wanglab/gogpt-training-data huggingface dataset:
Protein: Negative elongation factor complex member A (H0Y3X6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
RKAWGWGFSPGVWTGQGAVVHPQRQPAQLSHTVSSPVGAWQRHRHAMAWLSAFPRGRGFMWPKQALVWMDLASQMKGALMEIIQLASLDSDPWVLMVADILKSFPDTGSLNLELEEQNPNVQDILGELREKVGECEASAMLPLECQYLNKNALTTLAGPLTPPVKHFQLKRKPKSATLRAELLQKSTETAQQLKRSAGVPFHAKGRGLLRKMDTTTPLKGIPKQAPFRSPTAPSVFSPTGNRTPIPPSRTLLRKERGVKLLDISELDMVGAGREAKRRRKTLDAEVVEKPAKEETVVENATPDYAAGLVSTQKLGSLNNEPALPSTSYLPSTPSVVPASSYIPSSETPPAPSSREASRPPEEPSAPSPTLPAQFKQRAPMYNSGLSPATPTPAAPTSPLTPTTPPAVAPTTQTPPVAMVAPQTQAPAQQQPKKNLSLTREQMFAAQEMFKTANKVTRPEKALILGFMAGSRENPCQEQGDVIQIKLSEHTEDLPKADGQGSTTMLVDTVFEMNYATGQWTRFKKYKPMTNVS
Protein: Oxysterols receptor LXR-alpha (A0A060WYW4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- NR LBD domain-containing protein
- Retinoic acid receptor RXR
- Retinoic acid receptor RXR
- NR LBD domain-containing protein
- Retinoic acid receptor RXR
- NR LBD domain-containing protein
- NR LBD domain-containing protein
- Uncharacterized protein
- Retinoid X receptor beta
- Retinoic acid receptor RXR
Sequence:
MSTLSATDITDVGHGEVFDGDPELQLDCLCSGDDRSSAEMKHEGNLLPLEPPDHAGFSSSPQKRPSSLAEESSPLPMEPSDIKADPAGSMPANTEGQPVKRKKGPAPKMLGNEVCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKSAQYSCKNNGRCEMDMYMRRKCQQCRLRKCREAGMLEQCVLSEEQIRVKKMKKNEEETARTSAVVTPTPVPEVVPLAPEQLEMIEKLVAMQKQCNKRSFIDRPKVTPWPQSQDPQNREVRQQRFAHFTELAIMSVQEIVDFAKQLPGFLELTREDQIALLKTSTIEIMLLETSRRYNPAIESITFLKDFSYNKEDFAKAGLQLEFINPIFEFSKGMNDLHLDEAEYALLIAINIFSADRPNVQDHELVERLQQPYVDALRSYIMIKRPNDHLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Protein: Signal recognition particle receptor subunit beta (SR-beta) (P36057)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O13950}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Signal recognition particle receptor subunit alpha homolog
- Signal recognition particle subunit SRP54
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SEC65
- Signal recognition particle subunit SRP21
- Signal recognition particle subunit SRP14
- Serine/threonine-protein kinase MEC1
- Protein transport protein SEC61
- Large ribosomal subunit protein uL18
Sequence:
MLSNTLIIACLLVIGTTIALIAVQKASSKTGIKQKSYQPSIIIAGPQNSGKTSLLTLLTTDSVRPTVVSQEPLSAADYDGSGVTLVDFPGHVKLRYKLSDYLKTRAKFVKGLIFMVDSTVDPKKLTTTAEFLVDILSITESSCENGIDILIACNKSELFTARPPSKIKDALESEIQKVIERRKKSLNEVERKINEEDYAENTLDVLQSTDGFKFANLEASVVAFEGSINKRKISQWREWIDEKL
Protein: Transcription factor TCP15 (AtTCP15) (Q9C9L2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved the regulation of plant development. Together with TCP14, modulates plant stature by promoting cell division in young internodes. Represses cell proliferation in developing leaf blade and specific floral tissues. Together with TCP15, acts downstream of gibberellin (GA), and the stratification pathways that promote seed germination. Involved in the control of cell proliferation at the root apical meristem (RAM) by regulating the activity of CYCB1-1. Acts together with SPY to promote cytokinin responses that affect leaf shape and trichome development in flowers. Involved in gynoecium and silique development. Modulates the development of the different tissues of the gynoecium through its participation in auxin and cytokinin responses. Modulates the expression of the cytokinin-responsive genes ARR7 and ARR15. May repress the expression of the auxin biosynthetic genes YUC1 and YUC4. Acts as negative regulator of anthocyanin accumulation under high light conditions. Modulates the expression of transcription factors involved in the induction of anthocyanin biosynthesis genes. Transcription factor involved in the regulation of endoreduplication. Represses endoreduplication by activating the gene expression of the key cell-cycle regulators RBR1 and CYCA2-3. Regulates the expression of the defense gene pathogenesis-related protein 2 (PR2) in antagonism to SRFR1, a negative regulator of effector-triggered immunity.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:29250092}.
