wanglab/gogpt-training-data huggingface dataset:
Protein: Complement component C9 (A0SEG9)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}. Target cell membrane {ECO:0000256|ARBA:ARBA00004276}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004276}.
Interaction partners:
Sequence:
MRVRRRFTFAVCILEISILSAGPTPSYHPKPVDCNGTPSPIDCRMSPWGEWSRCDPCLKQMFRSRSIETFGQFNGQKCVDAVGDRRQCVPTEPCEDLEEDCGSDFQCGTGRCIKRRLLCNGDNDCGDFSDEDDCDSDPRPPCRERVVEESELARTAGYGINILGMDPLTTPFDNEYYNGLCDRVRDGNTLTYYRKPWNVAALIYETKVDKNFRTEYHERQIQVLKTIIEEKKSNFNADLTIKFTPTEAIEQLKSKNVELANEENSNPMNNKAHFRFTYSKTETYKLLLSYSSKKEKIFLHVKGVIHLGRFVMRKRDVMLTKTFLDDVKYLPSTYEKGEYFAFLETYGTHYSSSGSLGGLYELIYVLDKATMTEKGIELRDVHRCLGFNLDLSLNFGVEIKGKIDSENCLKRGDGKTENIMNDDFIDDVISFIRGGTRKYATELKEKLLKGAKMINVTDFVNWASSLNDAPVLINQKLSPIYDLIPVKLNDAHLKRQNLERAIEDYINEFNVRKMPTVPEWRDSDSAGWTVFVFLPKQISGNCL
Protein: Protein translocation protein SEC63 (Protein NPL1) (Sec62/63 complex 73 kDa subunit) (P14906)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC63 may affect SEC1-polypeptide interactions by increasing the affinity of targeting pathways for SEC61 and/or by modifying SEC61 to allow more efficient polypeptide interaction. May also be involved in SRP-dependent cotranslational translocation. Is essential for cell growth and for germination.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein.
Interaction partners:
- Protein transport protein SEC61
- Translocation protein SEC72
- Translocation protein SEC62
- Protein transport protein SSS1
- Translocation protein SEC66
- Protein transport protein SBH1
- Endoplasmic reticulum chaperone BiP
- Heat shock protein 70 homolog LHS1
- ER-localized J domain-containing protein 5
- Protein transport protein SBH2
Sequence:
MPTNYEYDEASETWPSFILTGLLMVVGPMTLLQIYQIFFGANAEDGNSGKSKEFNEEVFKNLNEEYTSDEIKQFRRKFDKNSNKKSKIWSRRNIIIIVGWILVAILLQRINSNDAIKDAATKLFDPYEILGISTSASDRDIKSAYRKLSVKFHPDKLAKGLTPDEKSVMEETYVQITKAYESLTDELVRQNYLKYGHPDGPQSTSHGIALPRFLVDGSASPLLVVCYVALLGLILPYFVSRWWARTQSYTKKGIHNVTASNFVSNLVNYKPSEIVTTDLILHWLSFAHEFKQFFPDLQPTDFEKLLQDHINRRDSGKLNNAKFRIVAKCHSLLHGLLDIACGFRNLDIALGAINTFKCIVQAVPLTPNCQILQLPNVDKEHFITKTGDIHTLGKLFTLEDAKIGEVLGIKDQAKLNETLRVASHIPNLKIIKADFLVPGENQVTPSSTPYISLKVLVRSAKQPLIPTSLIPEENLTEPQDFESQRDPFAMMSKQPLVPYSFAPFFPTKRRGSWCCLVSSQKDGKILQTPIIIEKLSYKNLNDDKDFFDKRIKMDLTKHEKFDINDWEIGTIKIPLGQPAPETVGDFFFRVIVKSTDYFTTDLDITMNMKVRDSPAVEQVEVYSEEDDEYSTDDDETESDDESDASDYTDIDTDTEAEDDESPE
Protein: Transcription factor MYB41 (Myb-related protein 41) (AtMYB41) (Q9M0J5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in salt stress response. Confers tolerance to salt stress. Involved in distinct cellular processes in response to osmotic stress, including control of primary metabolism and negative regulation of short-term transcriptional responses to osmotic stress. Can activate the steps necessary for aliphatic suberin synthesis and deposition of cell wall-associated suberin-like lamellae. Involved in the production of aliphatic suberin under abiotic stress conditions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Cytochrome P450 86B1
