wanglab/gogpt-training-data huggingface dataset:
Protein: Utx histone demethylase, isoform B (EC 1.14.11.68) (Utx histone demethylase, isoform C) (Q76NQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLKHCGEFHIALKHLQLALLYTYPSTFSELQVKFQIAHLYEVQNKHKAAKDGYEFLLNEKNISLELKADVYRQLGWMYHCVECLGEKKEREANALNFLQKSIEADPKSGQSLYLLGRCYAGINKVHDAFLAYRNSVEKSEGNADTWCSIGVLYQQQNQPTDALQAYICAVQLDKDHKAAWTNLGILYESCGQLRDAYACYLNATKQISFQKSSLIRKKQAIRMKKDTIGLSKGLSQRITFLEGQLSQAPLPSITSKRRQLCSIEEAWNLPISLEMNSRQQQTAQMLPRQVTKQSPVQGPPPPYPHSQLSQSPIPSKRIKEDGTSQQEVTQNNSQTSAQNLINISESLNQRNFNAMPESNKSSEQSVLDTFDDISNDIYKQNESIKLERLSQDALSNNEDSRHDFIGGDNADISTTFKIQMDSKQLMVAVKLLPIDEPPVHCTILQVNAPPPSPPDCPPQKLTRDQLLPPTPSVHLENKKHAFSPQLQEFCLKHPIAVVRGLAGVLKLDLGLFSTKTLVEANPDHSVEVRTQVHQSPDENWDTSQGKRVWACISHRSHTTIAKYAQYQASSFQDSLKLILPQDESDKGFPGSQAMSDSDSKDSVSNSNIVLKRKKHKINSKMLRFGTNVDLSDEKKWKPQLTELQKLPAFARVISAANMLSHVGHVILGMNTVQLYMKVPGSRTPGHQENNNFCSININIGPGDCEWFAVPDAYWGGVHNLCEKNNISYLHGSWWPVLEDLYKENIPVYRFIQKPGDLVWVNAGCVHWVQSIGWCNNIAWNVGPLTARQYSLAIERYEWNKVQAFKSIVPMVHLSWNLARNIKVSDTKLFELIKMCLLQTLKNVLHIQEYVKSKGVEIRFNGRGKNEASHYCGQCEVEVFNVLFIKEQEKRHVVHCLSCALKLSPSLQGIVCLEEYRLSELQRVYDSFTLHRTQGLAYTQ
Protein: Nascent polypeptide-associated complex subunit alpha-like protein 1 (NAC-alpha-like protein 1) (Alpha-NAC-like protein 1) (Q9LHG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May promote appropriate targeting of ribosome-nascent polypeptide complexes.
Interaction partners:
- Nascent polypeptide-associated complex subunit beta
- Basic transcription factor 3
- Large ribosomal subunit protein uL18y
- Probable elongation factor 1-gamma 2
- Large ribosomal subunit protein P2y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL22y
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein eL8y
Sequence:
MTTEEKEILAAKLEEQKIDLDKPEVEDDDDNEDDDSDDDDKDDDEADGLDGEAGGKSKQSRSEKKSRKAMLKLGMKPITGVSRVTVKKSKNILFVISKPDVFKSPASDTYVIFGEAKIEDLSSQIQSQAAEQFKAPDLSNVISKGESSSAAVVQDDEEVDEEGVEPKDIELVMTQAGVSRPNAVKALKAADGDIVSAIMELTT
Protein: Interleukin-12 subunit beta (IL-12B) (Cytotoxic lymphocyte maturation factor 40 kDa subunit) (IL-12 subunit p40) (W5PUF3)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU281113}.
