wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 268 (Zinc finger protein HZF3) (Q14587)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional repressor. Inhibits erythroid differentiation and tumor cell proliferation. Plays a role during ovarian cancer development and progression.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23665872}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:23665872}. Cytoplasm {ECO:0000269|PubMed:23665872}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:37926288}. Note=Under resting conditions, degraded by autophagosomes in the cytosol, resulting in low expression at the protein level. Accumulates in the cytoplasm during viral infection. {ECO:0000269|PubMed:37926288}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MATRVRTASIWVPPLQERNSSWDRIRKLQGQESILGQGTPGLQPLPGTPRQKQKSRRIEKVLEWLFISQEQPKITKSWGPLSFMDVFVDFTWEEWQLLDPAQKCLYRSVMLENYSNLVSLGYQHTKPDIIFKLEQGEELCMVQAQVPNQTCPNTVWKIDDLMDWHQENKDKLGSTAKSFECTTFGKLCLLSTKYLSRQKPHKCGTHGKSLKYIDFTSDYARNNPNGFQVHGKSFFHSKHEQTVIGIKYCESIESGKTVNKKSQLMCQQMYMGEKPFGCSCCEKAFSSKSYLLVHQQTHAEEKPYGCNECGKDFSSKSYLIVHQRIHTGEKLHECSECRKTFSFHSQLVIHQRIHTGENPYECCECGKVFSRKDQLVSHQKTHSGQKPYVCNECGKAFGLKSQLIIHERIHTGEKPYECNECQKAFNTKSNLMVHQRTHTGEKPYVCSDCGKAFTFKSQLIVHQGIHTGVKPYGCIQCGKGFSLKSQLIVHQRSHTGMKPYVCNECGKAFRSKSYLIIHTRTHTGEKLHECNNCGKAFSFKSQLIIHQRIHTGENPYECHECGKAFSRKYQLISHQRTHAGEKPYECTDCGKAFGLKSQLIIHQRTHTGEKPFECSECQKAFNTKSNLIVHQRTHTGEKPYSCNECGKAFTFKSQLIVHKGVHTGVKPYGCSQCAKTFSLKSQLIVHQRSHTGVKPYGCSECGKAFRSKSYLIIHMRTHTGEKPHECRECGKSFSFNSQLIVHQRIHTGENPYECSECGKAFNRKDQLISHQRTHAGEKPYGCSECGKAFSSKSYLIIHMRTHSGEKPYECNECGKAFIWKSLLIVHERTHAGVNPYKCSQCEKSFSGKLRLLVHQRMHTREKPYECSECGKAFIRNSQLIVHQRTHSGEKPYGCNECGKTFSQKSILSAHQRTHTGEKPCKCTECGKAFCWKSQLIMHQRTHVDDKH
Protein: Exocyst complex component 4 (Exocyst complex component Sec8) (O35382)
Organism: Mus musculus (Mouse)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96A65}. Cell projection {ECO:0000250|UniProtKB:Q62824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96A65}. Note=Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). Localizes at the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:Q62824, ECO:0000250|UniProtKB:Q96A65}.