- Omega-hydroxypalmitate O-feruloyl transferase
- Glycerol-3-phosphate acyltransferase 5
- Probable fatty acyl-CoA reductase 5
- Cytochrome P450 86A1
- Ethylene-responsive transcription factor WIN1
- ABC transporter G family member 6
- 3-ketoacyl-CoA synthase 2
- Wall-associated receptor kinase-like 4
- Probable fatty acyl-CoA reductase 4
Sequence:
MGRSPCCDKNGVKKGPWTAEEDQKLIDYIRFHGPGNWRTLPKNAGLHRCGKSCRLRWTNYLRPDIKRGRFSFEEEETIIQLHSVMGNKWSAIAARLPGRTDNEIKNHWNTHIRKRLVRSGIDPVTHSPRLDLLDLSSLLSALFNQPNFSAVATHASSLLNPDVLRLASLLLPLQNPNPVYPSNLDQNLQTPNTSSESSQPQAETSTVPTNYETSSLEPMNARLDDVGLADVLPPLSESFDLDSLMSTPMSSPRQNSIEAETNSSTFFDFGIPEDFILDDFMF
Protein: Actin-binding LIM protein 3 (abLIM-3) (Actin-binding LIM protein family member 3) (O94929)
Organism: Homo sapiens (Human)
Function: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Actin-binding Rho-activating protein
- Actin-binding LIM protein 1
- Cell division control protein 42 homolog
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
Sequence:
MNTSIPYQQNPYNPRGSSNVIQCYRCGDTCKGEVVRVHNNHFHIRCFTCQVCGCGLAQSGFFFKNQEYICTQDYQQLYGTRCDSCRDFITGEVISALGRTYHPKCFVCSLCRKPFPIGDKVTFSGKECVCQTCSQSMASSKPIKIRGPSHCAGCKEEIKHGQSLLALDKQWHVSCFKCQTCSVILTGEYISKDGVPYCESDYHAQFGIKCETCDRYISGRVLEAGGKHYHPTCARCVRCHQMFTEGEEMYLTGSEVWHPICKQAARAEKKLKHRRTSETSISPPGSSIGSPNRVICAKVDNEILNYKDLAALPKVKSIYEVQRPDLISYEPHSRYMSDEMLERCGYGESLGTLSPYSQDIYENLDLRQRRASSPGYIDSPTYSRQGMSPTFSRSPHHYYRSGPESGRSSPYHSQLDVRSSTPTSYQAPKHFHIPAGDSNIYRKPPIYKRHGDLSTATKSKTSEDISQTSKYSPIYSPDPYYASESEYWTYHGSPKVPRARRFSSGGEEDDFDRSMHKLQSGIGRLILKEEMKARSSSYADPWTPPRSSTSSREALHTAGYEMSLNGSPRSHYLADSDPLISKSASLPAYRRNGLHRTPSADLFHYDSMNAVNWGMREYKIYPYELLLVTTRGRNRLPKDVDRTRLERHLSQEEFYQVFGMTISEFDRLALWKRNELKKQARLF
Protein: Pyridoxal dependent decarboxylase domain containing 1 (H3BQ54)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSILEGCRREVRRETWKPGPGSEAAGKSLVNNPPGILPPSPAHVREGRRGAQIADPTLAEMGKNLKEAVKMLEDSQRRTEEENGKKLISGDIPGPLQGSGQDMVSILQLVQNLMHGDEDEEPQSPRIQNIGEQGHMALLGHSLGAYISTLDKEKLRKLTTRILSDTTLWLCRIFRYENGCAYFHE
Protein: Tubulin polymerization-promoting protein (TPPP) (EC 3.6.5.-) (25 kDa brain-specific protein) (TPPP/p25) (p24) (p25-alpha) (O94811)
Organism: Homo sapiens (Human)
Function: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath. Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath. Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes. Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear. In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network. Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6. Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility. Plays a role in cell proliferation by regulating the G1/S-phase transition. Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2.
