wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase CYL) (P41240)
Organism: Homo sapiens (Human)
Function: Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN, CSK or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Mainly cytoplasmic, also present in lipid rafts. {ECO:0000250}.
Interaction partners:
- Phosphoprotein associated with glycosphingolipid-enriched microdomains 1
- Tyrosine-protein phosphatase non-receptor type 22
- Proto-oncogene tyrosine-protein kinase Src
- Paxillin
- Tyrosine-protein kinase Lyn
- SHC-transforming protein 1
- Caveolin-1
- Epidermal growth factor receptor
- Docking protein 3
- Tyrosine-protein kinase Lck
Sequence:
MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCDGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTSDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMKNCWHLDAAMRPSFLQLREQLEHIKTHELHL
Protein: Mothers against decapentaplegic homolog 2 (MAD homolog 2) (Mothers against DPP homolog 2) (Mad-related protein 2) (mMad2) (SMAD family member 2) (SMAD 2) (Smad2) (Q62432)
Organism: Mus musculus (Mouse)
Function: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:33548622}. Nucleus {ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:33548622}. Note=Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 or with IPO7 (PubMed:21145499, PubMed:33548622). On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (By similarity). Localized mainly to the nucleus in the early stages of embryo development with expression becoming evident in the cytoplasm at the blastocyst and epiblast stages (PubMed:21145499). {ECO:0000250|UniProtKB:Q15796, ECO:0000269|PubMed:21145499, ECO:0000269|PubMed:33548622}.
Interaction partners:
- E3 ubiquitin-protein ligase SMURF2
- Mothers against decapentaplegic homolog 4
- Forkhead box protein H1
- Mothers against decapentaplegic homolog 3
- TGF-beta receptor type-1
- Ski-like protein
- E3 ubiquitin-protein ligase TRIM33
- Zinc finger FYVE domain-containing protein
- TGF-beta receptor type-2
- Catenin beta-1
Sequence:
MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTVDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
Protein: Paired box protein Pax-4 (Pax4 transcription factor) (G2ZGB0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MRKPPSNEISVYFSGEGSVNQLGGVFLNGRPLPVYKRRLMIELATEGMRPCEISRILKVSNGCVSKILGRFQRTGAIGPKAVGGSRPRLLTPEVISIIVQHKRQNPTLFAWEIRQKLATERACRGDQVPSVSSINRILKKIHQDVDIAYPNEKHYHTEHLNVQSHFQQQMNTNLRRTAHRSRTAFTADQSGRLEKEFTCGLYPDLLTREKLAEETNLSQDTIKVWFSNRRARMRRERKFEHNDCGIARRGFLGNCRNALISLSSTAGCSLDDYRAHHAPSAFPLAAQRDRNTFPLAHLNSNALSSCSFDQTESLMPMCHHGNEALAYRLVSPNIDERILLANGTQWMNHKTLTGQNSPMF
Protein: Protein-tyrosine-phosphatase MKP1 (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 1) (AtMKP1) (Q9C5S1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein-tyrosine-phosphatase that acts as a negative regulator of MPK6 and MPK3 signaling by dephosphorylating and repressing MPK6 and MPK3. Modulates defense response by repressing salicylic acid (SA) production, camalexin biosynthesis and SNC1-mediated responses. Acts as a negative regulator of MPK6-mediated pathogen-associated molecular pattern (PAMP) responses, including MPK6 and MPK3 activation, accumulation of extracellular reactive oxygen species and inhibition of seedling growth. Involved in UV-B stress tolerance. May be involved in salt and genotoxic stress responses.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19789277}.
