLKEAQHINKSLSALGDVIASLAQKNPHVPYRNSKLTQLLQDSLGGQAKTLMFVHISPEPDALGETISTLKFAERVATVELGAARVNKDTSDVKELKEQIASLKAALARKEGEMDQSQHSVSSSSEKYRTKASDLSPFNPNQQVGDVLGAREPVANVGNIEVCTNSALRQKRQSVDLDELLANSPPWPPVVSPAQNFRDDEKELGSGEWVDKVMVNKQDTINRVGSPLGCWEAENGNLSDVFYQKYLHDSSKIYPEKSYNMFLGANGFNMASADDIDDIDVATSDSSEPDLLWQFNSTKLSSITNGIESKTKRPTPKSARNPDMSKNLHPMSGPSPSRKLANGAGQPLHRNMRQPPAADGKRRTGSRK
Protein: ACT domain-containing protein ACR3 (Protein ACT DOMAIN REPEATS 3) (O49285)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May bind amino acids.
Interaction partners:
- Probable aquaporin NIP7-1
- Dual specificity phosphatase Cdc25
- Aquaporin NIP6-1
- Probable aquaporin NIP5-1
- Protein TIC 214
- ACT domain-containing protein ACR10
- Glutathione gamma-glutamylcysteinyltransferase 1
- Protein HIGH ARSENIC CONTENT 1, mitochondrial
- Aquaporin NIP1-2
- Farnesyl pyrophosphate synthase 1, mitochondrial
Sequence:
MAKVYWPYFDPEYENLSSRINPPSVSIDNTSCKECTLVKVDSMNKPGILLEVVQVLTDLDLTITKAYISSDGGWFMDVFHVTDQQGNKVTDSKTIDYIEKVLGPKGHASASQNTWPGKRVGVHSLGDHTSIEIIARDRPGLLSEVSAVLADLNINVVAAEAWTHNRRIACVLYVNDNATSRAVDDPERLSSMEEQLNNVLRGCEEQDEKFARTSLSIGSTHVDRRLHQMFFADRDYEAVTKLDDSASCGFEPKITVEHCEEKGYSVINVSCEDRPKLMFDIVCTLTDMQYIVFHATISSSGSHASQEYFIRHKDGCTLDTEGEKERVVKCLEAAIHRRVSEGWSLELCAKDRVGLLSEVTRILREHGLSVSRAGVTTVGEQAVNVFYVKDASGNPVDVKTIEALRGEIGHSMMIDFKNKVPSRKWKEEGQAGTGGGWAKTSFFFGNLLEKLLP
Protein: Protein NDRG4 (N-myc downstream-regulated gene 4 protein) (Protein Ndr4) (Q8BTG7)
Organism: Mus musculus (Mouse)
Function: Contributes to the maintenance of intracerebral BDNF levels within the normal range, which is necessary for the preservation of spatial learning and the resistance to neuronal cell death caused by ischemic stress. May enhance growth factor-induced ERK1 and ERK2 phosphorylation. May attenuate NGF-promoted ELK1 phosphorylation in a microtubule-dependent manner.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Popeye domain-containing protein 1
Sequence:
MPECWDGEHDIETPYGLLHVVIRGSPKGNRPAILTYHDVGLNHKLCFNTFFNFEDMQEITKHFVVCHVDAPGQQVGASQFPQGYQFPSMEQLAAMLPSVVQHFGFKYVIGIGVGAGAYVLAKFALIFPDLVEGLVLMNIDPNGKGWIDWAATKLSGLTSTLPDTVLSHLFSQEELVNNTELVQSYRQQISNVVNQANLQLFWNMYNSRRDLDINRPGTVPNAKTLRCPVMLVVGDNAPAEEGVVECNSKLDPTTTTFLKMADSGGLPQVTQPGKLTEAFKYFLQGMGYIAHLKDRRLSGGAVPSASMTRLARSRTASLTSASSVDGSRPQPCAHSDSSEGMGQVNHTMEVSC
Protein: Transcriptional regulator of yeast form adherence 6 (Q5ADL8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor required for yeast cell adherence to silicone substrate.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSLPSPPVLKTTIIQLNKELDPEDDNNNYEILTNDYNNYGSSNTSDAGSIPTSPIIEVSGTTKSGSGLPNKKKRRRSTANIDSEELAKRKNETKQLHSIIEKRRRIKINREFEALKYLIPACRNCNTGSSGGSATPTSSTKKASTNSNNNGNKIDGMYKLTILKSSVEYILYLHHIIQKQHQLLSSISAKDTNGGILAEKLKAFEDFDIDFAKVPLNVNQYRNIDKDFNFKDLMQDLDGRSVNTESPETIIEENEPVSETSSTNNTTTLHYSNSSVLPSRTSSIVSSRQSSSLPTPELTPILSILNKYSTSNNQLNNRKNSNPISPQTVCIKSQNPSPFTMPMKSSLSTSIVNSPSSSSSLSGSKSYMAGNNAVNTVKFSLPDPVVNPNSTLNDNIPRKGLISGIPEEEEEEKINKGSANTETVNSGSASSDENNDNDRGVLLKLTDQDVSKTLLALRKSSIDSLLN
Protein: SWR1-complex protein 4 (Q5AAJ7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein AF-9 homolog
- Actin-related protein 4
