wanglab/gogpt-training-data huggingface dataset:
Protein: POU domain, class 2, transcription factor 1 (NF-A1) (Octamer-binding protein 1) (Oct-1) (Octamer-binding transcription factor 1) (OTF-1) (P31503)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR.
Subcellular location: Nucleus.
Interaction partners:
- POU domain protein
- POU domain, class 2, transcription factor 3
- POU class 2 homeobox associating factor 1
- Host cell factor 1
- Transcription factor Sp1
- Breast cancer type 1 susceptibility protein homolog
Sequence:
LTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQPQPSITLTSQPTTPTRTIAATPIQTLPQSQTTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSTASSPSALNSPGLGAEGLNRRRKKRTSIETNIRVALEKSFMENQKPTSEDITLIAEQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSTATTLTVNPVLPLTSAAMTNLSLTGTTDSTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLPSPLGASQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPGLMAPSQFAAGGALLSLNPGTLGGALSPALMSNSTLATIQALASSGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASTGNSAPTASLHASSTSTESIQNSLFTVASASGAASTTTAASKAQ
Protein: Chemotaxis protein CheW (Q56311)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Methyl-accepting chemotaxis protein
- Chemotaxis protein CheY
- Methyl-accepting chemotaxis protein
- Methyl-accepting chemotaxis protein 4
- Chemotaxis protein CheA
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Methyl-accepting chemotaxis protein 2
- Methyl-accepting chemotaxis protein, putative
- Purine-binding chemotaxis protein
- Chemotaxis protein methyltransferase
Sequence:
MKTLADALKEFEVLSFEIDEQALAFDVDNIEMVIEKSDITPVPKSRHFVEGVINLRGRIIPVVNLAKILGISFDEQKMKSIIVARTKDVEVGFLVDRVLGVLRITENQLDLTNVSDKFGKKSKGLVKTDGRLIIYLDIDKIIEEITVKEGV
Protein: Aquaporin-9 (Q21473)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aquaporin
- Aquaporin
- TPR_REGION domain-containing protein
- Probable glycerol kinase
- Sodium/hydrogen exchanger
Sequence:
MAAELERTEQVRAKIQIKNPLLRNALSEFFGTFLLLFIGIGIVMQFILSNEKLNTWININLGWGLAIAFTVYTCSKTSGGHFNPAVSIAFLTLGKLPFKDFLVYCVVQTIGAALGSAAAFGLYYDQFVKFAGAYRTILGPKATAGCFCSYPALHVSNTTAFFDQFAGTALLVLFVCVVIDKRNGIPGAAHPLLFGLVVMMIGTAYGMNLGYPINPARDLGPRLFSFFIYGSGVFSYHSYYFWIPVIAPLFGAIFGAWSYTFFVGAHIPDQRETTYVLVDEANQPLKLATDA
Protein: Double-stranded RNA-binding protein 5 (dsRNA-binding protein 5) (AtDRB5) (Q8GY79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds double-stranded RNA. May be involved in RNA-mediated silencing.
Interaction partners:
- Endoribonuclease Dicer homolog 3
- Endoribonuclease Dicer homolog 1
- Dicer-like protein 4
- Endoribonuclease Dicer homolog 2
- Protein DCL homolog, chloroplastic
- Double-stranded RNA-binding protein 1
Sequence:
MYKNQLQELAQRSCFNLPSYTCIREGPDHAPRFKASVNFNGEIFESPTYCSTLRQAEHAAAEVSLNVLSSRVPSKSLTAKILDETGIYKNLLQETAHRAGLDLPMYTSVRSGSCHFPGFSCTVELAGMTFTGESAKTKKQAEKNAAIAAWSSLKKMSSLDSQDEEKEQEAVARVLSRFKPKEVRRRETTNQWRRRTSQQDSNKDLLIERLRWINLLTNQASSSSSTSTPNQHKNSSFISLIPPPPPPKSSKILPFIQQYKDRSSQEAKTETATEMINSKAKVNETSTRLSKQMPFSDMNRYNFVGGCSVNPYSLAPAVQMRSVIPVFAAPPPKPNPNLNPSSLSSSVNEFTSSNNSCSVLNTPGLGGQEKKNLTREMIKLGSESRILDQTHDS
Protein: Rhodopsin kinase GRK1 (RK) (EC 2.7.11.14) (G protein-coupled receptor kinase 1) (Q9WVL4)
Organism: Mus musculus (Mouse)
Function: Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade. This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination. May play a role in the maintenance of the outer nuclear layer in the retina.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P28327}; Lipid-anchor {ECO:0000250|UniProtKB:P28327}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:15961391}. Note=Subcellular location is not affected by light or dark conditions. {ECO:0000269|PubMed:15961391}.