Interaction partners:
Sequence:
MHPQQLVVSWFSLVLLASPIVAIWELEKNVYVVELDWYPNAPGETVVLTCDTPEEDGITWTSDQSSEVLGSGKTLTIQVKEFGDAGQYTCHKGGEVLSRSLLLLHKKEDGIWSTDILKDQKDPEPKAKSFLKCEAKDYSGHFTCSWLTAISTNLKFSVKSSRGSSDPRGVTCRAASLSAEKVSMDHREYNKYTVECQEGAEESLPIEVVMEAVHKLKYENYTSSFFIRDIIKPDPPKNLQLRPLKNSRQVEVSWEYPDTWSTPHSYFSLTFCVQVQGKNKREKKLFTDQTSAKVTCHKDANIRVQARDRYYSSFWSEWASVSCS
Protein: Eukaryotic translation initiation factor 4 gamma 1 (eIF-4-gamma 1) (eIF-4G 1) (eIF-4G1) (Q6NZJ6)
Organism: Mus musculus (Mouse)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q04637}. Nucleus {ECO:0000250|UniProtKB:Q04637}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q04637}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4A-I
- Eukaryotic initiation factor 4A-II
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 3 subunit B
- Polyadenylate-binding protein 1
- Eukaryotic translation initiation factor 4 gamma 2
- Eukaryotic translation initiation factor 4E type 1B
- Eukaryotic translation initiation factor 4E type 2
- Ras GTPase-activating protein-binding protein 1
Sequence:
MNKAPQPTGPPPARSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQGGFRSLQHFYPSRAQPPSSAASRVQSAAPARPGPAPHVYPAGSQVMMIPSQISYSASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPASVAPAPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGSLEPQPNGESPQVAVIIRPDDRSQGAAIGGRPGLPGPEHSPGTESQPSSPSPTPSPPPILEPGSESNLGVLSIPGDTMTTGMIPMSVEESTPISCETGEPYCLSPEPTLAEPILEVEVTLSKPIPESEFSSSPLQVSTALVPHKVETHEPNGVIPSEDLEPEVESSTEPAPPPLSPCASESLVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKKVSSAALASILSPAPPVAPSDTSPAQEEEMEEDDDDEEGGEAESEKGGEDVPLDSTPVPAQLSQNLEVAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEVDPAVPEVENQPPTGSNPSPESEGSMVPTQPEETEETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHITDVVLDKANKTPLRQLDPSRLPGINCGPDFTPSFANLGRPALSNRGPPRGGPGGELPRGPAGLGPRRSQQGPRKETRKIISSVIMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFAKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRQSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPINRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDTASEATRPATLNRFSALQQTLPAENTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRGRDPVKREATLPPVSPPKAALSVDEVEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRLGIESTLERSTIAREHMGRLLHQLLCAGHLSTAQYYQGLYETLELAEDMEIDIPHVWLYLAELITPILQEDGVPMGELFREITKPLRPMGKATSLLLEILGLLCKSMGPKKVGMLWREAGLSWREFLAEGQDVGSFVAEKKVEYTLGEESEAPGQRTLAFEELRRQLEKLLKDGGSNQRVFDWIDANLNEQQIASNTLVRALMTTVCYSAIIFETPLRVDVQVLKVRARLLQKYLCDEQKELQALYALQALVVTLEQPANLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFNWLREAEDEESDHN
Protein: Beta-galactosidase 4 (Lactase 4) (EC 3.2.1.23) (Q9SCV8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Preferentially hydrolyzes para-nitrophenyl-beta-D-galactoside. Can hydrolyze para-nitrophenyl-beta-D-fucoside with 5 time less efficiency.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000305|PubMed:17234672}.
Interaction partners:
- LIMR family protein At3g08930
- Putative mannan endo-1,4-beta-mannosidase 4
- En/Spm-like transposon protein-like
- At5g19440
- F13F21.11 protein
- T-complex protein 11
Sequence:
MVLNFRDKSCIFLAILCCLSLSCIVKASVSYDRKAVIINGQRRILLSGSIHYPRSTPEMWPGLIQKAKEGGLDVIETYVFWNGHEPSPGQYYFGDRYDLVKFIKLVHQAGLYVNLRIGPYVCAEWNFGGFPVWLKFVPGMAFRTDNEPFKAAMKKFTEKIVWMMKAEKLFQTQGGPIILAQIENEYGPVEWEIGAPGKAYTKWVAQMALGLSTGVPWIMCKQEDAPGPIIDTCNGYYCEDFKPNSINKPKMWTENWTGWYTDFGGAVPYRPVEDIAYSVARFIQKGGSLVNYYMYHGGTNFDRTAGEFMASSYDYDAPLDEYGLPREPKYSHLKALHKAIKLSEPALLSADATVTSLGAKQEAYVFWSKSSCAAFLSNKDENSAARVLFRGFPYDLPPWSVSILPDCKTEVYNTAKVNAPSVHRNMVPTGTKFSWGSFNEATPTANEAGTFARNGLVEQISMTWDKSDYFWYITDITIGSGETFLKTGDSPLLTVMSAGHALHVFVNGQLSGTAYGGLDHPKLTFSQKIKLHAGVNKIALLSVAVGLPNVGTHFEQWNKGVLGPVTLKGVNSGTWDMSKWKWSYKIGVKGEALSLHTNTESSGVRWTQGSFVAKKQPLTWYKSTFATPAGNEPLALDMNTMGKGQVWINGRNIGRHWPAYKAQGSCGRCNYAGTFDAKKCLSNCGEASQRWYHVPRSWLKSQNLIVVFEELGGDPNGISLVKRT
Protein: Golgin subfamily A member 3 (Golgi complex-associated protein of 170 kDa) (GCP170) (Golgin-160) (Q08378)
Organism: Homo sapiens (Human)
Function: Golgi auto-antigen; probably involved in maintaining Golgi structure.