- Enhancer of polycomb-like protein 1
- Chromatin modification-related protein EAF6
- Histone acetyltransferase
- RuvB-like helicase 1
- Chromatin modification-related protein EAF7
- Chromatin modification-related protein EAF1
- RuvB-like helicase 2
- SWR1-complex protein 5
Sequence:
MSANDILDVLNIQRDESNQPPKKKQKSSSTPTLPDGKQLTGMARELYNLVGPNTPPINLNSNSYTANKEKMKKFKPSPWTRMPFTPKQGIELNHWVKGSKELIEQQEFEEDGTPKPYFFEKYNVQLEIPEFVDEDTYDLYMIEIKEYESKMKEERARREKERKEREKRDLEEKKKKQQQQQQKSQQNPQNQIKDDEKNQDTRNNTDKKDSEQKSEDKPTVEAKKETDEKKDDVVLKDNTNETKPVTETTKSETETTEQNNSEKTNENETNKTNDKDGEGNLTKSKDSATEDQSNNKKENDEDTESEWTYKETKHLFELCQAFELKWPIIHDRFPNPNRTAEDLKEQFYRICIKILENQKNKNQALIDSLKAYCKPRELERKQYLENLLKRTPAEIAEEESLVIEARRFEIAAKKMLMERSNLLTLLDSPQTTQNVSQYQSSQGITNLYNNLLIYDKHQKKKQMANKSNPQQEPVPPPIPLAASSSVKRDRGFQTQLQQYLSSFLKQNHHTNPAVKQEINSIQQLLMKRLTQKEEEAYGLYFHGTEKLNPGVMLRSQQKLPGLNQRQSILKSVNILLQEMDIPTGGGTSWKPIMPTRKTMAKYDELIRSVVTLLDVKKAKDKLESEIKLIKSQRGL
Protein: Uncharacterized protein YPR063C (Q12160)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Eukaryotic translation initiation factor 1A
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS15
- Eukaryotic translation initiation factor 3 subunit C
- Small ribosomal subunit protein uS19
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS12
Sequence:
MTLNNVARPDLCVSYKKIAPPKGLYSATPSISGVVNQSMPMAAIFLRNKFIAWFSLIQSVHYYLNTDEDIIVAYKENKAPSPMDQPPAIKLFMSLIGLCVCYMNLVFPQQIAQPSSSGSKGNTETTIETTTEVETETAKQ
Protein: 25S rRNA adenine-N(1) methyltransferase (EC 2.1.1.-) (Q9UUH2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of an adenine present in helix 65 in 25S rRNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03044, ECO:0000269|PubMed:16823372}.
Interaction partners:
- CTP synthase
- Elongation factor Ts, mitochondrial
- Eukaryotic translation initiation factor 5B
- Translation initiation factor IF-2, mitochondrial
- Large ribosomal subunit protein bL17m
- rRNA biogenesis protein rrp5
- Putative peptide chain release factor 1, mitochondrial
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase II subunit RPB3
- Putative ribosomal recycling factor
Sequence:
MRPIPVKNRIGKNNIDNAKGLKGNKLIRHYHNLLKEKSRLIASSAPIEKIKNVESELENIGIDAYQRASRSGQAEGKGGDSSKILIKWIRTTPCFSYCARLKEPKDLLEIGSVSVDNKCSTCGLFRVSRIDLHSVHPLIKQQDFLERTPEEGLFTGISCSLVLNFAPPELRAKMLLHCTGLLMPPNKEQPPWLFLVLPSPCITNSRYMDEKTLHSIMIQFGFICRQKSISKKIAYYLYSYECFPMKEIDWKKKIVNDGATRNNFFIPCIL
Protein: Interferon-gamma-inducible GTPase 10 (Irgb10) (EC 3.6.5.-) (Q0GUM3)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000269|PubMed:27693356}; Multi-pass membrane protein {ECO:0000269|PubMed:27693356}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23785284}; Multi-pass membrane protein {ECO:0000269|PubMed:27693356}. Note=Recruited to the membrane of pathogens in the cytosol in a GBP (Gbp1, Gbp2, Gbp3, Gbp5 ad/or Gbp7)-dependent manner (PubMed:27693356). Recruited to the membrane of pathogen-containing vacuoles: vacuoles may serve as a cellular transport mechanism to deliver Gm12250/Irgb10 to the pathogen membrane (Probable) (PubMed:23785284, PubMed:27693356). {ECO:0000269|PubMed:27693356, ECO:0000305|PubMed:23785284, ECO:0000305|PubMed:27693356}.