Interaction partners:
- Mitogen-activated protein kinase 6
- Protein-tyrosine-phosphatase PTP1
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase 12
- Inositol diphosphatase DSP4
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN1
- At4g21108/At4g21108
Sequence:
MVGREDAMGNDEAPPGSKKMFWRSASWSASRTASQVPEGDEQSLNIPCAISSGPSRRCPAAPLTPRSHHNSKARACLPPLQPLAISRRSLDEWPKAGSDDVGEWPHPPTPSGNKTGERLKLDLSSTQQRVTDKSSGLAKREKIAFFDKECSKVADHIYVGGDAVAKDKSILKNNGITHILNCVGFICPEYFKSDFCYRSLWLQDSPSEDITSILYDVFDYFEDVREQSGRIFVHCCQGVSRSTSLVIAYLMWREGQSFDDAFQYVKSARGIADPNMGFACQLLQCQKRVHAFPLSPTSLLRMYKMSPHSPYDPLHLVPKLLNDPCPGSLDSRGAFIIQLPSAIYIWVGRQCETIMEKDAKAAVCQIARYEKVEAPIMVVREGDEPVYYWDAFASILPMIGGSVIKVQPGDRKVDAYNLDFEIFQKAIEGGFVPTLASSNNEHETHLPARENSWSSLKCKFASRFDKGFRYVSKTPLSRVYSDSMMIVHSSGSPSSTTSSSSTASPPFLSPDSVCSTNSGNSLKSFSQSSGRSSLRPSIPPSLTLPKFSSLSLLPSQTSPKESRGVNTFLQPSPNRKASPSLAERRGSLKGSLKLPGLADSNRGTPAFTLHPDDSNDIVFNLEGIRNGDLYPPSDCKGTSVDSDLPEKEIISLISCSKSDRHKSGGDTDSSGQPLACRWPSMEMITKLSRAYLDSESVIAIPLPSDAVGETGSRNLYIWIGKSFSLDNNCSLVDSNKAADTVENVDWVQIGESILCQMDLPKDTPIKIVRESEDQTELLALLSAL
Protein: NADPH:adrenodoxin oxidoreductase, mitochondrial (AR) (Adrenodoxin reductase) (EC 1.18.1.6) (Ferredoxin--NADP(+) reductase) (Ferredoxin reductase) (EC 1.18.1.-) (P22570)
Organism: Homo sapiens (Human)
Function: Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:29040572}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Adrenodoxin, mitochondrial
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Ferredoxin-2, mitochondrial
- Delta-1-pyrroline-5-carboxylate synthase
- Steroidogenic acute regulatory protein, mitochondrial
- Bis
- Electron transfer flavoprotein subunit beta
- Sterol 26-hydroxylase, mitochondrial
- Voltage-gated monoatomic cation channel TMEM109
- Glutamyl-tRNA
Sequence:
MASRCWRWWGWSAWPRTRLPPAGSTPSFCHHFSTQEKTPQICVVGSGPAGFYTAQHLLKHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKNVINTFTQTAHSGRCAFWGNVEVGRDVTVPELREAYHAVVLSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH
Protein: Putative prenylated protein tyrosine phosphatase PRL-1 (Q7KPK2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSITMRQKDLRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEFFVVLYRYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARLKHKNGHKNSCSVQ
Protein: DnaJ homolog subfamily B member 9 (Endoplasmic reticulum DNA J domain-containing protein 4) (ER-resident protein ERdj4) (ERdj4) (Microvascular endothelial differentiation gene 1 protein) (Mdg-1) (P97554)
Organism: Rattus norvegicus (Rat)
Function: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (By similarity). In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q9QYI6}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Hypoxia up-regulated protein 1
- Endoplasmin
- Heat shock 70 kDa protein 4
- Heat shock cognate 71 kDa protein