Interaction partners:
- Exocyst complex component 2
- Exocyst complex component 6
- Exocyst complex component 8
- Exocyst complex component 1
- Exocyst complex component 5
- Exocyst complex component 3
- Exocyst complex component 7
- Ras-related protein Ral-A
- Exocyst complex component 6B
- Exocyst complex component 3-like protein
Sequence:
MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIEELHRHLYIKSTSRVVQRNKEKGKMSSHGKDPSPGPLIDVSNIPTPRKFLDASQYSAAGGSSVREMNLQDVKEDLECDPEENSTLFMGILIQGLARLKKIPETVKAIKERLEQELKQIVKRSTTQVADSAYQRGESLTVDNQPRLLLELLELLFDKFNAVATAHSVVLGYLQDSVGTQLTQQEEIKLYDMADVWVKIQDVLQMLLTEYLDMKNTRTASEPSAQLSYASTGREFAAFFAKKKPQRPKNSLFKFESSSHAISMSAYLREQRRELYSRSGELQGGPDDNLIEGGGTKFVCKPGARNITVIFHPLLRFIQEIEHALGLGPAKQCPLREFLTVYIKSIFLNQVLAEINKEIEGVTKTSDPLKILANADTMKVLGVQRPLLQSTIIVEKTVQDLMNLMHDLSAYSDQFLNMVCVKLQEYKDTCSTAYRGIVQSEEKLVISASWAKDDDISRLLKSLPNWTNMAQPKQLRPKREEEEDFIRAAFGKESEVLIGNLGDKLIPPQDILRDVSDLKALANMHESLEWLAGRTKSAFSNLSTSQMLSPAQESHVNMDLPPVSEQIMQTLSELAKTFQDMADRCLLVLHLEVRVHCFHYLIPLAKEGNYAIVANVESMDYDPLVVKLNKDISAMEEAMSASLQQHKFQYIFEGLGHLISCILINGAQYFRRISESGIKKMCRNIFVLQQNLTNITMSREADLDFARQYYEMLYNTADELLNLVVDQGVKYTELEYIHALTLLHRSQTGVGDQTTQNTRLQRLKEIICEQAAIKQATKDKKITTV
Protein: DNA-directed RNA polymerases II and IV subunit 5A (RPB5a) (DNA-directed RNA polymerase II subunit E) (RNA polymerase I, II and III 24.3 kDa subunit) (AtRPB24.3) (O81098)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerase IV which mediates short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of target sequences.
Subcellular location: Nucleus {ECO:0000269|PubMed:10231567}.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 9A
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II, IV and V subunit 12
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerase II subunit 4
Sequence:
MLTEEELKRLYRIQKTLMQMLRDRGYFIADSELTMTKQQFIRKHGDNMKREDLVTLKAKRNDNSDQLYIFFPDEAKVGVKTMKMYTNRMKSENVFRAILVVQQNLTPFARTCISEISSKFHLEVFQEAEMLVNIKEHVLVPEHQVLTTEEKKTLLERYTVKETQLPRIQVTDPIARYFGLKRGQVVKIIRPSETAGRYVTYRYVV
Protein: At4g36660 (Polyol transporter, putative (DUF1195)) (Q6NLX7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKEDDALPTTTTTGTATGTAMANSKKESSDSVLFGRGRYKFWAFAAILLLAFWSMFTGTVTLRLSTGNLNRLSEDLGIPNYDNLDVLEMEEREKVVKHMWDVYTNSRRIKLPRFWQEAFVAAYEELTSDVPGVREAAIGEIAKMSARSITLDPPPSRSMSARDLGRNLKRILHKPAASS
Protein: Max dimerization protein 3 (Max dimerizer 3) (Class C basic helix-loop-helix protein 13) (bHLHc13) (Max-associated protein 3) (Max-interacting transcriptional repressor MAD3) (Myx) (Q9BW11)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Protein max
- Paired amphipathic helix protein Sin3a
- Max-binding protein MNT
Sequence:
MEPLASNIQVLLQAAEFLERREREAEHGYASLCPHRSPGPIHRRKKRPPQAPGAQDSGRSVHNELEKRRRAQLKRCLERLKQQMPLGADCARYTTLSLLRRARMHIQKLEDQEQRARQLKERLRSKQQSLQRQLEQLRGLAGAAERERLRADSLDSSGLSSERSDSDQEELEVDVESLVFGGEAELLRGFVAGQEHSYSHGGGAWL