Interaction partners:
- Transcription factor TCP13
- Transcription factor TCP3
- Suppressor of RPS4-RLD 1
- Transcription factor TCP5
- Transcription factor TCP2
- Transcription factor TCP24
- Protein DA1-related 1
- Transcription factor TCP4
- Transcription factor TCP10
- Protein DA1-related 2
Sequence:
MDPDPDHNHRPNFPLQLLDSSTSSSSTSLAIISTTSEPNSEPKKPPPKRTSTKDRHTKVEGRGRRIRMPAMCAARVFQLTRELGHKSDGETIEWLLQQAEPAVIAATGTGTIPANFTSLNISLRSSRSSLSAAHLRTTPSSYYFHSPHQSMTHHLQHQHQVRPKNESHSSSSSSSQLLDHNQMGNYLVQSTAGSLPTSQSPATAPFWSSGDNTQNLWAFNINPHHSGVVAGDVYNPNSGGSGGGSGVHLMNFAAPIALFSGQPLASGYGGGGGGGGEHSHYGVLAALNAAYRPVAETGNHNNNQQNRDGDHHHNHQEDGSTSHHS
Protein: Solute carrier family 35 member D3 (Fringe connection-like protein 1) (Q8BGF8)
Organism: Mus musculus (Mouse)
Function: May play a role in hemostasis as a regulator of the biosynthesis of platelet-dense granules.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5M8T2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:22611153}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24550737}; Multi-pass membrane protein {ECO:0000255}. Note=Active at early endosome membrane in the biosynthesis of mature platelet-dense granules. {ECO:0000269|PubMed:22611153}.
Interaction partners:
- UDP-sugar transporter protein SLC35A5
Sequence:
MRQLCRGRVLGISVAIAHGVFSGSLNILLKFLISRYQFSFLTLVQCLTSSTAALSLELLRRLGLIAVPPFGLSLARSFAGVAVLSTLQSSLTLWSLRGLSLPMYVVFKRCLPLVTMLIGVLVLKNGAPSPGVLAAVLITTCGAALAGAGDLTGDPIGYVTGVLAVLVHAAYLVLIQKASADTEHGPLTAQYVIAVSATPLLVICSFASTDSIHAWTFPGWKDPAMVSIFVACILIGCAMNFTTLHCTYINSAVTTSFVGVVKSIATITVGMVAFSDVEPTSLFIAGVVVNTLGSIIYCVAKFLETRRQSNYEDLESQAEGEERQPSGDQLPFVMEELPAKSGNSEPESAEGAGDSVQQGGQESRGSIRGISLAARSSRAEGHSDEVGRRSLKDTYLEVWRLVRGTKYMKKDYLMENEALPSP
Protein: Nuclear transcription factor Y subunit B-2 (OsNF-YB-2) (Transcriptional activator HAP3A) (Q5QMG3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of the NF-Y/HAP transcription factor complex. The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters. May regulate the expression of photosynthetic genes, and may be involved in chloroplast and amyloplast development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit C-4
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit C-6
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit
- Nuclear transcription factor Y subunit
Sequence:
MMMMDLGFLEGGAGMADAGHDESGSPPRSGGVREQDRFLPIANISRIMKKAVPANGKIAKDAKETLQECVSEFISFVTSEASDKCQKEKRKTINGEDLLFAMGTLGFEEYVDPLKIYLHKYREVIGDSKLSSKAGDGSVKKDTIGPHSGASSSSAQGMVGAYTQGMGYMQPQYHNGDT
Protein: Calnexin (F1QKS4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Melanosome membrane {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004573}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004583}.
