wanglab/gogpt-training-data huggingface dataset:
Protein: NADPH-dependent aldehyde reductase 2, chloroplastic (AtChlADR2) (EC 1.1.1.-) (Short-chain type dehydrogenase/reductase) (Q9SQR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes with more than 5 carbons. No activity on alpha,beta-unsaturated ketones. Can use propionaldehyde, butyraldehyde, methylglyoxal, (e)-2-pentenal, (E)-2-hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, but not propenal (acrolein), crotonaldehyde, 2-butanone, 3-buten-2-one or 1-penten-3-one.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21169366}.
Interaction partners:
- EMBRYO DEFECTIVE 3147
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- 3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
- AT4g13180/F17N18_70
- 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
Sequence:
MAAASSVSSPPLCLAGRVAIVTGSSRGIGRAIAIHLAELGARVVVNYSTSPVEAEKVATAITTNCSKDAEVAGKSPRVIVVKADISEPSQVKSLFDEAERVFESPVHILVNSAAIADPNHSTISDMSVELFDRIISVNTRGAFICAREAANRLKRGGGGRIILLSTSLVQTLNTNYGSYTASKAAVEAMAKILAKELKGTEITVNCVSPGPVATEMFYTGLSNEIVEKVKSQNLFGRIGETKDIAPVVGFLASDAGEWINGQVIMANGGCLL
Protein: 4-hydroxyproline 2-epimerase (4Hyp 2-epimerase) (4HypE) (EC 5.1.1.8) (Q8P833)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Function: Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with 500-fold lower efficiency. Displays no proline racemase activity.
Interaction partners:
- D-amino acid oxidase
- Oxidoreductase
- Sarcosine oxidase alpha subunit
- Pyrroline-5-carboxylate reductase
- Dihydrodipicolinate synthetase
- Fe2OG dioxygenase domain-containing protein
- Proline--tRNA ligase
- 2,5-dioxovalerate dehydrogenase
- D-amino acid oxidase
- Transcriptional regulator
Sequence:
MHTIDVIDSHTAGEPTRVVLAGFPDLGDGDLAQCRERFRSDFDHWRSAIACEPRGSDTMVGALLLPPRDPSACTGVIFFNNVGYLGMCGHGTIGVVRTLAELGRIAPGQHRIETPVGTVGVALADDGTVSIDNVESYRHAAGVEVDVPGHGRVRGDVAWGGNWFFITEQAPCALGLAQQRELTAYTEAIRLALEAAGITGEAGGEIDHIEISGVAPDGSGAARNFVLCPGLAYDRSPCGTGTSAKLACLAADGKLAEGERWLQQGILGSAFEGSYRHSGRGIAPRISGHAFITARSQLLIDPADPFAWGIVA
Protein: Transglutaminase 3 (H0VT19)
Organism: Cavia porcellus (Guinea pig)
Interaction partners:
Sequence:
LTALELQNVNWQVAGNRREHHTDQFSTKDIVLRRGQMFHVIMNFNRTLDSEEGLNLTTETGPNPSVSARTKTTFPVSRGRNTGGSWAAEVRENNGNALTVAISSPASAPIGWYTMSLQISSKGRVSSVKLGTFVLLFNPWSLTTYTPTDDVFMSNQAERQEYVEEDSGNIFVGSINRIGMVGWNFGQYEEDILNISLSILDKSLNFRRDPITDVARRNDPKYVGRVLSAMINSNDDNGVIAGNWSGSYTGGMDPRTWNGSVEILKEWKKSGFRPVRFGQCWVFAGTLNTVLRCLGIPSRVITNFNSAHDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEAWFVRPDLGPSYNGWQVLDATPQERSQGVFQCGPASVIAVREGDVDLNFDMPFIYAEVNADRITWIYTASNDSKKQNYVDTRSVGRYISTKAVGSRSRMDVTDKYKYPEGSNEERRVQQKALSKLKPDASFGPTSAQRSPGREQAPSISGRFKVNGVLAVGQEVNLALLLKNLTRDRKTVAVNMTAWTIVYNGTLVHEVWKDSVTISLDPEEEVQHPVKITYAQYEKYLKADNMIRTTAICKVSDEVEVVVERDVILDNPTLTLEVLDRAQVRKPVNVQMLFSNPLDEPVKDCVLMVEGSGLLRGNLKIEVPALRPKERSRIRFEILPTRSGTKQLVADFSCNKFPAIKAMLSIDVNE
Protein: Hydroxyacylglutathione hydrolase, cytoplasmic isozyme (EC 3.1.2.6) (Glyoxalase II) (Glx II) (Q05584)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9261170}.