Interaction partners:
Sequence:
MGQSSSKPDAKAHNMASSLTEFFKNFKMESKIISKETIDSIQSCIQEGDIQKVISIINAALTDIEKAPLNIAVTGETGAGKSTFINALRGIGHEESESAESGAVETTKDRKKYTHPKFPNVTIWDLPGVGTTNFKPEEYLKKMKFQEYDFFLIISSARFRDNEAQLAEAIKKMKKKFYFVRTKIDSDLWNEKKAKPSSYNREKILEVIRSDCVKNLQNANAASTRVFLVSSFEVAQFDFPSLESTLLEELPAHKRHIFVQCLPTITEPAIDRRRDVLKQTIWLEALKAGASATIPMMSFFNDDIEEFEKILSHYRACFGLDDESLENMAKEWSMSVEELESTIKSPHLLSSEPNESVADKLVKTMEKIFAVTGGFVATGLYFRKSYYMQNYFLDTVTEDAKVLLKKKVFLQDSVDSE
Protein: Nuclear envelope morphology protein 1 (EC 3.1.3.16) (P38757)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1. Essential for the formation of a spherical nucleus and meiotic division. The NEM1-SPOo7 protein phosphatase is required for efficient mitophagy under prolonged respiration, as well as for reticulophagy and pexophagy.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9822591}; Single-pass membrane protein {ECO:0000269|PubMed:9822591}. Nucleus membrane {ECO:0000269|PubMed:9822591}; Single-pass membrane protein {ECO:0000269|PubMed:9822591}.
Interaction partners:
- Sporulation-specific protein SPO7
- Phosphatidic acid phosphohydrolase 1
- Sporulation-specific protein
- CTP-dependent diacylglycerol kinase 1
- Transcription initiation factor IIF subunit alpha
Sequence:
MNALKYFSNHLITTKKQKKINVEVTKNQDLLGPSKEVSNKYTSHSENDCVSEVDQQYDHSSSHLKESDQNQERKNSVPKKPKALRSILIEKIASILWALLLFLPYYLIIKPLMSLWFVFTFPLSVIERRVKHTDKRNRGSNASENELPVSSSNINDSSEKTNPKNCNLNTIPEAVEDDLNASDEIILQRDNVKGSLLRAQSVKSRPRSYSKSELSLSNHSSSNTVFGTKRMGRFLFPKKLIPKSVLNTQKKKKLVIDLDETLIHSASRSTTHSNSSQGHLVEVKFGLSGIRTLYFIHKRPYCDLFLTKVSKWYDLIIFTASMKEYADPVIDWLESSFPSSFSKRYYRSDCVLRDGVGYIKDLSIVKDSEENGKGSSSSLDDVIIIDNSPVSYAMNVDNAIQVEGWISDPTDTDLLNLLPFLEAMRYSTDVRNILALKHGEKAFNIN
Protein: Intermediate conductance calcium-activated potassium channel protein 4 (SKCa 4) (SKCa4) (hSK4) (Gardos channel) (IKCa1) (hIK1) (KCa3.1) (Putative Gardos channel) (hKCa4) (O15554)
Organism: Homo sapiens (Human)
Function: Forms a voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. Plays a role in the late stages of EGF-induced macropinocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15831468, ECO:0000269|PubMed:24591580, ECO:0000269|PubMed:26148990}; Multi-pass membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:24591580}. Note=Targeted to membrane ruffles after EGF stimulation. {ECO:0000269|PubMed:24591580}.
