wanglab/gogpt-training-data huggingface dataset:
Protein: Protein S100-B (S-100 protein beta chain) (S-100 protein subunit beta) (S100 calcium-binding protein B) (P04631)
Organism: Rattus norvegicus (Rat)
Function: Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04271}. Nucleus {ECO:0000250|UniProtKB:P04271}. Secreted {ECO:0000250|UniProtKB:P50114}. Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. {ECO:0000250|UniProtKB:P50114}.
Interaction partners:
- F-actin-capping protein subunit alpha-1
- F-actin-capping protein subunit alpha-2
- Advanced glycosylation end product-specific receptor
- Fibroblast growth factor 2
- Glial fibrillary acidic protein
- Cellular tumor antigen p53
- Gamma-enolase
- Ribosomal protein S6 kinase alpha-1
- High mobility group protein B1
- 45 kDa calcium-binding protein
Sequence:
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDEDGDGECDFQEFMAFVSMVTTACHEFFEHE
Protein: Predicted S. cerevisiae Got1 homologue (Q389A1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}.
Interaction partners:
- Orotidine 5'-phosphate decarboxylase
- Dihydroorotate dehydrogenase
- Transmembrane protein
- Dihydroorotase, putative
- Carbamoyl phosphate synthase arginine-specific large chain
- aspartate carbamoyltransferase
Sequence:
MDSLYSWNDSTKIGIALTSLGVFFNFIGIVMFLDSVLLTMGNVLFVAGIALVMGPSRFKSFFLFRRRASCCFFIGMLLIMLGRSLIGLMIQGFGTLNLFGNFFPMVARVLESVPLLGPVMLSPPVQKLLSLLGLQARGNRNV
Protein: Mitochondrial thiamine diphosphate carrier 1 (B4FIJ0)
Organism: Zea mays (Maize)
Function: Mitochondrial transporter that mediates uptake of thiamine diphosphate (ThDP) into mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:22426856}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSGEEPSQMRRALVDSLAGAISGGISRTVTSPLDVIKIRFQVQLEPTTSWGILRRDVYGPSKYTGLLQATKDILREEGLPGFWRGNVPALFMYMPYTAIQFTVLHKLKTFASGSSRTEDHLDLSPYLSYVSGAIAGCTATIGSYPFDLLRTILASQGEPKVYPNMRSAFIDIIKTRGVQGLYSGLSPTLVEIIPYAGLQFGSYDTFKRSMMTWNRYKYSHLSFGSEDDSVSSFQLFLCGFAAGTFSKAACHPLDVVKKRFQIEGLKRHPRYGAPIESSTYKGMYHALKEIVVKEGFGGLYKGLFPSLVKSAPAGAVTFVVYEYISDWIGCKAGVE
Protein: Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC 2.7.11.10) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (A0A8I5ZSH4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKKLNHANVVKACDVPEELNFLINDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIMHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMTGEVRFSSHLPQPNNLCSLIVEPMESWLQLMLNWDPQQRGGPIDPPLKQPKCFVLMDNILNLKIVHILNMTSAKIISFLLPYDESLHSLQSRIERETGINTGSQELLSETGISLDPRKPASQCVLDGVRGCDSYMVYLFDKSKTVYEGPFASRSLSDCVNYIVQDSKIQLPVTQLRKVWAEAVHYVSGLKEDYSRLFQGQRAAMLSLLRYNANLTKMKNTLISASQQLKAKLEFFRKSIQLDLERYSEQMTYGISSEKMLKAWKEMEEKAIHYSEVGVIGYLEDQIMSLHTEIMELQKSPYGRRQGDLMESLEQRAIDLYKQLKHRPTDHSYSDSTEMVKIIVHTVQSQDRVLKELFGHLSKLLGCKQKIIDLLPKVEVALSNIKEADNTVMFMQGKRQKEIWHLLKIACTQSSARSLVGSSLEGTVTPPVSAWLPPTLADREHPLTCVVTPQDGWVCFVTIGSCASGERVGQRQQAWWLMNSVFRLGLRLGRSLLFNSTE
Protein: Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 1) (Ketol-acid reductoisomerase type I) (P9WKJ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. It is also able to use 3-hydroxypyruvate (HP).