Interaction partners:
- Glyoxalase I
- Hydroxyacylglutathione hydrolase, mitochondrial
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3
- Glutathione-independent glyoxalase HSP31
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
- Probable glutathione-independent glyoxalase HSP32
- Probable glutathione-independent glyoxalase HSP33
- Probable glutathione-independent glyoxalase SNO4
Sequence:
MQVKSIKMRWESGGVNYCYLLSDSKNKKSWLIDPAEPPEVLPELTEDEKISVEAIVNTHHHYDHADGNADILKYLKEKNPTSKVEVIGGSKDCPKVTIIPENLKKLHLGDLEITCIRTPCHTRDSICYYVKDPTTDERCIFTGDTLFTAGCGRFFEGTGEEMDIALNNSILETVGRQNWSKTRVYPGHEYTSDNVKFVRKIYPQVGENKALDELEQFCSKHEVTAGRFTLKDEVEFNPFMRLEDPKVQKAAGDTNNSWDRAQIMDKLRAMKNRM
Protein: T3SS structure protein EscF (B7UM90)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Subcellular location: Cell surface {ECO:0000256|ARBA:ARBA00004241}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MNLSEITQQMGEVGKTLSDSVPELLNSTDLVNDPEKMLELQFAVQQYSAYVNVESGMLKTIKDLVSTISNRSF
Protein: Lipopolysaccharide-induced tumor necrosis factor-alpha factor homolog (LPS-induced TNF-alpha factor homolog) (Estrogen-enhanced transcript protein) (mEET) (LITAF-like protein) (NEDD4 WW domain-binding protein 3) (Q9JLJ0)
Organism: Mus musculus (Mouse)
Function: Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation. Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps down-regulate downstream signaling cascades. Helps recruit the ESCRT complex components TSG101, HGS and STAM to cytoplasmic membranes. Probably plays a role in regulating protein degradation via its interaction with NEDD4 (By similarity). May also contribute to the regulation of gene expression in the nucleus. Binds DNA (in vitro) and may play a synergistic role with STAT6 in the nucleus in regulating the expression of various cytokines. May regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99732}. Nucleus {ECO:0000250|UniProtKB:Q99732}. Lysosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Early endosome membrane {ECO:0000250|UniProtKB:Q99732}. Late endosome membrane {ECO:0000250|UniProtKB:Q99732}. Endosome membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Cell membrane {ECO:0000250|UniProtKB:Q99732}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99732}; Cytoplasmic side {ECO:0000250|UniProtKB:Q99732}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99732}. Note=Associated with membranes of lysosomes, early and late endosomes. Can translocate from the cytoplasm into the nucleus (By similarity). Detected at Schmidt-Lanterman incisures and in nodal regions of myelinating Schwann cells (PubMed:22729949). {ECO:0000250|UniProtKB:Q99732, ECO:0000269|PubMed:22729949}.
Interaction partners:
- E3 ubiquitin-protein ligase NEDD4
Sequence:
MSAPGPYQAAAGPSVVPTAPPTYEETVGVNSYYPTPPAPMPGPATGLITGPDGKGMNPPSYYTQPVPVPNANAIAVQTVYVQQPVSFYDRPVQMCCPSCSKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCCFIPFCVDALQDVDHYCPNCKALLGTYKRL
Protein: Uncharacterized protein C323.03c (Q9UT96)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Note=Localizes also at the barrier septum.
