wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein, isoform A (Q9VAF3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- Degringolade, isoform A
- IP10578p
- 7SK snRNA methylphosphate capping enzyme bin3
Sequence:
MSSIWTKRKDSFCNNENIRAQKFEDVIVIDDNDRGDSLRSVKSEPPEEKPRLSPQDANQKRAVKEEKEMSRRARARAKKIRNTEARAAKSVVTRGAGKKARKRKKQNKAALKKASELEPKKAKGSKEASAHKKAKGPKNTSPPMAAKPNLAKSDNLTMALVDELHEDGRLLNERWQEVEAQLAYMVTDRVMAMPGGPVPSFDSSDVVRGHRVIRCEDGFSKVFLSDCVAAISNSWHDMRIKLVHVSDVPFAPQARIWLPTGQTDHNRIMICLRAQNLNVDMSDWSILRAEEVMEISQSFLLLINRRCIPQLDAVDYKLRYGIRMAQIQLILSEADDLPSEFDNYHPFCHFPH
Protein: Apolipoprotein C-I (Apo-CI) (ApoC-I) (Apolipoprotein C1) (Liver regeneration-related protein LRRG04) [Cleaved into: Truncated apolipoprotein C-I] (P19939)
Organism: Rattus norvegicus (Rat)
Function: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P02654}.
Interaction partners:
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein B-100
- Apolipoprotein C-II
- Apolipoprotein A-II
- Apolipoprotein A-I
- Apolipoprotein A-IV
- Phosphatidylcholine-sterol acyltransferase
- Apolipoprotein A-V
- Beta-2-glycoprotein 1
Sequence:
MRLFIALPVLIVVVAMALEGPAPAQAAPDFSSAMESLPDKLKEFGNTLEDKARAAIEHIKQKEIMIKTRNWFSETLNKMKEKLKTTFA
Protein: GH11677p (Q7K554)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEHAGAPISTSASNIATVLEDGENQQLPPLTGSGPSRQRSLRDRLKDGITGSFSWQSKSRSVDHGLAAPFDLDSLRSKVEQRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVPDKSAKDDASSSSTHDADGASLSGKSSPVERKLSGDESREKDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSR
Protein: Anthranilate synthase component 2 (AS) (ASII) (EC 4.1.3.27) (Anthranilate synthase, GATase component) (Anthranilate synthase, glutamine amidotransferase component) (P00900)
Organism: Serratia marcescens
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable).
Interaction partners:
- Anthranilate synthase component 1
- Fused indole-3-glycerolphosphatesynthetase/N-
- Para-aminobenzoate synthase component 1.
- Anthranilate phosphoribosyltransferase
- Tryptophan synthase alpha chain
- Tryptophan synthase, beta subunit
- Chorismate synthase
- Fused chorismate mutase P/prephenate dehydratase.
- Isochorismate synthase.
- Fused chorismate mutase T/prephenate dehydrogenase.
Sequence:
MADILLLDNVDSFTYNLVDQLRASGHQVVIYRNQIGAEVIIERLQHMEQPVLMLSPGPGTPSEAGCMPELLQRLRGQLPIIGICLGHQAIVEAYGGQVGQAGEILHGKASAIAHDGEGMFAGMANPLPVARYHSLVGSNIPADLTVNARSGEMVMAVRDDRRRVCGFQFHPESILTTHGARLLEQTLAWALAK
Protein: Troponin I (Troponin T type 3a (skeletal, fast)) (B2DBF2)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MSEKRMTSSRKHHLKSLMLQIAATLIEEEKKQIKEEKANFMAKISALDLSGDQAALMEMLKKLSQTIDKVDEERYDAEAKVKKTEKEIEDLKMKVIEVQGIKKPALKKVRMSADAMLAALLGTKHKASMDFRANLKEVKKEVKEEEEVGDWRKNVDEQAGMDGRKKKFEST