Interaction partners:
- Putative acetolactate synthase small subunit
- Acetolactate synthase large subunit IlvB1
- Dihydroxy-acid dehydratase
- Acetolactate synthase large subunit IlvG
- Putative acetolactate synthase large subunit IlvB2
- Putative acetolactate synthase large subunit IlvX
- 3-isopropylmalate dehydrogenase
- 3-isopropylmalate dehydratase small subunit
- 3-isopropylmalate dehydratase large subunit
- 2-isopropylmalate synthase
Sequence:
MALEMFYDDDADLSIIQGRKVGVIGYGSQGHAHSLSLRDSGVQVRVGLKQGSRSRPKVEEQGLDVDTPAEVAKWADVVMVLAPDTAQAEIFAGDIEPNLKPGDALFFGHGLNVHFGLIKPPADVAVAMVAPKGPGHLVRRQFVDGKGVPCLVAVEQDPRGDGLALALSYAKAIGGTRAGVIKTTFKDETETDLFGEQTVLCGGTEELVKAGFEVMVEAGYPAELAYFEVLHELKLIVDLMYEGGLARMYYSVSDTAEFGGYLSGPRVIDAGTKERMRDILREIQDGSFVHKLVADVEGGNKQLEELRRQNAEHPIEVVGKKLRDLMSWVDRPITETA
Protein: Peptidyl-prolyl cis-trans isomerase sig-7 (EC 5.2.1.8) (Cyclophilin-like protein sig-7) (Silencer in germline 7) (G5EEW6)
Organism: Caenorhabditis elegans
Function: Probable PPIase that accelerates the folding of proteins (By similarity). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Involved in RNA polymerase II (RNA pol II)-mediated transcription elongation, and in primary transcript splicing, including co-transcriptional trans-splicing, in association with the catalytic subunit of the RNA pol II complex ama-1. Also plays a role in the regulation of elongation-dependent phosphorylation of ama-1 to control transcription. Involved in the transcription of several genes during embryogenesis and in particular, of genes related to developmental processes such as gastrulation, and also regulates transcription in germ cells from embryogenesis to adulthood.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:27541139}. Chromosome {ECO:0000269|PubMed:27541139}. Note=Co-localizes with transcriptionally active chromatin in all autosomes of mitotic and meiotic nuclei in germ cells. In transcriptionally inactive diakinetic oocytes, diffusely localized in the nucleoplasm. {ECO:0000269|PubMed:27541139}.
Interaction partners:
- peptidylprolyl isomerase
- Pre-mRNA-splicing factor syf-2
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing factor 17
- Peptidyl-prolyl cis-trans isomerase
- Peptidyl-prolyl cis-trans isomerase 10
- Pre-mRNA-splicing factor CWC25 homolog
- Nuclear speckle splicing regulatory protein 1 homolog
- Very Early Transcript
- SKN-1 Dependent Zygotic transcript
Sequence:
MAVLIETTLGDLIIDLFVKERPRCSLNFLKLCKKKYYNLNQFHSIERNYVAQTGDPTGTGKGGESVYSDMYGEQGRYFEREDLPKMRHTRMGIVSFVNNGDNMLGSQFFITLGENLDYLDDQHTIFGQVTEGLETLEKLNEQLADTNNRPFKDIRISHTIVLDDPFDEDARISFPPRSPSPTYEMLVKTDQIALDEKEDEDEGKTAEEIAEELQQREMAEQAQILEMVGDLKDADEVPPENVLFVCKLNPVTTDEDLEIIFSRFGKINNCEIVRDRRSGDSLQYAFIEFDNAKSCEQAFFKMDNVLIDDRRIHVDFSQSVSQNYKYKPKSQQQEAPKRRQSPQRRPEVKRSHQRSPSPRRRRSPSPKKDKKRDYRREPARRRRSSDNHRDRDRSYRDNNRDRRDNHRDSDRDRRRHDRSPDRRRDRR
Protein: Transcription initiation factor TFIID subunit 12 (Transcription initiation factor TFIID 20/15 kDa subunits) (TAFII-20/TAFII-15) (TAFII20/TAFII15) (Q16514)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Component of the TATA-binding protein-free TAF complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
Interaction partners:
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 11
- Transcriptional adapter 3
- TATA-box-binding protein
- Transcriptional adapter 1
- Transcription initiation factor TFIID subunit 4
- Transcription initiation protein SPT3 homolog
- Ataxin-7
Sequence:
MNQFGPSALINLSNFSSIKPEPASTPPQGSMANSTAVVKIPGTPGAGGRLSPENNQVLTKKKLQDLVREVDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWIPGFGSEEIRPYKKACTTEAHKQRMALIRKTTKK
Protein: Peroxisomal membrane protein 11B (Peroxin-11B) (Peroxisomal biogenesis factor 11B) (Protein PEX11 homolog beta) (PEX11-beta) (O96011)
Organism: Homo sapiens (Human)
Function: Involved in peroxisomal proliferation. May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane. Promotes membrane protrusion and elongation on the peroxisomal surface.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}; Single-pass membrane protein {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:9792670, ECO:0000269|PubMed:9826565}.
