wanglab/gogpt-training-data huggingface dataset:
Protein: Growth arrest-specific protein 7 (GAS-7) (Q60780)
Organism: Mus musculus (Mouse)
Function: May play a role in promoting maturation and morphological differentiation of cerebellar neurons.
Subcellular location: Cytoplasm.
Interaction partners:
- Intersectin-2
- Intersectin-1
- Protein AF-9
- AF4/FMR2 family member 1
- Calcium load-activated calcium channel
Sequence:
MATALQKPGMVPPPPGEESQTVILPPGWHSYLSPQGRRYYVNTTTNETTWERPSSSPGISASPAPHRSSLPTTVNGYHASGTPAHPPETAHMSLRKSTGDSQNLGSSSPGRKQSKENTITINCVTFPHPDTMPEQQLLKPTEWSYCDYFWADKKDPQGNGTVAGFELLLQKQLKGKQMQKEMSEFIRERIKIEEEYAKNLAKLSQNSLAAQEEGSLGEAWAQVKKSLADEAEVHLKFSAKLHSEVEKPLMNFRENFKKDMKKCDHHIADLRKQLASRYASVEKARKALTERQKDLEMKTQQLEIKLSNKTEEDIKKARRKSTQAGDDLMRCVDLYNQAQSKWFEEMVTTTLELERLEVERVEMIRQHLCQYTQLRHETDMFNQSTVEPVDQLLRKVDPAKDRELWVREHKTGNIRPVDMEI
Protein: Glutamate decarboxylase 2 (EC 4.1.1.15) (65 kDa glutamic acid decarboxylase) (Glutamate decarboxylase 65 kDa isoform) (F1R9E8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Presynaptic cell membrane {ECO:0000256|ARBA:ARBA00037840}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037840}.
Interaction partners:
- 4-aminobutyrate aminotransferase, mitochondrial
- glutamate dehydrogenase [NAD
- Glutamate dehydrogenase 1a
- Cysteine dioxygenase type 1
- Glutamine synthetase
- Vesicular inhibitory amino acid transporter
- Glutamine synthetase
- Glutamine synthetase
- Glutamate decarboxylase 1b.
- Aldehyde dehydrogenase
Sequence:
MASHGFWFLGAENAAGNGSQSPNTPRAWCQAAAQKFSGGIGSKLCALLNVGEAEKAAQAPVKAEDESTAESCGCNKPCNCSKATACFSDLYSTDLLPALDGDAKTMNFLQEVVDILLAYIVESFDRSTKVIDFHYPNELLQRNNWELSDEPETLDDILISCRATLKYAIKTAHPRYFNQLSTGLDMVGLAADWLTSTANTNMFTYEVAPVFVLLEYVTLKKMREIIGWQDGHGDGIFSPGGAISNMYAMLLARYKMFPEVKEKGMSSVPRLVAFTSEHSHFSIKKGAAALGIGTESVICIKADERGKMIPSDLERRIIEAKQKGYVPFFVSATAGTTVYGAFDPLIAIADICKKHDVWMHVDGAWGGSLLMSRKHRWKLNGVERANSMTWNPHKMMAVPLQCSALLVREEGLMQSCNQMQACYLFQQDKHYDLQYDTGDKALQCGRHVDIFKLWLMWRAKGTIGFEAQIDKCLELSEYLYNKIKDREGYQMVFDGKPQHTNVCFWYLPPGVRYLEDKVERMKRLHKVAPVIKARMMEYGTTMVSYQPQGDKVNFFRMVISNPAATFEDIDFLIEEIERLGQDL
Protein: Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (EC 3.1.4.17) (Q64338)
Organism: Mus musculus (Mouse)
Function: Calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for cAMP and cGMP, which are key regulators of many important physiological processes. Exhibits high affinity for both cAMP and cGMP (By similarity). Modulates the amplitude and duration of the cAMP signal in sensory cilia in response to odorant stimulation, hence contributing to the generation of action potentials. Regulates smooth muscle cell proliferation. Regulates the stability of growth factor receptors, including PDGFRB (Probable).