Interaction partners:
- Calmodulin-1
- Calcium-activated potassium channel subunit alpha-1
- Calcium-activated potassium channel subunit beta-4
- Potassium channel subfamily K member 5 channel 2)
- Potassium channel subfamily U member 1
- Potassium voltage-gated channel subfamily E member 3
- Calcium-activated potassium channel subunit beta-1
- Small conductance calcium-activated potassium channel protein 1
- Potassium voltage-gated channel subfamily KQT member 1
- Calcium-activated potassium channel subunit beta-3
Sequence:
MGGDLVLGLGALRRRKRLLEQEKSLAGWALVLAGTGIGLMVLHAEMLWFGGCSWALYLFLVKCTISISTFLLLCLIVAFHAKEVQLFMTDNGLRDWRVALTGRQAAQIVLELVVCGLHPAPVRGPPCVQDLGAPLTSPQPWPGFLGQGEALLSLAMLLRLYLVPRAVLLRSGVLLNASYRSIGALNQVRFRHWFVAKLYMNTHPGRLLLGLTLGLWLTTAWVLSVAERQAVNATGHLSDTLWLIPITFLTIGYGDVVPGTMWGKIVCLCTGVMGVCCTALLVAVVARKLEFNKAEKHVHNFMMDIQYTKEMKESAARVLQEAWMFYKHTRRKESHAARRHQRKLLAAINAFRQVRLKHRKLREQVNSMVDISKMHMILYDLQQNLSSSHRALEKQIDTLAGKLDALTELLSTALGPRQLPEPSQQSK
Protein: Ceramide synthase 2 (G3V8V4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MLQTLYDYFWWERLWLPVNLTWADLEDKDGRVYAKASDLYITLPLALLFLIIRYFFELYVATPLAALLNVKEKTRLRAPPNATLEHFYLTVGKQPKQVEVDLLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTYYLIAFVAGMAVTVDKPWFYDLRKVWEGYPIQSIIPSQYWYYMIELAFYWSLLFSIASDVKRKDFKEQIIHHVATIILLCFSWFANYVRAGTLIMALHDSSDYLLESAKMFNYAGWKNTCNNLFIVFAVVFIITRLVIMPFWILHCTMIYPLEFYPAFFGYYFFNSMMVVLQMLHVFWAYFIVRMAHKFITGKLVEDERSDREETESSEGEEAAAGAGAKSRLLANGHPILNNNHPKND
Protein: Uncharacterized protein Rv2047c (P9WIH5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Mycoketide-CoA synthase
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Possible oxygenase
- Small ribosomal subunit protein uS14A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein uS8
Sequence:
MRIAVTGASGVLGRGLTARLLSQGHEVVGIARHRPDSWPSSADFIAADIRDATAVESAMTGADVVAHCAWVRGRNDHINIDGTANVLKAMAETGTGRIVFTSSGHQPRVEQMLADCGLEWVAVRCALIFGRNVDNWVQRLFALPVLPAGYADRVVQVVHSDDAQRLLVRALLDTVIDSGPVNLAAPGELTFRRIAAALGRPMVPIGSPVLRRVTSFAELELLHSAPLMDVTLLRDRWGFQPAWNAEECLEDFTLAVRGRIGLGKRTFSLPWRLANIQDLPAVDSPADDGVAPRLAGPEGANGEFDTPIDPRFPTYLATNLSEALPGPFSPSSASVTVRGLRAGGVGIAERLRPSGVIQREIAMRTVAVFAHRLYGAITSAHFMAATVPFAKPATIVSNSGFFGPSMASLPIFGAQRPPSESSRARRWLRTLRNIGVFGVNLVGLSAGSPRDTDAYVADVDRLERLAFDNLATHDDRRLLSLILLARDHVVHGWVLASGSFMLCAAFNVLLRGLCGRDTAPAAGPELVSARSVEAVQRLVAAARRDPVVIRLLAEPGERLDKLAVEAPEFHSAVLAELTLIGHRGPAEVEMAATSYADNPELLVRMVAKTLRAVPAPQPPTPVIPLRAKPVALLAARQLRDREVRRDRMVRAIWVLRALLREYGRRLTEAGVFDTPDDVFYLLVDEIDALPADVSGLVARRRAEQRRLAGIVPPTVFSGSWEPSPSSAAALAAGDTLRGVGVCGGRVRGRVRIVRPETIDDLQPGEILVAEVTDVGYTAAFCYAAAVVTELGGPMSHAAVVAREFGFPCVVDAQGATRFLPPGALVEVDGATGEIHVVELASEDGPALPGSDLSR
Protein: Claudin-8 (P56748)
Organism: Homo sapiens (Human)
Function: Tight-junction protein required for paracellular chloride transport in the kidney. Mediates recruitment of CLDN4 to tight junction in the kidney. Claudins play a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:17287494}. Cell membrane {ECO:0000250|UniProtKB:Q9Z260}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to tight junctions in all 3 segments of the epididymis, in the caput found in the lateral margins of principal cells, and in the corpus at the interface between basal and principal cells. {ECO:0000269|PubMed:17287494}.