Interaction partners:
- Peroxisomal membrane protein 11C
- Peroxisomal biogenesis factor 19
- Peroxisome biogenesis factor 2
- Mitochondrial fission 1 protein
- Peroxisomal membrane protein PEX16
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Peroxisomal targeting signal 1 receptor
- Peroxisomal membrane protein PEX14
Sequence:
MDAWVRFSAQSQARERLCRAAQYACSLLGHALQRHGASPELQKQIRQLESHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQESSACSRRLKGSGGGVPGGSETGGLGGPGTPGGGLPQLALKLRLQVLLLARVLRGHPPLLLDVVRNACDLFIPLDKLGLWRCGPGIVGLCGLVSSILSILTLIYPWLRLKP
Protein: Ubiquitin-conjugating enzyme E2 G1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G1) (E217K) (UBC7) (Ubiquitin carrier protein G1) (Ubiquitin-protein ligase G1) [Cleaved into: Ubiquitin-conjugating enzyme E2 G1, N-terminally processed] (P62255)
Organism: Rattus norvegicus (Rat)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 1
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 G2
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-like modifier activating enzyme 7
- Ubiquitin conjugating enzyme E2 V1 like 1
- Ubiquitin-conjugating enzyme E2 variant 2
- E2 ubiquitin-conjugating enzyme
Sequence:
MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLTFPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETIMISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE
Protein: Tyrosine-protein kinase Src42A (EC 2.7.10.2) (Tyrosine-protein kinase Src41) (Dsrc41) (Q9V9J3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required directly or indirectly for the phosphorylation of drpr which is necessary for the interaction of drpr with shark and subsequent glial phagocytic activity. Together with drpr and shark, promotes the migration of macrophages to sites of wounding as part of a signaling cascade where Scr42a detects production of hydrogen peroxide at wound sites which triggers phosphorylation of drpr and subsequent recruitment and activation of shark. Essential for correct eye morphogenesis (ommatidial R7 neuron formation) which requires the Ras1/MAPK signal transduction pathway. May be involved in the regulation of cytoskeleton organization and cell-cell contacts in developing ommatidia. During embryogenesis, involved in regulation of dorsal closure where it may have a role in activating the JNK pathway in leading edge cells during this process.
Interaction partners:
- Downstream of kinase
- Raf homolog serine/threonine-protein kinase Raf
- Ras-like protein 1
- Dual specificity mitogen-activated protein kinase kinase dSOR1
- Tyrosine-protein kinase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Connector enhancer of KSR protein CNK
- MAP/microtubule affinity-regulating kinase 3
- AT08303p
- Protein aveugle
Sequence:
MGNCLTTQKGEPDKPADRIKLDDPPTIGVGVGVPQIPMPSHAGQPPEQIRPVPQIPESETAGANAKIFVALYDYDARTDEDLSFRKGEHLEILNDTQGDWWLARSKKTRSEGYIPSNYVAKLKSIEAEPWYFRKIKRIEAEKKLLLPENEHGAFLIRDSESRHNDYSLSVRDGDTVKHYRIRQLDEGGFFIARRTTFRTLQELVEHYSKDSDGLCVNLCKPCVQIEKPVTEGLSHRTRDQWEIDRTSLKFVRKLGSGQFGDVWEGLWNNTTPVAIKTLKSGTMDPKDFLAEAQIMKKLRHTKLIQLYAVCTVEEPIYIITELMKHGSLLEYLQAIAGKGRSLKMQTLIDMAAQIAAGMAYLESQNYIHRDLAARNVLVGDGNIVKIADFGLARLIKEDEYEARVGARFPIKWTAPEAANYSKFSIKSDVWSFGILLTELVTYGRIPYPGMTNAEVLTQVEHGYRMPQPPNCEPRLYEIMLECWHKDPMRRPTFETLQWKLEDFYTSDQSDYKEAQAY
Protein: Hemoglobin subunit beta-1 (Beta-1-globin) (Hemoglobin beta-1 chain) (P83624)
Organism: Pseudaphritis urvillii (Congolli) (Freshwater flathead)
Function: Involved in oxygen transport from gills to the various peripheral tissues.
