wanglab/gogpt-training-data huggingface dataset:
Protein: Calaxin (EF-hand calcium-binding domain-containing protein 1) (Q32L26)
Organism: Bos taurus (Bovine)
Function: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule. Seems to regulate the assembly of both ODAs and their axonemal docking complex onto ciliary microtubules. Regulates ciliary and flagellar motility and is required for cilia-driven determination of body laterality (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96M63}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9HAE3}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q9HAE3}.
Interaction partners:
- Outer dynein arm-docking complex subunit 4
- Outer dynein arm-docking complex subunit 2
- Outer dynein arm-docking complex subunit 1
- Outer dynein arm-docking complex subunit 3
- Piercer of microtubule wall 1 protein
- Armadillo repeat containing 3
- EF-hand domain-containing family member C2
- Tektin bundle-interacting protein 1
- IQ motif and ubiquitin domain containing
- Tektin-3
Sequence:
MNRKKLQKLTDSLTKNCKHFSKFEVKCLINLFYNLVGEVTERQGVIIGLDRNAFRNILHMTFGMTDDMIMDRVFRGFDKDNDGCISVTEWVYGLSVFLRGTLEEKMKYCFEVFDLNGDSFISKEEMFHMLKNSLLKQPSEEDPDEGIKDLVEITLKKMDHDHDGKLSFADYEQAVREETLLLEAFGPCLPDPKSQSEFEAQVFKDPNEFNEV
Protein: Ribosome quality control complex subunit TCF25 (Nuclear localized protein 1) (Transcription factor 25) (TCF-25) (Q9BQ70)
Organism: Homo sapiens (Human)
Function: May play a role in cell death control. Acts as a transcriptional repressor. Has been shown to repress transcription of SRF in vitro and so may play a role in heart development.
Subcellular location: Nucleus {ECO:0000269|PubMed:16574069, ECO:0000269|PubMed:18068114}. Cytoplasm, cytosol {ECO:0000269|PubMed:18068114}. Note=Mainly nuclear. {ECO:0000269|PubMed:18068114}.
Interaction partners:
- G-protein coupled receptor-associated sorting protein 2
- Ribosome quality control complex subunit NEMF
- E3 ubiquitin-protein ligase listerin
- Transitional endoplasmic reticulum ATPase
- tRNA endonuclease ANKZF1
- Diamine acetyltransferase 1
Sequence:
MSRRALRRLRGEQRGQEPLGPGALHFDLRDDDDAEEEGPKRELGVRRPGGAGKEGVRVNNRFELINIDDLEDDPVVNGERSGCALTDAVAPGNKGRGQRGNTESKTDGDDTETVPSEQSHASGKLRKKKKKQKNKKSSTGEASENGLEDIDRILERIEDSTGLNRPGPAPLSSRKHVLYVEHRHLNPDTELKRYFGARAILGEQRPRQRQRVYPKCTWLTTPKSTWPRYSKPGLSMRLLESKKGLSFFAFEHSEEYQQAQHKFLVAVESMEPNNIVVLLQTSPYHVDSLLQLSDACRFQEDQEMARDLVERALYSMECAFHPLFSLTSGACRLDYRRPENRSFYLALYKQMSFLEKRGCPRTALEYCKLILSLEPDEDPLCMLLLIDHLALRARNYEYLIRLFQEWEAHRNLSQLPNFAFSVPLAYFLLSQQTDLPECEQSSARQKASLLIQQALTMFPGVLLPLLESCSVRPDASVSSHRFFGPNAEISQPPALSQLVNLYLGRSHFLWKEPATMSWLEENVHEVLQAVDAGDPAVEACENRRKVLYQRAPRNIHRHVILSEIKEAVAALPPDVTTQSVMGFDPLPPSDTIYSYVRPERLSPISHGNTIALFFRSLLPNYTMEGERPEEGVAGGLNRNQGLNRLMLAVRDMMANFHLNDLEAPHEDDAEGEGEWD
Protein: Protein FAM209B (Q5JX69)
Organism: Homo sapiens (Human)
Function: May play a role in sperm acrosome biogenesis.
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:A2APA5}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:31429579}.