Interaction partners:
- Uncharacterized protein C2C4.10c
Sequence:
MEEAINNVLLLLREDSISLETVLWETHYVLLNLHNEQNLRLVVAQLIACGRIWDYWNEHRSEYFAFWVELISRKKVTNNGLPFSSFVKSIVGILEVDASNEILCFRRICLLCVFYKLLSCDHIVNLQYPLKRAVSKALSKQIKTHQFSGFEANFLLQQLFASVDSSASDISFDAFSLLPHLLKWEEIVWSGFINYLDTEHKRDSLPTAVLCHLLLRLSTYQQISIIKRLITLIDKAIPSWKSRSSDSKYNDHQFVKKNFFSIIMVLESLAKSQYRKSNVLAADRSLCEYIILTLFHMEYLFSFVASSWSTLDFVITTCLSRVAQPAKFISETVREAIIDSIQLEGYVDLQKLSGSPVLVTLSFINNWQNLICRRLEKQTVNEKVITLSSTAKEISSLGLSFAEKLISQSDESTLCKHYVYASLYACLFCNLNEGSPKDYLDNDIYVHARCLFLLTKTLNLDSLKSILCSRVRLYYNIEIAYYFTDVLLKWFQPIIRYEFDNALIFYKASISLVSVLAPAAQKQFLSNYLNSIQGFSTETKEDLIFLVSSQIRQMPYQNATSLLSFWLSIVVGRAV
Protein: Tat proofreading chaperone DmsD (DMSO reductase maturation protein) (Twin-arginine leader-binding protein DmsD) (P69853)
Organism: Escherichia coli (strain K12)
Function: Required for biogenesis/assembly of DMSO reductase, but not for the interaction of the DmsA signal peptide with the Tat system. May be part of a chaperone cascade complex that facilitates a folding-maturation pathway for the substrate protein.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12813051}; Peripheral membrane protein {ECO:0000269|PubMed:12813051}. Cytoplasm {ECO:0000269|PubMed:12813051}. Note=Mainly cytoplasmic under aerobic conditions, and found in the inner membrane under anaerobic conditions.
Interaction partners:
- Dimethyl sulfoxide reductase DmsA
- Probable dimethyl sulfoxide reductase chain YnfF
- Putative dimethyl sulfoxide reductase chain YnfE
- Anaerobic dimethyl sulfoxide reductase chain YnfH
- Probable anaerobic dimethyl sulfoxide reductase chain YnfG
- Anaerobic dimethyl sulfoxide reductase chain C
- Trimethylamine-N-oxide reductase 1
- Chaperone protein TorD
- Anaerobic dimethyl sulfoxide reductase chain B
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
Sequence:
MTHFSQQDNFSVAARVLGALFYYAPESAEAAPLVAVLTSDGWETQWPLPEASLAPLVTAFQTQCEETHAQAWQRLFVGPWALPSPPWGSVWLDRESVLFGDSTLALRQWMREKGIQFEMKQNEPEDHFGSLLLMAAWLAENGRQTECEELLAWHLFPWSTRFLDVFIEKAEHPFYRALGELARLTLAQWQSQLLIPVAVKPLFR
Protein: Protein kreg-1 (Q20689)
Organism: Caenorhabditis elegans
Function: Plays a role in the stress response to heavy metals such as copper, probably in a fos-1/kgb-1-dependent manner.