Subcellular location: Cytoplasm. Golgi apparatus, Golgi stack membrane; Peripheral membrane protein.
Interaction partners:
- Golgin subfamily A member 2
- Golgin subfamily A member 7
- Male-enhanced antigen 1
- Golgi-associated PDZ and coiled-coil motif-containing protein
- Golgi resident protein GCP60
- Golgi reassembly-stacking protein 1
- Translin-associated protein X
- Spermatogenesis-associated protein 16
- Palmitoyltransferase ZDHHC9
- Golgin subfamily B member 1
Sequence:
MDGASAEQDGLQEDRSHSGPSSLPEAPLKPPGPLVPPDQQDKVQCAEVNRASTEGESPDGPGQGGLCQNGPTPPFPDPPSSLDPTTSPVGPDASPGVAGFHDNLRKSQGTSAEGSVRKEALQSLRLSLPMQETQLCSTDSPLPLEKEEQVRLQARKWLEEQLKQYRVKRQQERSSQPATKTRLFSTLDPELMLNPENLPRASTLAMTKEYSFLRTSVPRGPKVGSLGLPAHPREKKTSKSSKIRSLADYRTEDSNAGNSGGNVPAPDSTKGSLKQNRSSAASVVSEISLSPDTDDRLENTSLAGDSVSEVDGNDSDSSSYSSASTRGTYGILSKTVGTQDTPYMVNGQEIPADTLGQFPSIKDVLQAAAAEHQDQGQEVNGEVRSRRDSICSSVSLESSAAETQEEMLQVLKEKMRLEGQLEALSLEASQALKEKAELQAQLAALSTKLQAQVECSHSSQQRQDSLSSEVDTLKQSCWDLERAMTDLQNMLEAKNASLASSNNDLQVAEEQYQRLMAKVEDMQRSMLSKDNTVHDLRQQMTALQSQLQQVQLERTTLTSKLKASQAEISSLQSVRQWYQQQLALAQEARVRLQGEMAHIQVGQMTQAGLLEHLKLENVSLSQQLTETQHRSMKEKGRIAAQLQGIEADMLDQEAAFMQIQEAKTMVEEDLQRRLEEFEGERERLQRMADSAASLEQQLEQVKLTLLQRDQQLEALQQEHLDLMKQLTLTQEALQSREQSLDALQTHYDELQARLGELQGEAASREDTICLLQNEKIILEAALQAAKSGKEELDRGARRLEEGTEETSETLEKLREELAIKSGQVEHLQQETAALKKQMQKIKEQFLQQKVMVEAYRRDATSKDQLISELKATRKRLDSELKELRQELMQVHGEKRTAEAELSRLHREVAQVRQHMADLEGHLQSAQKERDEMETHLQSLQFDKEQMVAVTEANEALKKQIEELQQEARKAITEQKQKMRRLGSDLTSAQKEMKTKHKAYENAVGILSRRLQEALAAKEAADAELGQLRAQGGSSDSSLALHERIQALEAELQAVSHSKTLLEKELQEVIALTSQELEESREKVLELEDELQESRGFRKKIKRLEESNKKLALELEHEKGKLTGLGQSNAALREHNSILETALAKREADLVQLNLQVQAVLQRKEEEDRQMKHLVQALQASLEKEKEKVNSLKEQVAAAKVEAGHNRRHFKAASLELSEVKKELQAKEHLVQKLQAEADDLQIREGKHSQEIAQFQAELAEARAQLQLLQKQLDEQLSKQPVGNQEMENLKWEVDQKEREIQSLKQQLDLTEQQGRKELEGLQQLLQNVKSELEMAQEDLSMTQKDKFMLQAKVSELKNNMKTLLQQNQQLKLDLRRGAAKTRKEPKGEASSSNPATPIKIPDCPVPASLLEELLRPPPAVSKEPLKNLNSCLQQLKQEMDSLQRQMEEHALTVHESLSSWTPLEPATASPVPPGGHAGPRGDPQRHSQSRASKEGPGE
Protein: Rho GTPase-activating protein 4 (Rho-GAP hematopoietic protein C1) (Rho-type GTPase-activating protein 4) (p115) (P98171)
Organism: Homo sapiens (Human)
Function: Inhibitory effect on stress fiber organization. May down-regulate Rho-like GTPase in hematopoietic cells.