- Heat shock cognate 71 kDa protein
- alpha-1,2-Mannosidase
- Heat shock 70 kDa protein 13
- X-box-binding protein 1
- Heat shock 70 kDa protein 1A
Sequence:
MATPQSVFVFAICILMITELILASKNYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDIIGHSAFTNGKGQRSNGSPFEQSFNFNFDDLFKDFNLFGQNQNTRSKKHFENHFQTRQDGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDSTNRRTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ
Protein: Tumor necrosis factor receptor superfamily member 1A (Tumor necrosis factor receptor 1) (TNF-R1) (Tumor necrosis factor receptor type I) (TNF-RI) (TNFR-I) (p55) (p60) (CD antigen CD120a) (O19131)
Organism: Bos taurus (Bovine)
Function: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Lymphotoxin-alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- FAS-associated death domain protein
- NF-kappa-B essential modulator
- TNF receptor-associated factor
- Mitogen-activated protein kinase kinase kinase 7
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
Sequence:
MGLPTVPGLLLPLVLPALLADVYPAGVQGLVPHPGDLEKRESPCPQGKYNHPQNSTICCTKCHKGTYLYNDCPGPGRDTDCRVCAPGTYTALENHLRRCLSCSRCRDEMFQVEISPCVVDRDTVCGCRKNQYREYWGETGFRCLNCSLCPNGTVNIPCQERQDTICHCHMGFFLKGAKCISCHDCKNKECEKLCPTRPSTGKDSQDPGTTVLLPLVIVFGLCLASFASVVLACRYQRWKPKLYSIICGQSTLVKEGEPELLVPAPGFNPTTTICFSSTPSSSPVSIPPYISCDRSNFGAVASPSSETAPPHLKAGPILPGPPASTHLCTPGPPASTHLCTPGPPASTHLCTPVQKWEASAPSAPDQLADADPATLYAVVDGVPPSRWKELVRRLGLSEHEIERLELENGRHLREAQYSMLAAWRRRTPRREATLELLGRVLRDMDLLGCLENIEEALGGAARLASEPRLLW
Protein: Regulator of G-protein signaling 20 (G3V716)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MRTANGGPRAGASPSASPEDPNLPVESEQTEMRMRQMCSGSETQGSVPSQQQGVGGRGSNACCFCWCCCCSCSCLTVRNQEDQRPQRAAHELRTDIPACEESPMPTLEEVCAWAQSFDNLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKREANKSTIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVDPSQHIFDDAQLQIYTLMHRDSYPRFMNSTVYKDLLKSLAEKAVEA
Protein: Hemomucin (Q58SM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VTPPKDLKGALESNFHLEGAERLLEGRVYGPECLIARNNEIYTGIHGGEVIKLTSNHVTHVTKIGQPCEDIYEESRCGRPLGLAFDTQGNNLIIADAYYGLWQVDLGTNKKTLLVSPAQELAGKSINRPAKIFNGVTVSKEGDVYWTDSSSDFTIEDLVFASFANPSGRLFKYNRSKNVSEVLLDELAFANGLALSPNEDFIVVAETGAMRLTKYHLKGAKAGQSEVFVDGLPGLPDNLTPDAEGIWVPLVQSADSEHPNGFTLFTRFPSVRLFLARMLALFELPFRYLNSVYPNKFSQRFIHFVGHMESITVLAPKRTTVVRVDWNGNIVGSLHGFDKSAATISHVLEFQDFLFLGSPTNQYLARVKSPKAKQPTLKVRNVRVEGEGLQASIGVPPSKATPKPKAAPSTTTPKPTATTTTTTPKPTTKTTTTTTTPKPTTTTTTKKPTTTTTTTTTTPKPTTTKPPTAKPFTTTTTTTTPKPTTTTTPTTPTPEPSKPKVKRTVPEKPAPVEEDIPSD
Protein: Small ribosomal subunit protein uS3 (30S ribosomal protein S3) (P9WH37)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Interaction partners:
- Large ribosomal subunit protein bL25
- Large ribosomal subunit protein bL33B
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein bL31
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein bL17