Interaction partners:
- Lysozyme-like protein 3
Sequence:
MSYYGNGGYNPYGAYGNVPPPVYGTPGLAPPTVHVHTDGGHHHGHHHHHHSFLHELGHALTGHHHHHHGHHFGHHHHHHHGHH
Protein: Folr1 protein (A9UMV5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAHLMAGQWLLLLMWMAECAQSRATRARTELLNVCMDAKHHKEKPGPEDKLHDQCSPWKTNACCSTNTSQEAHKDISYLYRFNWNHCGTMTPECKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERILDVPLCKEDCVLWWEDCKSSFTCKSNWHKGWNWTSGHNECPVGASCHPFTFYFPTPAVLCEKIWSHSYKLSNYSRG
Protein: SHSP domain-containing protein (O01263)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHTIPITTDSAASWDWPLQHNDGVVKVTNTSEKFEVGLDAGFFGPNDIDVKVNGIEIIIHLRHDNRPTEYGIVNREVHRTYKLPEDVDPSTVRSHLNSSGVLTITANKL
Protein: Putative RNA-binding protein Luc7-like 1 (Putative SR protein LUC7B1) (SR+89) (Q9NQ29)
Organism: Homo sapiens (Human)
Function: May bind to RNA via its Arg/Ser-rich domain.
Interaction partners:
- RNA-binding protein 25
- U1 small nuclear ribonucleoprotein 70 kDa
- U1 small nuclear ribonucleoprotein C
- Pre-mRNA-processing factor 40 homolog A
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D2
- Splicing factor 3B subunit 3
- Small nuclear ribonucleoprotein Sm D3
- Putative RNA-binding protein Luc7-like 2
- U1 small nuclear ribonucleoprotein A
Sequence:
MSAQAQMRALLDQLMGTARDGDETRQRVKFTDDRVCKSHLLDCCPHDILAGTRMDLGECTKIHDLALRADYEIASKERDLFFELDAMDHLESFIAECDRRTELAKKRLAETQEEISAEVSAKAEKVHELNEEIGKLLAKAEQLGAEGNVDESQKILMEVEKVRAKKKEAEEEYRNSMPASSFQQQKLRVCEVCSAYLGLHDNDRRLADHFGGKLHLGFIQIREKLDQLRKTVAEKQEKRNQDRLRRREEREREERLSRRSGSRTRDRRRSRSRDRRRRRSRSTSRERRKLSRSRSRDRHRRHRSRSRSHSRGHRRASRDRSAKYKFSRERASREESWESGRSERGPPDWRLESSNGKMASRRSEEKEAGEI
Protein: Aspartokinase 1, chloroplastic (EC 2.7.2.4) (Aspartate kinase 1) (Q9LYU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- aspartate-semialdehyde dehydrogenase
- Homoserine dehydrogenase
- Homoserine kinase
- Argininosuccinate synthase, chloroplastic
- Diaminopimelate epimerase, chloroplastic
- Asparagine synthetase 1
- 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- Asparagine synthetase 2
Sequence:
MAATRVRCCHSNAAFTRLPLTRHRNSPTLPISLNRVDFPTLKKLSLPIGDGSSIRKVSGSGSRNIVRAVLEEKKTEAITEVDEKGITCVMKFGGSSVASAERMKEVADLILTFPEESPVIVLSAMGKTTNNLLLAGEKAVSCGVSNASEIEELSIIKELHIRTVKELNIDPSVILTYLEELEQLLKGIAMMKELTLRTRDYLVSFGECLSTRIFAAYLNTIGVKARQYDAFEIGFITTDDFTNGDILEATYPAVAKRLYDDWMHDPAVPIVTGFLGKGWKTGAVTTLGRGGSDLTATTIGKALGLKEIQVWKDVDGVLTCDPTIYKRATPVPYLTFDEAAELAYFGAQVLHPQSMRPAREGEIPVRVKNSYNPKAPGTIITKTRDMTKSILTSIVLKRNVTMLDIASTRMLGQVGFLAKVFSIFEELGISVDVVATSEVSISLTLDPSKLWSRELIQQELDHVVEELEKIAVVNLLKGRAIISLIGNVQHSSLILERAFHVLYTKGVNVQMISQGASKVNISFIVNEAEAEGCVQALHKSFFESGDLSELLIQPRLGNGSPVRTLQVEN
Protein: Akirin-2 (XAkirin2) (Q6GQB5)
Organism: Xenopus laevis (African clawed frog)
Function: Molecular adapter that acts as a bridge between a variety of multiprotein complexes, and which is involved in embryonic development, immunity, myogenesis and brain development. Plays a key role in nuclear protein degradation by promoting import of proteasomes into the nucleus: acts by bridging fully assembled 20S proteasomes with nuclear import receptor ipo9 (By similarity). Involved in both neural precursor maintenance and terminal neural differentiation: bridges gmnn and actl6a/baf53a in neural progenitor cells, antagonizing the activity of gmnn, thereby suppressing sox2 expression. Also required for proper activation of neurod1 and neuronal differentiation. Involved in myogenesis: required for skeletal muscle formation and skeletal development, possibly by regulating expression of muscle differentiation factors (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:B1AXD8}.