Subcellular location: Lysosome {ECO:0000269|PubMed:29860631}.
Interaction partners:
- Calmodulin-1
- Calmodulin 5
- Calmodulin-like protein 3
- Calmodulin-4
- Calmodulin-like protein 4
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenine phosphoribosyltransferase
Sequence:
MESPTKEIEEFESNSLKHLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVDLKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRRSDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIDALKDVDTWSFDVFSLNEASGDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTVHYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENHHLSAAYRLLQEDEEMNILVNLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPEAIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKSTMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDESSQTGGTGQRRSSLNSINSSDAKRSGVKSSGSDGSAPINNSVIPVDYKSFKATWTEVVQINRERWRAKVPKEEKAKKEAEEKARLAAEEKQKEMEAKSQAEQGTTSKGEKKTSGEAKSQVNGTRKGDNPRGKNSKGEKAGEKQQNGDLKDGKNKADKKDHSNTGNESKKTDGTKKRSHGSPAPSTSSTSRITLPVIKPPLRHFKRPAYASSSYAPSVPKKTDDHPVRYKMLDQRIKMKKIQNISHHWNKK
Protein: Nuclear distribution protein nudE homolog 1 (Zgc:114109) (Q4V8W6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MSDPEPASFDSVEQERDYWKEQADKCKQRAEEAQEELQEFQQMSRDYEVELETELKQCDARNRELLTANNRLRMELENYKEKYETQHSEAVRQISTLERDLAETTAIKDQLHKYIRELEQSNDDLERAKRATIMSLEDFEQRMNHVIERNAFLESELDEKENLLESVQRLKDEARDLRQELAVQQKQERKPSISLAKDAEKPEATPARPSSVVNSALPSLLATPSRPPGSGSAFNTPSASYSRIEGLTGTPLTTSARISALDIVGELLRKVGNLESKLASCRELHIPEKTSNRALIGQSSPSIARETPEIPSNTNGLYDKGMVKRLDFGTGSKIML
Protein: Baculoviral IAP repeat-containing protein 7-A (EC 2.3.2.27) (E3 ubiquitin-protein ligase EIAP-A) (Embryonic/Egg IAP) (xEIAP/XLX) (Inhibitor of apoptosis-like protein) (IAP-like protein) (RING-type E3 ubiquitin transferase EIAP-A) (XIAP homolog XLX) (XLX) (Q8JHV9)
Organism: Xenopus laevis (African clawed frog)
Function: Weak apoptotic suppressor. Has E3 ubiquitin-protein ligase activity. Weak inhibitor of caspase activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P98170}.
Interaction partners:
Sequence:
MSRWSVSQGCGNSHKALTMAGHGEQLFRGWGMVRPSMRSEAERLRSFSAWPRTCPQPSPVEMARSGFYYLGPGDRVQCFSCGGVLRSWEPGDRPDTEHRKFFPSCTFLQQQQRDPGATDSQILGQHSGEEPDRTWESVYPEMAEERDRLDSFRNWPMYAHGNPEHLAGSGFFYTGHRDNVKCFHCDGGLRNWEQGDDPWTEHAKWFPMCDFLLHVKGEAFIRRVQESLFRSPESSPDSLGSYIYDRSPASSPGSPESWRYLQSSVAQDALQMGFKQSLVASLIQSKFLLTGSSYSSVSDLVTDLLVAEEETHSTESVSVSRAPTRMERSEPPKESAPPLSTEEQLRRLKEERMCKVCMDKDVSMLFVPCGHLVVCTECAPNLRHCPICRAAIRGSVRAFMS
Protein: Regulation of longevity by E3 ubiquitin-protein ligase (EC 2.3.2.27) (RING-type E3 ubiquitin transferase rle-1) (O45962)
Organism: Caenorhabditis elegans
Function: E3 ubiquitin-protein ligase. Regulates the activity of daf-16 and is thereby involved in regulating aging and stress resistance. Regulates nsy-1 activity and thereby attenuates the activation of sek-1 and pmk-1, two components of the p38 pathway, which results in susceptibility to pathogenic bacterial infection.
Interaction partners:
- Endoribonuclease rege-1
- Forkhead box protein O
- CCR4-NOT transcription complex subunit let-711
Sequence:
MAPTGQGGQWQEVLCCSICNRHFNETFLPVSLICGHVICRKCAEKPENQTKPCPHDDWKTTHSPSEYPNNVALLSVIFPRKQCMTLSGAVSEAEKRVDQLSIQIAKFFREADSERGGTVSSREISRTLQRKVLALLCYQWREVDGRLKTLKMCRGISERVMIEIILSIQSNTHVSSQLWSAVRARGCQFLGPAMQDDVLRLILMTLETGECIARKNLVMYVVQTLASDYPQVSKTCVGHVVQLLYRASCFNVLKRDGESSLMQLKEEFRTYESLRREHDSQIVQIAFESGLRIGPDQWSALLYADQSHRSHMQSIIDKLQSKNSYQQGVEELRALAGSQTSMLVPAYRYFLTQVIPCLEFFAGIEHEDTSMRMIGDALHQIRILLKLHCSQDDLRKMPKEERRGVILQAEVPGGMGGGPGGSGGAEAGRIGGLHPLYSQIDETGRSISRTNPKDNSHNSPQTPPKQPRQKRYQMGIPPNRMGYSSDAPPFIPSHQQQPPPQFFNSQHLPQRFRGGRQRGAPPPPPPQPMPMLIGYDMPGAPMMQATEVLTADGQMVNGTPQRVVIMQSPTHLPGGPVVMIPQQQMVPPPQSMTPVGGPMGPMGPMTPSIPVQVPPNTMWTATSPTGSVIYPAASPPGQPPHTIWIQSTDGNMFPMFDRGSGGMVWGPGTMLRESGADAEQLLAKRYEILKRLQPSEDDDDPEDGGIGHVSYTVASSVLDDRMDHHPLTMIPVPTIDLPAIPISFANMPTEETMTMIGEMVQNRPRAPSLTAPSSNQPMNVNASASATVQAECGTMSVMDSICQPISTSAIHNSATIPQPVIPMVQVPVQVPIVPAENFNPNVPPPPPPPQGQPMLVDSAIGLLTPIRPILVAHPQNVVSNSLDKIVDVKERISEAQGNASEAENAHLRMELRMAESQMAHLDPYTKNNCLLRALQQVDMELQQLHLNPTVEG
Protein: Eppin (Epididymal protease inhibitor) (Serine protease inhibitor-like with Kunitz and WAP domains 1) (Q9DA01)
Organism: Mus musculus (Mouse)
Function: Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility (By similarity).
Subcellular location: Secreted. Cell surface. Note=Present on the surface of spermatozoa both before and after capacitation.
Interaction partners:
- Lactotransferrin
- Homeobox protein Rhox5
- Seminal vesicle secretory protein 3A
- Clusterin
Sequence:
MKLSGFVSILVLFGLLARVQGPSLADLLFPRRCPRFREECEHQERDLCTRDRDCPKKEKCCVFNCGKKCLNPQQDICSLPKDSGYCMAYFRRWWFNKENSTCQVFIYGGCQGNNNNFQSQSICQNACEKKSSLT
Protein: Bonus, isoform F (A0A0B4KHG7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMDLEQLKNDFLPLIAGIKQEQLDAVPTDALPQMSTPNTASGAPTTSSLSSSSLSLSNPCDSAEKRSESNSSASAKFTLFKCVYCAQLLGSNDRPKLLECLHVACAQCVSTKFSELDRSLPPLIHCPVCDNASQQEFIVDNQFLIEQCTAGDSGDGVGLLGLTGEGQKSSAAASIQCSSCSDGAVATSWCVDCSEYICDSCVQAHQRLKITKDHTIKPKDEANNEQLAGAAGVDKLHMCQLHPQEKLSLFCETCDKLTCRDCQLSDHRDHKYKFAHEIATESRQALSTLVSEINYKRFLLSSATKVIDDRQQLIHDKKKDLIKEITAMAVKITNTVNTRGKQLIMRLNEVCDSKLKVLVEKKETLQLLSDNTDHCIDFMQNALEKGSDFAILSSKKSLVRHLQKLKCQRADIPNPEIPVRIQVQLNQVSDLQKVISQLGIIIVDGKPYPPTPSPNGTPQPQHPPRQPPSPNMAPPLRPGLPPGMPAGLSPNGPPVNFGPQNGPPLYSNAAQQQFNNLSMSRSFPGDGSVRFGGMPPVGMQRHGQPHVSSSTHPQNMDISLRGLLNNQAAQSPNAHMAFNGPPSYPGGPQGAPAPAHQPMGPQMRPHFMPGQQGFSQGGGPGGGPRDANFMNSNARFQSQYQRMANHAQQAAAAAAMAGAAGGGGGQIPSPGALQRPQMMSNPMQNVSAMQNSLGFHGSQAGFNTGPPQTSPQLGGGGMHSLAKWHIPQSAQQSNMCSQQGPLLPFANGRQTSENFKISLKSPNTLKNSTPPSLGGGGAGHQGHGNGSSSAQLNAAALGLGPAVSILSNVTSTNPKTPSPSTHENTKDFTEPIDKVRDDSINDLIATIAKLDSNGVQVLPEGRTKTTSPQVHSSTDLSNTQEDDPNEDWCAVCLDGGELMCCDKCPKVFHQNCHIPAISSLPDESESWQCLLCVNIKELTKTEGSEKSSSGELSALELRILQRICLELYCQYEQSLNFREPESPANTSYYEIVSSPMSLDVIRTRLDPSSPNHYKDIAGFVSDVRLIFSNTYLFYQDTKTYSNAKYLENFFEEQLAKWLPQFEGTKPQGKRNTSNSPALLGVNATGSPSPIENGRKSCGSASLGDSDGACLPAKRARRSAHE
Protein: MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2) (Q9HBH9)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal.
Subcellular location: [Isoform 2]: Nucleus, PML body.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
Interaction partners:
- Mitogen-activated protein kinase 1
- MAP kinase-interacting serine/threonine-protein kinase 1
- Mitogen-activated protein kinase 3
- Eukaryotic translation initiation factor 4E type 1B
- Cyclic AMP-dependent transcription factor ATF-4
- Eukaryotic translation initiation factor 4E type 2
- Mitogen-activated protein kinase 14
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4E
- Copper-transporting ATPase 1
Sequence:
MVQKKPAELQGFHRSFKGQNPFELAFSLDQPDHGDSDFGLQCSARPDMPASQPIDIPDAKKRGKKKKRGRATDSFSGRFEDVYQLQEDVLGEGAHARVQTCINLITSQEYAVKIIEKQPGHIRSRVFREVEMLYQCQGHRNVLELIEFFEEEDRFYLVFEKMRGGSILSHIHKRRHFNELEASVVVQDVASALDFLHNKGIAHRDLKPENILCEHPNQVSPVKICDFDLGSGIKLNGDCSPISTPELLTPCGSAEYMAPEVVEAFSEEASIYDKRCDLWSLGVILYILLSGYPPFVGRCGSDCGWDRGEACPACQNMLFESIQEGKYEFPDKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWVQGCAPENTLPTPMVLQRNSCAKDLTSFAAEAIAMNRQLAQHDEDLAEEEAAGQGQPVLVRATSRCLQLSPPSQSKLAQRRQRASLSSAPVVLVGDHA
Protein: Tyrosine-protein kinase receptor (EC 2.7.10.1) (F7DGW1)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Neurotrophin-4
- Neurotrophic factor BDNF precursor form
- Neurotrophin-3
- SHC-transforming protein 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Beta-nerve growth factor
- Growth factor receptor-bound protein 2
- SHC adaptor protein 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma
- Insulin receptor substrate 1
Sequence:
MSSWIRWHGPAMARLWGFCWLVVGFWRAALACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIKTLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDYGTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKDFSWFGFGKVKSRQGVGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG
Protein: Acetolactate synthase isozyme 2 large subunit (AHAS-II) (EC 2.2.1.6) (ALS-II) (Acetohydroxy-acid synthase II large subunit) (P0DP90)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the first step in the biosynthesis of branched-chain amino acids.
Interaction partners:
Sequence:
MNGAQWVVHALRAQGVNTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSIPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLEELPRIMAEAFDVACSGRPGPVLVDIPKDIQLASGDLEPWFTTVENEVTFPHAEVEQARQMLAKAQKPMLYVGGGVGMAQAVPALREFLAATKMPATCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPHASVIHMDIDPAEMNKLRQAHVALQGDLNALLPALQQPLNQYDWQQHCAQLRDEHSWRYDHPGDAIYAPLLLKQLSDRKPADCVVTTDVGQHQMWAAQHIAHTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVVCISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIHGQHITRKDQVEAALDTMLNSDGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS
Protein: Solute carrier family 13 member 5a (A0A2R8QQN0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMASRALKLVWKMKNTLILFCTPFLLLPLPLVIGSKEAGCAYVVVLMAVYWCTEVLPLAVTALLPAVLFPLFRIMESKDVCMQYLKDTNMLFLGGLMVAVAVEHWNLHKRIALRVLLLVGVRPALLMLGFMGVTAFLSMWISNTATTAMMVPIVQAVLEQLNNTAQQEQSSIPETEEKSTEKQPESPGEEKVVLNGDNFSMESDPEEHSREAEERLKMSKGLTLCVCYAASIGGTATLTGTGPNLVLMGQMSQLFPDNPDIINFASWFGFAFPNMIIMLTLAWLWLQIVFLGINFKKTWGCGTVKTEKEIAAYNVIKEEHRSLGPMTFGELSVLALFILLVVLWFTRDPGFVDGWATRFFNADKEFVTDATVAVFVAALLFVFPSKPPRLCFWRTESFDTVPQQESGPTPALLTWKVTQKKMPWSIILLLGGGFALAKGSEISGLSKWLGDQMSPLQSIPPWAIAIVICLMIATFTECTSNVATATLFLPILASMSQSIGVNPLYVMVPCTLSASFAFMLPVATPPNAIVFSYGYLKVSDMAKTGIVMNIIGILSITLAINSWGRAIFSLDTFPSWANTTDV
Protein: Small ubiquitin-related modifier 1 (SUMO-1) (SMT3 homolog 3) (Ubiquitin-homology domain protein PIC1) (Ubiquitin-like protein SMT3C) (Smt3C) (P63166)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (By similarity).
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. Nucleus speckle {ECO:0000269|PubMed:18681895}. Cytoplasm {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body {ECO:0000250|UniProtKB:P63165}. Cell membrane {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. Note=Recruited by BCL11A into the nuclear body (PubMed:18681895). In the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the nucleus some of which overlap or closely associate with PML body (By similarity). {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:18681895}.
Interaction partners:
- SUMO-conjugating enzyme UBC9
- E3 SUMO-protein ligase RanBP2
- SUMO-activating enzyme subunit 2
- Ran GTPase-activating protein 1
- Death domain-associated protein 6
- SUMO-activating enzyme subunit 1
- E3 SUMO-protein ligase PIAS2
- Small ubiquitin-related modifier 2
- Sentrin-specific protease 1
- E3 SUMO-protein ligase PIAS4
Sequence:
MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit P (Down syndrome critical region protein 5 homolog) (Phosphatidylinositol-glycan biosynthesis class P protein) (PIG-P) (Q9JHG1)
Organism: Mus musculus (Mouse)
Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Protein preY
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Dolichol phosphate-mannose biosynthesis regulatory protein
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI alpha-1,6-mannosyltransferase 2
Sequence:
MVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFVPESWLNSLGLTYWPQKYWAVALPVYLLITVVIGYVLLFGINMMSTSPLDSIHTITDNYAKNQQRKNYQEDAIPALRDVPISEVNKMFFLGAKELNT
Protein: Phospholipid-transporting ATPase VD (EC 7.6.2.1) (ATPase class V type 10D) (P4-ATPase flippase complex alpha subunit ATP10D) (Q9P241)
Organism: Homo sapiens (Human)
Function: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:30530492}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25947375}; Multi-pass membrane protein {ECO:0000255}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not that of TMEM30B. {ECO:0000269|PubMed:25947375}.
Interaction partners:
- Cell cycle control protein 50A
- Phospholipid-transporting ATPase VA
- Phospholipid-transporting ATPase VB
- Phospholipid-transporting ATPase IH
- Phospholipid-transporting ATPase IA
- Phospholipid-transporting ATPase IC
- Cell cycle control protein 50B
Sequence:
MTEALQWARYHWRRLIRGATRDDDSGPYNYSSLLACGRKSSQTPKLSGRHRIVVPHIQPFKDEYEKFSGAYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQKEITMLPLVVVLTIIAIKDGLEDYRKYKIDKQINNLITKVYSRKEKKYIDRCWKDVTVGDFIRLSCNEVIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYAEQDSEVDPEKFSSRIECESPNNDLSRFRGFLEHSNKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKAMLNNSGPRYKRSKLERRANTDVLWCVMLLVIMCLTGAVGHGIWLSRYEKMHFFNVPEPDGHIISPLLAGFYMFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSIVQCRALNIAEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENARRLESYQEAVSEDEDFIDTVSGSLSNMAKPRAPSCRTVHNGPLGNKPSNHLAGSSFTLGSGEGASEVPHSRQAAFSSPIETDVVPDTRLLDKFSQITPRLFMPLDETIQNPPMETLYIIDFFIALAICNTVVVSAPNQPRQKIRHPSLGGLPIKSLEEIKSLFQRWSVRRSSSPSLNSGKEPSSGVPNAFVSRLPLFSRMKPASPVEEEVSQVCESPQCSSSSACCTETEKQHGDAGLLNGKAESLPGQPLACNLCYEAESPDEAALVYAARAYQCTLRSRTPEQVMVDFAALGPLTFQLLHILPFDSVRKRMSVVVRHPLSNQVVVYTKGADSVIMELLSVASPDGASLEKQQMIVREKTQKHLDDYAKQGLRTLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQEGVPESIEALHKAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSKDACGMLMSTILKELQKKTQALPEQVSLSEDLLQPPVPRDSGLRAGLIITGKTLEFALQESLQKQFLELTSWCQAVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQAVMASDFAVSQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGTSMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYRSGQKSEAYLPHTFWITLLDAFYQSLVCFFVPYFTYQGSDTDIFAFGNPLNTAALFIVLLHLVIESKSLTWIHLLVIIGSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHMLDPVFYLVCILTTSIALLPRFVYRVLQGSLFPSPILRAKHFDRLTPEERTKALKKWRGAGKMNQVTSKYANQSAGKSGRRPMPGPSAVFAMKSASSCAIEQGNLSLCETALDQGYSETKAFEMAGPSKGKES
Protein: Cyclin A2 (G3V802)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-dependent kinase inhibitor 1B
- Cell division cycle protein 20 homolog
- Cyclin-dependent kinase 1
- Cyclin-dependent kinase 2
- cyclin-dependent kinase
- Cell division control protein
- Transcription factor E2F1
- Cyclin-dependent kinase 4
- S-phase kinase-associated protein 2
- Cyclin-dependent kinase inhibitor 1
Sequence:
MSTSLLFLHGKQSVNSLPSPFMWMKLKRLRRGQLSKKKLSVKMPWLLVPLSLYPEPENHWYLLIIQWMVVLIAGQTHGRQNSCYRQLCRCYDLTVETRDVESPHAMDISIVLEDEKPVNVNEVPDYHEDIHTYLREMEVKCKPKVSYMKRQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYSKKQVLRMEHLVLKVLAFDLAAPTVNQFLTQYFLHLQPANCKVESLAMFLGELSLIDADPYLKYLPSLIAGAAFHLALYTVTGQSWPESLVQKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKHSKYHSVSLLNPPETLNV
Protein: Pipsqueak, isoform D (Pipsqueak, isoform E) (Pipsqueak, isoform F) (Pipsqueak, isoform G) (Pipsqueak, isoform H) (Q0E9C8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00320}.
Interaction partners:
Sequence:
MTSLGMGMNGGLLGVPMGFLDFTPEPPAPSATPVTVTEHVDLSCNPSTDTRDLSNTTEPLDIDNHLAQQIHRLDQSPMHSISHHHTGDESNSNLVQHIKSEVIEAKHLAAQHHALSQAQQQHAHHQAHQQHQQHQQQQHQQQQQHLHAQQLLAQSQLQQQQQQQQQQQQHHQQQQQQAAAAAAAAGVHGQHGGHVTHADIGGATVMEIDPSQIKHEPGMIITPEIVNMMSSGHMDMYNSDTSEDSMMIANGSPHDQKEPHYTNLDQQHGLGGSVCGPGPGGAGGGGGMSGGAGSGSGEKGQFNGPKAWTQDDMNSALDALKNQNMSLTKASAIYGIPSTTLWQRAHRMGIETPKKEGGTKSWNEDALQNALEALRSGQISANKASKAFGIPSSTLYKIARREGIRLAAPFNAAPTTWTPEDLERALEAIRAGNTSVQKASAEFGIPTGTLYGRCKREGIELSRSNPTPWSEDAMNEALNSVRVGQMSINQAAIHYNLPYSSLYGRFKRGKYDVVANTSGVALLNTSGNTTGSIEIIEHSQENSLHMLQQQFPYSPSPHPPTPQHHSTPQHHSSAQQGPPTPQHMQQHVVHMQQQQQQQQQQSPHPGHHPQHMQQDVVTSSSQVVHSQQQQQLQQIYQHHGTPERS
Protein: Cystathionine beta-synthase (EC 4.2.1.22) (B2LXT5)
Organism: Emericella nidulans (Aspergillus nidulans)
Interaction partners:
Sequence:
MSSKTTPTVPPVALDSITQHIGNTPLVRLNKLPQNLGINATVYAKLEYFNAGGSVKDRIALRMIEEAERSGRIKPGDTLIEPTSGNTGIGLALVAAVKGYKTIITLPEKMSAEKVSVLRALNATIIRTPNEAAYDSPESHIGVAKRLEKELPNAHILDQYGNENNPLAHELGTAQEIWSQTKGQIKAIVAGAGTGGTITGLSRGLKKHNSNVQVIAADPQGSILALPAALNEEHANEPYKVEGIGYDFIPQVLDQHAVDKWYKTDDKESFQYARRLIAEEGLLVGGSSGSAIAALVKAARDNMFKEGDVVVVILPDSIRSYLTKFADDDWLAANDLLPSLPTEVILQSSNKQTQGQDDAFAGSKVSSLRLKPVTTVHSNVPCETAIEVMRDKGFDQLPVLAPSGRKLVGLVTLGNVLSRLTHNRATGRSPVADVMFDFRTISEVVTDPRDMGLASLEPNQNGRDAPKPQTRSRKFVEITMDTSLSVLNRFFEWNSAAIVTERDEGGTLRPVAVVTKVDLLTWMLHHKKNGASE