Sequence:
MGQKINPHGFRLGITTDWKSRWYADKQYAEYVKEDVAIRRLLSSGLERAGIADVEIERTRDRVRVDIHTARPGIVIGRRGTEADRIRADLEKLTGKQVQLNILEVKNPESQAQLVAQGVAEQLSNRVAFRRAMRKAIQSAMRQPNVKGIRVQCSGRLGGAEMSRSEFYREGRVPLHTLRADIDYGLYEAKTTFGRIGVKVWIYKGDIVGGKRELAAAAPAGADRPRRERPSGTRPRRSGASGTTATGTDAGRAAGGEEAAPDAAAPVEAQSTES
Protein: Uncharacterized protein (Q384X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Adrenodoxin reductase, putative
- Peptidyl-prolyl cis-trans isomerase
- Flavoprotein monooxygenase, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Sulfotransferase
- Uncharacterized protein
- NADH dehydrogenase subunit NI8M
- Uncharacterized protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
Sequence:
MLRRVLSGAGVRLTACDSCVALLHHSQRRGVRYANMQEALKPQAGHSAGQMSILNEICCNPDAEEERRKPIFRHEVAPRLSPGSPAKNYLRTMYQWGYNSLTLFLKTNEDPGPWWNANSSTLVSNWSQVGDYANAGMWSGVWRYTYGVGEYNLRPYEVRGRAWGRRHNKAGAMSVDYYYNCNNQAEQKRPRQYFMFPHTPEHQMHRRLKNPELPGFKVIDGLHGKRVVREIQYHLGQGLRFYLIDGVFGSHPSTNTPYRIITDNPTHAYFASLAAIRKFNYVAQQEIMLSKRITQSPIDEWGWRRPGVLVYHAPSWDFESPRIVEEFGGPRPRDLGLEHPKFIALEPYSIPMKAVVAAEPSCDILLDATAFLCARWGFYADDKGLLTLVAESILSPDAQHLTLVVCENEREADILRSSKYIFGARHHRIGDGWISRAWDVVSAPKSKVEACAHDLVEESLDRVHKPLPCRVGMPHARSHRHYGRRHVSGFGYKRKHSYTEDVTALAAAGGHLLSPKAKDVFASHPVRPSAFNLSSVDIVVVGSGSSASKIIIDGLQKRAMLYADPEKLQPALEAALNQAKSVKVVGSAEAKKLMQKLSETGSAHASV
Protein: RCG38839 (Zinc finger protein HIT-40) (Q99PJ6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEALGADMGSVTFEDVAVNFTVEEWALLGPSQKKLHRDVMEETFRNLAAIGKTQEDQNIDDDHRYSRRNQRNGVVERLLEHRKGCECKAIFRQIPDTTGNRKTSHRTVLCENHVYKDNMLISHASLNVSVPLQTAHKPPAYELCGENLYTFGECEKAFIYPECLLKHEDSDSRQRSCEFNQCGKIFKSSDHIQMRVSDETREEMCISKQHGDAFPYPDFLQYVEKIYTGKKPYACKQCGKTFSFLSNIRRHERTHTGEKPYRCNTCDKAFTCLTNFQEHERTHTGEKPYLCTQCGKAFSFLSNIRRHERTHTGEKPYRCNICGKAFSYLTNFQDHERTHTGEKPYVCTQCGKAFTYYYSFQTHKRCHTGEKPYVCKQCGKAFSYYNSIQTHKRCHTGEKPYVCKLCEKAFTTLSSLRYHERIHSGEKPHVCLQCGKGFNSSSTLRIHERTHTGEKPYKCKQCGKVFSVDSSLRCHERIHSGEKPYVCKQCGKAFTRHTSLRCHERIHCGEKPYKCKQCGKGFISSSNFRKHEWTHSGEKHCVCKLCGKAFTGHSSLRRHERIHSGEKPYVCKHCGKGFSSLSGCQRHEQIHTGEKPHVCKSCGKAFTNPSALRNHERIHSGEKPCICEQCGKGFISFSKFRIHERIHTGEKPYKCKQCGKAFTGHSSLRRHERIHSGEKPFVCKQCGKSFYTLSDCQRHEQIHTGEKPFICKQCGKAFTRSSSLKIHEKTHSRRNS
Protein: DnaD domain-containing protein (A0A0H2UQU9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MTYLDAFKSGTLVLPSALLLHFKELFPSSDDFLVWQFFYLQNTTGLEEMSPSQIAERIGKEISDVNQSISNLTERGLLQYRTIELNGEIELLFDASLALERLDDLFGAVHSSSDQLTPQNQLKDLVETFQQELGRLLTPFEIEDLTKTLKEDGTSADLIKEALREAVLNGKPNWKYIQAILRNWRHEGIKSVAQIEAKRAEREASNPQLTQVSADFINAMDLWKD
Protein: DNA polymerase delta subunit 2 (DNA polymerase delta subunit p50) (P49005)
Organism: Homo sapiens (Human)
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:0000269|PubMed:22801543}. Note=Recruited to DNA damage sites within 2 hours following UV irradiation. {ECO:0000269|PubMed:22801543}.