Interaction partners:
- Protein disulfide-isomerase.
- Endoplasmin
- Immunoglobulin binding protein
- Si:ch211-274f20.2.
- Calreticulin
- Interleukin 12 receptor, beta 2a,-like.
- alpha-1,2-Mannosidase
- SEC63 homolog, protein translocation regulator.
- Calreticulin
- Calreticulin
Sequence:
MELKMRLCVALLSLSLCLLLMGPVRAQEEEADDMEMDVEDAIDDMQEEDIEEEEQKAPAPPSAPTVTYKAPEPMGEHYFAEAFDKGTLQGWVLSQAKKDGIDEDIAKYDGKWEVEEMQDSKLPGDKGLVLKSKAKHHAISALLLRPFTFDTKPLIVQYEVNFQTGIDCGGAYVKLLSQTPDLDLEEFVDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGEFEEKHAKKPDSDLRSYYTDKKTHLYTLVLNPDNTFEILIDQTVVNSGSLLNDVTPPVNPPAEIEDPDDHKPEDWDERPKIQDPDAVKPEDWDEDAPAKIADEDAVKPDGWLDDEPEYISDPDAVKPEDWDEDMDGEWEAPQIPNPVCETAPGCGAWERPMIDNPNYKGKWKSPMIDNPNYQGVWKPRKIPNPDFFEDLHPFRMTPFSAVGLELWSMSSDIFFDNFFITSDRNVAERWANDGWGLKKAAEGAAEPGLVNQMITAAEERPWLWIVYVLTVALPLVLIIVFCCTGKKSSASTPAAEYKKTDEPQPDVKEEAEEEEAKDEEPEAKKSEEEDSTGDGDGDDTAENGDKDDNTSNEKSEDDILRRSPRNRKSRKD
Protein: Neuronal acetylcholine receptor subunit beta-4 (P30926)
Organism: Homo sapiens (Human)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-3
- Proteasome subunit alpha type-4
- Neuronal acetylcholine receptor subunit alpha-7
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit beta-2
- Tyrosine-protein kinase JAK2
- Neuronal acetylcholine receptor subunit beta-3
Sequence:
MRRAPSLVLFFLVALCGRGNCRVANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIKLQLSLAQLISVNEREQIMTTNVWLKQEWTDYRLTWNSSRYEGVNILRIPAKRIWLPDIVLYNNADGTYEVSVYTNLIVRSNGSVLWLPPAIYKSACKIEVKYFPFDQQNCTLKFRSWTYDHTEIDMVLMTPTASMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLTTLLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDVPLIGKYLMFTMVLVTFSIVTSVCVLNVHHRSPSTHTMAPWVKRCFLHKLPTFLFMKRPGPDSSPARAFPPSKSCVTKPEATATSTSPSNFYGNSMYFVNPASAASKSPAGSTPVAIPRDFWLRSSGRFRQDVQEALEGVSFIAQHMKNDDEDQSVVEDWKYVAMVVDRLFLWVFMFVCVLGTVGLFLPPLFQTHAASEGPYAAQRD
Protein: Regulator of microtubule dynamics protein 1 (RMD-1) (mRMD-1) (Microtubule-associated protein) (Protein FAM82B) (Q9DCV4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. {ECO:0000250}.