Protein: Phospholipid scramblase (Q8IQD8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTENPASCVSTLDLSGGENRGNPEESHSRGVRSGSKVLRLIWHSLYSQYNQICSRSQTLRQLVCREANKPLPKKLRHTMRLNKSAKRKGYEFYMSDEDRSIPTGIPNCPRGLEYLTTIDQLLVKQKVELLEAFTGFETNNKFTIKNALGQKVYFAAEDNDCCTRNCCGPARPFDMRVFDNFQQEVIHMHRPLACSSCLFPCCLQSIEVSAPPGNVIGTIEQEWSICSPSFRILNHVGDTVMRIEGPFCTFSLCGDVEFNVVSLTGEKIGKISKQWSGLAREIFTDADFFGINFPLDLDVRMKAVLLGATFLIDAMFFEKAGNQETDRPGML
Protein: ATP synthase subunit beta, mitochondrial (EC 7.1.2.2) (P00830)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit 4
- F
- ATP synthase subunit J, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit H
Sequence:
MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN
Protein: Uncharacterized protein BTRF1 (Q1HVD3)
Organism: Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4)
Interaction partners:
Sequence:
MLKCKQPGARFIHGAVHLPSGQIVFHTIHSPTLASALGLPGENVPIPALFRASGLNVRESLPMTNMRAPIISLARLILAPNPYILEGQLTVGMTQDNGIPVLFARPVIEVKSGPESNIKASSQLMIAEDSCLNQIAPFSASEHPAFSMVESVKRVRVDEGANTRRTIRDILEIPVTVLSSLQLSPTKSILKKAPEPPPPEPQATFDAAPYARIFYDIGRQVPKLGNAPAAQVSNVLIANRSHNSLRLVPNPDLLPLQHLYLKHVVLKSLNLENIVQDFEAIFTSPSDTISEAETKAFEKLVEQAKNTVENIVFCLNSICSTSTLPDVVPDVNNPNISLALEKYFLMFPPSGTIMRNVRFATPIVRLLCQGAELGTMAQFLGKYIKVKKETGMYTLVKLYYLLRI
Protein: Proline-rich protein 20D (P86480)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEPRPSKRLRSMAPNQASGGPPPEPGCCVADPEGSVEADGPAQPAQPAKPIAYVKPFRRQPPARPESPPPAERGRRRGGSRRPGRGRGRRAGPRGDAGQRQGAEGLMAPDVHIQLDHHGEPGHQGEPEITETAAFSLSETGPPPGTVQEGPGPDVAQPELGFQEPPAAPGPQAVDWQPVLTLYPCIGFRALGDSAVLQVIQTPQGTYVQGVPVFLTDIAY
Protein: Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein) (Q2M1Z3)
Organism: Homo sapiens (Human)
Function: Functions as a GTPase-activating protein (GAP) for RAC1 and CDC42. Required for cell spreading, polarized lamellipodia formation and cell migration.
Subcellular location: Cell projection, lamellipodium. Cell junction, focal adhesion {ECO:0000250}.
Interaction partners:
- Kalirin
- Cell division control protein 42 homolog
- Zinc finger E-box-binding homeobox 2
- Myosin light chain kinase, smooth muscle
- Transforming protein RhoA
- Intersectin-1
- Dedicator of cytokinesis protein 6
Sequence:
MKNKGAKQKLKRKGAASAFGCDLTEYLESSGQDVPYVLKSCAEFIETHGIVDGIYRLSGVTSNIQRLRQEFGSDQCPDLTREVYLQDIHCVGSLCKLYFRELPNPLLTYELYEKFTEAVSHCPEEGQLARIQNVIQELPPSHYRTLEYLIRHLAHIASFSSKTNMHARNLALVWAPNLLRSKEIEATGCNGDAAFLAVRVQQVVIEFILNHVDQIFNNGAPGSLENDENRPIMKSLTLPALSLPMKLVSLEEAQARSLATNHPARKERRENSLPEIVPPMGTLFHTVLELPDNKRKLSSKSKKWKSIFNLGRSGSDSKSKLSRNGSVFVRGQRLSVEKATIRPAKSMDSLCSVPVEGKETKGNFNRTVTTGGFFIPATKMHSTGTGSSCDLTKQEGEWGQEGMPPGAEGGFDVSSDRSHLQGAQARPPPEQLKVFRPVEDPESEQTAPKMLGMFYTSNDSPSKSVFTSSLFQMEPSPRNQRKALNISEPFAVSVPLRVSAVISTNSTPCRTPPKELQSLSSLEEFSFHGSESGGWPEEEKPLGAETSAASVPKKAGLEDAKAVPEAPGTVECSKGLSQEPGAHLEEKKTPESSLSSQHLNELEKRPNPEKVVEEGREAGEMESSTLQESPRARAEAVLLHEMDEDDLANALIWPEIQQELKIIESEEELSSLPPPALKTSPIQPILESSLGPFIPSEPPGSLPCGSFPAPVSTPLEVWTRDPANQSTQGASTAASREKPEPEQGLHPDLASLAPLEIVPFEKASPQATVEVGGPGNLSPPLPPAPPPPTPLEESTPVLLSKGGPEREDSSRKLRTDLYIDQLKSQDSPEISSLCQGEEATPRHSDKQNSKNAASEGKGCGFPSPTREVEIVSQEEEDVTHSVQEPSDCDEDDTVTDIAQHGLEMVEPWEEPQWVTSPLHSPTLKDAHKAQVQGLQGHQLEKRLSHRPSLRQSHSLDSKPTVKSQWTLEVPSSSSCANLETERNSDPLQPQAPRREITGWDEKALRSFREFSGLKGAEAPPNQKGPSGVQPNPAETSPISLAEGKELGTHLGHSSPQIRQGGVPGPESSKESSPSVQDSTSPGEHPAKLQLKSTECGPPKGKNRPSSLNLDPAIPIADLFWFENVASFSSPGMQVSEPGDPKVTWMTSSYCKADPWRVYSQDPQDLDIVAHALTGRRNSAPVSVSAVRTSFMVKMCQARAVPVIPPKIQYTQIPQPLPSQSSGENGVQPLERSQEGPSSTSGTTQKPAKDDSPSSLESSKEEKPKQDPGAIKSSPVDATAPCMCEGPTLSPEPGSSNLLSTQDAVVQCRKRMSETEPSGDNLLSSKLERPSGGSKPFHRSRPGRPQSLILFSPPFPIMDHLPPSSTVTDSKVLLSPIRSPTQTVSPGLLCGELAENTWVTPEGVTLRNKMTIPKNGQRLETSTSCFYQPQRRSVILDGRSGRQIE
Protein: Integrin alpha-6 (CD49 antigen-like family member F) (VLA-6) (CD antigen CD49f) [Cleaved into: Integrin alpha-6 heavy chain; Integrin alpha-6 light chain; Processed integrin alpha-6 (Alpha6p)] (P23229)
Organism: Homo sapiens (Human)
Function: Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for laminin on platelets (By similarity). Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome (By similarity). ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling. ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22314500}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:22314500}; Lipid-anchor {ECO:0000269|PubMed:22314500}.
Interaction partners:
- Integrin beta-1
- Integrin beta-4
- Laminin subunit alpha-5
- Laminin subunit gamma-1
- Laminin subunit beta-1
- CD151 antigen
- Focal adhesion kinase 1
- Collagen alpha-1
- Laminin subunit alpha-3
- Fibronectin
Sequence:
MAAAGQLCLLYLSAGLLSRLGAAFNLDTREDNVIRKYGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQRANRTGGLYSCDITARGPCTRIEFDNDADPTSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETEHDESLVPVPANSYLGLLFLTSVSYTDPDQFVYKTRPPREQPDTFPDVMMNSYLGFSLDSGKGIVSKDEITFVSGAPRANHSGAVVLLKRDMKSAHLLPEHIFDGEGLASSFGYDVAVVDLNKDGWQDIVIGAPQYFDRDGEVGGAVYVYMNQQGRWNNVKPIRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSANGINTKPTQVLKGISPYFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINIQKTITVTPNRIDLRQKTACGAPSGICLQVKSCFEYTANPAGYNPSISIVGTLEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLKRQKQKVCMEETLWLQDNIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSDEPKTAHIDVHFLKEGCGDDNVCNSNLKLEYKFCTREGNQDKFSYLPIQKGVPELVLKDQKDIALEITVTNSPSNPRNPTKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSNVTFYLVLSTTEVTFDTPDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLTNLGTATLNIQWPKEISNGKWLLYLVKVESKGLEKVTCEPQKEINSLNLTESHNSRKKREITEKQIDDNRKFSLFAERKYQTLNCSVNVNCVNIRCPLRGLDSKASLILRSRLWNSTFLEEYSKLNYLDILMRAFIDVTAAAENIRLPNAGTQVRVTVFPSKTVAQYSGVPWWIILVAILAGILMLALLVFILWKCGFFKRSRYDDSVPRYHAVRIRKEEREIKDEKYIDNLEKKQWITKWNENESYS