Interaction partners:
- Rhodopsin
- Recoverin
- S-arrestin
- Beta-arrestin-1
- Beta-arrestin-2
- Guanine nucleotide-binding protein G
- Neuronal calcium sensor 1
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Guanylyl cyclase-activating protein 1
- Arrestin-C
Sequence:
MDFGSLETVVANSAFIAARGSFDGSSTPSSRDKKYLAKLRLPPLSKCEGLRDNLSLEFESLCSEQPIGKRLFQQFLKTDERHVPALELWKDIEDYDTADDDLRPQKAQAILAEYLDPQGTLFCNFLDQGMVTRVKEGPTGSQDGLFQPLLQATMEHLSQAPFQEYLESLYFLRFLQWKWLEAQPIGEDWFLDFRVLGKGGFGEVSACQMKATGKMYACKKLNKKRLKKKKGYQGAIVEKRILTKVHSRFIVSLAYAFETKTDLCLVMTIMNGGDVRYHIYNVDEDNPGFSEPRAIYYTAQIISGLEHLHQRRIVYRDLKPENVLLDNDGNIRISDLGLAVELKEGQNKTKGYAGTPGFMAPELLRGEEYDFSVDYFALGVTLYEMIAARGPFRARGEKVENKELKQRIISEPVKYPEKFSQASKDFCEQLLEKDPEKRLGFRDGTCDALRANVLFKDISWRQLEAGMLIPPFIPDSRTVYAKNIQDVGAFSTVKGVVFDKADTEFFQEFASGNCSIPWQEEMIETGLFGDLNVWRADGQMPDDMKGITTEEAAPTAKSGMCLIS
Protein: Adenylyl cyclase-associated protein 2 (CAP 2) (Q9CYT6)
Organism: Mus musculus (Mouse)
Function: May have a regulatory bifunctional role.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Drebrin
- Profilin-4
- Cofilin-1
- Cofilin-2
- Twinfilin-2
- Drebrin-like protein
- Twinfilin-1
- PH domain leucine-rich repeat-containing protein phosphatase 2
- PH domain leucine-rich repeat-containing protein phosphatase 1
Sequence:
MTDMAGLMERLERAVIRLEQLSAGLDGPPRGCGEVNGVNGGVAPSVEAFDKLINSMVAEFLKNSRVLAGDVETHAEMVHGAFQAQRAFLLMVSQYQQPQENEVAVLLKPISEKIQEIQTFRERNRGSNMFNHLSAVSESIAALGWIAVSPKPGPYVKEMNDAATFYTNRVLKDYKHSDLRHVDWVRSYLNIWSELQAYIREHHTTGLTWSKTGPVASTASAFSILSSGPGLPPPPPPPPPPGPPPPFENEDKKEEPSPSRSALFAQLNQGEAITKGLRHVTDDKKTYKNPSLRAQGQIRSPTKTHTPSPTSPKSNSPQKHTPVLELEGKKWRVEYQEDRNDLVISETELKQVAYIFKCDKSTLQIKGKVNSITVDNCKKFGLVFDHVVGIVEVINSKDIQIQVMGRVPTISINKTEGCHLYLSEDALDCEIVSAKSSEMNVLVPQDDDYREFPIPEQFKTIWDGSKLVTEPAEIMA
Protein: Oxysterols receptor LXR-alpha (Liver X receptor alpha) (Nuclear receptor subfamily 1 group H member 3) (Q13133)
Organism: Homo sapiens (Human)
Function: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity. Interaction with retinoic acid receptor (RXR) shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES (By similarity). LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides (By similarity). Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles. Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:25661920}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z0Y9}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Retinoic acid receptor RXR-beta
- Nuclear receptor coactivator 1
- Phospholipid-transporting ATPase ABCA1
- Sterol regulatory element-binding protein 1
- Retinoic acid receptor RXR-gamma
- Nuclear receptor subfamily 0 group B member 2
- ATP-binding cassette sub-family G member 1
- Oxysterols receptor LXR-beta
- ATP-binding cassette sub-family G member 5
Sequence:
MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLPPRASSPPQILPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPMAPDPHSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLLETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRAMNELQLNDAEFALLIAISIFSADRPNVQDQLQVERLQHTYVEALHAYVSIHHPHDRLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Protein: Uncharacterized protein (Q389U0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHTGDKRVLPCFDNHYNSGVLVDNWFDARINEAHGKFTIAVDGQSPLPSSVYKADYSTPCVTAVRPMLRQRGLGKSLIFGSGLPTVDEVVATSKDYGATQRYLIDSRYGKPKHHCKPLNTLSGVDRFALTGKLSKPVNQPTVDDAMVDRFRTTKSAMDVTILNHHVQRQLSAGRNCGARTQM
Protein: Synaptophysin-like protein 1 (Pantophysin) (Q16563)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Cytoplasmic transport vesicles (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250}.