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA polymerase delta subunit 4
- DNA polymerase delta catalytic subunit
- DNA polymerase zeta catalytic subunit
- DNA polymerase delta subunit 3
- Proliferating cell nuclear antigen
- Flap endonuclease 1
- DNA polymerase alpha catalytic subunit
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase alpha subunit B
Sequence:
MFSEQAAQRAHTLLSPPSANNATFARVPVATYTNSSQPFRLGERSFSRQYAHIYATRLIQMRPFLENRAQQHWGSGVGVKKLCELQPEEKCCVVGTLFKAMPLQPSILREVSEEHNLLPQPPRSKYIHPDDELVLEDELQRIKLKGTIDVSKLVTGTVLAVFGSVRDDGKFLVEDYCFADLAPQKPAPPLDTDRFVLLVSGLGLGGGGGESLLGTQLLVDVVTGQLGDEGEQCSAAHVSRVILAGNLLSHSTQSRDSINKAKYLTKKTQAASVEAVKMLDEILLQLSASVPVDVMPGEFDPTNYTLPQQPLHPCMFPLATAYSTLQLVTNPYQATIDGVRFLGTSGQNVSDIFRYSSMEDHLEILEWTLRVRHISPTAPDTLGCYPFYKTDPFIFPECPHVYFCGNTPSFGSKIIRGPEDQTVLLVTVPDFSATQTACLVNLRSLACQPISFSGFGAEDDDLGGLGLGP
Protein: Limbic system-associated membrane protein (LSAMP) (Q8BLK3)
Organism: Mus musculus (Mouse)
Function: Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hippocampal mossy fiber projection (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
Interaction partners:
- Major prion protein
Sequence:
MVGRVQPDRKQLPLVLLRLLCLLPTGLPVRSVDFNRGTDNITVRQGDTAILRCVVEDKNSKVAWLNRSGIIFAGHDKWSLDPRVELEKRHALEYSLRIQKVDVYDEGSYTCSVQTQHEPKTSQVYLIVQVPPKISNISSDVTVNEGSNVTLVCMANGRPEPVITWRHLTPLGREFEGEEEYLEILGITREQSGKYECKAANEVSSADVKQVKVTVNYPPTITESKSNEATTGRQASLKCEASAVPAPDFEWYRDDTRINSANGLEIKSTEGQSSLTVTNVTEEHYGNYTCVAANKLGVTNASLVLFSKYAKTEPDSMQVIEFLHIDLKSIRHPLKVNPIQK
Protein: FLYWCH-type zinc finger-containing protein peb-1 (Pharyngeal enhancer binding protein peb-1) (A0A5S9MMK5)
Organism: Caenorhabditis elegans
Function: Putative transcription factor. Binds to specific sequence motif 5'-[TC][AGT]TGCC[GA][AT]-3' in regulatory elements of target genes such as myosin myo-2. May modulate gene expression, perhaps acting in opposition to transcription factor pha-4. Involved in morphogenesis, perhaps especially in formation of the pharynx. Plays roles in molting, feeding and morphology.
Subcellular location: Nucleus {ECO:0000269|PubMed:11203704, ECO:0000269|PubMed:15165844}. Note=Localization to nucleus dependent, in part, on FLYWCH-type domain. {ECO:0000269|PubMed:15165844}.