Interaction partners:
Sequence:
MALSSRLWRRLPPLRVCQQTRTWGSRGRCGAWGVRACEVIGNTRPFKRGFLFSALSYLGFETYQIISQAAVVHATAKVEEILAQADYLYESGETEKLYQLLIQYKESEDGELLWRLARASRDIAQLSKTSEEEKKVLVYEALDYAKRALEKKESSSAAHKWYAICISDVGDYEGIKVKIANAYVIKEHFEKAIELNPKDATSIHLMGIWCYTFAEMPWYQRRIAKVLFANPPSSTYEEALRYFHKAEEVDPNFYSKNLLLLGKTYLKLNNKKLAAFWLVKAKGYPAHTEEDKQIQTEAAQLLTGL
Protein: Torsin-1A (Dystonia 1 protein) (Torsin ATPase 1) (EC 3.6.4.-) (Q68G38)
Organism: Rattus norvegicus (Rat)
Function: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non-neural tissues (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:O14656}. Nucleus inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, growth cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus envelope is mediated by the interaction with TOR1AIP2. Upon oxidative stress, redistributes to protusions from the cell surface.
Interaction partners:
- Torsin-1A-interacting protein 2
- Torsin-1A-interacting protein 1
- Torsin.
- Protein-glutamine gamma-glutamyltransferase 2
- Epsilon-sarcoglycan
- COP9 signalosome complex subunit 4
- CDKN1A interacting zinc finger protein 1
- THAP domain-containing protein 1
Sequence:
MKLGRATLALLLLVPCVVRAVEPISLGLALAGVLTGYISYPRLYCLFAECCGQKRSLSREALQKDLDNKLFGQHLAKRVILNAVSGFLSNPKPKKPLTLSLHGWTGTGKNFASKIIAENIYEGGLNSDYVHLFVATLHFPHASNITLYKDQLQMWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDYYDVVDEVSYQKAIFIFLSNAGAERITDVALDFWRSGKQREEIKLRDMEHALAVSVFNNKNSGFWHSSLIDRNLIDYFVPFLPLEYKHLKMCIRVEMQSRGYEEDEDIINKVAEEMTFFPKEEKVFSDKGCKTVFTKLDYYLDD
Protein: Vacuolar protein-sorting-associated protein 25 (ESCRT-II complex subunit VPS25) (Q55GD9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Vacuolar-sorting protein SNF8
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting-associated protein 28
- Charged multivesicular body protein 6
- Charged multivesicular body protein 4
- Charged multivesicular body protein 3
- ESCRT-I complex subunit tsg101
- Charged multivesicular body protein 1
- Charged multivesicular body protein 7
- Uncharacterized protein
Sequence:
MSNQVFQFPPYYHKEPFFTIQPILNTRKKQFQMWQDLILQYCRYYKIYELDINESIKSNSVLFNNEKINRKLSREALKSIIDDIIENGFAEWVDKEKEKEKEKDKDNNNNNRVLIMWRKPDEWASLIYKWVADCGLLNTVLTVWEIQNGDDSKKQEFHQLNTTILMKSLKVLEKQSKCQTFSQDENVGVKFFSI
Protein: Cell adhesion molecule CEACAM5 (Carcinoembryonic antigen) (CEA) (Carcinoembryonic antigen-related cell adhesion molecule 5) (CEA cell adhesion molecule 5) (Meconium antigen 100) (CD antigen CD66e) (P06731)
Organism: Homo sapiens (Human)
Function: Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6. Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10864933, ECO:0000269|PubMed:18086185, ECO:0000269|PubMed:2317824}. Apical cell membrane {ECO:0000269|PubMed:10436421}. Cell surface {ECO:0000269|PubMed:2317824, ECO:0000269|PubMed:2803308}. Note=Localized to the apical glycocalyx surface. {ECO:0000269|PubMed:10436421}.