Interaction partners:
Sequence:
VVWTNEERSIISSIFSNLDYDDIGPKALCRCLIVYPWTQRHFTTFGNLYTPEAIMTNSKVAEHGVKVLHGLDRAVKNMDNIKATYYDLSILHSEKLHVDPDNFKLLSDCLTIVVAAKMGSGFTPETQAAFQKFLAVVVSALGKQYH
Protein: Intraflagellar transport protein 20 homolog (mIFT20) (Q61025)
Organism: Mus musculus (Mouse)
Function: Part of intraflagellar transport (IFT) particles involved in ciliary process assembly. May play a role in the trafficking of ciliary membrane proteins from the Golgi complex to the cilium. Regulates the ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway. Required for protein stability of E3 ubiquitin ligases CBL and CBLB that mediate ubiquitination and internalization of PDGFRA for proper feedback inhibition of PDGFRA signaling. Essential for male fertility. Plays an important role in spermatogenesis, particularly spermiogenesis, when germ cells form flagella. May play a role in the transport of flagellar proteins ODF2 and SPAG16 to build sperm flagella and in the removal of redundant sperm cytoplasm. Also involved in autophagy since it is required for trafficking of ATG16L and the expansion of the autophagic compartment.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:16775004, ECO:0000269|PubMed:19253336, ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:15337773}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15337773, ECO:0000269|PubMed:16775004}. Cell projection, cilium {ECO:0000269|PubMed:25243405, ECO:0000269|PubMed:29237719, ECO:0000269|PubMed:31637240}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825, ECO:0000269|PubMed:29690537}. Golgi apparatus {ECO:0000269|PubMed:29237719}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:31816150}. Cytoplasm {ECO:0000269|PubMed:29690537}. Note=Present at the centrosomes during the cell cycle and associated with the proximal portion of the mother centriole and the lateral aspect of the daughter centriole (PubMed:15337773). Associated with basal body at the base of primary cilia (PubMed:15337773). Detected in the Golgi apparatus of round spermatids and late spermatocytes (PubMed:19889948, PubMed:28619825). Also detected in the manchette of step 10-12 spermatids (PubMed:19889948, PubMed:28619825). In step 14 spermatids, found in the basal body of the sperm tail (PubMed:19889948). Localization in the manchette of elongating spermatids is dependent on SPAG17 (PubMed:29690537). {ECO:0000269|PubMed:15337773, ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825, ECO:0000269|PubMed:29690537}.
Interaction partners:
- Intraflagellar transport protein 52 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 80 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein 46 homolog
- Thyroid hormone receptor interactor 11
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 25 homolog
Sequence:
MAKDILGEAGLHFDELNKLRVLDPEVTQQTVELKEECKDFVDKIGQFQKIVGGLIELVDQLAKEAENEKMKAIGARNLLKSIAKQREAQQQQLQALIAEKKTQLERYRVEYEALCKVEAEQNEFIDQFIFQK
Protein: Oxysterol-binding protein-related protein 5 (ORP-5) (OSBP-related protein 5) (Oxysterol-binding protein homolog 1) (Q9H0X9)
Organism: Homo sapiens (Human)
Function: Lipid transporter involved in lipid countertransport between the endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner. May cooperate with NPC1 to mediate the exit of cholesterol from endosomes/lysosomes. Binds 25-hydroxycholesterol and cholesterol.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21220512, ECO:0000269|PubMed:26206935}; Single-pass membrane protein {ECO:0000269|PubMed:21220512}. Note=Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS). Localizes to the cortical endoplasmic reticulum at the EPCS. {ECO:0000269|PubMed:26206935, ECO:0000269|PubMed:30220461}.