Interaction partners:
Sequence:
MACGATLKRTIEFDPLLSPAASPKRRRCAPLSPSGPSPQKYLRLEPSPFGEVSPRLTAEQILYNIKQEYKRMQKRRHLESSFQPTDPCCSSEGQPQTFIPSGPTLPGTSATSPLRKEQPLFSLRQVGMICERLLKEREDNVREEYEEILTTKLAEQYDAFVKFTHDQIMRRFGEQPASYVS
Protein: Elongation of very long chain fatty acids protein (EC 2.3.1.199) (Very-long-chain 3-oxoacyl-CoA synthase) (Q5JZZ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Very long chain fatty acid elongase F
- Elongation of very long chain fatty acids protein
- very-long-chain enoyl-CoA reductase
- Elongation of very long chain fatty acids protein
- Very-long-chain
- Very-long-chain
- RH59310p)
- Elongation of very long chain fatty acids protein
Sequence:
MASLGISFHPFPDQPDERTRNWPLVDSFWTVPVLLSIYLLMVRYAPKWTTRHKPLQLRAPLFCHSLAMVFLNGYICLELYAATRDLDYNFGCQPCRVSFDPHEMRLTKAFWWFYISKILEFADTAFFILRQKWSQLSFLHVYHHSTMFVFCWILIKWMPTGSTYVPAMINSFVHIIMYGYYALSVLGPRVQRFLWWKRYLTGLQLVQFTIIFFWASQMLVRGCEYGTWITLSMAIYSLPFLFMFGKFYMQKYTVSAVGKKPI
Protein: Runt-related transcription factor (Q8UVG3)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009374}.
Interaction partners:
- Transcription factor SOX-9
- Core-binding factor subunit beta
- Bone morphogenetic protein 2
- Osteopontin
- Collagen alpha-1
- Indian hedgehog protein
- Collagen alpha-1
- Aggrecan core protein
- ZnMc domain-containing protein.