Interaction partners:
Sequence:
MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVPCGEHFRIRQNLPEHTQGWLGSKWLWLLFAVVPFVILQCQRDSEKNKEQSPPGLRGFPFRTPLKKNQNASLYKDCVFNTLNELEVELLKFVSEVQNLKGAMATGSGSNLKLRRSEMPADPYHVTICKIWGEESSS
Protein: Chromosome 11 open reading frame 54 (E9PLC5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MACAEFSFHVPSLEELAGVMQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFILGAGAG
Protein: Transcription elongation factor A protein-like 8 (TCEA-like protein 8) (Transcription elongation factor S-II protein-like 8) (Q8IYN2)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MQKSCEENEGKPQNMPKAEEDRPLEDVPQEAEGNPQPSEEGVSQEAEGNPRGGPNQPGQGFKEDTPVRHLDPEEMIRGVDELERLREEIRRVRNKFVMMHWKQRHSRSRPYPVCFRP
Protein: Ubiquinone biosynthesis protein (F4IE14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU366063}.
Interaction partners:
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- Protein ABC transporter 1, mitochondrial
- AT5g10730/MAJ23_90
- NAD
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Polyketide cyclase / dehydrase and lipid transport protein
- FAD/NAD
- RING-box protein 1a
Sequence:
MYRTAAKRLLAGGGITTTRLLRLPKLRSTIIPSSYTSGLCTSSIGGNTESPMGKQSVNPNQSGPTASSSTGTGEGQRRHESRKPRAEFQEEQARVLSASLRHVPRLGWTEEAMMAGSRDVGVSPSIVGSFSRKEAALVEFFMDECLQLLMDRIDSGLDLQNLIPSERISKLIRIRLEMQVPYMSKWPQALSIQAHPLNVPTSFKQRAMLVDEIWHAVGDGASDLDWYVKRTILGGVYSTTEIYMLTDDSLAEHRDTWAFLDDRVKDAFDLKKSIQEAKYFAEDIGAGVGKSVQGLMNGVMQTMSRRSGGSAF
Protein: Ankyrin repeat and SOCS box protein 9 (ASB-9) (Q96DX5)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes at least two forms of creatine kinase, CKB and CKMT1A.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:20302626}.
Interaction partners:
- Elongin-C
- Creatine kinase B-type
- Elongin-B
- Cullin-5
- Creatine kinase U-type, mitochondrial
- Creatine kinase M-type
- Hypoxia-inducible factor 1-alpha inhibitor
- E3 ubiquitin-protein ligase ARIH2
- Creatine kinase S-type, mitochondrial
Sequence:
MDGKQGGMDGSKPAGPRDFPGIRLLSNPLMGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQPESDLASPIHEAARRGHVECVNSLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVNQGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL
Protein: Aspartic proteinase A2 (EC 3.4.23.-) (Aspartic protease 57) (AtASP57) (Q8VYL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the breakdown of propeptides of storage proteins in protein-storage vacuoles.
Subcellular location: Vacuole {ECO:0000250}.
Interaction partners:
- Pulmonary surfactant-associated protein B)
- Pulmonary surfactant-associated protein B)
- BTB/POZ domain-containing protein At3g44820
- Aspartic proteinase Asp1
- Aspartic proteinase Asp1
- Eukaryotic aspartyl protease family protein
- At3g50050
- Eukaryotic aspartyl protease family protein
- Eukaryotic aspartyl protease family protein
- Eukaryotic aspartyl protease family protein
Sequence:
MGVYSRAVAFSVFVSFLLFFTAYSKRNDGTFRVGLKKLKLDPNNRLATRFGSKQEEALRSSLRSYNNNLGGDSGDADIVPLKNYLDAQYYGEIAIGTPPQKFTVIFDTGSSNLWVPSGKCFFSLSCYFHAKYKSSRSSTYKKSGKRAAIHYGSGSISGFFSYDAVTVGDLVVKDQEFIETTSEPGLTFLVAKFDGLLGLGFQEIAVGNATPVWYNMLKQGLIKRPVFSFWLNRDPKSEEGGEIVFGGVDPKHFRGEHTFVPVTQRGYWQFDMGEVLIAGESTGYCGSGCSAIADSGTSLLAGPTAVVAMINKAIGASGVVSQQCKTVVDQYGQTILDLLLAETQPKKICSQIGLCAYDGTHGVSMGIESVVDKENTRSSSGLRDAGCPACEMAVVWIQSQLRQNMTQERIVNYINEICERMPSPNGESAVDCSQLSKMPTVSFTIGGKVFDLAPEEYVLKIGEGPVAQCISGFTALDIPPPRGPLWILGDVFMGKYHTVFDFGNEQVGFAEAV