Protein: Putative transcription factor C15C8.2 (G5EFA5)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTTVPLHASSFSSGTTGAGGGVQQALQLQHCAYHVGASVGSSGSALNNNSINVPNNNTMGMSSAGSSNGSNLVNGQQRSTRGASKQRRDQINVEIQKLRDLLPLSDLIKDRLFQLQVMSLGCIFIRKHRYQQTVLQPQLQMLQMQMSSPMPRGIDICKALRGFMLMVTRSGKILHVSDNASEYLGHSVEEIMCQGDSIYDLVDGRDHGAVQAELASGPPGAATFPEERVFICRLNLARTAKRQLQYHKFVLFQGRYIQPAEFYQQLNAQNSQPDCDQPVFSAYCQPLINPENAEGMSTGNTHVFSTQHYLDMKFKEADTMASQHLGFSKEQLKGMSWYGMIHPNHVPEIAHKHRLLCQEKEGSVLALIRLQAANGEWIWLHTVFSIRPNNELNSDGKRLRHVIHCFHQKLTDLEAATLQANSWIYSMRHTYPTVFSCQDSPPPSEEQQPSSPQTPPFTEQPPMLVEQKPLIGAGIAPGFPSLDYNQIKVEIPMRPINTQIPLFTPESSSPESSASLHTSLLPHHNAFPLDILEDILPSNDVLPELKDEVDEILRQVEQSPATSPAHSFPSNVNFGHRHSMPNAFDSAELYKYLGPALFDGNFAMQHQHHLQQQHQSQPPHPYHFDYYNRKRSWAV
Protein: Ubiquitin protein ligase E3 component n-recognin 5 (E7EMW7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSIHFVVHPLPGTEDQLNDRLREVSEKLNKYNLNSHPPLNVLEQATIKQCVVGPNHAAFLLEDGRVCRIGFSVQPDRLELGKPDNNDGSKLNSNSGAGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQPQPVIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDEDGDDGDDTASESYLPGEDLMSLLDADIHSAHPSVIIDADAMFSEDISYFGYPSFRRSSLSRLGSSRERDSELLRERESVLRLRERRWLDGASFDNERGSTSKEGEPNLDKKNTPVQSPVSLGEDLQWWPDKDGTKFICIGALYSELLAVSSKGELYQWKWSESEPYRNAQNPSLHHPRATFLGLTNEKIVLLSANSIRATVATENNKVATWVDETLSSVASKLEHTAQTYSELQGERIVSLHCCALYTCAQLENSLYWWGVVPFSQRKKMLEKARAKNKKPKSSAGISSMPNITVGTQVCLRNNPLYHAGAVAFSISAGIPKVGVLMESVWNMNDSCRFQLRSPESLKNMEKASKTTEAKPESKQEPVKTEMGPPPSPASTCSDASSIASSASMPYKRRRSTPAPKEEEKVNEEQWSLREVVFVEDVKNVPVGKVLKVDGAYVAVKFPGTSSNTNCQNSSGPDADPSSLLQDCRLLRIDELQVVKTGGTPKVPDCFQRTPKKLCIPEKTEILAVNVDSKGVHAVLKTGNWVRYCIFDLATGKAEQENNFPTSSIAFLGQNERNVAIFTAGQESPIILRDGNGTIYPMAKDCMGGIRDPDWLDLPPISSLGMGVHSLINLPANSTIKKKAAVIIMAVEKQTLMQHILRCDYEACRQYLMNLEQAVVLEQNLQMLQTFISHRCDGNRNILHACVSVCFPTSNKETKEEEEAERSERNTFAERLSAVEAIANAISVVSSNGPGNRAGSSSSRSLRLREMMRRSLRAAGLGRHEAGASSSDHQDPVSPPIAPPSWVPDPPAMDPDGDIDFILAPAVGSLTTAATGTGQGPSTSTIPGPSTEPSVVESKDRKANAHFILKLLCDSVVLQPYLRELLSAKDARGMTPFMSAVSGRAYPAAITILETAQKIAKAEISSSEKEEDVFMGMVCPSGTNPDDSPLYVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAGQKSARLDLLYRLLTATNLVTLPNSRGEHLLLFLVQTVARQTVEHCQYRPPRIREDRNRKTASPEDSDMPDHDLEPPRFAQLALERVLQDWNALKSMIMFGSQENKDPLSASSRIGHLLPEEQVYLNQQSGTIRLDCFTHCLIVKCTADILLLDTLLGTLVKELQNKYTPGRREEAIAVTMRFLRSVARVFVILSVEMASSKKKNNFIPQPIGKCKRVFQALLPYAVEELCNVAESLIVPVRMGIARPTAPFTLASTSIDAMQGSEELFSVEPLPPRPSSDQSSSSSQSQSSYIIRNPQQRRISQSQPVRGRDEEQDDIVSADVEEVEVVEGVAGEEDHHDEQEEHGEENAEAEGQHDEHDEDGSDMELDLLAAAETESDSESNHSNQDNASGRRSVVTAATAGSEAGASSVPAFFSEDDSQSNDSSDSDSSSSQSDDIEQETFMLDEPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAASSAGLIYIDPSNLRRSGTISTSAAAAAAALEASNASSYLTSASSLARAYSIVIRQISDLMGLIPKYNHLVYSQIPAAVKLTYQDAVNLQNYVEEKLIPTWNWMVSIMDSTEAQLRYGSALASAGDPGHPNHPLHASQNSARRERMTAREEASLRTLEGRRRATLLSARQGMMSARGDFLNYALSLMRSHNDEHSDVLPVLDVCSLKHVAYVFQALIYWIKAMNQQTTLDTPQLERKRTRELLELGIDNEDSEHENDDDTNQSATLNDKDDDSLPAETGQNHPFFRRSDSMTFLGCIPPNPFEVPLAEAIPLADQPHLLQPNARKEDLFGRPSQGLYSSSASSGKCLMEVTVDRNCLEVLPTKMSYAANLKNVMNMQNRQKKEGEEQPVLPEETESSKPGPSAHDLAAQLKSSLLAEIGLTESEGPPLTSFRPQCSFMGMVISHDMLLGRWRLSLELFGRVFMEDVGAEPGSILTELGGFEVKESKFRREMEKLRNQQSRDLSLEVDRDRDLLIQQTMRQLNNHFGRRCATTPMAVHRVKVTFKDEPGEGSGVARSFYTAIAQAFLSNEKLPNLECIQNANKGTHTSLMQRLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSIDTRPFRPASEGNPSDDPEPLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAHGRENGADSILDLGLVDSSEKVQENRKRHGSSRSVVDMDLDDTDDGDDNAPLFYQPGKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLLQFKRWFWSIVEKMSMTERQDLVYFWTSSPSLPASEEGFQPMPSITIRPPDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIKTKNFGFV
Protein: Basic helix-loop-helix (BHLH) DNA-binding superfamily protein (F4JHC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLTMADGVEAAAGRSKRQNSLLRKQLALAVRSVQWSYAIFWSSSLTQPGVLEWGEGCYNGDMKKRKKSYESHYKYGLQKSKELRKLYLSMLEGDSGTTVSTTHDNLNDDDDNCHSTSMMLSPDDLSDEEWYYLVSMSYVFSPSQCLPGRASATGETIWLCNAQYAENKLFSRSLLARSASIQTVVCFPYLGGVIELGVTELISEDHNLLRNIKSCLMEISAHQDNDDEKKMEIKISEEKHQLPLGISDEDLHYKRTISTVLNYSADRSGKNDKNIRHRQPNIVTSEPGSSFLRWKQCEQQVSGFVQKKKSQNVLRKILHDVPLMHTKRMFPSQNSGLNQDDPSDRRKENEKFSVLRTMVPTVNEVDKESILNNTIKYLQELEARVEELESCMGSVNFVERQRKTTENLNDSVLIEETSGNYDDSTKIDDNSGETEQVTVFRDKTHLRVKLKETEVVIEVRCSYRDYIVADIMETLSNLHMDAFSVRSHTLNKFLTLNLKAKFRGAAVASVGMIKRELRRVIDFREPICDVPLSLHQVFRVFVCKVCQSLVGIFDNVVSSSSTKPRSILIHNSWAICIFH
Protein: DNA polymerase eta (EC 2.7.7.7) (Q9VNX1)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS). Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Inserts one or 2 nucleotide(s) opposite the lesion. During homologous recombination (HR) repair, has a overlapping role with the error-prone translesion polymerase PolZ1/DNApol-zeta to initiate repair synthesis that is completed by end joining or another polymerase that can bind and reinitiate synthesis. Particularly important for the repair of UV-induced pyrimidine dimers and for hydroxyurea (HU)-induced DNA damage. Although inserts the correct base, may cause base transitions and transversions depending upon the context (By similarity). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have any lyase activity, preventing the release of the 5'-deoxyribose phosphate (5'-dRP) residue (By similarity). This covalent trapping of the enzyme by the 5'-dRP residue inhibits its DNA synthetic activity during base excision repair, thereby avoiding high incidence of mutagenesis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24553286}. Note=Localizes to interphase nuclei but undetectable during mitosis. {ECO:0000269|PubMed:24553286}.