Subcellular location: Cytoplasm. Note=Just below the plasma membrane.
Interaction partners:
- Vasopressin V2 receptor
- Actin nucleation-promoting factor WAS
Sequence:
MAAHGKLRRERGLQAEYETQVKEMRWQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSFRKEPSLLSPLHCWAVLLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTAKKTYQAYHMESVNAEAKLREAERQEEKRAGRSVPTTTAGATEAGPLRKSSLKKGGRLVEKRQAKFMEHKLKCTKARNEYLLSLASVNAAVSNYYLHDVLDLMDCCDTGFHLALGQVLRSYTAAESRTQASQVQGLGSLEEAVEALDPPGDKAKVLEVHATVFCPPLRFDYHPHDGDEVAEICVEMELRDEILPRAQNIQSRLDRQTIETEEVNKTLKATLQALLEVVASDDGDVLDSFQTSPSTESLKSTSSDPGSRQAGRRRGQQQETETFYLTKLQEYLSGRSILAKLQAKHEKLQEALQRGDKEEQEVSWTQYTQRKFQKSRQPRPSSQYNQRLFGGDMEKFIQSSGQPVPLVVESCIRFINLNGLQHEGIFRVSGAQLRVSEIRDAFERGEDPLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPPDLFGELLASSELEATAERVEHVSRLLWRLPAPVLVVLRYLFTFLNHLAQYSDENMMDPYNLAVCFGPTLLPVPAGQDPVALQGRVNQLVQTLIVQPDRVFPPLTSLPGPVYEKCMAPPSASCLGDAQLESLGADNEPELEAEMPAQEDDLEGVVEAVACFAYTGRTAQELSFRRGDVLRLHERASSDWWRGEHNGMRGLIPHKYITLPAGTEKQVVGAGLQTAGESGSSPEGLLASELVHRPEPCTSPEAMGPSGHRRRCLVPASPEQHVEVDKAVAQNMDSVFKELLGKTSVRQGLGPASTTSPSPGPRSPKAPPSSRLGRNKGFSRGPGAPASPSASHPQGLDTTPKPH
Protein: Cholinergic receptor, nicotinic, alpha 2a (neuronal) (Neuronal acetylcholine receptor subunit alpha-2a precursor) (Zgc:136717) (Q1RLX8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
- Cholinergic receptor nicotinic beta 3 subunit b
- Acetylcholine receptor subunit alpha
- Cholinergic receptor, nicotinic, alpha 4b
- Cholinergic receptor, nicotinic, beta 4
- Cholinergic receptor, nicotinic, beta 1
- Acetylcholine receptor subunit gamma precursor
- Acetylcholine receptor subunit epsilon precursor
- Cholinergic receptor, nicotinic, alpha 7
- Acetylcholine receptor subunit beta
- Neuronal acetylcholine receptor subunit beta-2
Sequence:
MAENRIKTLLNNLWMLILIADHVQPVLSDGWIHAHAEDKLFHKLFIGYNKWSRPVRNISDVVIVKFGLSIAQLIDVDEKNQMMTTNVWLKQEWNDYKLRWNPSEFDNVTSIRVPSEMIWVPDIVLYNNADGEFAVTHMTKAHLFHTGKVSWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQIEGTVDLKDYWESGEWAIINAVGTYNTKKYDCCHEIYPDITYFFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSDCGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHSMPRWVHSVFLDHIPRWLFMRRPEPEKKPKKTANLSTSKSWFQQETGVDGLVCQDMEFGIGLSTSISSPSATSLHLSDSEPLLQKYELQHLGHVVNLCQHPAKLGNLVSEPGLLFSPCVLRALEGVRYIADHLRAEDEDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTIGLFLPPWLSGMI
Protein: Zinc transporter ZIP9 (Solute carrier family 39 member 9) (Zrt- and Irt-like protein 9) (ZIP-9) (Q5BL29)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Has dual functions as membrane-bound androgen receptor and as an androgen-dependent zinc transporter both of which are mediated through G protein activation and are required for the androgen-dependent apoptotic response. Upon androgen binding, mediates apoptosis by directly activating a stimulatory G protein that leads to increased cAMP levels and MAP kinase activity and which is accompanied by increased intracellular free zinc levels (By similarity). May play a role in the proper zinc modulation during egg activation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A0A3Q7ZPG5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:A0A3Q7ZPG5}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NUM3}. Mitochondrion {ECO:0000250|UniProtKB:Q9NUM3}. Nucleus {ECO:0000250|UniProtKB:Q9NUM3}.
Interaction partners:
- Zinc transporter Slc39a7
- Zinc transporter ZIP10
- Zinc transporter ZIP13
- Solute carrier family 39 member 6.
- Zinc transporter ZIP1
- Proton-coupled zinc antiporter SLC30A5
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Solute carrier family 39 member 11.
- Zinc transporter 6
- Solute carrier family 39 member 8.
Sequence:
MDDFSSISLLSLSMLIGCYVAGTIPLAVNFSEEKLKLVTVLGAGLLCGTALAVIIPEGVHALYEEMLEGVHNHGHGQVEAEVSEQKVAEGVVRPSGEHGHGHEQLHAYIGISLVLGFVFMLLVDQIGSAHMHSSDDPEAARAASSKITTTLGLVVHAAADGVALGAAASTSQTSVQLIVFVAIMLHKAPAAFGLVSFLMHAGLERNRIRKHLLVFALAAPVLAMVTYVGLSQSSKEALSDVNATGVAMLFSAGTFLYVATVHVLPEVGGMGGHSHSPGGSAGKGLSKLEVGALVLGCLIPLVLSIGHQH
Protein: Solute carrier family 8 member 1a (F1R4F4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Calcium-transporting ATPase
- Calcium-transporting ATPase
- Transient receptor potential cation channel subfamily V member 6 isoform X1
Sequence:
MGQSGTSSYFSLALNLSIFLLVFSYELTPVIAGSSKSSLDVDTSNANSSQETCGGSYECKEGVILPIWTPVNPSFGDKLARATVYFVGLFYMFLGVSIIADRFMASIEVITSQEKEITIKKPNGETTTTTVRIWNETVSNLTLMALGSSAPEILLSVVEVCGHNFDAGELGPNTIVGSAAFNMFVIIGLCVSVIPEGEHRKVKHLRVFFVTATWSIFAYTWLYLILAVISPGIVEVWEGLLTLFFFPICVLFAWVADRRLLFYKYVYKRYRVGKKRGIIIETEGEPELQSKADIEMDGGMLNSHAEEFLDGAVDNEDKDADEDEARREMAKILKELKQKHPEKEMEQLVELANYHVLSQQQKSRAFYRCQATRLMTGAGNILKKHAADQARKALGIHELRSEVSDNDISSKIFFDPGTYQCLENCGTVALNVVRRGGDLTSTVSVEYRTEDGTANAGSDYQFTEGVIIFKPGETEKEIRVDIIDDDIFEEDEHFLVHLSNVKVISEGANNGNPGTNHVDALAGLGLPSTATVTIFDDDHAGIFLFEEPIVHISESIGMMEVKVVRTSGARGVVVIPYKTIEGTAKGGGEDFEDTHGVLEFQNDEISKTIQINIIDDEEYEKNKNFFLEIGEPQLVEMSERKAMLLHECGGFVKTGRDVYRKVQGRDKPIPSTIISISEDGEEETLTKKEKDERRIAEMGRPTLGEHVKLEVIIEESYEFKSTVDKLIKKTNLALLVGTNSWRDQFVEAITVNSGDDDDEECGQEKMPSCFDYVMHFLTVFWKVLFAFVPPTDYWNGWACFIVSIMMIGVLTAFIGDIASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAAIQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIFHQSQGRQFRVDPGTLAFSVTLFTIFAFVCIAVLMYRRRPEIGGELGGPRHPKIITTTLFFSLWLMYIILSSMEAYCIIKGF