Protein: Probable 3-ketoacyl-CoA thiolase (EC 2.3.1.16) (Hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta 1) (P34255)
Organism: Caenorhabditis elegans
Function: Mitochondrial enzyme that catalyzes reactions of the mitochondrial beta-oxidation pathway.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P55084}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Hydroxymethylglutaryl-CoA synthase
- Enoyl-CoA Hydratase
- Enoyl-CoA Hydratase
- Probable 3-hydroxyacyl-CoA dehydrogenase B0272.3
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Probable 3-hydroxyacyl-CoA dehydrogenase F54C8.1
- 3-hydroxyacyl-CoA dehydrogenase
- Delta
Sequence:
MLRAVSTSFGTARAASAVAKKNMPNIVLVDAVRTPFVVSGTVFKDLMAVDLQKEAIKALVEKTKLPYEQLDHIICGTVIQECKTSNIAREAALLAGVPDKIPAHTVTLACISSNVAMTTGMGMLATGNANAIIAGGVELLSDVPIRYNRNARKAMLGMNKAKDVPSKLKIGGQIVKNLLSPELPAVAEFSTGETMGHSGDRLAAAFNVSRREQDEFAIRSHTLASEAAKNGKFTDVVPVFLDGKKPKTIKEDNGIRVSTLEKLSSLKPAFVKPHGTVTAANASYLTDGASAALIMTEEYALANGYKPKAYLRDYLYVAQDPKDQLLLSPAYVIPKLLDKAGLTLKDVDVFEIHEAFAGQVLANLNAMDSDYFCKEQMKRSGKFGRVPMDKLNLWGGSLSIGHPFGATGVRLATHSAHRLKEEKGQYAVIAACAAGGHGVGMLIEAYGK
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15) (Q8CGK3)
Organism: Mus musculus (Mouse)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:12657466}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- ATP-dependent clpX-like chaperone, mitochondrial
- 60 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Mitochondrial disaggregase
- 10 kDa heat shock protein, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- DnaJ homolog subfamily A member 3, mitochondrial
Sequence:
MAASTGYVRLWAAARCWVLRRPLLAVTGGRVPSASGSWLRRGCRACDMSAPWGGRVLPGGVQWRGLWDSGNRGGSDETSEGGAEDGATASTGEGPVVTALAPMTVPDVFPHLPLIAITRNPVFPRFIKIVEVKNKKLVELLRRKVRLAQPYVGVFLKRDDNNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVTGHRRIHISRQLEVEPEGLEPEAEKQKSRRKLKRGKKEVEDELGPKPQLEMVTEAATDTSKEVLMVEVENVAHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNILKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLRELVVPKHVMDVVDEELSKLALLDNHSSEFNVTRNYLDWLTSIPWGRQSDENLDLARAQAVLEEDHYGMEDVKKRVLEFIAVSQLRGSTQGKILCFHGPPGVGKTSIARSIARALGREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLVLIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVIDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARTLCGLDESKAQLSAAVLTLLIKQYCRESGVRNLQKQVEKVLRKAAYKIVSGEAQTVQVTPENLQDFVGKPVFTVERMYEVTPPGVVMGLAWTAMGGSTLFVETSLRRPQPSGSKEDKDGSLEVTGQLGDVMKESARIAYTYARAFLMEQDPENDFLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLALGQPVLQNLAMTGEVSLTGKVLPVGGIKEKTIAAKRAGVTCIILPAENRKDYSDLAPFITEGLEVHFVEHYRDIFPIAFPRREHREALAVER
Protein: Cell division cycle-associated protein 2 (Q14B71)
Organism: Mus musculus (Mouse)
Function: Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Present in nucleoplasm throughout the G1, S and G2 stages of the cell cycle. During M phase, it becomes diffuse throughout the cell as the nuclear membrane breaks down, and faintly accumulates later on metaphase chromatin. As the cell progresses to anaphase, it accumulates on chromatin (By similarity). {ECO:0000250}.