Interaction partners:
- Vesicle-associated membrane protein 2
Sequence:
MAPNIYLVRQRISRLGQRMSGFQINLNPLKEPLGFIKVLEWIASIFAFATCGGFKGQTEIQVNCPPAVTENKTVTATFGYPFRLNEASFQPPPGVNICDVNWKDYVLIGDYSSSAQFYVTFAVFVFLYCIAALLLYVGYTSLYLDSRKLPMIDFVVTLVATFLWLVSTSAWAKALTDIKIATGHNIIDELPPCKKKAVLCYFGSVTSMGSLNVSVIFGFLNMILWGGNAWFVYKETSLHSPSNTSAPHSQGGIPPPTGI
Protein: Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129) (P0A722)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Subcellular location: Cytoplasm.
Interaction partners:
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Lipid-A-disaccharide synthase
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- UDP-3-O-
- Tetraacyldisaccharide 4'-kinase
- 3-deoxy-D-manno-octulosonic acid transferase
- Lipid A biosynthesis lauroyltransferase
- 2-dehydro-3-deoxyphosphooctonate aldolase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
Sequence:
MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRGLIR
Protein: N-alpha-acetyltransferase 50 (EC 2.3.1.258) (N-acetyltransferase NAT13) (N-epsilon-acetyltransferase 50) (EC 2.3.1.-) (NatE catalytic subunit) (Q6DBY2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (By similarity). The relevance of N-epsilon-acetyltransferase activity is however unclear (By similarity). Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin (By similarity). Essential in embryonic cell proliferation and survival.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9GZZ1}. Nucleus {ECO:0000250|UniProtKB:Q9GZZ1}. Note=Localizes to the cytoplasm in interphase cells. {ECO:0000250|UniProtKB:Q9GZZ1}.
Interaction partners:
- Huntingtin-interacting protein K
- N-terminal amino-acid N
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 15, NatA auxiliary subunit a
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-alpha-acetyltransferase 15, NatA auxiliary subunit b
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 30
Sequence:
MKGRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYQKFGFEIIETKKNYYKRIEPADAHVLQKSLRSPCAPPAGELQKAD
Protein: cAMP-dependent protein kinase type II-beta regulatory subunit (P31323)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:21423175}. Note=Colocalizes with PJA2 in the cytoplasm and at the cell membrane.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- A-kinase anchor protein 5
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- A-kinase anchor protein 1, mitochondrial
- cAMP-dependent protein kinase catalytic subunit PRKX
- cAMP-dependent protein kinase type I-beta regulatory subunit
- cAMP-dependent protein kinase type I-alpha regulatory subunit
- Hormone-sensitive lipase
Sequence:
MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGTARFGHEGRTWGDLGAAAGGGTPSKGVNFAEEPMQSDSEDGEEEEAAPADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCSRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA
Protein: Transient receptor potential cation channel, subfamily M, member 5 (F1LMD7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Calcium homeostasis modulator 1
- Taste receptor type 1 member 3
- Guanine nucleotide-binding protein G
- Polycystin 2 like 1, transient receptor potential cation channel