Protein: Transposon Ty2-LR1 Gag-Pol polyprotein (TY2A-TY2B) (Transposon Ty2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA); Ty2 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)] (P0C2J3)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty2 RNA and initiation of reverse transcription (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MESQQLHQNPHSLHGSAYASVTSKEVPSNQDPLAVSASNLPEFDRDSTKVNSQQETTPGTSAVPENHHHVSPQPASVPPPQNGQYQQHGMMTPNKAMASNWAHYQQPSMMTCSHYQTSPAYYQPDPHYPLPQYIPPLSTSSPDPIDLKNQHSEIPQAKTKVGNNVLPPHTLTSEENFSTWVKFYIRFLKNSNLGDIIPNDQGEIKRQMTYEEHAYIYNTFQAFAPFHLLPTWVKQILEINYADILTVLCKSVSKMQTNNQELKDWIALANLEYDGSTSADTFEITVSTIIQRLKENNINVSDRLACQLILKGLSGDFKYLRNQYRTKTNMKLSQLFAEIQLIYDENKIMNLNKPSQYKQHSEYKNVSRTSPNTTNTKVTTRNYHRTNSSKPRAAKAHNIATSSKFSRVNNDHINESTVSSQYLSDDNELSLGQQQKESKPTHTIDSNDELPDHLLIDSGASQTLVRSAHYLHHATPNSEINIVDAQKQDIPINAIGNLHFNFQNGTKTSIKALHTPNIAYDLLSLSELANQNITACFTRNTLERSDGTVLAPIVKHGDFYWLSKKYLIPSHISKLTINNVNKSKSVNKYPYPLIHRMLGHANFRSIQKSLKKNAVTYLKESDIEWSNASTYQCPDCLIGKSTKHRHVKGSRLKYQESYEPFQYLHTDIFGPVHHLPKSAPSYFISFTDEKTRFQWVYPLHDRREESILNVFTSILAFIKNQFNARVLVIQMDRGSEYTNKTLHKFFTNRGITACYTTTADSRAHGVAERLNRTLLNDCRTLLHCSGLPNHLWFSAVEFSTIIRNSLVSPKNDKSARQHAGLAGLDITTILPFGQPVIVNNHNPDSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQDNQSKLDQFNYDTLTFDDDLNRLTAHNQSFIEQNETEQSYDQNTESDHDYQSEIEINSDPLVNDFSSQSMNPLQLDHEPVQKVRAPKEVDADISEYNILPSPVRSRTPHIINKESTEMGGTIESDTTSPRHSSTFTARNQKRPGSPNDMIDLTSQDRVNYGLENIKTTRLGGTEEPYIQRNSDTNIKYRTTNSTPSIDDRSSNSESTTPIISIETKAVCDNTPSIDTDPPEYRSSDHATPNIMPDKSSKNVTADSILDDLPLPDLTHKSPTDTSDVSKDIPHIHSRQTNSSLGGMDDSNVLTTTKSKKRSLEDNETEIEVSRDTWNNKNMRSLEPPRSKKRINLIAAIKGVKSIKPVRTTLRYDEAITYNKDNKEKDRYVEAYHKEISQLLKMNTWDTNKYYDRNDIDPKKVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSDMQSNTVHHYALMTSLSIALDNDYYITQLDISSAYLYADIKEELYIRPPPHLGLNDKLLRLRKSLYGLKQSGANWYETIKSYLINCCDMQEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGERDNEIQYDILGLEIKYQRSKYMKLGMEKSLTEKLPKLNVPLNPKGKKLRAPGQPGHYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH
Protein: EP300-interacting inhibitor of differentiation 3 (EID-3) (E1A-like inhibitor of differentiation 3) (EID-1-like inhibitor of differentiation 3) (Non-structural maintenance of chromosomes element 4 homolog B) (NS4EB) (Non-SMC element 4 homolog B) (Q8N140)
Organism: Homo sapiens (Human)
Function: Tissue-specific component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components.
Subcellular location: Nucleus {ECO:0000269|PubMed:15987788}. Cytoplasm {ECO:0000269|PubMed:15987788}. Chromosome, telomere {ECO:0000305|PubMed:15987788}. Note=May shuttle between nucleus and cytoplasm. {ECO:0000269|PubMed:15987788}.