Interaction partners:
- NPC intracellular cholesterol transporter 1
- Regulator of microtubule dynamics protein 3
- Vesicle-associated membrane protein-associated protein A
- Oxysterol-binding protein-related protein 8
- StAR-related lipid transfer protein 3
- Pleckstrin-2
- Pleckstrin homology-like domain family A member 2
- Pleckstrin
- Solute carrier family 67 member A1
- U5 small nuclear ribonucleoprotein TSSC4
Sequence:
MKEEAFLRRRFSLCPPSSTPQKVDPRKLTRNLLLSGDNELYPLSPGKDMEPNGPSLPRDEGPPTPSSATKVPPAEYRLCNGSDKECVSPTARVTKKETLKAQKENYRQEKKRATRQLLSALTDPSVVIMADSLKIRGTLKSWTKLWCVLKPGVLLIYKTPKVGQWVGTVLLHCCELIERPSKKDGFCFKLFHPLDQSVWAVKGPKGESVGSITQPLPSSYLIFRAASESDGRCWLDALELALRCSSLLRLGTCKPGRDGEPGTSPDASPSSLCGLPASATVHPDQDLFPLNGSSLENDAFSDKSERENPEESDTETQDHSRKTESGSDQSETPGAPVRRGTTYVEQVQEELGELGEASQVETVSEENKSLMWTLLKQLRPGMDLSRVVLPTFVLEPRSFLNKLSDYYYHADLLSRAAVEEDAYSRMKLVLRWYLSGFYKKPKGIKKPYNPILGETFRCCWFHPQTDSRTFYIAEQVSHHPPVSAFHVSNRKDGFCISGSITAKSRFYGNSLSALLDGKATLTFLNRAEDYTLTMPYAHCKGILYGTMTLELGGKVTIECAKNNFQAQLEFKLKPFFGGSTSINQISGKITSGEEVLASLSGHWDRDVFIKEEGSGSSALFWTPSGEVRRQRLRQHTVPLEEQTELESERLWQHVTRAISKGDQHRATQEKFALEEAQRQRARERQESLMPWKPQLFHLDPITQEWHYRYEDHSPWDPLKDIAQFEQDGILRTLQQEAVARQTTFLGSPGPRHERSGPDQRLRKASDQPSGHSQATESSGSTPESCPELSDEEQDGDFVPGGESPCPRCRKEARRLQALHEAILSIREAQQELHRHLSAMLSSTARAAQAPTPGLLQSPRSWFLLCVFLACQLFINHILK
Protein: Kelch like family member 8 (Uncharacterized protein DKFZp781C1855) (Q68DU9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASDSMSSKQARNHITKGKRQQQHQQIKNRSSISDGDGEDSFIFEANEAWKDFHGSLLRFYENGELCDVTLKVRLPLLPVDFLMGVVAKEQIVKQNLKCRDLLDEARNYHLHLSSRAVPDFEYSIRTTPRKHTAGVLFCVGGRGGSGDPFRSIECYSINKNSWFFGPEMNSRRRHVGVISVEGKVYAVGGHDGNEHLGSMEMFDPLTNKWMMKASMNTKRRGIALASLGGPIYAIGGLDDNTCFNDVERYDIESDQWSTVAPMNTPRGGVGSVALVNHVYAVGGNDGMASLSSVERYDPHLDKWIEVKEMGQRRAGNGVSKLHGCLYVVGGFDDNSPLSSVERYDPRSNKWDYVAALTTPRGGVGIATVMGKIFAVGGHNGNAYLNTVEAFDPVLNRWELVGSVSHCRAGAGVAVCSCLTSQIRDVGHGSNNVVDCM
Protein: Sodium chloride cotransporter 69, isoform C (Sodium chloride cotransporter 69, isoform D) (Sodium chloride cotransporter 69, isoform