- Collagen alpha-1
Sequence:
MASNSLFSSVTPCQQNFFWDPSTSRRFSPPSSSLQPGKMSEVSPVVVAQQQQQQQQQQQQEAAVPRLRPHDNRTMVEIIADHPAELVRTDSPNFLCSVLPSHWRCNKTLPVAFKVVALGEVPDGTVVTVMAGNDENYSAELRNASAVMKNQVARFNDLRFVGRSGRGKSFTLTITVLTNPPQVATYHRAIKVTVDGPREPRRHRQKLDDSKPSLFPERLSDLGRIPHPSMRVGVPTQSPRPSLNSAPSPFNPQGQSQITDPRQAQSSPPWSYDQSYPSYLSQMTSPSIHSTTPLSSTRGTGLPAITDVPRRLSGASELGPFSDPRQFTSISSLTESRFSNPRMHYPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQNQSGPFQTSSTPYLYYGTSSGSYQFPMVPGGDRSPSRMLPPCTTTSNGSTLLNPNLPNQSDGVEADGSHSSSPTVLNSSGRMDESVWRPY
Protein: WAP-type 'four-disulfide core (G5EDX1)
Organism: Caenorhabditis elegans
Interaction partners:
- Sulfotransferase domain-containing protein
- Probable syndecan
- Sulfotransferase domain-containing protein
- Neuroglian
- Chromodomain and Helicase Domain protein
- GlyPicaN
- Heparan-sulfate 6-O-sulfotransferase
Sequence:
MILLLLLFILGSVSPDELISTRCQAQCLHLMDQRLQNNMELRKTLKHHIIQLCKEDATCSACSAPCREQFDDIKACKKSCVASDDRETCEDSCHYLQRIYQEKPGACPSVSNQSNYECSALCQMDGECPETQKCCSSGCSRQCLKPRSSDIKLLPIPRNISVQERKRKRSIIIRWATGRLSKAQQNENANLFLVQWRWGLHADESAMTEWQTVTVRNKPYAILKHLLSPGRFYEFRTAAVSQEGSLGFSSPSKPFKISKEAKAPPPPKDLSLGASKVVASGLWNQMVHWNPPPSDLPIKNYQISWASSTKSEADAFEEQMRKKSTLEFAAHEKRSLQSDDDEEFIGIQERDRQSVVVPSHATSSEITGLFPNSVYLVEIHASVDSSDGELHGEKGVVFIRTADSLSAVPEDREPYTGPKARIAHGSEELKIEASLKDLKTSSHAPNRPNSPQPAHLEIQTPFFDTELQTQLNWLNAAHCTPAKRQFSVKVRKTLCREYQPNHHSDTRWHDLRVTDCSALLKGLSFDCDYKVEVTDTLTGDFVVDGVFSTDTCDQTSSLTPIDCSSVTTPIQCQVTSESSAHCHWTRHHDAMQTVIGYRILLSSPINHDTNTTINQPQLREVRYENLAPGYVYTVEVQSITNKGLGRTVSTQFVTHPDLDSNAIQRFPGGEIIELPLESSGKLSIFSIFSSFFLVLLLRLL
Protein: EF-hand calcium-binding domain-containing protein 4A (Calcium release-activated calcium channel regulator 2B) (CRAC channel regulator 2B) (Calcium release-activated channel regulator 2B) (Q8N4Y2)
Organism: Homo sapiens (Human)
Function: Plays a role in store-operated Ca(2+) entry (SOCE).
Interaction partners:
Sequence:
MASPGKPGADEAQEEEGELEGGSAGPRAAILEQAEELFLLCDKEAKGFITKHDLQGLQSDLPLTPEQLEAVFESLDRAHTGFLTAREFCLGLGMFVGVASAQGANPCRTPEETFESGGLDVQGTAGSLDEEEEEEERFHTVLEQLGVAPVLGKQRAVRTLWARLQRERPELLGSFEDVLIRASACLEEAARERDGLEQALRRRESEHEREVRALYEETEQLREQSRRPPSQNFARGERRSRLELELQSREQDLERAGLRQRELEQQLHAQAAEHLEAQAQNSQLWRAHEALRTQLEGAQEQIRRLESEARGRQEQTQRDVVAVSRNMQKEKVSLLRQLELLRELNTRLRDDRDACEARRAGSSCRKALTTARLPGPTCCCCCCWARPPRRGSGHLPSAR
Protein: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 4 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 4) (HACD4) (Protein-tyrosine phosphatase-like A domain-containing protein 2) (Q5VWC8)
Organism: Homo sapiens (Human)