Interaction partners:
- Alpha-fetoprotein
- Mucin-1
- Gamma-enolase
- CD209 antigen
- Cell adhesion molecule CEACAM1
- Keratin, type II cytoskeletal 7
- Keratin, type I cytoskeletal 19
- Keratin, type I cytoskeletal 20
- Prostate-specific antigen
- Mesothelin
Sequence:
MESPSAPPHRWCIPWQRLLLTASLLTFWNPPTTAKLTIESTPFNVAEGKEVLLLVHNLPQHLFGYSWYKGERVDGNRQIIGYVIGTQQATPGPAYSGREIIYPNASLLIQNIIQNDTGFYTLHVIKSDLVNEEATGQFRVYPELPKPSISSNNSKPVEDKDAVAFTCEPETQDATYLWWVNNQSLPVSPRLQLSNGNRTLTLFNVTRNDTASYKCETQNPVSARRSDSVILNVLYGPDAPTISPLNTSYRSGENLNLSCHAASNPPAQYSWFVNGTFQQSTQELFIPNITVNNSGSYTCQAHNSDTGLNRTTVTTITVYAEPPKPFITSNNSNPVEDEDAVALTCEPEIQNTTYLWWVNNQSLPVSPRLQLSNDNRTLTLLSVTRNDVGPYECGIQNELSVDHSDPVILNVLYGPDDPTISPSYTYYRPGVNLSLSCHAASNPPAQYSWLIDGNIQQHTQELFISNITEKNSGLYTCQANNSASGHSRTTVKTITVSAELPKPSISSNNSKPVEDKDAVAFTCEPEAQNTTYLWWVNGQSLPVSPRLQLSNGNRTLTLFNVTRNDARAYVCGIQNSVSANRSDPVTLDVLYGPDTPIISPPDSSYLSGANLNLSCHSASNPSPQYSWRINGIPQQHTQVLFIAKITPNNNGTYACFVSNLATGRNNSIVKSITVSASGTSPGLSAGATVGIMIGVLVGVALI
Protein: Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (EC 2.7.1.93) (80 kDa diacylglycerol kinase) (Diglyceride kinase alpha) (DGK-alpha) (P20192)
Organism: Sus scrofa (Pig)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8809050}.
Interaction partners:
- Acyltransferase
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Phosphoinositide phospholipase C
- Phosphoinositide phospholipase C.
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Phospholipase
Sequence:
MSKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAEYLQGDAIGYEGFQQFLKIYLEVDSVPSHLSLALFQSFQTSYCSEETVKRDVVCLSDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDRIIIQMMRMAEYLDWDVSELRPILQEMMKEIDYDGSGSVSLAEWLRAGATTVPLLVLLGLEMTLKDNGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGVQTHVWVRGGCESGRCDRCQKKIRIYHSLVGLHCVWCHLEIHDDCLPAMGHECDCGLLRDHILPPSSIYPSVLASGQERKVSKTSQKTTDDLNLSTSEALRIDPVSNTHPLLVFVNPKSGGKQGERVLWKFQYLLNPRQVFNLLKDGPEPGLRFFREVPDYRILVCGGDGTVGWILETIDKANLPFVPPVAVLPLGTGNDLARCLRWGGGYEGQNLGKILKDLEASKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSTHGGSNLWGDTKRPHGDIHGINQALGAMAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAGHRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHRNQMPMLVGPPPRSSNFFGFLC
Protein: Ferric uptake regulation protein (Q8PAL3)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
- Outer membrane protein assembly factor BamE
- Alkyl hydroperoxide reductase C
Sequence:
MNGERMETHDLRKVGLKVTHPRMRILELLEQKSNQHHLSAEDIYRQLLDHGDEIGLATVYRVLTQFEAAGLVLKHNFEGGQAVYELDRGGHHDHMVDVDTGHVIEFESEEIEALQRQIAAKHGYELEEHSLVLYVRKKRPR
Protein: UPF0716 protein FxsA (Suppressor of F exclusion of phage T7) (P37147)
Organism: Escherichia coli (strain K12)
Function: Overexpression alleviates the exclusion of phage T7 in cells harboring the F plasmid.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Small heat shock protein IbpA
- Chaperedoxin
- UPF0250 protein YbeD
- ATP-dependent protease subunit HslV
- UPF0283 membrane protein YcjF
Sequence:
MRWLPFIAIFLYVYIEISIFIQVAHVLGVLLTLVLVIFTSVIGMSLVRNQGFKNFVLMQQKMAAGENPAAEMIKSVSLIIAGLLLLLPGFFTDFLGLLLLLPPVQKHLTVKLMPHLRFSRMPGGGFSAGTGGGNTFDGEYQRKDDERDRLDHKDDRQD
Protein: Phosphatidylinositol 4-kinase type 2 (EC 2.7.1.67) (E9PAM4)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00037864}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037864}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane {ECO:0000256|RuleBase:RU367084}; Peripheral membrane protein {ECO:0000256|RuleBase:RU367084}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}. Presynaptic cell membrane {ECO:0000256|ARBA:ARBA00034111}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MLGPQVWSSVRQGLSRSLSRNVGVWASGEGKKVDIAGIYPPVTTPFTATAEVDYGKLEENLHKLGTFPFRGAVGGVCALANVLGAQVCQLERLCCTGQWEDAQKLQHRLIEPNAARIIAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDCPMDSSSSRDTDWVVVKEPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW
Protein: Chaperone protein ClpB2, chloroplastic (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 2) (Casein lytic proteinase B2) (Q75GT3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Molecular chaperone that may play a role in chloroplast development.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:20141629}.