Subcellular location: Golgi outpost {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17105200}. Nucleus {ECO:0000269|PubMed:18028908}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22328514}. Note=Specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity). Mainly localizes to the cytoskeleton (PubMed:18028908). Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences (PubMed:18028908). Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies (PubMed:15590652, PubMed:17027006). During mitosis, colocalizes with LIMK2 at the mitotic spindle (PubMed:22328514). {ECO:0000250|UniProtKB:D3ZQL7, ECO:0000269|PubMed:15590652, ECO:0000269|PubMed:17027006, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:22328514}.
Interaction partners:
- Dynactin subunit 2
- Dynactin subunit 1
- Alpha-synuclein
- F-actin-capping protein subunit alpha-2
- F-actin-capping protein subunit alpha-1
- Actin-related protein 10
- Actin-related protein 3C
- Actin-related protein 3B
- Protein deacetylase HDAC6
- Dynactin subunit 4
Sequence:
MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
Protein: Structural maintenance of chromosomes protein (A0A384MR33)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
Interaction partners:
Sequence:
MGFLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEDSVSGSQRISSIYAREALIEIDYGDLCEDLKDAQAEEEIKQEMNTLQQKLNEQQSVLQRIAAPNMKAMEKLESVRDKFQETSDEFEAARKRAKKAKQAFEQIKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTCNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ
Protein: Spermidine transporter DUR31 (A0A1D8PNR5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- GATA-type domain-containing protein
- tRNA
- Glycerophosphocholine acyltransferase 1
- Uncharacterized protein
- Dur32p
- Trifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase/thiaminase
- Phosducin domain-containing protein
Sequence:
MAQLSSQGNNAIIYLSYAFMLATGLFLAWKFSSNKDFLSSNGTQRGIPLALNFVASAMGVGIITTYAQIANIAGLHGLLVYTICGAIPIVGFAVVGPVIRRKCPDGFILTEWVRHRFGMVTALYLSAFTCLTMFLFMVGELSAIRSAIETLTGLNALGAVIVECVVTTIYTFFGGFRVSFITDNFQGVCVLLLLIICAAGMGSYIEIDTSKIGPSGLLKANKLGWQLVYILFVAIVTNDCFMSGFWLRTFASKTDKDLWIGTSIAAFVTFAICTLIGTTGFLAVWSGDLIVGDENGYDAFFILLSKMPRWLVAFVLIFCIVLSTCTFDSLQSAMVSTISNDVFRNKLHINYVRIMLILIMVPIVVLAVKVADNILQIYLIADLVSAAIIPSVFLGLADTWFWYLRGFDVMAGGLGALLGVFIFGTVYYHSAREGGKLLLIWNGLYDSSDWGPFGAFVIAPVGGVIITLASAALRIAVLYAYSKVTGKEFTALDKPVTVEVENQDHTYGSIDDDESDTKKVV
Protein: Patched-related, isoform D (A0A0B4KED8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTCGISCVDKTLNKSFYHLGICIAKHPGYFIIIPVLLTLLCMTGYQQLKYQIDPEYLFSPIAGEGKTERAIVEQYFKVNYTHRFNVGRITRPGY
Protein: Transcription factor CPC (Protein CAPRICE) (O22059)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Determines the fate of epidermal cell differentiation. Represses trichome development by lateral inhibition. Together with GL3 or BHLH2, promotes the formation of hair developing cells (H position) in root epidermis, probably by inhibiting non-hair cell formation. Represses the expression of GL2 and WER in H cells. Positively regulates stomatal formation in the hypocotyl.
Subcellular location: Nucleus {ECO:0000269|PubMed:16291794}. Note=Moves from developing non-hair cells (atrichoblasts) to developing hair cells (trichoblasts).
