wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear migration protein nudC (Nuclear distribution protein C homolog) (G5EE74)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Lissencephaly-1 homolog
- Protein nud-2
- DNA polymerase V
- Cyclin-dependent kinase 5 activator 1
- Serine/threonine-protein kinase plk-2
- Probable elongation factor 1-gamma
- Large ribosomal subunit protein uL10
- Co-chaperone protein daf-41
- Dynein heavy chain, cytoplasmic
- Reticulocalbin-3
Sequence:
MSQYERFDSVLLSMAQQLSGGVPEMLDVLFEFLSRKTDFYSGAGVDQARTLLLEKFDKHGGKAMKEAEEAKKRKEEQERKLAERRAAQKAKEEEEFRNAKVVEVTDEEAAAFEKEQAKNSVENLEKFVDNEGETSKDAEVEDEDSKLMKPNSGNGADLAKYQWTQTLQELEVKIPIAAGFAIKSRDVVVKIEKTSVSVGLKNQAPIVDGKLPHAIKVENCNWVIENGKAIVLTLEKINDMEWWNRFLDSDPPINTKEVKPENSKLSDLDGETRAMVEKMMYDQRQKEMGLPTSDEKKKHDMLQQFMKQHPEMDFSNAKIG
Protein: RING finger protein Z (Protein Z) (Zinc-binding protein) (Q6UY62)
Organism: Sabia mammarenavirus (isolate Human/Brasil/SPH114202/1990) (SABV) (Sabi mammarenavirus)
Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
Interaction partners:
Sequence:
MGNSKSKSKLSANQYEQQTVNSTKQVAILKRQAEPSLYGRHNCRCCWFANTNLIKCSDHYICLKCLNIMLGKSSFCDICGEELPTSIVVPIEPSAPPPED
Protein: Pre-mRNA-processing protein 40A (AtPRP40a) (B6EUA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries (Probable). May be involved in pre-mRNA splicing (Probable).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
- Mediator of RNA polymerase II transcription subunit 25
- AT5g17440/K3M16_10
- Arginine-aspartate-rich RNA binding protein-like
- RNA-binding motif protein 25
- LUC7 related protein
- Pre-mRNA-processing factor 39-2
- Tetratricopeptide repeat
- ATP-dependent DNA helicase Q-like 2
- U1 small nuclear ribonucleoprotein 70 kDa
Sequence:
MANNPPQSSGTQFRPMVPGQQGQHFVPAASQPFHPYGHVPPNVQSQPPQYSQPIQQQQLFPVRPGQPVHITSSSQAVSVPYIQTNKILTSGSTQPQPNAPPMTGFATSGPPFSSPYTFVPSSYPQQQPTSLVQPNSQMHVAGVPPAANTWPVPVNQSTSLVSPVQQTGQQTPVAVSTDPGNLTPQSASDWQEHTSADGRKYYYNKRTKQSNWEKPLELMTPLERADASTVWKEFTTPEGKKYYYNKVTKESKWTIPEDLKLAREQAQLASEKTSLSEAGSTPLSHHAASSSDLAVSTVTSVVPSTSSALTGHSSSPIQAGLAVPVTRPPSVAPVTPTSGAISDTEATTIKGDNLSSRGADDSNDGATAQNNEAENKEMSVNGKANLSPAGDKANVEEPMVYATKQEAKAAFKSLLESVNVHSDWTWEQTLKEIVHDKRYGALRTLGERKQAFNEYLGQRKKVEAEERRRRQKKAREEFVKMLEECEELSSSLKWSKAMSLFENDQRFKAVDRPRDREDLFDNYIVELERKEREKAAEEHRQYMADYRKFLETCDYIKAGTQWRKIQDRLEDDDRCSCLEKIDRLIGFEEYILDLEKEEEELKRVEKEHVRRAERKNRDAFRTLLEEHVAAGILTAKTYWLDYCIELKDLPQYQAVASNTSGSTPKDLFEDVTEELEKQYHEDKSYVKDAMKSRKISMVSSWLFEDFKSAISEDLSTQQISDINLKLIYDDLVGRVKEKEEKEARKLQRLAEEFTNLLHTFKEITVASNWEDSKQLVEESQEYRSIGDESVSQGLFEEYITSLQEKAKEKERKRDEEKVRKEKERDEKEKRKDKDKERREKEREREKEKGKERSKREESDGETAMDVSEGHKDEKRKGKDRDRKHRRRHHNNSDEDVSSDRDDRDESKKSSRKHGNDRKKSRKHANSPESESENRHKRQKKESSRRSGNDELEDGEVGE
Protein: N-acetylglutamate synthase, mitochondrial (EC 2.3.1.1) (Amino-acid acetyltransferase) [Cleaved into: N-acetylglutamate synthase long form; N-acetylglutamate synthase short form; N-acetylglutamate synthase conserved domain form] (Q8R4H7)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of ureagenesis by producing the essential cofactor N-acetylglutamate (NAG), thus modulating carbamoylphosphate synthase I (CPS1) activity.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N159}.
Interaction partners:
- Argininosuccinate lyase
- Argininosuccinate synthase
- Ornithine aminotransferase, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
- Ornithine transcarbamylase, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Alanine aminotransferase 2
- Alanine aminotransferase 1
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, cytoplasmic
Sequence:
MATAWVATALRSAAAARRLRSPGGPGGSRRLSGSARRRGAKSASPGRRLSTARAHAEDAEGAKGRVQSPAVEEPSWTPLPTPLESPAPPAGRSLVQRDIQAFLNQCGASPGEARHWLTQFQTCYHSVDKPFAVMEVDEEVIRCPQAVSRLAFALAFLQRMDMKPLVVLGLPTPTAPSGCLSFWEAKAQLAQSCKVLVDELRHNAATAVPFFGGGSVLSAAEPAPHASYGGIVAVETDLLQWCLESNSIPILCPIGETAARRSVLLDSLEVTASLAKALQPTKIIFLNNSGGLRNNSQKILSNVNLPADLDLVTNAEWLSIKERQQIRLIVDVLSRLPHYSSAVITAASTLLTELFSNKGCGTLFKNAERMLRVRNLDSLDQGRLVNLVNASFGKKLREDYLESLRPRLHSIYVSEGYNAAAILTVEPVLGGTPYLDKFVVSSSRQGQGSGQMLWECLRRDLQTLFWRSRVTNPINPWYFKHSDGSFSNKQWIFFWFGLADIRDSYELVNHAKGLPDSFCKPASDPGS
Protein: Zn-finger domain protein, putative (Q580M0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDAPLQLRTLGPNGASSPQGAVEARGISDGAYVEVAHEDACGASPHRDSVEMVDSKERNSTQITRGIEPVGPSGSQNDSTTSVVADARECWICREASDTPENRLTSGLCRCRGSIGLVHTGCLNYWVFSQRRVRCPSCNATYNVISVSSEDFPKGFLHEAVLLVRHLYLPLFCKCASILLGLVINGFAIAFAVGCAFYHGEVFADAGDQAPKSFGNVGAAADLGGSTATTRANAPNGGVGGSSGVWLWVGVMLFGWCSTALWRSLWVSWGQWRAEFINDAVDDAPKPPPYTLVECLHYYFDIVVSMTGCTRQMLWLRSMELCALTAIAYIISFTYGRVLVFTLIFLGAVLMRLLFQRKKINDNMRRFDEAQERRHNATYSDLVKWFITYITEMALFSFALTIIGGLVIHYALSPHILTFPTSIPALNESITFLRLLLYWASGTLSSILLMCIETTVIVNIFAPGVDLFFVRSVDLNVDSDSAYWSFILAQIFDSDPLQVLFDFPRLALIEVVTLFAFLALPLQAMFFLNDLLATKVFGSAGIKLAWVLHNSGEYLMGNSPANGVIPPFDGSFESGWGSLQELLTEPLEVPSLVVSGLLANTLPFVKSLIHFLSSTSSINILLGAGTGVIVSCLKVFPIKRTQLRVMRAIAVWLAAHVVYMEDFLFDKERLQTLDNWLQAGGEGDVPTQRVPLAFVFLRRERVLPPEQKRPAWLKVRLIIFSAMFFIASTGVFWALPVLLAALLLLVMPCNAALLCCAFNASFLLLDYKLYLKAVGEFVFISAVLLVGLPLQLLHALRLAVNFGYPRKRLVKETFEYCLNINRTIGKYCGEPRDEQQEDVKAELGEVDSNSSDDIIAVNDDDDEDFE
Protein: VAMP-like protein YKT62 (AtYKT62) (ATGP1-like protein) (Q9LVM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the secretory pathway. Essential for membrane fusion mediated by either SYP41 or SYP61; triggers the fusion of phospholipid vesicles containing SYP41 or SYP61 and VTI12.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Syntaxin-32
- Golgi SNAP receptor complex member 1-1
- Syntaxin-31
- Tlg2p-like protein a
- Golgi SNAP receptor complex member 1-2
- Membrin-11
- Vesicle transport v-SNARE 12
- Vesicle transport v-SNARE 13
- Vesicle transport v-SNARE family protein
- Vesicle transport v-SNARE 11
Sequence:
MKITALLVLKCDPETREPVILANVSDLSQFGKFSFYRSNFEEFIVFIARTVARRTPPGQRQSVKHEEYKVHAYNINGLCAVGFMDDHYPVRSAFSLLNQVLDVYQKDYGDTWRFENSSQPWPYLKEASDKFRDPAEADKLLKIQRELDETKIILHKTIDGVLARGEKLDSLVEKSSELSLASKMFYKQAKKTNSCCTLL
Protein: Amoebiasin-1 (Cysteine protease inhibitor 1) (EhICP1) (ICP-1) (Q6KCA4)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Cysteine protease inhibitor. Inhibits cysteine proteases CP1, CP2 and CP5. May protect the cytosol against cysteine proteases released by damaged intracellular vesicles (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15757643, ECO:0000269|PubMed:16979632, ECO:0000269|PubMed:21440496}.
Interaction partners:
Sequence:
MSLTEDNNNTTITIAKGENKEIILHGNPTTGYSWVVDSCEGLSNTVEYVADQHAPGICGCGGKYHIKITGTQTGEGKIVLVYRRPWAPNANDRTFTLKVNVQ
Protein: M1-specific T cell receptor beta chain (TR beta chain TRBV19*01J2S7*01C*02) (P0DSE2)
Organism: Homo sapiens (Human)
Function: The beta chain of TRAV27*01J42*01C*01/TRBV19*01J2S7*01C*02 alpha-beta T cell receptor (TR) clonotype that is specific for HLA-A*02:01-restricted M/matrix protein 1 immunodominant epitope GILGFVFTL of influenza A virus (IAV). Classified as a public TCR clonotype, it is preferentially selected in effector memory CD8-positive T cells among multiple HLA-A*02:01 carriers/individuals and confers long-lived immunity against IAV infection. Can cross-recognize sporadically emerging IAV variants by molecular mimicry, inducing immunity toward different influenza strains. Antigen recognition initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell differentiation into effector/memory T cells (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:29997621}.
Interaction partners:
Sequence:
MSNQVLCCVVLCLLGANTVDGGITQSPKYLFRKEGQNVTLSCEQNLNHDAMYWYRQDPGQGLRLIYYSQIVNDFQKGDIAEGYSVSREKKESFPLTVTSAQKNPTAFYLCASSIRSSYEQYFGPGTRLTVTEDLKNVFPPKVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG
Protein: Voltage-dependent calcium channel subunit alpha-2/delta-2 (Voltage-gated calcium channel subunit alpha-2/delta-2) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-2; Voltage-dependent calcium channel subunit delta-2] (Q9NY47)
Organism: Homo sapiens (Human)
Function: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosis.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with CACNA1A in lipid raft fractions. {ECO:0000250}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent L-type calcium channel subunit beta-4
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent T-type calcium channel subunit alpha-1G
Sequence:
MAVPARTCGASRPGPARTARPWPGCGPHPGPGTRRPTSGPPRPLWLLLPLLPLLAAPGASAYSFPQQHTMQHWARRLEQEVDGVMRIFGGVQQLREIYKDNRNLFEVQENEPQKLVEKVAGDIESLLDRKVQALKRLADAAENFQKAHRWQDNIKEEDIVYYDAKADAELDDPESEDVERGSKASTLRLDFIEDPNFKNKVNYSYAAVQIPTDIYKGSTVILNELNWTEALENVFMENRRQDPTLLWQVFGSATGVTRYYPATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHLVQANVRNKKVFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRTVRVFTFSVGQHNYDVTPLQWMACANKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKEAKQVQWTNVYEDALGLGLVVTGTLPVFNLTQDGPGEKKNQLILGVMGIDVALNDIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQTTNFREPVTLDFLDAELEDENKEEIRRSMIDGNKGHKQIRTLVKSLDERYIDEVTRNYTWVPIRSTNYSLGLVLPPYSTFYLQANLSDQILQVKLPISKLKDFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVERVWRDQDLNTYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNHGYVFKPPHQDALLRPLELENDTVGILVSTAVELSLGRRTLRPAVVGVKLDLEAWAEKFKVLASNRTHQDQPQKCGPNSHCEMDCEVNNEDLLCVLIDDGGFLVLSNQNHQWDQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTVADFLNLAWWTSAAAWSLFQQLLYGLIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAEKPLCSQCEAGRLLQKETHSDGPEQCELVQRPRYRRGPHICFDYNATEDTSDCGRGASFPPSLGVLVSLQLLLLLGLPPRPQPQVLVHASRRL
Protein: Cytoplasmic dynein 1 light intermediate chain 2 (Dynein light intermediate chain 2, cytosolic) (LIC-2) (LIC53/55) (O43237)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}.
Interaction partners:
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynein light chain roadblock-type 1
- Dynein light chain 1, cytoplasmic
- Dynactin subunit 1
- Dynactin subunit 2
- Dynein light chain Tctex-type 1
- Dynactin subunit 6
Sequence:
MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPGAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA
Protein: Inorganic pyrophosphatase, mitochondrial (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (P28239)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in energy production. Its activity is stimulated by uncouplers of ATP synthesis.
Subcellular location: Mitochondrion.
Interaction partners:
- Inorganic pyrophosphatase
- Plasma membrane ATPase 2
- Plasma membrane ATPase 1
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit gamma, mitochondrial
- Adenylyl-sulfate kinase
- V-type proton ATPase subunit c
- V-type proton ATPase subunit D
- V-type proton ATPase subunit c''
Sequence:
MNLLRMNALTSKARSIERLKQTLNILSIRNHRQFSTIQQGSKYTLGFKKYLTLLNGEVGSFFHDVPLDLNEHEKTVNMIVEVPRWTTGKFEISKELRFNPIVQDTKNGKLRFVNNIFPYHGYIHNYGAIPQTWEDPTIEHKLGKCDVALKGDNDPLDCCEIGSDVLEMGSIKKVKVLGSLALIDDGELDWKVIVIDVNDPLSSKIDDLEKIEEYFPGILDTTREWFRKYKVPAGKPLNSFAFHEQYQNSNKTIQTIKKCHNSWKNLISGSLQEKYDNLPNTERAGNGVTLEDSVKPPSQIPPEVQKWYYV
Protein: Gamma-aminobutyric acid receptor subunit alpha-1 (GABA(A) receptor subunit alpha-1) (GABAAR subunit alpha-1) (P62813)
Organism: Rattus norvegicus (Rat)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel (By similarity). The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor exhibit synaptogenic activity (By similarity). GABRA1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000269|PubMed:30044221}. Cell membrane {ECO:0000269|PubMed:1376242, ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000269|PubMed:30044221}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25172774}. Note=The alpha-1 subunits (alpha-1-beta-2/3-gamma-2 receptors) are present in Golgi synapses and on the extrasynaptic membranes (PubMed:9464994). Mainly located in GABAergic synapses on granule cells (PubMed:9464994). {ECO:0000269|PubMed:9464994}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit beta-3
- Vesicle-fusing ATPase
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
- Gamma-aminobutyric acid type B receptor subunit 2
- Inactive phospholipase C-like protein 1
- Gamma-aminobutyric acid type B receptor subunit 1
Sequence:
MKKSRGLSDYLWAWTLILSTLSGRSYGQPSQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ
Protein: Plexin-C1 (Virus-encoded semaphorin protein receptor) (CD antigen CD232) (Q9QZC2)
Organism: Mus musculus (Mouse)
Function: Receptor for SEMA7A, for vaccinia virus semaphorin A39R and for herpesvirus Sema protein. Binding of semaphorins triggers cellular responses leading to the rearrangement of the cytoskeleton and to secretion of IL6 and IL8 (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Semaphorin-7A
- Semaphorin-4D
- Semaphorin-3E
- Semaphorin-6B
- Semaphorin-6D
- Semaphorin-3B
- Semaphorin-6A
- Semaphorin-3A
Sequence:
MEVSRRKTPPRPPYPAAPLPLIAYLLALAAPARGADEPVWRSEQAIGAIAASRADGVFVASGSCLDQLDYSLKNRLSRLYRDQAGNCTEPVSLAPPARPRPGSSFSKLLLPYREGATGLEGLLLTGWTFDRGACEVRPLGNLNRSSLRNGTEVVSCHPQGSTAGVVYRASGTDLWYLAVAATYVLPEPETANRCNPAASDRDTAIALKNTEGRSLATQELGRLKLRGSAGSLHFVDAFLWNGSVYFPYYPYNYTSGAATGWPSMARIAQSTEVLFQGQAALDCDHGHPEGRRLLLSSSLVEAVDIWAGVFSAATGEGQERRSPATTALCLFRMSEIQAHARSCSWDFQATEHNCKEGDRPERVQPIASSTLIHSDLTSVYGTVVMNRTVLFLGTGDGQLLKVVLGENLTSNCPEVIYEIKEETPVFYKLVPHPMKNIYIYLTAGKEVRRIPVANCSKRKSCSECLAAADPHCGWCLPLQRCTFQGDCTHAGSFENWLDISSGPKKCPKIQILRSLRERTTVTIVGSISARHSECVVKNADTGKLLCQGRSQLNWTCACNIPSRPSYNVLVVNATFSFPSWNLSERFNFTNCASLKECPACIRSGCAWCKRDKKCIHPFTPCEPSDYERNQELCQVAVEKSPKDSGGGRVKESKRNRTDGAVQVFYIKAIEPQKISTLGKSNVIVTGANFTQASNITMILRGTSTCERDVIRVSHVLNDTHMKFSLPSSRKEMKDVCIQFDGGTCSSAGALSYIALPHCSLIVPATTWISGGQNITIMGRNFDVIDNLIISHELKGNANVNINVSEYCAATFCRFLAPNLKSSKVRTNVAVKLRVQDTYLDCGTLQYLEDPRFTGYRVESEIDTELEVKIQKENDNFNISKDDIDITLFHGENKQFNCSFENITRNQDLTTILCKIKSIKNANTIASSSKKVRVKLGNLELYVEQESVPSTWYFLIALPILLAIVIVVAVVVTRYKSKELSRKQSQQLELLESELRKEIRDGFAELQMDKLDVVDSFGTVPFLDYKHFALRTFFPESGGFTHIFTEDMHNRDANDKNESLTALDALICNKSFLVTVIHTLEKQKNFSVKDRCLFASFLTIALQTKLVYLTSILEVLTRDLMEQCSNMQPKLMLRRTESVVEKLLTNWMSVCLSGFLRETVGEPFYLLVTTLNQKINKGPVDVITCKALYTLNEDWLLWQVPEFNTVALNVVFEKIPENESADVCRNISVNVLDCDTIGQAKEKVFQAFLSKNGSPYGLQLNEIGLELQVGTRQKELLDIDSSSVILEDGITKLNTIGHYEISNGSTIKVFKKIANFTSDVEYSDDHCHLILPDSEAFQVVQGKRHRGKHKFKVKEMYLTKLLSTKVAIHSVLEKLFRSIWSLPNSRAPFAIKYFFDFLDAQAENKKITDPDVVHIWKTNSLPLRFWVNILKNPQFVFDIKKTPHIDSCLSVIAQAFMDAFSLTEQQLGKEAPTNKLLYAKDIPTYKEEVKSYYKAIRDLPPLSSLEMEEFLTQESKKHENEFNEEVALTEIYKYIVKYFDEILNKLERERGLEEAQKQLLHVKVLFDEKKKCKWM
Protein: Quemao, isoform A (Quemao, isoform B (EC 2.5.1.29)) (RE65121p) (Q9VS54)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Farnesyl pyrophosphate synthase
- Diphosphomevalonate decarboxylase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- isopentenyl-diphosphate Delta-isomerase
- Decaprenyl diphosphate synthase subunit 2, isoform A
- Protein farnesyltransferase subunit beta
- All trans-polyprenyl-diphosphate synthase PDSS1
- Alkyl transferase
- ditrans,polycis-polyprenyl diphosphate synthase [
- Pre-mRNA-splicing factor 18
Sequence:
MEELNIILQKTKDKSTQKEQDEILLQPFTYIQQIPGKQFRSELALAFNHWLLIPGEKLAQIGDIVQMLHNSSLLIDDIEDNSILRRGVPVAHSIYGVASTINAANYALFLALEKVQQLDHPEATKVYTEQLLELHRGQGMEIYWRDSFTCPSESDYKLMTVRKTGGLFMLAIRLMQLFSSNKEDYSKLTAILGLYFQIRDDYCNLSLKEYTENKSFAEDLTEGKFGFPVIHAVRTQKQDKQVLHILRQRTHDIEVKKYCITLLEKLGSFQYTRKVLESLDAEARSEVARLGSNPYMDRLLNKLLSWKTSDSASITQSNQINHNNVSRSSPNQNTLNCN
Protein: Early transcribed membrane protein 11.1 (Q7KQK8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVTRILYFVFFIFALNFIAPNNEHNGYVEAKKKLTPAEIKKRNQKLMMYSAIASGVAVLLGASIGLGVHFSKKKSPKKKVIRQVVKKTPA
Protein: Chitin synthase csmA (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase csmA) (Class-V chitin synthase csmA) (G5EB74)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cell membrane {ECO:0000269|PubMed:15703213, ECO:0000269|PubMed:25955346}; Multi-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:15703213, ECO:0000269|PubMed:25955346}. Cell tip {ECO:0000269|PubMed:15703213, ECO:0000269|PubMed:25955346}. Note=Localization to the hyphal tips depends on conventional kinesin kinA (PubMed:15703213). Concentrates at the hyphal tips and septation sites near actin structures, which is dependent on the actin-binding ability of the N-terminal myosin motor-like domain (MMD) (PubMed:15703213). {ECO:0000269|PubMed:15703213}.
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- Chitin synthase export chaperone
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MVGTLPAGHTPSHVQSSLPSLPAHLQSDTHLTAHLASRFHVGLPTARLSSHALISLNNYTSSSKGPDGGKEGSAMGETEDLARRAYTRLGARGENQAIVFLGESGAGKTTLRSHLLSSFLSFSSTPLSSKLSYAAFIFDTLTTTKSLTTPTASKAGLFLELQYDASSSVNPTLIGGKIIDHRLERSRIASVPTGERSFHVLYYLLAGTSAAEKAHLGLDSPIHVTTAGGRLSSADHKRWRYLGHPTQLKVGINDADGFQHFKTALRKLEFPRSEIAEICQILAAILHIGQLDFGSGQATLTGAEESGGYSHEGGETVTVVKNKDVLSIIAAFLGLGVGELEASFGYRTKTIHRERVTVMLDPKGARRSADELSRVLYSLLVAYVIENVNQRICAAEDSVANTVSIIDFPGFAQACSTGSTLDQLLNNAACESLYNFCLRSFFDRKADMLEREEVAVPATSYFDNTDAVRGLLKQGNGLLSILDDQTRRGRTDAQFVEAVRRRFENKNPAITAGASGSGNGYGMVSQNARSSFTVKHFAGEVDYSATGLLEENGEVISGDLMNLMKSTRSDFVRELFGQEALQTVAHPKEKTAIMQAQVSSKPLRMPSMARRKTSPASRLTFDATPAEDPYETESQTGSSAKNSSAKRKSGMLMGGMQCAAGQFLSSLDIVNKCLTSGNLNPYFVFCLKPNDRRIANQFDSKCVRTQIQTLGIAEISQRLRNADFSVFLPFAEFLGLAEVGNVVVGSDKEKSEVVLDEKRWPGNEARVGSTGVFLSERCWADLAKVGERVIPSFAAEDDGGDALLHPRTANYADSKVRLLNPSDHSPGAYIYGDESKQASNTSRDFDGRSDAGYSAFNSGDMFHNLETREQMLEKGNEKQMEEVDEVPVSGSRKRWMAIVWLLTFYIPTPAIRYIGRMKRKDIQIAWREKFAINLLIWLACAIAVFIIVGFPSLICPTQHVYSPAELSSHDGKDGHSSYTSIRGLVLDLGEFMDSHYPGIVPDSALKKYAGVDSTALFPVQVSALCLGKDGNVDPKVLLDYKPTNFSGSVTSTSSGDPNSVYHDFRYFRDDYRPDWYAEQMIYLRANYYKGWIGYSSEYLHTLASKSQNVASINGKIYDLTSYIAGGRRIQGREGDDTTGIDTDFMDSLVVDLFQQKAGEDITKYWEDLPLTPKLRVDMMDCLNNLFIVGHVDTRNSTQCQFARYFILAISVLICSVIVFKFFAALQFGKKNVPENLDKFIICQVPAYTEDEESLRRAIDSMARMQYDDKRKLLVVICDGMIIGQGNDRPTPRIVLDILGVPESVDPEPLSFESLGEGMKQHNMGKVYSGLYEVQGHIVPFLVVVKVGKPSEVSRPGNRGKRDSQMVLMRFLNRVHYNLPMSPMELEMHHHIRNIIGVNPTFYEFILQVDADTVVAPDAATRMVSSCLNDTRIIGVCGETSLTNAKTSAVTMIQVYEYYISHNLTKAFESLFGSITCLPGCFTMYRIRSAESGKPLFVSKEIVEAYSEIRVDTLHMKNLLHLGEDRYLTTLLLKHHPKFKTKYNFRAQAYTIAPESWTVFLSQRRRWINSTVHNLVELIPLQQLCGFCCFSMRFVVFIDLISTIIMPVTVAYIVYLIVWLVRDTSTIPWTSFLLLAAIYGLQAIIFIVRRKWEMIGWMIIYILAIPVYSLALPLYSFWHMDDFSWGNTRIITGEKGRKIVISDEGKFDPASIPKKRWEEYQAELWEAQTSRDDRSEISGISYGTKYHPATQSEYGFPGSRPMSQLELPRHMSRMSLAPSEMMSRHMDMELEDVNLPSDDAILSEIRDILRTADLMTVTKKNIKQELERRFGVNLDAKRPYINSATEAVLSGNL