- POU domain, class 2, transcription factor 3
- Taste receptor type 1 member 1
- Serine/threonine-protein kinase DCLK1
- Polycystin-1-like protein 3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MTRFPGDPLQKPLESCVEGVGIQMPGVRKVTMPMAQSSCPGSPPDTGDGWEPVLCKGEVNFGGSGKKRSKFVKVPSNVAPSMLFELLLTEWHLPAPNLVVSLVGEERLFAMKSWLRDVLRKGLVKAAQSTGAWILTSALHVGLARHVGQAVRDHSLASTSTKVRVVAIGMASLDRILHRQLLDGVQEDTPIHYPADEGSTQGPLCPLDSNLSHFILVEPGTLGSGNDGLAELQLSLEKHISQQRTGYGGTSSIQIPVLCLLVNGDPSTLERMSRAVEQAAPWLILAGSGGIADVLAALVGQPHLLVPQVTEKQFREKFPSECFSWEAIVHWTELLQNIAAHPHLLTVYDFEQEGSEDLDTVILKALVKACKSHSRDAQDYLDELKLAVAWDRVDIAKSEIFNGDVEWKSCDLEEVMTDALVSNKPDFVRLFVDSGADMAEFLTYGRLQQLYHSVSPKSLLFELLERKHEEGRLTLAGLGAQQTRELPVGLPAFSLHEVSRVLKDFLHDACRGFYQDGRRMEERGPPKRPAGQKWLPDLSRKSEDPWRDLFLWAVLQNRYEMATYFWAMGREGVAAALAACKIIKEMSHLEKEAEVARTMREAKYEQLALDLFSECYSNSEDRAFALLVRRNHSWSRTTCLHLATEADAKAFFAHDGVQAFLTKIWWGDMATGTPILRLLGAFTCPALIYTNLISFSEDAPQRMDLEDLQEPDSLDMEKSFLCSHGGQLEKLTEAPRAPGDLGPQAAFLLTRWRKFWGAPVTVFLGNVVMYFAFLFLFSYVLLVDFRPPPQGPSGSEVTLYFWVFTLVLEEIRQGFFTNEDTRLVKKFTLYVEDNWNKCDMVAIFLFIVGVTCRMVPSVFEAGRTVLAIDFMVFTLRLIHIFAIHKQLGPKIIIVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSLHPLLLDSSASCPNLYANWLVILLLVTFLLVTNVLLMNLLIAMFSYTFQVVQGNADMFWKFQRYHLIVEYHGRPALAPPFILLSHLSLVLKQVFRKEAQHKQQHLERDLPDPVDQKIITWETVQKENFLSTMEKRRRDSEEEVLRKTAHRVDLIAKYIGGLREQEKRIKCLESQANYCMLLLSSMTDTLAPGGTYSSSQNCGRRSQPASARDREYLEAGLPHSDT
Protein: Magnesium transporter NIPA2 (G4S7C7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Inheritance of peroxisomes protein 1
- Spastin homolog
- GB1/RHD3-type G domain-containing protein
- GB1/RHD3-type G domain-containing protein
Sequence:
MNEQPHVAVESYLVGNDSIMASVASSSQVILPVAADSSSIGSVNTMDEVHYASTDFYIGLGLAVSSSLFIGSSFIIKKKALLKLASGDTSQRASEGGYGYLREWMWWMGVITMGIGEACNFAAYAFAPASLVTPLGALSVIVTAILSSRMLNERLNLLGSIGCALCLLGSTVIVIHSPKEEEVGSMADLALKMKDAGFLIYVILIILATGFIVVYVAPRYGHSNILVYISVCSLIGSLSVLSVKGLGLAIKETLAGNQQFTNWLTYFWLASVAMCVSVQLIYLNKALDIFNTSMVTPIYYVFFTTFVILASSILYKEWSCLGASDVIGNFVGFLTTIIGIFQMQLFRDVNISLYQVQRLVSRPSATLANADFSSSSTNLVDDYCMRQSNSNRRMVYT
Protein: HAUS augmin like complex subunit 1 (K7ES67)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MEPQEERETQVNPRTTEILHHLSERNRVRDRDVYLVIEDLKQKASEYESEAKYLQDLLMESVNFSPANLSSTGSRYLNALVDSAVALETKDTSLASFIPAVNDLTSD
Protein: DNA polymerase delta subunit 4 (DNA polymerase delta subunit p12) (Q9HCU8)
Organism: Homo sapiens (Human)
Function: As a component of the tetrameric DNA polymerase delta complex (Pol-delta4), plays a role in high fidelity genome replication and repair. Within this complex, increases the rate of DNA synthesis and decreases fidelity by regulating POLD1 polymerase and proofreading 3' to 5' exonuclease activity. Pol-delta4 participates in Okazaki fragment processing, through both the short flap pathway, as well as a nick translation system. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR), a mechanism that may induce segmental genomic duplications of up to 200 kb. Involved in Pol-delta4 translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites. Its degradation in response to DNA damage is required for the inhibition of fork progression and cell survival.