Interaction partners:
- Kinesin-like protein KIF11
- Cell division cycle-associated protein 3
- Kinesin-like protein KIF2C
- Kinetochore protein Nuf2
- Borealin
- Chromosome-associated kinesin KIF4
- SKA complex subunit 3
- Dual specificity protein kinase TTK
- Disks large-associated protein 5
- Mis18-binding protein 1
Sequence:
MDASSHDKPLSESKECVLNNSENDVFRLGTEPFVTPQKHVADATPNLCTPDTFKSPLDFTTVTVEQLGITPESFVKTSSGKSTSSLQKARRRSTVGVRGSPETNCLIRFIAQQRNLKKAVLSPLAREPHFEGSPRLYRNASVLRERMSAFRSAFHSIQETKMASSPSAAEADGESRISDLTRKEDLLEYQQSGFPVNSSSKRRRISSQDSPDNYLSGTKALADEACAGGASTDLAEKSPDIGSAQPGCMAAPLPELRETSQGLAVTDCVEGPVTPLSSGTATATRSPETPMCGSSSPSAKTTATRSPATPVCGSSTPSAKTFVLRSVLKKPGKLFSENGKESNLCDDGAHLISYPSNSCKEGRAGRENCKTPGCLNPRKRKRVTFGEDLSPEVFDESLPANTPLCKGGTPVRPRTVKTTSPLQSPVHEQFLQPNFDDKEENLENIEPPQGSFANLSLSKSSLSETPPGTNTCSSLNKDEEIICSIVRPTRTSQRRKQTLSSTGVCSSYTTQAEPRKEKMSRRKSREKKHTSAALPKKKQVLKSYRKKKKGKKDVEKCFYGPRDIASKKPLLSPIPELPEVSEATPLADCTQGTSSDDFNKCGQLEEVNSFEIPTQRKRRLPQKADSPELDPAHHQSQVSDKCCYLLPLTTASERGPNASTRDTGSEGNTRAESKCQSAKEPKPGTKMESGLVPRASVTQDHIVSKNPKPLGSPQSQDLFKAGQNLENPCEILIVSESMNLKCEKESECLAPQGSLQGSPVSTDSKRDLNCSEDVLIQNIKEPASHSENVGRKCAGNGSPGSGRERKWRRRTVCCGGQSSYLEQNGNPASSCSGENFVEISLESVQLIEELSNTIEQSFQRTSSKTKVRRSTRLQRDLENTGLVWLSPSPSTLQKPRRRMTICTLDSRGFECPSSKEETISSGQNPGPLPAVSGSESQGVGSSALPRKRRSLCGSTLTDANSATQPPDCKRKPSLKGESAQLP
Protein: Rib72 protein-like protein (Q38AJ5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- CFA20 domain-containing protein
Sequence:
MTDRTIYDALPKLPGFSFPELNPPPTNGIPQLCTIRKGIRTVFDPSGSSKRSEKQGGDGCGGLQPAQIFAKFPDWKSLDDKALRFFGYYVERVDESSIEKMRVRKVKMYLHLSDGSISVYETPAVVNSGLRRGLTVSRTIIDGVGVRSLFVGSVVNIRGLQYHIVDCDGATREFCEAMGIPQAEPLDYPSDTFEQSVLVQRNPKDELHVDLRHNVEVMAATAAGTHVSLLTPEERETARNFFEHDREVLRFAATWEQRAFKLLYYIADKTMSVMVESVRNDGRDPNPVFIRRTKIPKYPVTRVKETETLNVPLTRPVEYITEDDLQTGQTINLMTREFYIYDCDKFTRDYYAAKGVGQPSFPKPKTESDSLMPTVKPSKQPTKPTARKEARGVSTMTFEDTVVEKDRLKLIHYCNDVFRFAARLVSDRYEDEGRKFLFCYYLADDTVGMYEIPVHNSGHLGGKCFARSPVAEIPEPSKLYVGAKVKLAGAEYELIDMDERTKRYIEMGFPHMDESYFSTQELIGHVKNVIFQRFSNVTDAFRHFKSREEGLTGEDLKRLFLECGRRLDAAEFDRVMASVDKDNDQIISMTEFCENLLCQQFLSDFSQTKDNGLPNVSGPLRSQQDLEAYKNREKEAHEALRNLISCVEARRTLLIRAFQQEANASYDGNLAMEDFKRALTERMGLTFTDKQMDSLIFKFYSVPGTTDWSRRRLPLKEIKRLIMF
Protein: Dihydrolipoamide dehydrogenase, point mutation (EC 1.8.1.4) (Q57YU0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- pyruvate dehydrogenase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase, putative
- 3-methyl-2-oxobutanoate dehydrogenase
- 2-oxoisovalerate dehydrogenase subunit alpha
- Aminomethyltransferase
- oxoglutarate dehydrogenase
Sequence:
MLRHTRFSFTHQRPHLVHWQSLGKTHFDVCVIGAGPAGIAAALRAVDYNKRVCLVEAKRIGGCDLWNGTLQSKTLWEMSNFLGRARGSSAERVYGTTISNFMELDDERMLQTLQEVSETREKQVLSALSASNVALLYGRAAFASPHELEVSSREAKEYRTVTADYFIIATGSVPVTQPHVPVDHKNVVTSDDLMTLPLPKSMVVVGGGALGSEFATTYGRLGKTKVFLLDKKERIMPKEDDDVAATIQKGMEKHGVEVHQDCLLYSLQSLTKSESDGQETPNDGTSGNGVRYTIMHRKTHELQTYEVERALIVTGRRPNYFGLGLRNTNCEVRDGVLVLDEFGRCVNQKHIYAVGDATGRDRSVSMGEAKGRLAVDHIYSPHITEPLHPDHSRIVFLDTAVASVGKNEKQCREKNVSYVVAKYGFELCSRNVAASNTEGFVKILASNDSKKTLLGVHVVGWSASTIVEFATAAIQRKQSAYELSEMLTAYPSVSQAFLECLRVILGTSMLKPGTFPGLVCNTWTPSDCERGRGYCSLGNAQGGGKQ
Protein: B-box zinc finger protein 32 (EIP6, EMF1-INTERACTING PROTEIN 6) (Q9LJB7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Repressor of light-mediated regulation of seedling development. Functions by suppressing the activities of positive cofactors like BBX21 and HY5 involved in modulating light-regulated gene expression and growth.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9LQZ7}.
Interaction partners:
- Zinc finger protein CONSTANS-LIKE 3
- B-box zinc finger protein 19
- B-box zinc finger protein 24
- Zinc finger protein CONSTANS-LIKE 15
- B-box zinc finger protein 21
- B-box zinc finger protein 25
- B-box zinc finger protein 18
- B-box zinc finger protein 20
- Transcription factor HY5
- Zinc finger protein CONSTANS-LIKE 5
Sequence:
MVSFCELCGAEADLHCAADSAFLCRSCDAKFHASNFLFARHFRRVICPNCKSLTQNFVSGPLLPWPPRTTCCSESSSSSCCSSLDCVSSSELSSTTRDVNRARGRENRVNAKAVAVTVADGIFVNWCGKLGLNRDLTNAVVSYASLALAVETRPRATKRVFLAAAFWFGVKNTTTWQNLKKVEDVTGVSAGMIRAVESKLARAMTQQLRRWRVDSEEGWAENDNV
Protein: Clathrin assembly protein AP180 (Q9U6M6)
Organism: Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii)
Interaction partners:
Sequence:
MSGQSIMDRVNAARHSISGQGLAKSVCKATTEEIMGPKKKHLDYLVQCTNEPNVSIPHLADLLIERTQHGNWVVVFKALIAVQNLMNFGNERFTQYLASNNCSFNLNSFLDKGGVQAEMAPQQPIPGSPDFHAMKQGYDMSTFIRRYAKYLNEKAISYRLMAFDFCKIKRGKEDGTLRTMNAEKLLKTLPVLQKQMDALLEFDCTPNELTNGVVDACFLLLFKDLIRLFACYNDGIINLLEKYFDMNKKQCKEALDIYKKFLVRMDKVSEFLKVAENVGIDKGDIPDLARAPSSLLDALEQHYASLEGKKLPASTSKPAGFTAALNTMADQNLGFSGVSDEEKKKMLDDENQRLNQMKSTEFSETTSTTSEQRIKELNQVSPAASPHHQPTTFAPTNPFISAAASTTDPASDLLLDTGVAAPSKPIDDLLGLSTTSTNPFADSLPATAVSPGQPSTMTSMGWGAQPTASPAISAANHAGVMDIISPSNAAATSASPLAATLAPSPTPVPPTVHTELDDLLDPLDSLDPLAPIRPVSPAFARPVSPAIVPPASPVVNRPVSPAAGSTFNPPVSPSTAAFNPPASPSASGFRPPASPSAQRSVTPTFMDTLDTGFNAFGDVLQPQTKTPQKKEPVKLIQGDLDLSLAQMAASLNISGPASQVKKTEHQWQPKGEQKKTGGAGWTAPVMSSSTTWSMNQPAQQPVGLSPTAQPSGGPRMPASGLAGTDLFGVQPPTTQSQSSSQSQPNDPFGAL
Protein: Methionine-R-sulfoxide reductase B1 (EC 1.8.4.12) (EC 1.8.4.14) (Selenoprotein X) (A8MYR2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFCSFFGGEVFQNHFEPGVYVCAKCGYELFSSRSKYAHSSPWPAFTETIHADSVAKRPEHNRSEALKVRGHRGGGGTGAARESREPVPPSSLCLPHSSRGLEASIPGLLPLPGSCHPRLSGEPGLLVQMWETGQVSCTGSRTKVNLLCRRSAWEIGVWEETPSASPSKGLHCGCIMARSSPSCLVIFPGVLWQVWQWVGPRVPERRPQAGAVPILNIQQLAEVCP
Protein: WW domain-binding protein 11 (WBP-11) (Splicing factor that interacts with PQBP-1 and PP1) (Q923D5)
Organism: Mus musculus (Mouse)
Function: Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity.