Interaction partners:
- Transcription factor EGL1
- Transcription factor GLABRA 3
- Uncharacterized protein At2g30430
- Homeobox-leucine zipper protein GLABRA 2
- Transcription factor GTE2
- Probable F-box protein At2g36090
- Protein TRANSPARENT TESTA GLABRA 1
Sequence:
MFRSDKAEKMDKRRRRQSKAKASCSEEVSSIEWEAVKMSEEEEDLISRMYKLVGDRWELIAGRIPGRTPEEIERYWLMKHGVVFANRRRDFFRK
Protein: ORC1-type DNA replication protein 3 (Q97WM8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Involved in regulation of DNA replication. May play essential roles in origin recognition and cell cycle control of replication. Binds to DNA, with a preference for molecules that contain a bubble, a fork, or a tail. Inhibits the binding of the MCM helicase to the origin DNA and inhibits its DNA helicase activity. Also regulates the DNA polymerase and the nuclease activities of PolB1. Inhibits the DNA-binding activity of Cdc6-1 and Cdc6-2.
Interaction partners:
- Minichromosome maintenance protein MCM
- DNA primase large subunit PriL
- ORC1-type DNA replication protein 1
- DNA primase small subunit PriS
- DNA polymerase 1
- Single-stranded DNA binding protein Ssb
- Flap endonuclease 1
- DNA primase DnaG
- DNA polymerase 2
Sequence:
MHVIRETLKGGKGEVIKNPKVFIDPLSVFKEIPFREDILRDAAIAIRYFVKNEVKFSNLFLGLTGTGKTFVSKYIFNEIEEVKKEDEEYKDVKQAYVNCREVGGTPQAVLSSLAGKLTGFSVPKHGINLGEYIDKIKNGTRNIRAIIYLDEVDTLVKRRGGDIVLYQLLRSDANISVIMISNDINVRDYMEPRVLSSLGPSVIFKPYDAEQLKFILSKYAEYGLIKGTYDDEILSYIAAISAKEHGDARKAVNLLFRAAQLASGGGIIRKEHVDKAIVDYEQERLIEAVKALPFHYKLALRSLIESEDVMSAHKMYTDLCNKFKQKPLSYRRFSDIISELDMFGIVKIRIINRGRAGGVKKYALVEDKEKVLRALNETFEDSISIGDFDDVGEN
Protein: Alpha-mannosidase (EC 3.2.1.-) (Q8IPB7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSAKTSVWLVFFCALGCLIHDADLRSIQPKASQCGYQSCHPTKPNMLNVHLVAHTHDDVGWLKTVDQYYYGSETKIQKAGVQYIIDSVVEALLRDPEKRFIYVESAFFFKWWKEQKPKVQEAVKMLVEQGRLEFIGGAWSMNDEATTHYQSVIDQFSWGLRLLNDTFGECGRPRVGWQIDPFGHSREMASMFAQMGFDGMFFGRLDYQDKDERLMTKNAEMIWHGSANLGEEADLFSGALYNNYQAPDGFCFDILCNDAPIIDGKHSPDNNVKERVDAFLAYVTEMAEHFRTPNVILTMGEDFHYQNADMWYKNLDKLIKYGNERQANGSNINLLYSTPSCYLKSLHDAGITWPTKSDDFFPYASDPHAYWTGYFTSRPTLKRFERDGNHFLQVCKQLSALAPKKPEEFDPHLTFMRETLGIMQHHDAITGTEKEKVALDYAKRMSVAFRACGATTRNALNQLTVQSKDNVKDTSAKYVFEFKTCALLNITSCPVSEANDRFALTLYNPLAHTVNEYVRIPVPYSNYRIIDNKGVTLESQAVPIPQVLIDIKHRNSTAKYEIVFLATNIPALGYRTYYVEKLDSTEGNTRSKALPKRTSSVTVIGNSHIQLGFDTNGFLSEVTADGLTRLVSQEFLFYEGAVGNNAEFLNRSSGAYIFRPNENKIHFATDQVEIEVYKGDLVHEVHQKFNDWISQVVRVYNKDSYAEFEWLVGPIPIDDGIGKEVITRFNSDIASDGIFRTDSNGREMIKRKINHRDTWSVKINEAVAGNYYPITTKIDVEDDTARMAILTDRAQGGSSLKDGSLELMVHRRLLKDDAFGVGEALNETEYGDGLIARGKHHLFFGKSTDREGVSLKGIERLTQLEKLLPTWKFFSNMEDYSADEWQTAFTNIFSGISLVLPKPVHLLTLEPWHENQLLVRFEHIMENGEDASYSQPVQFNVKNVLSAFDVEGIRETTLDGNAWLDESRRLQFAPDPEEAAFNTYATFSQPAESVHLLSAEKPMLGVKYADEALPAGQLGAESNRIRRETETRQEKKDEGRSSKSTEGPYNSFKSDSSNQEYIIELSPMEIRTFIVYLTPA
Protein: E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) (Constitutive photomorphogenesis protein 1 homolog) (hCOP1) (RING finger and WD repeat domain protein 2) (RING finger protein 200) (RING-type E3 ubiquitin transferase RFWD2) (Q8NHY2)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif (Probable).