Interaction partners:
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6
- E3 SUMO-protein ligase NSE2
- Non-structural maintenance of chromosomes element 1 homolog
- Non-structural maintenance of chromosomes element 3 homolog
- Small ubiquitin-related modifier 4
- EP300-interacting inhibitor of differentiation 2
- Non-structural maintenance of chromosomes element 4 homolog A
- EP300-interacting inhibitor of differentiation 1
- Structural maintenance of chromosomes protein 3
Sequence:
MKMDVSVRAAGCSDDLSSGEADVDPKLLELTADEEKCRSIRRQYRQLMYCVRQNREDIVSSANNSLTEALEEANVLFDGVSRTREAALDARFLVMASDLGKEKAKQLNSDMNFFNQLAFCDFLFLFVGLNWMEGDPDKLSDCDDSIALSFWKAIEKEATSWMVKAETFHFVFGSFKLERSAPKPRLEHQKKVRKMEENGNMPTKLQKLDLSSYPEATEKNVERILGLLQTYFRKYPDTPVSYFEFVIDPNSFSRTVENIFYVSFIVRDGFARIRLDEDRLPILEPMNVNQMGEGNDSSCHGRKQGVISLTLQEWKNIVAAFEISEAMITYSSY
Protein: DNA replication licensing factor REC (Protein mini chromosome maintenance-related) (Protein recombination-defective) (Q9VF30)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for meiotic DNA recombination in females. Probably not involved in DNA repair and recombination in somatic cells.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cell division control protein
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm7
- DNA replication licensing factor Mcm2
- Origin recognition complex subunit 2
- Double parked, isoform A
- FI21203p1
- CDC45L
- Protein MCM10 homolog
Sequence:
MNPTLSRGGAPSRFVRGRGRGGGAYRPYFYFRRNGRVIPAGGNRQPNQGEPGAPDAPSVPPATRQPRGWSRTAGKRGRNAHLDCSFLRPENYAAPEDGLQVQSIAVDNPRAYSGWRLYFLREKYEEGNELATRIMAVEAYYQRNPHTFDFVMIRDRGFFPLCAAGIKSDAQLKEVWPSLSEDIREHPLRTLGTLSLAMHTVVVNHQLDCNDSTTAMVSTPEQYVLPTPRVRKIYARPDDFVPVESIEGISHSRVDTLFSIRGFVSNVGEPSYSLTWQAFRCSRCQMEIAMRQRGTFQPRPYQCKRSECVARDEFVPLRSSPYTRLSIRQIIRVEESSLNLVHDFETSMPAEMDVELRHDLVDAVRVGQEVVVTGILKLQELGDDTTTGDTSNQMQPYLKAVSIRDASSIKREFSERDLEAIVMINAEPNSFKLLVQSIAPEVYGHELPKAACLLSLLGGKGAETEAINVLLVGDPGIGKTKILQSCAQIAERGAHVSGKRGAQSAQQLGVTFAGRNKRVLQAGSLMMASGGGHCTLDDVDKLASKQAVLLQCLQSEEVNLPLAGAFASFPAQPSVIACANPQRGQYDEGRYLLQNINISPSLLREFHLVYILLDKPSERDMSLTAHVRALHAGARKRARIAARYALKPKMSDSMCEVSLNVPAAGKDDDTIKTEDDNDSIMQQDYDLDKRLEVLPEEGDLDLLPPILIKKFLSYARQELNPVLNEDASNAVLRYFLELKGSCNLDEDVSSQIGAGQLLAIIHLSQARARLDLSHVVSPQHVRDVIALLTESITQTSLKEGSSRQGTRGGGGAGGGAGKSAQLRNFLELTKRRSAALGRRIFEFDELKEIGTRAGILTGFSQLVEMANLGGYLLMKGANMYEVVPD
Protein: Nucleoporin (Q57XK4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleoporin
- Uncharacterized protein
- Nucleoporin NSP1-like C-terminal domain-containing protein
- Nuclear pore complex protein
- Poly
- Nuclear pore protein
- Long-chain-fatty-acid-coA ligase protein,putative
- Protein transport protein sec13, putative
- Protein transport protein Sec13, putative
- Telomerase-associated protein, putative
Sequence:
MMSTAPTGGFGGFGAAAKGGFGAVTATGGTGFGTAATGSTGNFGGFGTATGSGFAAVTTTGTFGGFGAGKGFGTTVATPAQPHLPQYKGIKGPGSSTEWLHGVNLSILRDDVVFEDLPVPLQQHLTDFHNFIQAEHDAKQVVEAFLTDSATPNATPAPSYRELVKKMNQLASGENAVDGIRVECFEREVQAHRLGQTLDKCEDDILDYMKNVWKPLSEIDFTQRAGGNRPKPASEPFQRILREIQGCMDAISAAVSELEAAVVPCGRRVRGPVTDDASRSNAAPEPPCASASEFLTKLTGGVELPDVPPPGLGSAASAHPVSRINASLSNQLTTLLNLAAWTLRLHTRADSARDLFVHNYGTSEAELLLAQQHQQAESSAGPRRPFLLPSSTGAAAAEVNQDTVGDIHRRSAFPHRSKALSNGERKMQYDVLLERKYQTAAPAAAPLSTATASGTASSVAGATLGATSSTSTIATGFGAPQSLGTIGGATIFGAGTSAADPRKTLNKTGRS