Subcellular location: Nucleus. Cytoplasm. Note=Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin.
Interaction partners:
- Polyglutamine-binding protein 1
- Serine/arginine repetitive matrix protein 1
- Pre-mRNA-splicing factor 38A
- Transcription elongation regulator 1
- Spliceosome-associated protein CWC15 homolog
- Zinc finger matrin-type protein 2
- Pleiotropic regulator 1
- Thioredoxin-like protein 4A
- Cell division cycle 5-like protein
- Ubiquitin-like protein 5
Sequence:
MGRRSTSSTKSGKFMNPTDQARKEARKRELKKNKKQRMMVRAAVLKMKDPKQIIRDMEKLDEMEFNPVQQPQLNEKVLKDKRKKLRETFERILRLYEKENPDIYKELRKLEVEYEQKRAQLSQYFDAVKNAQHVEVESIPLPDMPHAPSNILIQDIPLPGAQPPSILKKTSAYGPPARAVSILPLLGHGVPRLPPGRKPPGPPPGPPPPQVLQMYGRKVGFALDLPPRRRDEDMLYSPELAQRGHDDDMSSTSEDDGYPEDMDQDKHDDSTEDSDTDRSDAESDGDEFGHREDSERDNTEEKKSGLSVRFADMPGKSRKKKKNMKELTPLQAMMLRMAGQEIPEEGREVEEFSEEEDADDSDDSEAEKQSQKQHKDDGHSDSTAAASSQQQAPPQSAPASQIQAPPMPGPPPLGPPPAPPLRPPGPPTGLPPGPPPGAPPFLRPPGMPGIRGPLPRLLPPGPPPGRPPGPPPGPPPGLPPGPPPRGPPPRLPPPAPPGIPPPRPGMMRPPLVPPLGPAPPGLFPPAPLPNPGVLSAPPSLIQRPKADDASAATIEKKATATISAKPQITNPKAEVTRFVPTALRVRRENKGATAVPQRRSEDDSAVPVAKAAPRSGPSVAVSVQTKDDVYEAFMKEMEGLL
Protein: Meis homeobox 1 (A0A8I6GI80)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MAQRYDDLPHYGGMDGVGIPSTMYGDPHAARSMQPVHHLNHGPPLHSHQYPHTAHTNAMAPSMGSSVNDALKRDKDAIYGHPLFPLLALIFEKCELATCTPREPGVAGGDVCSSESFNEDIAVFAKQIRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDDREGGSKSDSEDVTRAANLTDQPSWNRDHDDTASTRSGGTPGPSSGGHTSHSGDNSSEQGDGLDNSVASPSTGDDDDPDKDKKRHKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGKSPLVTVFKSGKRKPTSSHSPGGLLPVSQGTPYNPDGQPMGGFVMDGQQHMGIRAPGPMSGMGMNMGMEGQWHYM
Protein: Serine palmitoyltransferase small subunit A (Small subunit of serine palmitoyltransferase A) (ssSPTa) (Q969W0)
Organism: Homo sapiens (Human)
Function: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. Plays a role in MBOAT7 location to mitochondria-associated membranes (MAMs), may me involved in fatty acid remodeling phosphatidylinositol (PI).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23510452}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 2
- ORM1-like protein 3
- Serine palmitoyltransferase 3
- Serine palmitoyltransferase small subunit B
- Palmitoyltransferase ZDHHC9
- Golgin subfamily A member 7
- ORM1-like protein 1
- ORM1-like protein 2
Sequence:
MAGMALARAWKQMSWFYYQYLLVTALYMLEPWERTVFNSMLVSIVGMALYTGYVFMPQHIMAILHYFEIVQ