F) (M9PCA7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSDTISFELGSAADRPPNRFQVNPVNGNSRKSQGADGPGSGSGAGAGAGAGAGEDGPHEVYRRLTNAEGELLEDDTFDATQMLNQRQPRQQRQSIKSSFRDKDKPSRFKDLQTTTRFQVDPQNEESDESNDSQEERELLDNEYDTKYGKSFRHFTREALPRLDNYRNMMSIQAAYRPTLDELHNATLVGKNTHSLTRNQDPESGILNGVLKFGWIKGVLVRCLLNIWGVMLFLRLSWVVGQAGVIEGFVLILTTTAVTTITALSMSAISTNGVIKGGGTYYMISRSLGPEFGGSIGLIFSLANAVACAMYVVGFCESMLAMMTTFGWEIIDGGVQDVRIIGCITILLLLIIVVVGMEWEAKAQIGLLIILLVAIGDFVIGSFIGPKSDAEMAKGFLGYNATLFKNNLFADYRPEKGGIQHDFFSVFAIFFPAATGILAGANISGDLKDPQKSIPKGTILAIVITTGTYLIMVLQCGATVARDATGNLSDVVNGTFAFLDCQPGECNYGLQNSFQVIELVSAFGPLIYAGCYAATLSSALASLVSAPKVFQALCKDELYPKIVWFAKGYGKNNEPVRGYVLTFIIACAFILIGELNLIAPLISNFFLAAYMLINFSTFHASLAKPVGWRPTFKYYNMWLSLLGAILCVAVMFLISWATALITFAAVLALYLIVAYRKPDVNWGSTTQAQTYKNALMSVQQLNNVEEHVKNYRPQILVLSGLPNTRPVLVDLAYMLTKNLSLLVCGHVLKGSSSQKYRTYLQERAGNWFRKHRVKGFYALVDGEDFESGTRALMQATGIGKLKPNIILMGYKTDWQTCDHKELDQYFNVMHKALDMYLSVAILRVPQGLDCSQVLGSQDGWKTVSDVPRTLQPNESSGDLQAVDSSVRNGLSGSIDSLSRNVSQEDRNRNQLVHSEQNSLKIVKSSSTSDLSFIAGNQSKDVSGMPDPLDAKSANLVSNSLRKSKLKHDDPASLYKGPGGAELPKEVLADLTQFTRKRSHAVIDVWWLYDDGGLTLLLPYIISTRRTWQSCKLRVYALANKNSELEFEQRSMASLLSKFRIDYSDLTLIPDITKKPQETSTQFFNELIKDFVVTEKDGENGTSSRATLNEDDALITDDDLLAVQDKTNRYLRLREYLREQSTKSDLVVMTLPMPRKNIVSAPLYMAWLESLSRDMPPFLFVRGNQTSVLTFYS
Protein: Plastid-lipid-associated protein 6, chloroplastic (Fibrillin-4) (Fibrillin-6) (Harpin-binding protein 1) (HrBP1) (Plastoglobulin 30.4) (AtPGL30.4) (Q9LW57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for plastoglobule development and resistance to multiple stresses. Regulates plastoglobule osmiophilic content. May be involved in the transport of lipophilic antioxidants in and out of the plastoglobule.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16414959, ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Interaction partners:
- Probable plastid-lipid-associated protein 2, chloroplastic
- Probable plastid-lipid-associated protein 8, chloroplastic
- Probable plastid-lipid-associated protein 13, chloroplastic
- Probable plastid-lipid-associated protein 9, chloroplastic
- Probable plastid-lipid-associated protein 1, chloroplastic
- Probable plastid-lipid-associated protein 3, chloroplastic
- Probable plastid-lipid-associated protein 10, chloroplastic
- Small ribosomal subunit protein uS4c
- Ankyrin repeat family protein
- Ankyrin repeat family protein
Sequence:
MATSSTFSSLLPSPPALLSDHRSPPPSIRYSFSPLTTPKSSRLGFTVPEKRNLAANSSLVEVSIGGESDPPPSSSGSGGDDKQIALLKLKLLSVVSGLNRGLVASVDDLERAEVAAKELETAGGPVDLTDDLDKLQGKWRLLYSSAFSSRSLGGSRPGLPTGRLIPVTLGQVFQRIDVFSKDFDNIAEVELGAPWPFPPLEATATLAHKFELLGTCKIKITFEKTTVKTSGNLSQIPPFDIPRLPDSFRPSSNPGTGDFEVTYVDDTMRITRGDRGELRVFVIA