Protein: DNA polymerase delta subunit 2 (DNA polymerase delta subunit p50) (O35654)
Organism: Mus musculus (Mouse)
Function: Accessory component of both the DNA polymerase delta complex and the DNA polymerase zeta complex. As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS as a component of the DNA polymerase zeta complex. Along with POLD3, dramatically increases the efficiency and processivity of DNA synthesis of the DNA polymerase zeta complex compared to the minimal zeta complex, consisting of only REV3L and REV7.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P49005}. Note=Recruited to DNA damage sites within 2 hours following UV irradiation. {ECO:0000250|UniProtKB:P49005}.
Interaction partners:
- DNA polymerase zeta catalytic subunit
- DNA polymerase delta subunit 3
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA polymerase delta catalytic subunit
- Proliferating cell nuclear antigen
- DNA polymerase delta subunit 4
- DNA polymerase alpha catalytic subunit
- DNA polymerase alpha subunit B
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit 2
Sequence:
MFSEQAAQRAHTLLAPPSASNATFARVPVATYTNSSQPFRLGERSFNRQYAHIYATRLIQMRPFLVSRAQQHWGSRVEVKKLCELQPGEQCCVVGTLFKAMSLQPSILREISEEHNLVPQPPRSKYIHPDDELVLEDELQRIKLKGTIDVSKLVTGTVLAVLGSAKDDGRFQVEDHCFADLAPQKPVPPLDTDRFVLLVSGLGLGGGGGESLLGTQLLVDVVTGQLGDEGEQCSAAHVSRVILAGNLLSHNTQSRDSINKAKYLTKKTQAASVEAVKMLDEILLQLSASVPVDVMPGEFDPTNYTLPQQPLHPCMFPLATAYSTLQLVTNPYQATIDGVRFLGTSGQNVSDIFRYSSMEDHLEILEWTLRVRHISPTAPDTLGCYPFYKTDPFIFPECPHVYFCGNTPSFGSKIIRGPEDQVVLLVAVPDFSSTQTACLVNLRSLACQPISFAGFGAEQEDLEGLGLGP
Protein: Glutamate racemase (EC 5.1.1.3) (Q836J0)
Organism: Enterococcus faecalis (strain ATCC 700802 / V583)
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Interaction partners:
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Multifunctional fusion protein
- Phosphoribosylformylglycinamidine synthase subunit PurQ
- Phosphoesterase
- Alanine racemase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase
Sequence:
MSNQEAIGLIDSGVGGLTVLKEALKQLPNERLIYLGDTARCPYGPRPAEQVVQFTWEMADFLLKKRIKMLVIACNTATAVALEEIKAALPIPVVGVILPGARAAVKVTKNNKIGVIGTLGTIKSASYEIAIKSKAPTIEVTSLDCPKFVPIVESNQYRSSVAKKIVAETLQALQLKGLDTLILGCTHYPLLRPVIQNVMGSHVTLIDSGAETVGEVSMLLDYFDIAHTPEAPTQPHEFYTTGSAKMFEEIASSWLGIENLKAQQIHLGGNEND
Protein: Rho GTPase activating protein at 1A, isoform E (X2JC00)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.