Interaction partners:
- DNA repair protein Rev1
- DNA polymerase zeta catalytic subunit
- Proliferating cell nuclear antigen 2
- Proliferating cell nuclear antigen
- DNA polymerase zeta subunit 2
- FI03607p
- DNA polymerase delta catalytic subunit
- GEO06356p1
- DNA repair protein Rad51 homolog
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MSSARSHVSMQNKYDRVVLLVDMDCFFCQVEEKQHPEYRNRPLAVVQYNPWRGGGIIAVNYAARAKGVTRHMRGDEAKDLCPEIVLCQVPNIREKADTSKYRDAGKEVANVLQRFTQLLERASVDEAYLDITETVNHRMQQMQSGAFALQPQELVNTFAVGYPSIGDYVNKITNRFANPYMDDERYQMSYDQNDLPAVRQSDIRLLIGASVAGEVRAAVKKETGYECSAGIAHNKILAKLAAGMNKPNKQTILPLTETASLFDSLPVGKIKGLGGKFGEVVCETLGIKFMGQVVKFSEVDLQRKFDEKNGTWLFNISRGIDLEAVTPRFYSKSIGCCKKFPGRNNITGLKTLQHWLGELSSEINDRLEKDFIENNRRAKHMVVQYVQDIDGEEVASSRSTALRDYDQESIVRLSLDLIKANTKTFLRPGSESALNNAIKFLGISVGKFETVSSGQNKLQEMFANQAAKKRRVSGDEPGQLPKVEMEKKQKQTDEFKMKSFFANYLQGAKKEDAKADGISANPLAAAAGAPNKNFVEEYKHKLHAAVRTEGTVLTSTPAEFKESFFSQYLKQQKKTGQQGSVTSREDSLDVQELAEELDAIEADNSKDFEEDTEEETELTSDTHMSKPEGQSSDAGQEQDPNTLNDSTGNDLYVETGIVPPTLTEDELKPSTSKRKFDEIESSVSNYKECYVEFAVPNLRTDILPTIKCDQCGANIPDEVKSLQTHRDHHFAQELSRTLRSTEREERTQSRQKISLKPTPPKKSKKTAGSGSSSYSTAPPSNSITKFFRAKPTQEQAPSDPQMNQCPECKAFIKCVDMPEHLDYHVARNLQRELNQQDLRTRTAALNKEKISPVQPKKQSQKKLNSTISASSSGTKTIAQFFSQSN
Protein: Os01g0230200 protein (cDNA clone:J013037L22, full insert sequence) (Q5NB28)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLSSGGELKSSSLVQQMVWVGTGNSSSSSIMGSLRQLPCSEEQDAASSPASMLFLPQQLLLHASSNSSPCLNIPEVNLSTGLHPLGSFHGDVQQQEIISGMPDQSWRQLLLGGLVGDHEKYSVATALLSKGLDDEASMPHEASAAAYDFYGHGGGAGDGILQASPEASSCKSQLSQMLLQAAASSPRSCVTTSGLGSSMMDFSNTAAVAPAAEPELTRKHHAGQSDNSSECNSTETGSALKKARVQASSSAQSTLKVRKERLGDRITALHQIVSPFGKTDTASVLQETIGYIRFLLGQIEALSYPYLGQCCSANPMQQQTGIMAGERSTDGLFPEFPAGQDAEKDGKKQQAKKDDDLRSRGLCLVPVSCMPHLAADNDVVVGSDFWAAAGGGGGGGAPPLAGMNLR
Protein: Cingulin (P59242)
Organism: Mus musculus (Mouse)
Function: Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:15292197}. Note=Localizes to the apical junction complex composed of tight and adherens junction (PubMed:15292197). Colocalizes with SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9P2M7, ECO:0000269|PubMed:15292197}.