Subcellular location: Nucleus {ECO:0000269|PubMed:22801543}. Note=Partially recruited to DNA damage sites within 2 hours following UV irradiation, before degradation. {ECO:0000269|PubMed:22801543}.
Interaction partners:
- DNA polymerase delta subunit 2
- DNA polymerase delta subunit 3
- DNA polymerase delta catalytic subunit
- Proliferating cell nuclear antigen
- Flap endonuclease 1
- DNA ligase 1
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase zeta catalytic subunit
- DNA polymerase alpha catalytic subunit
- Denticleless protein homolog
Sequence:
MGRKRLITDSYPVVKRREGPAGHSKGELAPELGEEPQPRDEEEAELELLRQFDLAWQYGPCTGITRLQRWCRAKQMGLEPPPEVWQVLKTHPGDPRFQCSLWHLYPL
Protein: Gelsolin (Q07171)
Organism: Drosophila melanogaster (Fruit fly)
Function: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed.
Subcellular location: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
Interaction partners:
- IP04855p
- Cofilin/actin-depolymerizing factor homolog
- Profilin
- RE12101p
- Caspase-8
- Adenylyl cyclase-associated protein
- Villin-like protein quail
- Formin 3, isoform B
- Conserved oligomeric Golgi complex subunit 8
- Vinculin
Sequence:
MDASGAATMAVLSSLLVFLALSSSLCSAGTLNARPAFPVQSGEIQPSGQNSKQAARRVMHPSFANAGRTPGLEIWRIENFEPVIYPKTNYGKFYTGDSFIVLNTIENKKDKKLSWDVHFWLGLETSTDEAGAAAILTVQLDDLLNGGPVQHREVQDHESQLFLSYFKNGIRYEQGGVGTGFKHVETNAQGETRLFQVKGKRNVRVRQVNLSVSSMNTGDCFILDAGSDIYVYVGSQAKRVEKLKAISAANQIRDQDHNGRARVQIVDDFSTDADKQHFFDVLGSGSADQVPDESTADEDSAFERTDAAAVSLYKVSDASGKLKVDIIGQKPLTQAMLDTRECFILDTGSGIFVWVGKGATQKEKTDAMAKAQEFLRTKKYPAWTQIHRIVEGSESAPFKQYFDTWRDAGMSHSRLIRSALGIGSDELLNDDEIDSVVTQLKKSGGRAFGFMPDHGQNVIETITQYVAKPGSDEIVVSTVPFDEKLPLLGFASYVLTYNYEANNGDTGSLTYVWHGVKASAAARKRAFEEGLVGSKDGLLVQTNQGHEPRHFYKIFKGKLLTSFTALPVTAQLFRIRGTVESDVHASEVAADSSSLASSDAFVLHSGKSHKIYIWNGLGASAFEKQAAVDRFSDYWDDVELEQVEEGAEPDEFWEELNGEGQYDRSLGDDGAPLLESRLFHCHLSSGGFLKVEEVAQYEQEDLDSDDIMLLDAGDEIYLWVGYGVSEEENGKLLDTAKLYFNLEPTARSFDTVSIIRVPQGKEPRVFKRMFPNWDDNYWQNQPSYEDMKQLVIDANNEV
Protein: Insulin-like growth factor 1 (Insulin-like growth factor I) (Q9NP10)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKEVHLKNASRGSAGNKNYRM
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (A0A0B4LGF5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MLRIYQNTYRRTARKAVVYSTKVACCNHSTLCGITSHPRRAQDSGSSSSNGRHRGHEEFLLAGNPARGWQMPPPSRGYGMLVVRILRGALKLRYIVLGGAIGGGVSLSKKYEEWKDGLPNFKWLEDAMPQGERWSQFSRNLIEVGSLVKNAIEVDPKLKQLGEDKLSEWRNWFDSRLDDAIEAADYQGVQIVETKDDLKAKTTVAALGITSDESRKKYEKLQSQVETLQTEIMNVQIKYQKELEKMEKENRELRQQYLILKTNKKTTAKKIKKSLIDMYSEVLDELSGYDTGYTMADHLPRVVVVGDQSSGKTSVLESIAKARIFPRGSGEMMTRAPVKVTLAEGPYHVAQFRDSDREYDLTKESDLQDLRRDVEFRMKASVRGGKTVSNEVIAMTVKGPGLQRMVLVDLPGIISTMTVDMASDTKDSIHQMTKHYMSNPNAIILCIQDGSVDAERSNVTDLVMQCDPLGRRTIFVLTKVDLAEELADPDRIRKILSGKLFPMKALGYYAVVTGRGRKDDSIDAIRQYEEDFFKNSKLFHRRGVIMPHQVTSRNLSLAVSDRFWKMVRETIEQQADAFKATRFNLETEWKNNFPRLRESGRDELFDKAKGEILDEVVTLSQISAKKWDDALSTKLWEKLSNYVFESIYLPAAQSDSFNTMVDIKLRQWAEQALPAKSVEAGWEALQQEFISLMERSKKAQDHDGIFDQLKSAVVDEAIRRHSWEDKAIDMLRVIQLNTLEDRFVHDKQEWDSAVKFLESSVNAKLVQTEETLAQMFGPGQMRRITHWQYLTQDQQKRRSVKNELDKILKNDTKHLPTLTHDELTTVRKNLQRDNVDVDTDYIRQTWFPVYRKHFLQQALQRAKDCRKAYYLYTQQGAECEISCSDVVLFWRIQQVIKITGNALRQQVINREARRLDKEIKAVLDEFSDDEEKKGYLLTGKRVLLAEELIKVRQIQEKLEEFINSLNQEK
Protein: Sodium-dependent multivitamin transporter (Solute carrier family 5 member 6) (A0A287BEL5)
Organism: Sus scrofa (Pig)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- PDZ domain-containing protein 11
Sequence:
MNVGVSPSTTPAPASDADVSASTFSTADYVVFVLLLVLSLIIGLYHAYRGWGRHSIGQLLLADRKMGCLPVALSLLATFQSAVAILGVPSEIYRFGTQYWFLGCCYFLGLLIPAHVFIPIFYRLHLTSAYEYLELRFNKAVRVCGTVTFIFQMVIYMGVVLYAPSLALNAVTGFDLWLSVLTLGIVCNIYTALGGLKAVIWTDVFQTLVMFLGQLAVIIVGSAKVGGLGHVWDVASQHGLISGIELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSHTEKAAVLSCYAVFPCQQVVLCMGCLIGLVMFAYYQEYPMSPQQMQAAPDQLVLYFVMDLLRALPGLPGLFVACLFSGSLSTISSAFNSLATVTMEDLIRPWFPHFSEARATMLSRIIAFGYGLLCLGMAYISSQMGPVLQAAISIFGMVGGPLLGLFCLGMFFPCANPPGAIVGLLAGLVMAFWIGIGSIVTNMAPGTAPPPANGSSFSLPSNLTTVTVATLMPSTTLSKPTGLQRFYSLSYLWYSAHNSTTVIVVGLAVSVLTGGMRGRTLNPRTIYPVWPRLLALLPVSCQKRLCCRAHSQDLSGDLAGFSEKMSNGMLRRSSDKVAMAVPEEDPAHQGISPTFVLQETSL
Protein: Alpha-amylase isozyme 3D (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (P27933)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Important for breakdown of endosperm starch during germination.
Interaction partners:
- 4-alpha-glucanotransferase DPE2
- Probable alpha-glucosidase Os06g0675700
- Isoamylase 1, chloroplastic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Os06g0676700 protein
- Isoamylase 3, chloroplastic
- Alpha-1,4 glucan phosphorylase
- 1,4-alpha-glucan branching enzyme
- Alpha-1,4 glucan phosphorylase
- Os05g0173800 protein
Sequence:
MKNTSSLCLLLLVVLCSLTCNSGQAQVLFQGFNWESWKQQGGWYNMLKGQVDDIAKAGVTHVWLPPPSHSVAPQGYMPGRLYDLDASKYGTAAELKSLIAAFHGKGVQCVADVVINHRCAEKKDARGVYCVFEGGTPDDRLDWGPGMICSDDTQYSDGTGHRDTGEGFGAAPDIDHLNPRVQRELTDWLNWLKSDVGFDGWRLDFAKGYSTDIAKMYVESCKPGFVVAEIWNSLSYNGDGKPAANQDQGRQELVNWVNAVGGPAMTFDFTTKGLLQAGVQGELWRLRDGNGKAAGMIGWLPEKAVTFVDNHDTGSTQKLWPFPSDKVMQGYAYILTHPGVPCIFYDHMFDWNLKQEITALAAIRERNGINAGSKLRIVVADADAYVAVVDEKVMVKIGTRYDVGNAVPSDFHQTVHGKDYSVWEKGSLRVPAGRHL