Interaction partners:
- Tight junction protein 1
- Tight junction protein ZO-3
- Occludin
- Claudin-12
- Tight junction protein 2
- Claudin-4
- Claudin-10
- Claudin-23
- Claudin-25
- Claudin-7
Sequence:
MATHALEIAGLFLGGVGMVGTVAVTVMPQWRVSAFIENNIVVFENFWEGLWMNCVRQANIRMQCKIYDSLLALSPDLQAARGLMCAASVMSFLAFMMAILGMKCTRCTGDNEKVKAHILLTAGIIFIITGMVVLIPVSWVANAIIRDFYNSIVNVAQKRELGEALYLGWTTALVLIVGGALFCCVFCCNEKSSSYRYSIPSHRTTQKSYHTGKKSPSVYSRSQYV
Protein: Diacylglycerol kinase (DAG kinase) (EC 2.7.1.107) (A1L4Q0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEAERRPAPGSPSEGLFADGHLILWTLCSVLLPVFITFWCSLQRSRRQLHRRDIFRKSKHGWRDTDLFSQPTYCCVCAQHILQGAFCDCCGLRVDEGCLRKADKRFQCKEIMLKNDTKVLDAMPHHWIRGNVPLCSYCMVCKQQCGCQPKLCDYRCIWCQKTVHDECMKNSLKNEKCDFGEFKNLIIPPSYLTSINQMRKDKKTDYEVLASKLGKQWTPLIILANSRSGTNMGEGLLGEFRILLNPVQVFDVTKTPPIKALQLCTLLPYYSARVLVCGGDGTVGWVLDAVDDMKIKGQEKYIPQVAVLPLGTGNDLSNTLGWGTGYAGEIPVAQVLRNVMEADGIKLDRWKVQVTNKGYYNLRKPKEFTMNNYFSVGPDALMALNFHAHREKAPSLFSSRILNKAVYLFYGTKDCLVQECKDLNKKVELELDGERVALPSLEGIIVLNIGYWGGGCRLWEGMGDETYPLARHDDGLLEVVGVYGSFHCAQIQVKLANPFRIGQAHTVRLILKCSMMPMQVDGEPWAQGPCTVTITHKTHAMMLYFSGEQTDDDISSTSDQEDIKATE
Protein: Peroxisomal biogenesis factor 3 (Peroxin-3) (P28795)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in peroxisome biosynthesis. Acts as a regulator of MSP1 by inhibiting the ability of MSP1 to unfold target proteins.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:1894692}; Single-pass membrane protein.
Interaction partners:
- Peroxisomal membrane protein import receptor PEX19
- Peroxisomal membrane protein PEX25
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Inheritance of peroxisomes protein 1
- Peroxisomal membrane protein PMP27
- Peroxisomal membrane protein PEX14
- Proteasome subunit beta type-6
- Peroxisomal membrane protein PEX15
- Peroxisomal targeting signal receptor
Sequence:
MAPNQRSRSLLQRHRGKVLISLTGIAALFTTGSVVVFFVKRWLYKQQLRITEQHFIKEQIKRRFEQTQEDSLYTIYELLPVWRMVLNENDLNLDSIVTQLKDQKNQLTRAKSSESRESSPLKSKAELWNELELKSLIKLVTVTYTVSSLILLTRLQLNILTRNEYLDSAIKLTMQQENCNKLQNRFYNWVTSWWSDPEDKADDAMVMAAKKSKKEGQEVYINEQAFLSLSWWILNKGWLSYNEIITNQIEIEFDGIHPRDTLTLEEFSSRLTNIFRNTNSQIFQQNNNNLTSILLPKDSSGQEFLLSQTLDADALTSFHSNTLVFNQLVNELTQCIESTATSIVLESLINESFHFIMNKVGIKTIAKKKPGQEDQQQYQMAVFAMSMKDCCQEMLQTTAGSSHSGSVNEYLATLDSVQPLDDLSASVYSNFGVSSSFSFKP