Interaction partners:
Sequence:
MMTTTVQKNCWRLDQTMLGLEKPGSSDISSSSTDTSAISPISVSSMPLSPDKEKKKISFVRYNPDIPQIVTSFKGYQKLMYQGYRYNIYQIAPERNFKSWRCVCAKKMHDGQWCKCRAETTMDNKNACTKGSHNHPPRHHVAEIEFIKSQLYSAALENPDHDAGDLVNQASMYLSDGVMFDNKESIKKSLVVARNKDGKPKKPRSKRMMKFEVDDDDENEYKMPKLETDISCFLPFINNMVKVEPPFSHTPTIQIPQPIPTPIQHQQQEQSNLLQPATLNGMNNPWMGMEDHLAMIWAANAMLNPGLDVLSTIAALSKHQQHVQGPSPQQAATAPTTASLSSNLSVSSFTPQMPKEASIAIPAPLQVLNLKDLKPLPPLANIQTSPVIQAANLLLPVAALKKDSSTQTTEEIKVSQCLTSGCGCRVIRICCCDEGVCRRTAAC
Protein: Chaperone protein dnaJ 8, chloroplastic (AtDjC8) (AtJ8) (Q9SAG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a continuous role in plant development probably in the structural organization of compartments.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Chaperone protein dnaJ 11, chloroplastic
- Chaperone protein dnaJ 20, chloroplastic
- Chaperone protein dnaJ C76, chloroplastic
- Heat shock 70 kDa protein 4
- ACT domain-containing protein ACR9
- Heat shock 70 kDa protein 7, chloroplastic
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- Heat shock protein DnaJ with tetratricopeptide repeat-containing protein
- AT4g39960/T5J17_130
- Amino acid transporter AVT6D
Sequence:
MTIALTIGGNGFSGLPGSSFSSSSSSFRLKNSRRKNTKMLNRSKVVCSSSSSVMDPYKTLKIRPDSSEYEVKKAFRQLAKKYHPDVCRGSNCGVQFQTINEAYDIVLKQIKNQMEGTEEFEPFDVYDEGLNGMNDPDCDTWEEWMGWEGAGTRDYSSHVNPYA
Protein: Headbutt, isoform E (A0A6H2EJZ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDYAQFYFRAVPISGQQQQQQQQQQHQQLVQQQLLAQQQQQLQIQQLQQQLLLQRLERELQQSYSCLRQRWLTDYAAPHQQHQQIAQQQQLFAAQQLQLQHQQLQHQQQQQQQQQQQQQQQQYSYYFSRGSTNTDLGLGLGLGFGLGSGNLASWYHLPSTSAHIYIGTTSSGGVPGSAPYPPYPYRSVGGYSGGGYPAAALINFDASPTPLLASAGTSPGYLPPLAIPAALPPPPPAPSVATDYYFSSRSTRTVPPPVPPTPAAVAAAASASAVSTSPFREYGSAAEELQAGYRYKATPRRRYDAYDNYGYLPGFASTTEDEEDLLEECLPQELLSTDCSSLEELRFFHLQEEDEDEDDEEVATQLAHILDLPDFLHPYGGSGRDSLHSHKTPPQHEYQTEHGSAAAGGAGSAGSDGRGGGGGQSQRVLEDQRYQPYQYQQQQQQQHHQQQQQQQHHQQHQSHFPQQHQHFQPSQQQLQQQSYHSYQYPSQDSCEGFNQFATNAGSCLGNQRMMVSKLWNSCFPEFTPDHVHRHNFYLCQWQRNTQVRIVYLFYRWITAITCLAALVCSLLDIGRTDEHFEHHYAKWWIYLTHWGLLFCTVQAWLAAWIVTQGMMVEREDFEIVRQAKKSRLHHLYWVLYTCATVYAFIVTMCYWLLVHNPEIHKIDALNIMVHVLNTIIMLIDLAIVGHPIKMSHAYFTTGIGLAYAIFTGIYFLAGGTDRKNQTAIYPMMDWTKPGKAIIVTACAIIFTFFVHFCCYLLYRGRVWLFTKLCIRGRRNRDGEMGEGLNDDSGSRMGGGGAGGSAGGGGAAGGSVAGAGAVGSSQDYAHQQQYPIAHTEQPRAGSHQQQQQQPPGNYQLPPQYSGYLQQPVVAGVNVGVISAEGVYQPIGTDTGRTSGGGGDGKHKSSSGSATGTGSGQGQGQGQGSGSGSGSGSALTRTVAHLDASQREQFLNPNKIVEYKMXRRCTRHRYTFHLSMKFLEKHCAQCEATRSAICEEERHLA