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18554506}; Multi-pass membrane protein {ECO:0000269|PubMed:18554506}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 4
- Very-long-chain
- Very long chain fatty acid elongase 2
- Very-long-chain
- Very long chain fatty acid elongase 6
- Stearoyl-CoA desaturase 5
- Stearoyl-CoA desaturase
- Very-long-chain
Sequence:
MGPLALPAWLQPRYRKNAYLFIYYLIQFCGHSWIFTNMTVRFFSFGKDSMVDTFYAIGLVMRLCQSVSLLELLHIYVGIESNHLLPRFLQLTERIIILFVVITSQEEVQEKYVVCVLFVFWNLLDMVRYTYSMLSVIGISYAVLTWLSQTLWMPIYPLCVLAEAFAIYQSLPYFESFGTYSTKLPFDLSIYFPYVLKIYLMMLFIGMYFTYSHLYSERRDILGIFPIKKKKM
Protein: Ral guanine nucleotide dissociation stimulator (RalGDS) (Ral guanine nucleotide exchange factor) (RalGEF) (Q12967)
Organism: Homo sapiens (Human)
Function: Functions as a guanine nucleotide exchange factor (GEF) activating either RalA or RalB GTPases and plays an important role in intracellular transport. Interacts and acts as an effector molecule for R-Ras, H-Ras, K-Ras, and Rap (By similarity). During bacterial clearance, recognizes 'Lys-33'-linked polyubiquitinated TRAF3 and subsequently mediates assembly of the exocyst complex.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q03385}. Nucleus {ECO:0000250|UniProtKB:Q03385}. Note=Localizes mainly in the peripheral region of the cytoplasmic membrane in oocytes and in preimplantation embryos until the 8-cell stage. Between the late 1-cell and the early 2-cell stages, nuclear localization becomes stronger. After the 4-cell stage, not detected in the nucleus. {ECO:0000250|UniProtKB:Q03385}.
Interaction partners:
- GTPase KRas
- Ras-related protein Ral-A
- Ras-related protein R-Ras
- Ras-related protein Rap-1A
- GTPase HRas
- Ras-related protein Ral-B
- Alpha-2-macroglobulin receptor-associated protein
- GTPase NRas
- Ras-related protein Rap-1b
- Ras-related protein M-Ras
Sequence:
MVQRMWAEAAGPAGGAEPLFPGSRRSRSVWDAVRLEVGVPDSCPVVLHSFTQLDPDLPRPESSTQEIGEELINGVIYSISLRKVQLHHGGNKGQRWLGYENESALNLYETCKVRTVKAGTLEKLVEHLVPAFQGSDLSYVTIFLCTYRAFTTTQQVLDLLFKRYGRCDALTASSRYGCILPYSDEDGGPQDQLKNAISSILGTWLDQYSEDFCQPPDFPCLKQLVAYVQLNMPGSDLERRAHLLLAQLEHSEPIEAEPEALSPVPALKPTPELELALTPARAPSPVPAPAPEPEPAPTPAPGSELEVAPAPAPELQQAPEPAVGLESAPAPALELEPAPEQDPAPSQTLELEPAPAPVPSLQPSWPSPVVAENGLSEEKPHLLVFPPDLVAEQFTLMDAELFKKVVPYHCLGSIWSQRDKKGKEHLAPTIRATVTQFNSVANCVITTCLGNRSTKAPDRARVVEHWIEVARECRILKNFSSLYAILSALQSNSIHRLKKTWEDVSRDSFRIFQKLSEIFSDENNYSLSRELLIKEGTSKFATLEMNPKRAQKRPKETGIIQGTVPYLGTFLTDLVMLDTAMKDYLYGRLINFEKRRKEFEVIAQIKLLQSACNNYSIAPDEQFGAWFRAVERLSETESYNLSCELEPPSESASNTLRTKKNTAIVKRWSDRQAPSTELSTSGSSHSKSCDQLRCGPYLSSGDIADALSVHSAGSSSSDVEEINISFVPESPDGQEKKFWESASQSSPETSGISSASSSTSSSSASTTPVAATRTHKRSVSGLCNSSSALPLYNQQVGDCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYELLQILSDDRKLKIPENANVFYAMNSTANYDFVLKKRTFTKGVKVKHGASSTLPRMKQKGLKIAKGIF