Subcellular location: Nucleus speckle. Cytoplasm. Note=In the nucleus, it forms nuclear speckles.
Interaction partners:
- DET1 homolog
- DNA damage-binding protein 1
- Cullin-4A
- E3 ubiquitin-protein ligase RBX1
- Cullin-4B
- Cellular tumor antigen p53
- DET1- and DDB1-associated protein 1
- DNA damage-binding protein 2
- Cyclin-dependent kinase inhibitor 1B
- DDB1- and CUL4-associated factor 11
Sequence:
MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAVSAAALVSGGVAQAAGSGGLGGPVRPVLVAPAVSGSGGGAVSTGLSRHSCAARPSAGVGGSSSSLGSGSRKRPLLAPLCNGLINSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDWLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGSSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYDTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALPDGESNVLIAANSQGTIKVLELV
Protein: Synapsin III (Q17R54)
Organism: Homo sapiens (Human)
Subcellular location: Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MNFLRRRLSDSSFMANLPNGYMTDLQRPDSSTSSPASPAMERRHPQPLAASFSSPGSSLFSSLSSAMKQAPQATSGLMEPPGPSTPIVQRPRILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVRSFKPDFILVRQHAYSMALGEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVKAVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKSQSLTNSLSTSDTSQRGTPSEDEAKAETIRNLRKSFASLFSD
Protein: phosphoinositide 5-phosphatase (EC 3.1.3.36) (F1QIY4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00004580}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004146}.
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1-A
- Phosphatidylinositol 4-kinase beta
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- Phosphatidylinositol-3-phosphatase SAC1-B
- Phosphatidylinositol 4-kinase type 2-alpha
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit beta
- Si:ch211-193c2.2.
- HESX homeobox 1.
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 gamma
Sequence:
MMEPSFGISESQCIATVRGHEIRSGQKEPRLLSLLECSGQFKLDILSNPDAIVLSPVSQLSIPINNHFRIIREAEEALLIDIDSISKTVRIRLRGERTPELLLELQDDGQTQSFLEHVTKAKQQAERSSLPRKMEPVVPAPVKDCVPVPPQRGTSKSFSNNINNSTLANPSNTDSTRSLATDFGFEENFNHVLKVEEKKNKQNRLVAQREPPPPPIPPLPPRKGTNTSLTGPATKERPPSVQNATPVRNEFQSVDRSVSWSESPSNSTIRQAMMSSHAGSREGLLKYRLSKKEKEYVDIKNFKFFVGTWNVNGQSPDSSLGPWLSSDPDPPDVYALGFQELDLSTEAFFYMDSSKEQLWVDAVERGLHQKARYIQVRIIRLVGMMLVVYIKKEHKDQIREIASESVGTGLMNKMGNKGGVAVRFVFHNTSFCFVNSHLAAHVDDFERRNQDYKDICARMSFHLLEYPPVSIVKHDVVIWLGDLNYRLCLPDAGEVKRLIAEKELRRLQEYDQLNLQRKTKRVFTDFMEGEINFIPTYKYDAKSDRWDSSGKCRIPAWCDRILWRGSNVKQLHYRSHMELKTSDHKPVSSVFSIGVKMVIEQRYKKIFEEIVRDMDRMENDFLPSLSLTRREFTFENVKFRQLQRQSFLITNDGQVACTFAFIPKLNDSQYCKPWLRAEPCEGVLDPNEKIEIFLEVYVSKDSVTLLNSGEDNIEDILVLHLDRGKDYFITVSGNYLPSCFGTSLETLCRMKKPIREIPITKLIDLEKARMTFLLDSAGTEDKPLKIPKEVWLLVNHLYTKACQQEDLFQTPGLQDELQSIIDCLDTSIPDSIPGCNHSVAEALLIFLEALPEPVLCYELFQRCLECSHDSRLCKQLISQLPRAHRNVFRYLMAFLRELLKHSIDNNLNANLLATLFASLLIRPPPNLAGKQTQHDRQKANDFILGFLMAGDED