Interaction partners:
- Protein still life, isoform SIF type 1
- Growth factor receptor-bound protein 2
- Ras-related protein Rac2
Sequence:
MSVFDDFQRLWMQRFPQSSLSDAWEQDVRASLERHKVRINELSKELEQETLYVEYLERLLSDVERYRVSGGDPKALFEAASGSCASSNNSNCSSTTNGATQEESNTNLDKDFKSSLNLRESPSSTGAKDKDRLSLNPDNKYTTHTNAVIGGIGSEKVSGPLHSTQITADGKRTGELYLKREEDKCKDSNSEDTDGALQQCITELAASLKAQPDNVAGGRLENDVDIDKPLRKSTSQYVTVIQVKEAKDKESADGTTSSSGIGEPQQQPTPPSTFSRYSEATAPPLSPSLTSYAAHVEAKKKMPPRPPPKNIRRVEPPTIPSQQLSSSPKRETYMINTMPSSSSGSLCIDSLGNSLERNIKPSDILRQKSSDNLDSKYSAKRKTTPELSKFVNVNNPELMEELGRKMVSKADSLEQTRRNDSSPSGCGSLGRTSSTPGRSLTPGRTGVGASPTGSLSKTGKLAMADSSSTSSLERRSCLQAVDADIGTESRESGANQRSVGSKESLTSQGISEVQIKSYESVSSLSSESAKAVASQQSAAAGGALAECEPYYDSVPLDNGDGEYVFIKPGRTGSSSSRDDLSTPGSSILPLPNVADPESPGRTSNYVNIDFFLQQGIETRSSSLDSDGEYEGPPILRTISHDDQTTTQTTPGAIRKNLVSAILVCGNARGAKIRSILSSIIQSETIYVECLNKMMQYKKAIHATLTTSQPVIREEEENTIFFKIDELYDLHTGFLSDLKTIVSHEGGDVLIGEPFRRLAEMFDLYSAFLHNYKNAIETVKKCSANNPQFKKIVSTIVLNLQTEQSLTLEDLLHKPVARVQINALVFNDLLRETPNAHPDHQPLRQAQKIIQMFLNQFNVVNQRLPIESNRNLRRMVRNSFIVELVDGHRKLRHLFLFNDVIACAKYKALGRDRIDYELKWFIPLKDVSIYEEADPAVELKESSPANISQVKRNLRSVRDQLAMEVANSGSGAFRSGDKYRRKLADLESQLVLATPNLVLRLGNKANNKTITFFLSSDFERTQWIDSILSLKQKCNLPGANTINSLEVTAFIVAMQKGMKTEMGSYLMRNTNDESLLVGDLYMGVHGLEGLEQANDLYICVEVDSYGHYFRKATTKKICRSQTPLWNESFMLELEGSQNVRILLYEAKERPLLKAKHILKLSLSWLTETTQPKSIKLTETLELGCSFRFIPGELFRGSTKPGALFGAKMSQVLKREKRDIPFIIGACIREVERRGMLEVGCYRVSGSASDLAKLKKAFESDAYEAEQLLREVDIHSVTGILKTFLRELPEALFTDQLYPRFFDTFSAFSNNNESTRINELLKVFEELPQANKASITSILDHLIRVHEKETDNKMSLHNLAMVFGPTLLRPGQTQVKQKDPLAASTVDVMAQAGILYCFLQARIKKD
Protein: Annexin A7 (Annexin VII) (Annexin-7) (Synexin) (P24639)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.