Protein: H(+)-exporting diphosphatase (EC 7.1.3.1) (Q8MTZ4)
Organism: Trypanosoma brucei
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MIKMSPLLLKAAVVTACLCSLAVATTVEEQTAPKPIENATTYQQELGGRGKVDSPTAPGDAVSITSGIKVMSVTTATAIIFLASAFGFSFAMYWWYVASDIKITPGKGNIMRNAHLTDEVMRNVYVISKRVSDGANAFLFAEYRYMGIFMLGFGALLYFLLGVAMSSPQGEGKDGRPPVAVEAPWVNAAFSLYAFVIGAFTSVLAGWIGMRIAVYTNSRTAVMATVGSGGSDNDVLANGSQSRGYALAFQTAFRGGITMGFALTSIGLFALFCTVKLMQTYFGDSAERLPELFECVAAFGLGGSSVACFGRVGGGIYTKAADVGADLVGKVEKNIPEDDARNPGVIADCIGDNVGDIAGMGSDLFGSFGEATCAALVIAASSAELSADFTCMMYPLLITAGGIFVCIGTALLAATNSGVKWAEDIEPTLKHQLLVSTIGATVVLVFITAYSLPDAFTVGAVETTKWRAMVCVLCGLWSGLLIGYSTEYFTSNSYRPVQEIAESCETGAATNIIYGLSLGYISVLPPILAMAFTIYLSHHCAGLYGYALAALGILSTMSIALTIDAYGPISDNAGGIAEMAHMGHEIREITDALDAAGNTTAAIGKGFAIGSAAFVALALYGAYVSRVGISTVNLLDARVMAGLLLGAMLPYWFSALTMKSVGVAAMDMVNEIRRQFQDPAVAAGTKEPDYESCVNIATGAALQQMVAPACLVMLAPIVTGILFGRYTLAGLLPGALVSGVQVAISASNTGGAWDNAKKYIEKGGLRDKSKGKGSPQHAAAVIGDTVGDPLKDTSGPALNILVKLMAIISVVFAPVVQSKLGGLLVK
Protein: Piercer of microtubule wall 2 protein (V9GXK1)
Organism: Mus musculus (Mouse)
Function: Microtubule inner protein involved in the attachment of outer dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A0A3Q1LFK7}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994}.
Interaction partners:
- Piercer of microtubule wall 1 protein
- Outer dynein arm-docking complex subunit 1
- Cilia- and flagella-associated protein 53
- WD repeat-containing protein 90
- EF-hand domain-containing family member C2
- Calaxin
- Outer dynein arm-docking complex subunit 3
- Outer dynein arm-docking complex subunit 4
- EF-hand calcium-binding domain-containing protein 6
Sequence:
MARETDCDLDKKTSLTSDAEMRPEPPALCVNPGNPVFSCMLDPKTLHTATSLSKAQMIMYKTSASQYGAFSPRPFFFPCKFLPQEQAFTEHLKTTGFYQNNSLNVGPDRTRTIDSPNYQHTL
Protein: B1 bradykinin receptor (Bradykinin receptor B1) (A8E7T8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Kininogen 1.
- Si:dkey-63b1.1
- Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein
Sequence:
MQPEEFTSSVTLHPPNASVTPAYLDFFNSTEWRLVFSIIPPYIFIVCLMGILGNSFVLLVFLLQRGRWSVPEIYLGNLALADLILLVCLPFWAMNILNYFMWLYGEFMCKVVNMSIMVNMYTSIYMLVMVNVDRYLALVLTMRARWLRRKRYAKLICVILWLFGLGMGAPTAAMRKLIDIPAHQSVECMLNYPNGNWRIAHLLQLNIVGFALPFLVITFCCFNIVRALKRRRDSGYWEDGNDRKATILVCAVTFLFFFCWGPFHFLTFLDLLCDLKVLDEKEWAHFLNIGNQFSVYLAFSNSCLNPVLYVCSGNYFRRKVSSIYKRRKQSSDATTLQRTALTSTTTTNQIKPVVLNEKD