Interaction partners:
- Os08g0432500 protein
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
- Os05g0278950 protein
Sequence:
MAAAPPLAAGLRPAMAAAQAPVVAAAWGVGARRGAALSSSARCRALRLSRGGGGGRDGWVPPPVVGRMPPRTLSVRCAASNGRITQQEFTEMAWQSIVSSPEVAKESKHQIVETEHLMKSLLEQRNGLARRIFSKAGVDNTRLLDATEKFIQRQPKVLGEDPGSMLGRDLEALIQRARDFKKEYGDSFVSVEHLVLGFAEDKRFGRQLFKDFQITVQSLKTAIESIRGKQNVIDQDPEGKYEALDKYGKDLTAMARQGKLDPVIGRDDEIRRCIQILSRRTKNNPVLIGEPGVGKTAIAEGLAQRIVQGDVPQALTNRRLIALDMGALIAGAKYRGEFEDRLKAVLKEVTDSDGQTILFIDEIHTVVGAGATNGAMDAGNLLKPMLGRGELRCIGATTLDEYRKYIEKDPALERRFQQVYVDQPSVEDTISILRGLRERYELHHGVRISDSALVAAALLSDRYISGRFLPDKAIDLVDESAAKLKMEITSKPTALDEIDRAVIKLEMERLSLTNDTDKASRDRLSRIEAELSLLKEKQKDLTEQWEREKSVMTKIQSIKEEIDRVNVEIQQAEREYDLNRAAELKYGSLNALQRQLQTTEKELDEYQSSGKSMLREEVTQDDIAEIVSRWTGIPVSKLKQSDREKLLYLEEELHKRVVGQDPAVKAVSEAIQRSRAGLSDPNRPIASFMFMGPTGVGKTELAKALAAFMFNTEEAVVRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSIILFDEIEKAHGDVFNVFLQILDDGRVTDSQGRKVSFTNSIIIMTSNVGSQFILNMDEEGGSTDSAYENIKKRVMDAARSVFRPEFMNRIDEYIVFKPLEREQINSIVKLQLARVQKRIADRKIKLEVSPGAVEFLGSLGYDPNYGARPVKRVIQQYVENELAKGILRGDFKDEDSILVDTQVTVPSNGQLPQQKLVFHKMSEESAPAAAEDEKFLPAV
Protein: Sm-like protein LSM36B (AtLSM6B) (U6 snRNA-associated Sm-like protein LSM6B) (O22823)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus {ECO:0000269|PubMed:23221597}.
Interaction partners:
- Sm-like protein LSM3A
- Sm-like protein LSM7
- Sm-like protein LSM4
- Sm-like protein LSM2
- Sm-like protein LSM5
- Sm-like protein LSM8
- Sm-like protein LSM3B
- Small nuclear ribonucleoprotein Sm D2
- Sm-like protein LSM1A
- Protein GOLVEN 6
Sequence:
MSGVGEKASGTTKTPADFLKSIRGKPVVVKLNSGVDYRGILTCLDGYMNIAMEQTEEYVNGQLKNTYGDAFVRGNNVLYISTTKGTLSDGA