Interaction partners:
Sequence:
MSYPPNQGYPPQSNSPQPGQYGAPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQQGYPPQGYPPQQGYPPVGVPVGVPVGFAPGMVVGYHQGYFVGTITHDCKHDAEVLRKAMKGIGTNESDLIKVLANRNWAEREQIKREFSAKYSKDLIQDIKSETSGNFEKCLVALLTEPAHFDVEQIHSACAGAGTNENTIIEILVTRSNVQMEYIKQIFKNKHGKSLKDRLESEASGDFKKLLEKLTEPRDESPVINPMQVSKDAEDLYKAGEGKIGTDEKEFIKILTSRSLPHIAAVASEYIKHHKKHSLIKAIDSEFSGSIKTGLIAIVTYALNPYGYFAEILNKSMKGAGTNDNKLIRTVVTQMHNMPQIKTAYSTLFKNSLAHDIQADCSGDFKKLLLDIIS
Protein: Catabolite gene activator (Cyclic AMP receptor protein) (O34015)
Organism: Vibrio cholerae
Interaction partners:
Sequence:
MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERTAWVRAKTPCEVAEISFKKFRQLIQVNPDILMRLSGQMARRLQMTSQKVGDLAFLDVTGRIAQTLLNLARQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVYGTR
Protein: Alpha/beta hydrolase (O05294)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty-acid-CoA ligase FadD36
- Conserved protein
- Probable ECF RNA polymerase sigma factor SigI
Sequence:
MLLPVLEPADRPCDAPGWFLYLTDIPRAGVEYGQLLAVLPLQRMLPAGDGHPVLVLPGLLAGDGSTWILRRILRRLGYAAYGWGLGRNIGPTAKAVSGMRDLLDKLHSRYHTPVSLIGWSLGGIFARGLARDHPSAVRQVITLGSPFGMRDTCETRSAWSFNRYAHLHTERHELPLEMESEPLPVPTTAIYSRCDGMVAWQTCMNSPSERAENIAVRSSHIGYGHNPPVVWAIADRLAQPQGAWAPFRPPKVLSPLFPRPDTPAEAVSTPQTRPA
Protein: GTPase-activating protein gyp2 (O94711)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Stimulates specifically the GTPase activity of ypt2 and ryh1. Inactivates ryh1 during recycling between the endosome and the Golgi compartments (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTPase-activating protein gyp7
- GTPase-activating protein gyp1
Sequence:
MNLLKHIFLEDDYDAYEGTLDPASFFRINKQEEIIASTVCEIGWEYSKSFGNAYICTSFLCFHSDDFKTRFTFPLAAVRKLERENSDNDTFTFDLSNFHSQIIHLRFKGTRQQSEFFCDRLVRQLHASLEDASSVGLFLLSLASERVCFSESANSQEIESIDLGLGSQFGYPIASSNTNGLINENNSKSWIQYLKKNGANFNLIQTPNFQKLVQSGIPNNLRADIWETCSGSLFPRWKSKGFYAKNIDSVINNRCEYSEEIEKDLTRSLPDYPAYQSPTGINTLRRILLFYSETNKEVGYCQAMNIVLAALLVYCTEEQAYFLFSQLCEFYIPGYYAKIIHGLLLDLTVFEYVLEHTLPHLYQKIIELDMDLKLITINWFFSLFIKDFRLDYAFRILDCLFVNGPRVLFQVALALFKVNAQGILNATDDSSVMKVFRQCFDHINQGTAADEKMAALGSRSSMCTLPQLFAVAFEYFDFITDSFVSAKRKEFKSSVLYSLRCFTKRSHLRSVYQTTLLSNTDLDLVYDAFINAIGENNICHGDVLEQKIDFNGFERLVDCAAPPLSVIREPLHYQRSKRKLFTRLYIWMKDGDSTETSLTFKRIIHGLERLKADIALHSEILCFQLYDLKRDGTLRTEEVVELSESLILLCCYEGDEKDEERLTVISEFLKSCFSGCQDRRSFQITMEDFQAIVDTTGLHATLEFFLKKLIDGLLGKLNAS
Protein: Putative phosphatidylinositol-3-phosphatase (Phosphatidylinositol phosphate phosphatase) (PIPPh) (EC 3.1.3.64) (Q8A7J9)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Function: May be responsible for the conversion of phosphatidylinositol phosphate diacylglycerol (PIP-DAG) to phosphatidylinositol diacylglycerol (PI-DAG), making it a key enzyme in the inositol glycerophospholipid biosynthesis pathway.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylinositol phosphate synthase
- GtrA/DPMS transmembrane domain-containing protein
- Phosphoinositol dihydroceramide synthase
- Cardiolipin synthase
- Cardiolipin synthase
- Cardiolipin synthase
- Inositol-3-phosphate synthase 1
Sequence:
MKRPSFLPVLIGTGFGSGFSPFAPGTAGALLASIIWIALYFLLPFTALLWTTAALVVLFTFAGIWAANKLESCWGEDPSRVVVDEMVGVWIPLLAVPDNDRWYWYVIAAFALFRIFDIVKPLGVRKMENFKGGVGVMMDDVLAGVYSFILIAVARWVIG