Interaction partners:
- Tight junction protein 1
- Occludin
- Rho guanine nucleotide exchange factor 2
- Junctional adhesion molecule A
- Tight junction protein 2
- Tight junction protein ZO-3
- Rho guanine nucleotide exchange factor 18
- Transcription factor GATA-4
- MARVEL domain-containing protein 2
- Transforming protein RhoA
Sequence:
MADPRGPVDHGVQIRFITEPEGATEMGTLRRSGRRPARDARASTYGVAVRVQGIAGQPFVVLNSGEKGTDSFGVQIKGGNNRGSPGALSSDSELPENPYSQVKGRPATSRSSTSDEEPKDHLNGKLIRSQSQASLTGLAFMSPSNRSTSLLELAPKPTSSINTIDTAPLSSVDSLINKFDSQKGGQVRGRTGRRTRTLPHEQRKRSQSLDSRLPRDTREEREHQSANHWTRGTKYDNHVDSSKNPSQKQSPFSSFSRSRQTQDWVLQSFEETRDPAMVQFKSTPDLLRDQRETAPPGSADHVKATIYGILREGSSESEASVRRKVSLVLEQMQPLGMVSPASTKALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKELRRTQGELKELQAEQQNQEVTGRHRNQVLEKQLAALREEADRGRELEQQNLQLQKTLQQLRQDCEEASKAKVASETEAMMLGQRRATVETTLRETQEENDEFRRRILGLEQQLKEARGLAEGGEAVEARLRDKVHRLEVEKQQLEEALNAAQEEEGNLAAAKRALEVRLDEAQRGLARLGQEQQALNRALEEEGKQREALRRSKAELEEQKRLLNRTVDRLNKELEQIGDDSKLALQQLQAQMEDYKEKARKEVADAQRQAKDWASEAEKNSGGLSRLQDELQRLRQALQTSQAERDTARLDKELLAQRLQGLEQEAENKKRFQDDKARQLKSLEEKVSRLEAELDEEKNTVELLTDRVNRGRDQVDQLRTELMQERSARQDLECDKISLERQNKDLKTRLASSEGFQKPSASLSQLESQNQLLQERLQAEEREKTVLQSTNRKLERRVKELSIQIDDERQHVNDQKDQLTLRVKALKRQVDEAEEEIERLDSLRKKAQRELEEQHEVNEQLQARIKSLEKDAWRKASRSAAESALKQEGLSSDEEFDNVYDPSSIASLLTESNLQTSSC
Protein: AP-3 complex subunit sigma (AP-3 complex sigma3A subunit) (Adaptor-related protein complex 3 subunit sigma) (Clathrin-associated/assembly/adaptor protein, small 3) (Sigma-adaptin 3A) (Sigma3-adaptin) (Q09905)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:P47064}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P47064}; Peripheral membrane protein {ECO:0000250|UniProtKB:P47064}; Cytoplasmic side {ECO:0000250|UniProtKB:P47064}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250|UniProtKB:P47064}.
Interaction partners:
- AP-3 complex subunit beta
- AP-3 complex subunit delta
- AP-1 complex subunit gamma-1
- AP-3 complex subunit mu
- AP-1 complex subunit mu-1
- AP-2 complex subunit alpha
- Large ribosomal subunit protein eL8
- AP-2 complex subunit mu
- AP-1 complex subunit sigma-1
- AP-1 complex subunit beta-1
Sequence:
MIYAVFIFNNKGKPRLTKFYTPIDESIQQKLIGDIYAAVSTRPPTACNFLESNLIAGKNRIIYRQYATLYFVFVVDEGESELGILDLIQVFVEALDRCFNNVCELDLVFKFQEIHAILAEVVSGGLVLETNLNEIVLAAQNQMPKTKRSNAMPFSNTLSSFATRF
Protein: A-kinase anchor protein 11 (AKAP-11) (A-kinase anchor protein 220 kDa) (AKAP 220) (Protein kinase A-anchoring protein 11) (PRKA11) (Q62924)
Organism: Rattus norvegicus (Rat)
Function: Binds to type II regulatory subunits of protein kinase A and anchors/targets them.
Subcellular location: Peroxisome.