Protein: Acyl-coenzyme A thioesterase THEM4 (Acyl-CoA thioesterase THEM4) (EC 3.1.2.2) (Carboxyl-terminal modulator protein) (Thioesterase superfamily member 4) (Q5T1C6)
Organism: Homo sapiens (Human)
Function: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11598301}. Cell projection, ruffle membrane {ECO:0000269|PubMed:11598301}. Cytoplasm {ECO:0000269|PubMed:19604401}. Mitochondrion {ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19421406, ECO:0000269|PubMed:19604401}. Mitochondrion inner membrane; Peripheral membrane protein {ECO:0000269|PubMed:19168129}. Mitochondrion intermembrane space {ECO:0000269|PubMed:19168129, ECO:0000269|PubMed:19604401}. Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. {ECO:0000269|PubMed:19168129}.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- Acyl-coenzyme A thioesterase THEM5
- RAC-beta serine/threonine-protein kinase
- Peroxisomal succinyl-coenzyme A thioesterase
- RAC-gamma serine/threonine-protein kinase
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Cytosolic acyl coenzyme A thioester hydrolase
- Acyl-coenzyme A thioesterase 1
- Very-long-chain enoyl-CoA reductase
- Enolase-phosphatase E1
Sequence:
MLRSCAARLRTLGALCLPPVGRRLPGSEPRPELRSFSSEEVILKDCSVPNPSWNKDLRLLFDQFMKKCEDGSWKRLPSYKRTPTEWIQDFKTHFLDPKLMKEEQMSQAQLFTRSFDDGLGFEYVMFYNDIEKRMVCLFQGGPYLEGPPGFIHGGAIATMIDATVGMCAMMAGGIVMTANLNINYKRPIPLCSVVMINSQLDKVEGRKFFVSCNVQSVDEKTLYSEATSLFIKLNPAKSLT
Protein: Protein kinase AMP-activated non-catalytic subunit gamma 3 (D4A7E4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Calcium/calmodulin-dependent protein kinase kinase 2
- Bifunctional epoxide hydrolase 2
- Serine/threonine-protein kinase STK11
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
Sequence:
MEPELEHTLPGTLTWSHSGGPESQEMDFLEPEENSWPSPTVATSSERTCAIRGVKASRWTRQEAVEEAEPPGLGEGAQSGPAAESTRQKATFPKATPLAQAVPLADAETSTTGWDLFLPDCAASAVGSSTGDLELTIEFPGPEVWDCELKGLEQDRPRPCPSPQAPLLSLSWDDELQKPGAQIYMHFMQEHTCYDAMATSSKLVIFDTTLEIKKAFFAMVANGVRAAPLWDSKKQSFVGMLTITDFILVLHRYYRSPLVQIYEIEEHKIETWRGFSAEIYLQGCFKPLVSISPNDSLFEAVYALIKNRIHRLPVLDPVSGTVLYILTHKRLLKFLHIFGALLPRPSFLCRTIQDLGIGTFRDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEALRQRTLCLEGVLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLSPAGIDALSA