wanglab/gogpt-training-data huggingface dataset:
Protein: Adenylate cyclase type 3 (EC 4.6.1.1) (ATP pyrophosphate-lyase 3) (Adenylate cyclase type III) (AC-III) (Adenylate cyclase, olfactive type) (Adenylyl cyclase 3) (AC3) (O60266)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis. Required for the perception of odorants. Required for normal sperm motility and normal male fertility. Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11549699}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:11549699}. Cell projection, cilium {ECO:0000250|UniProtKB:Q8VHH7}. Golgi apparatus {ECO:0000250|UniProtKB:P21932}. Note=Also detected in the cytoplasm, close to lipid droplets. {ECO:0000269|PubMed:11549699}.
Interaction partners:
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit alpha
- Regulator of G-protein signaling 2
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Calmodulin-like protein 5
Sequence:
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPESLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDIILFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFFITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCDYLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHSSGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESAQVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTNYVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMANVVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLMLLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKYSMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHVARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFDSLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVMGNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQVVDNS
Protein: Bone marrow stromal antigen 2 (BST-2) (HM1.24 antigen) (CD antigen CD317) (Q8R2Q8)
Organism: Mus musculus (Mouse)
Function: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells.
Subcellular location: Golgi apparatus, trans-Golgi network. Cell membrane; Single-pass type II membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Late endosome {ECO:0000250}. Membrane raft {ECO:0000250}. Cytoplasm {ECO:0000250}. Apical cell membrane {ECO:0000250}. Note=Shuttles between the cell membrane, where it is present predominantly in membrane/lipid rafts, and the trans-Golgi network. Forms a complex with MMP14 and localizes to the cytoplasm (By similarity). {ECO:0000250}.
Interaction partners:
- Interferon-induced 35 kDa protein homolog
- Ubiquitin-like protein ISG15
- E3 ubiquitin-protein ligase MARCHF8
- 2'-5'-oligoadenylate synthase-like protein 2
- Ubl carboxyl-terminal hydrolase 18
- Sialic acid binding Ig-like lectin H
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon regulatory factor 7
Sequence:
MAPSFYHYLPVPMDEMGGKQGWGSHRQWLGAAILVVLFGVTLVILTIYFAVTANSVACRDGLRAQAECRNTTHLLQRQLTRTQDSLLQAETQANSCNLTVVTLQESLEKKVSQALEQQARIKELENEVTKLNQELENLRIQKETSSTVQVNSGSSMVVSSLLVLKVSLFLLF
Protein: Myosin XIX (cDNA FLJ61374, highly similar to Homo sapiens myosin head domain containing 1 (MYOHD1), transcript variant 3, mRNA) (B4DSL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLQQTWTSRCLMKFYAVVATSPASWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQASSERNFHIFYQICKGASEDERLQWHLPEGAAFSWLPNPERSLEEDCFEVTREAMLHLGIDTPTQNNIFKVRRKATPLKFGRDDGQPFA
Protein: Cysteine desulfurase (EC 2.8.1.7) (Q9Y697)
Organism: Homo sapiens (Human)
Function: Cysteine desulfurase, of the core iron-sulfur cluster (ISC) assembly complex, that catalyzes the desulfuration of L-cysteine to L-alanine, as component of the cysteine desulfurase complex, leading to the formation of a cysteine persulfide intermediate at the active site cysteine residue and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU. The persulfide is then transferred on the flexible Cys loop from the catalytic site of NFS1 to the surface of NFS1. After the NFS1-linked persulfide sulfur is transferred to one of the conserved Cys residues of the scaffold, a reaction assisted by FXN (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:19454487, ECO:0000269|PubMed:23593335, ECO:0000269|PubMed:26702583, ECO:0000269|PubMed:30817134, ECO:0000269|PubMed:9885568}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:23593335, ECO:0000269|PubMed:30817134, ECO:0000269|PubMed:9885568}. Nucleus {ECO:0000269|PubMed:19454487, ECO:0000269|PubMed:23593335, ECO:0000269|PubMed:9885568}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30817134}.
Interaction partners:
- Iron-sulfur cluster assembly enzyme ISCU
- LYR motif-containing protein 4
- Frataxin, mitochondrial
- Adenylyltransferase and sulfurtransferase MOCS3
- 3-mercaptopyruvate sulfurtransferase
- Thiosulfate sulfurtransferase
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Acyl carrier protein, mitochondrial
- Ferredoxin-2, mitochondrial
- Adrenodoxin, mitochondrial
Sequence:
MLLRAAWRRAAVAVTAAPGPKPAAPTRGLRLRVGDRAPQSAVPADTAAAPEVGPVLRPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVASLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGFQVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHTDAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGMRSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYPGCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIGRFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
Protein: Calponin-homology (CH) domain-containing protein (G4SJU0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKTSASTRCRPQSSISLDEKRHRNRSLGCISRYSASPLPGFSAFLGTITRVSTGQTTFHPYGVQEPLSPQSCVGVFTSMYCSTPSEYSFQPMFSLSDTPPLVSPEPDDDVDFSPDMTRKKESASSGYGSAGSESEHDLMSLRSDDIKFRGRLRHRGSHVGGQAQDLHRRRSMPPTYNFESDVTRVVCHDGYATYETNVDTGEQIRMEIRGMSRPESVLQLARKFGEISAAQENDIHKSRLSLKLGGKENLTKPTLILSKSGPPTPIRHVAPTITHTLPNRPNIGGIASLKSEPKMSRPNMFKQMEKVESNTTTTAPPRQLNPNSIKDALLRWIQNRVAGYPNVNVTNFSSSWADGMAFCALIHRFAPNSFDFSKLDPNNRRYNFDLAFKVAEDNGIFPLLEVDDMIMMGDRPDWKCVFTYVQSFYKQFRDHP
Protein: Cytochrome c oxidase subunit 6C (Cytochrome c oxidase polypeptide VIc) (Cytochrome c oxidase subunit STA) (P04038)
Organism: Bos taurus (Bovine)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 7B, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 3
Sequence:
MSTALAKPQMRGLLARRLRFHIVGAFMVSLGFATFYKFAVAEKRKKAYADFYRNYDSMKDFEEMRKAGIFQSAK
Protein: Histone-lysine N-methyltransferase SETDB2 (EC 2.1.1.366) (Chronic lymphocytic leukemia deletion region gene 8 protein) (Lysine N-methyltransferase 1F) (SET domain bifurcated 2) (Q96T68)
Organism: Homo sapiens (Human)
Function: Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates 'Lys-9' of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:20404330}. Chromosome {ECO:0000305|PubMed:20404330}.
Interaction partners:
- PHD finger protein 11
- ARL14 effector protein
- Histone H3.2
- Histone H3.1
- Calmodulin-lysine N-methyltransferase
- Activating transcription factor 7-interacting protein 1
- Zinc finger MYM-type protein 6
Sequence:
MGEKNGDAKTFWMELEDDGKVDFIFEQVQNVLQSLKQKIKDGSATNKEYIQAMILVNEATIINSSTSIKGASQKEVNAQSSDPMPVTQKEQENKSNAFPSTSCENSFPEDCTFLTTENKEILSLEDKVVDFREKDSSSNLSYQSHDCSGACLMKMPLNLKGENPLQLPIKCHFQRRHAKTNSHSSALHVSYKTPCGRSLRNVEEVFRYLLETECNFLFTDNFSFNTYVQLARNYPKQKEVVSDVDISNGVESVPISFCNEIDSRKLPQFKYRKTVWPRAYNLTNFSSMFTDSCDCSEGCIDITKCACLQLTARNAKTSPLSSDKITTGYKYKRLQRQIPTGIYECSLLCKCNRQLCQNRVVQHGPQVRLQVFKTEQKGWGVRCLDDIDRGTFVCIYSGRLLSRANTEKSYGIDENGRDENTMKNIFSKKRKLEVACSDCEVEVLPLGLETHPRTAKTEKCPPKFSNNPKELTVETKYDNISRIQYHSVIRDPESKTAIFQHNGKKMEFVSSESVTPEDNDGFKPPREHLNSKTKGAQKDSSSNHVDEFEDNLLIESDVIDITKYREETPPRSRCNQATTLDNQNIKKAIEVQIQKPQEGRSTACQRQQVFCDEELLSETKNTSSDSLTKFNKGNVFLLDATKEGNVGRFLNHSCCPNLLVQNVFVETHNRNFPLVAFFTNRYVKARTELTWDYGYEAGTVPEKEIFCQCGVNKCRKKIL
Protein: A-kinase anchor protein 4 (AKAP-4) (A-kinase anchor protein 82 kDa) (AKAP 82) (hAKAP82) (Major sperm fibrous sheath protein) (HI) (Protein kinase A-anchoring protein 4) (PRKA4) (Q5JQC9)
Organism: Homo sapiens (Human)
Function: Major structural component of sperm fibrous sheath. Plays a role in sperm motility.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:31429579, ECO:0000269|PubMed:34415320, ECO:0000269|PubMed:9822690}. Note=Localizes to the principle piece of the sperm flagellum. {ECO:0000269|PubMed:9822690}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase catalytic subunit gamma
- Probable ATP-dependent RNA helicase DDX17
- A-kinase anchor protein 14
- Fibrous sheath-interacting protein 1
- A-kinase anchor protein 1, mitochondrial
- Translin
- Fibrous sheath-interacting protein 2
Sequence:
MMAYSDTTMMSDDIDWLRSHRGVCKVDLYNPEGQQDQDRKVICFVDVSTLNVEDKDYKDAASSSSEGNLNLGSLEEKEIIVIKDTEKKDQSKTEGSVCLFKQAPSDPVSVLNWLLSDLQKYALGFQHALSPSTSTCKHKVGDTEGEYHRASSENCYSVYADQVNIDYLMNRPQNLRLEMTAAKNTNNNQSPSAPPAKPPSTQRAVISPDGECSIDDLSFYVNRLSSLVIQMAHKEIKEKLEGKSKCLHHSICPSPGNKERISPRTPASKIASEMAYEAVELTAAEMRGTGEESREGGQKSFLYSELSNKSKSGDKQMSQRESKEFADSISKGLMVYANQVASDMMVSLMKTLKVHSSGKPIPASVVLKRVLLRHTKEIVSDLIDSCMKNLHNITGVLMTDSDFVSAVKRNLFNQWKQNATDIMEAMLKRLVSALIGEEKETKSQSLSYASLKAGSHDPKCRNQSLEFSTMKAEMKERDKGKMKSDPCKSLTSAEKVGEHILKEGLTIWNQKQGNSCKVATKACSNKDEKGEKINASTDSLAKDLIVSALKLIQYHLTQQTKGKDTCEEDCPGSTMGYMAQSTQYEKCGGGQSAKALSVKQLESHRAPGPSTCQKENQHLDSQKMDMSNIVLMLIQKLLNENPFKCEDPCEGENKCSEPRASKAASMSNRSDKAEEQCQEHQELDCTSGMKQANGQFIDKLVESVMKLCLIMAKYSNDGAALAELEEQAASANKPNFRGTRCIHSGAMPQNYQDSLGHEVIVNNQCSTNSLQKQLQAVLQWIAASQFNVPMLYFMGDKDGQLEKLPQVSAKAAEKGYSVGGLLQEVMKFAKERQPDEAVGKVARKQLLDWLLANL
Protein: Keratin-associated protein 3-2 (High sulfur keratin-associated protein 3.2) (Keratin-associated protein 3.2) (Q9BYR7)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 4-3
- Keratin-associated protein 3-1
- Keratin-associated protein 4-1
- Keratin-associated protein 1-1
- Keratin-associated protein 1-5
- Keratin, type I cytoskeletal 27
- Keratin-associated protein 1-3
- Keratin-associated protein 2-1
- Keratin-associated protein 9-3
- Keratin-associated protein 17-1
Sequence:
MDCCASRSCSVPTGPATTICSSDKSCRCGVCLPSTCPHTVWLLEPICCDNCPPPCHIPQPCVPTCFLLNSCQPTPGLETLNLTTFTQPCCEPCLPRGC
Protein: Chromosomal replication initiator protein DnaA (EC 3.6.4.-) (P9WNW3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). Binds its own promoter.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}. Cell membrane {ECO:0000269|PubMed:18296714}. Secreted, cell wall {ECO:0000269|PubMed:18296714}. Note=Very little protein is found in soluble extracts (PubMed:18296714). Nucleoid-associated protein is probably also in the cell membrane fraction (Probable). {ECO:0000269|PubMed:18296714, ECO:0000305}.
Interaction partners:
- Beta sliding clamp
- Replicative DNA helicase DnaB
- DNA replication and repair protein RecF
- Putative lipoprotein LppK
- Large ribosomal subunit protein bL34
- Cell division protein FtsZ
- DNA gyrase subunit B
- Ribonuclease P protein component
- Protein RecA
- DNA gyrase subunit A
Sequence:
MTDDPGSGFTTVWNAVVSELNGDPKVDDGPSSDANLSAPLTPQQRAWLNLVQPLTIVEGFALLSVPSSFVQNEIERHLRAPITDALSRRLGHQIQLGVRIAPPATDEADDTTVPPSENPATTSPDTTTDNDEIDDSAAARGDNQHSWPSYFTERPHNTDSATAGVTSLNRRYTFDTFVIGASNRFAHAAALAIAEAPARAYNPLFIWGESGLGKTHLLHAAGNYAQRLFPGMRVKYVSTEEFTNDFINSLRDDRKVAFKRSYRDVDVLLVDDIQFIEGKEGIQEEFFHTFNTLHNANKQIVISSDRPPKQLATLEDRLRTRFEWGLITDVQPPELETRIAILRKKAQMERLAVPDDVLELIASSIERNIRELEGALIRVTAFASLNKTPIDKALAEIVLRDLIADANTMQISAATIMAATAEYFDTTVEELRGPGKTRALAQSRQIAMYLCRELTDLSLPKIGQAFGRDHTTVMYAQRKILSEMAERREVFDHVKELTTRIRQRSKR
Protein: 3-hydroxyadipyl-CoA dehydrogenase (EC 1.1.1.-) (P76083)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-oxoadipyl-CoA.
Interaction partners:
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
- 2,3-dehydroadipyl-CoA hydratase
- 1,2-epoxyphenylacetyl-CoA isomerase
- Acyl-coenzyme A thioesterase PaaI
- Acetyl-CoA acetyltransferase
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- Probable acetyl-CoA acetyltransferase
- 1,2-phenylacetyl-CoA epoxidase, subunit B
Sequence:
MMINVQTVAVIGSGTMGAGIAEVAASHGHQVLLYDISAEALTRAIDGIHARLNSRVTRGKLTAETCERTLKRLIPVTDIHALAAADLVIEAASERLEVKKALFAQLAEVCPPQTLLTTNTSSISITAIAAEIKNPERVAGLHFFNPAPVMKLVEVVSGLATAAEVVEQLCELTLSWGKQPVRCHSTPGFIVNRVARPYYSEAWRALEEQVAAPEVIDAALRDGAGFPMGPLELTDLIGQDVNFAVTCSVFNAFWQERRFLPSLVQQELVIGGRLGKKSGLGVYDWRAEREAVVGLEAVSDSFSPMKVEKKSDGVTEIDDVLLIETQGETAQALAIRLARPVVVIDKMAGKVVTIAAAAVNPDSATRKAIYYLQQQGKTVLQIADYPGMLIWRTVAMIINEALDALQKGVASEQDIDTAMRLGVNYPYGPLAWGAQLGWQRILRLLENLQHHYGEERYRPCSLLRQRALLESGYES
Protein: Large ribosomal subunit protein eL43 (60S ribosomal protein L37a) (P61514)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS19
Sequence:
MAKRTKKVGIVGKYGTRYGASLRKMVKKIEISQHAKYTCSFCGKTKMKRRAVGIWHCGSCMKTVAGGAWTYNTTSAVTVKSAIRRLKELKDQ
Protein: Transmembrane protease serine 3 (EC 3.4.21.-) (Serine protease TADG-12) (Tumor-associated differentially-expressed gene 12 protein) (P57727)
Organism: Homo sapiens (Human)
Function: Probable serine protease that plays a role in hearing. Acts as a permissive factor for cochlear hair cell survival and activation at the onset of hearing and is required for saccular hair cell survival (By similarity). Activates ENaC (in vitro).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12393794}; Single-pass type II membrane protein {ECO:0000269|PubMed:12393794}.
Interaction partners:
- Pejvakin
- Transmembrane channel-like protein 1
- Unconventional myosin-XV
- Unconventional myosin-VI
- Transmembrane inner ear expressed protein
- Pendrin
- Gap junction beta-2 protein
- Otoferlin
- Lipoxygenase homology domain-containing protein 1
- Cadherin-23
Sequence:
MGENDPPAVEAPFSFRSLFGLDDLKISPVAPDADAVAAQILSLLPLKFFPIIVIGIIALILALAIGLGIHFDCSGKYRCRSSFKCIELIARCDGVSDCKDGEDEYRCVRVGGQNAVLQVFTAASWKTMCSDDWKGHYANVACAQLGFPSYVSSDNLRVSSLEGQFREEFVSIDHLLPDDKVTALHHSVYVREGCASGHVVTLQCTACGHRRGYSSRIVGGNMSLLSQWPWQASLQFQGYHLCGGSVITPLWIITAAHCVYDLYLPKSWTIQVGLVSLLDNPAPSHLVEKIVYHSKYKPKRLGNDIALMKLAGPLTFNEMIQPVCLPNSEENFPDGKVCWTSGWGATEDGAGDASPVLNHAAVPLISNKICNHRDVYGGIISPSMLCAGYLTGGVDSCQGDSGGPLVCQERRLWKLVGATSFGIGCAEVNKPGVYTRVTSFLDWIHEQMERDLKT
Protein: Eukaryotic translation initiation factor 3 subunit I (eIF3i) (Eukaryotic translation initiation factor 3 subunit 2) (TGF-beta receptor-interacting protein 1) (TRIP-1) (eIF-3-beta) (eIF3 p36) (Q13347)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit E
Sequence:
MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDNNEPYMKIPCNDSKITSAVWGPLGECIIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTTLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4IV25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS15c
- Probable S-adenosylmethionine-dependent methyltransferase At5g37970
- Cyclase-like protein 1
- Probable purine permease 18
- F14J9.2 protein
- Serine carboxypeptidase-like 51
- Plant self-incompatibility protein S1 family
- Germin-like protein subfamily 2 member 1
- Putative purine permease 19
- Myosin-3
Sequence:
MLEMERVAELKRLPSKGPVSGHLSRRPYLDFETRDAPGMHLESLRERAARYNTGRSVNPTTTLGRELSQVLNVHREDMMMTQFGGNMNDFQEFEPVVSSVRTMKAKYPLLEIEEIGAADDDVTCKGSNDMSEEAGSSSFRGVSHPPEPDDMDLITTVYVPISEKNKPDSVCLMKSMSTTKGPFIEDISLCVPPKKPSPRVLSPAESIVEEPATSLSPFSVARASQNTENSLLPPDSDKECVWDASLPPSTNVSPHSSSVESMNLARAMSIANSSSATSTTQRSDVVLSMDKNYFDRSISMVLDSFESTKTSASRASDSSGLSEESSWSNFTGSLNKPHKGNDPWWNAILAIRTRDGILGMSHFKLLKRLGCGDIGSVYLAELSGTRCHFAVKVMDKASLEDRKKLNRAQTERDILQLLDHPFLPTLYTHFETDRFSCLVMEYCPGGDLHTLRQRQPGKHFSEYAARFYAAEVLLALEYLHMLGVVYRDLKPENVLVRDDGHIMLSDFDLSLRCAVSPTLIKTFDSDPSRRGAFCVQPACMEPTSACIIQPSCFLPRSIFPNKNKKNKSRKTQADFFKSHSGSLPELVAEPNTRSMSFVGTHEYLAPEIIKGEGHGSAVDWWTFGIFVHELLYGKTPFKGSGNRATLFNVVGEQLKFPESPATSYAGRDLIQALLVKDPKNRLGTKRGATEIKQHPFFEGVNWALIRCSTPPEVPRQMETEPPPKYGPIDPVGFGSNSKRMMGPPAVSAAAADTKSGGKFLDFEFF