Interaction partners:
- A-kinase anchor protein 8
- IQ motif containing GTPase activating protein 2
- A-kinase anchor protein 1, mitochondrial
Sequence:
MQKMQCHLRRPLHSSSSFSSQAVMMTKPMQEHKKEYTAQQALFRPSGIVTSIPVPLAGSALLPYHVSSTLYQSKSLSSSEHNKANGGSPQEHIAMESSAEEVDCFKNTCLPSELSPCSQNDFKPTNGDIDMQSPSKLMSGSMIISNFSTAMVHTIVNETLESMTSFKATKPVDTNADYLTKTIKGKPVLSLCDQAAPQQNKASSKDMFAEHLSKSIIKHSLDKSKSVLPNIDKKPVSKEHMLVLGEESQLTLGETPKFLDFSDNSPQYCVPECKDSVGFGFSLEALPPCSMMTSQKSDLKGVMKDKVVTRHNLTNTAFEPLSFGQESSFRPSQTLSSAVLTCVDSLHVEDKQKIRDRNVIPDTPPSTPLVPSQTSSEWDIKKLTKQLKGELAKEFAPATPPSTPHNSSVGSLSENEQTTIEKEEFMLKLMRSLSEEVESSEGEEHPEMDVKSEHSGKKGQFADALATHIISLATEVAASHLDHEITQEFKVQNSHLTVPSQRSMLPALSHSDESIQTCSFASDMAAGVIAEAEKVANTRSCMLFGHERTICHVEGDRGKAEEKLDVEDIAHPREVETCVLSLPSCMPGLTYKYPSCESVTDEYAGHIIQVLKQEGGNSELIMDQYASRLAYRSVKSGVREAAKTVKVKCSLKLFPMHTSHVKTNKELLFSSKEHHQEVDKKRQRKKYGSHPCKYQTCDRTQDPCRNELSELYRFSASLASSITRDVKKQLTAPKVDLPKSSTDCCLFEKSECVDNRENVTGPEFSKSCQPLQNHGLCQNTSSLSGYSCGESAHTVEQYARKVVGDTLELSLGPAVFLNSETTTSPDRITYAEKLSPLINEACRYCDLKESHGCIRNSAQLFSKQGPCASAKPSSHSKLSSIRQKSRIFHLDVPQIHLNLDKRAVLAEKIVAEAIEKAERELSNTSLAADSGIGQDGISFAESLTTEIMTTAMTNAGHAVSSSKEVEDFQSTESLGSQQMNLSVGEDSTGSWSNLSFEDDHQDESSSFHHLSESSNGNSSSWSSLGLEGDLYENNLSFPTSDSDGPDDRESEQEDGAEGLQPSGKTLLIVNIDVEPGAVDPQLRVILQWLIPRRRKLENFIFSTLQRRSLSYFQSSYRREDGKWAMSCRL
Protein: N-acetylmuramoyl-L-alanine amidase (P73736)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- N-acetylmuramoyl-L-alanine amidase
- N-acetylmuramoyl-L-alanine amidase
- Apolipoprotein N-acyltransferase
- Sll0513 protein
Sequence:
MSRLPGFALTFLSVLLTSLPAMAGQLVNWNFNASQNRLTFYTDSRVQPTAQLIPNPTRIVVDLPGTTLRGPTVRQAGGGRVREIRIGEPDSFTTRVVIELDAGYTVDPQQVKVRGITPTQWVVELPTPELAPASNNNAPGPNPDGSSLPTQNLSAANPPSTGQQYLQVTGNGLFVRLDKNGDNSGIRIQPNARQSTVNFELNGAVLPESLVGQSLPVGQYGVEEIKFSDNPNNPRLSLALADSGGGWNAYYSRVGGGVVLLPKQISRSGGANPAPGSAAVPVSNNTSNSSPSSSGNRSPNDRLVSQASNRNLANITAIEVTRDDSQLIIRGDRQINARGNFNRLTGNYEIRLDRAQLSPQFQSPELATGGPLYQLNISQETNDSVLILVRPNTGRRFGRLFRSGGSLYALELISDTTASRPTGNLPANNPPRGNSGDQISIAVQPPPANATPSFPPEWSNPPAGNLPSVPRGGRLVVVDPGHGGKDPGAIGIRGVQEKDVVLAVSQYLQRYLEQQGVRVLMTRTGDYFISLQGRTDMANRAGADLFVSIHANSMGMGRPDVNGFEIYYHGNAGLSQAIHRNVVNSLNVRDRRVRQARFYVLRNSRMPSTLVEMGFVTGNEDNYKLTDPNFQQQMAQAIARGVLEYLQQR
Protein: Cell surface glycoprotein gp138A (P34115)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the sexual cell fusion of D.discoideum.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
Sequence:
MKIILILSIFLICFLQLGQSVIDPSQNEVMSDLLFNLYGYDKSLDPCNNNYVECEYINTTSTIQTVKSLSLGAPLHQYVITQDLTPLQNLTSFEVNEKIYLTSSFFNYINKFSQLERIVTYSLNLTIPDDTIFPAIFETFTIYKPSVPLSKVIFESPIKNLYVDSPLTGYSIPTLVNVNPYLGNLQLPVTYYSGFPSNLSQAFPNLQYLAIYVNNDMNQNNYHNFSISNIGVFKNLKGLDIEFTDSDNPQEFSIHSFLSNVPIIDNLYIYGQGVTIDPSVGIIDLSYINPKTFLKIQIQQTSLLNNCKGIILKSPKKASFNSYYNTFSYECIDFSNIADFSDYYNDYEQYLPNIDNAPLLTGVDIYQSVVVGDIPESYCRINYLSLYYNQLNGTVPSCIQCLGGVKGGDIVLPNPFLNFNKTTEPYCPTFKIDENYTHLVATDGTEKLIITGTNLGWDGNDITPIIANSKLGITIPKGVGTNKSITVTFQNGEQRTFNYSYVPPFIKSYGFLELDGHKYFTINGTGFDFVDSNNITINDQQITFDNAMGGGDNDGLIIFPIDELPNFATESKFTVSALVGGQSSNEVTFYYFNSINITEEKLVLNNTGGSVDINGSFGTNNTSLVSVSINGTNCLVTSYTNSKLTITYPSNQVGDNYVLTLNVGGYAVNLVVEYIEGGETPTPSTTPSTTPSTTPSSTPTQSPDDDGSTSSTLSTSFYLITLLFLIQQFI
Protein: Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain] (Q5ABC5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (By similarity). Important for virulence.
Subcellular location: [Phosphatidylserine decarboxylase 1 beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
Interaction partners:
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme 2
- diacylglycerol cholinephosphotransferase
- Phosphatidylethanolamine N-methyltransferase
- Lysophospholipid acyltransferase
- Phospholipase
- PNPLA domain-containing protein
- Bta1p
- Phosphatidate cytidylyltransferase
Sequence:
MPLKPISFRWSKTSVRSVPNPFMYGPDNLNKPLSRASQMAERVHQQTPSSTNYQQRRYFSYYYYQFPKIPRPKRNMLYYSTWSRNPVTNASNANKPSKRHMLPFGSFKISKRSFANANQKLKTKLKKLKMGKERRRFIRWWTVTSLTIVLGGVYAKIKYERGDHEENPYKIRPQSWHLYAYSALPLKTISRLWGQVNSINLPVWIRSPSYRVYSAIFGVNLDEMENPDLSSYKNLSEFFYRDIKPDARPIADGDLVSPADGKVLKFGVVENGEIEQVKGMTYSIDALLGIDTGKLAAPTHSLNFDYNSDDETIVKRDEEFAKINGISYSMDDLVGGNSKSTYHMNELTYKDEHDGTAAGERASFSKELRVAEELTPNPVEYFRKKNLYFAVIYLAPGDYHHFHSPTSWVTTLRRHFIGELFSVAPFFQKTLQGLFVLNERVALLGYWKYGFFSMVPVGATNVGSIVVNFDKDLKTNDIYEHEVYSSASSVNESTPLLDQKDYSANDILTITNSEYEDKKRKKLRKNTVYEATYTNASRLLGGYPLSKGQDIGGFKLGSTVVLVFEAPENFKFNLKVGEKVKVGQSLGGFV