Protein: Low density lipoprotein receptor adapter protein 1 (Autosomal recessive hypercholesterolemia protein homolog) (D3ZAR1)
Organism: Rattus norvegicus (Rat)
Function: Adapter protein (clathrin-associated sorting protein (CLASP)) required for efficient endocytosis of the LDL receptor (LDLR) in polarized cells such as hepatocytes and lymphocytes, but not in non-polarized cells (fibroblasts). May be required for LDL binding and internalization but not for receptor clustering in coated pits. May facilitate the endocytosis of LDLR and LDLR-LDL complexes from coated pits by stabilizing the interaction between the receptor and the structural components of the pits. May also be involved in the internalization of other LDLR family members. Binds to phosphoinositides, which regulate clathrin bud assembly at the cell surface (By similarity). Required for trafficking of LRP2 to the endocytic recycling compartment which is necessary for LRP2 proteolysis, releasing a tail fragment which translocates to the nucleus and mediates transcriptional repression.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8C142}.
Interaction partners:
- Low-density lipoprotein receptor
- Low-density lipoprotein receptor-related protein 2
- AP-2 complex subunit beta
- Apolipoprotein B-100
- Disabled homolog 2
- DCC-interacting protein 13-alpha
- DCC-interacting protein 13-beta
- AP-1 complex subunit beta-1
Sequence:
MDALKSAGRALIRSPSLAKQSWAGGRHRKLPENWTDTRETLLEGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTAQMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFEFWQVSKEEKEKREKANQEGGDVPGTRRDSTPSLKTSVATGNLLDLEELAKAPLSTVSANTKNMDDALRPQVLGNNSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDIHYAQCLSPTDWDKPDSSGFDQDDVFSF
Protein: ARF3-interacting protein 1 (Q99222)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in actin patch polarization. Required for maintaining a proper budding pattern in yeast cells. Required for proper polarized localization of the ADP-ribosylation factor ARF3 at the plasma membrane.
Subcellular location: Cytoplasm, perinuclear region. Cytoplasm, cell cortex. Note=Enriched at the nuclear envelope and at the plasma membrane, especially in daughter cells and at the bud neck.
Interaction partners:
- Guanine-nucleotide exchange factor YEL1
- ADP-ribosylation factor 3
- Chaotic nuclear migration protein 67
- L-2-aminoadipate reductase
- ADP-ribosylation factor-like protein 1
Sequence:
MLRRELNNSISNRSIENESFPFERPNVSYIISAEFDNKLGPILKHQYPKDIPGFNQFSHEQRNGNTSVSMNLASLMIPSSIERNPGKQDITVFTLYYNKFTQNYQLFPVPKDPRFSFNLHHREQSDGSVTNSIYYDAENHQDAKNNRYTIVLEDDELECQEVQNNQKAIDNEPLFFINVANTVLDTTNDRGAVIKSIAIGTPLKTFFAFKNIIVLVLDLYMKAPTQAAATDILLDCFNMLNSIDLTLINDIHSKSSIQEVLHSIHDESIITKVFLDPDSTLKKLFCINGFDTKDKYGNIVTFHDQLIQYHFTRFQPKTLPPFLLKIPLQFNMIRREPIYIENDYNELVLKFLDKFVPYLLKAGQKVNAWKLVINSTKLSKEDLCAFILSLANITATYASDPQSYFKGNAALIFPYMDISLVDGLRAYVASNSDFVGCFAIIGTANPIFRYQLDIWDYYYDVDEGVFYENNSPEKEKPDTVAEVKIGPNPLRKIFNRPHFSTNAVNESQVNLGQKLFSLLIDEYHDSDTIMSVLRRLNVLQLENLLDALKRREIPPNIALKDEYIMFYKDFFIFPEFFDYFTLHSIELLSNLDNCLFSLGNTCQLFSTEQIYSQLSQILDIVKELFRMVSVSRTNIEKFLNACLNYSPFKILPTAQLHGDNISRWSFESEVRQGFDNFNSYMGIEKDPHGVIVSAIDLFTQIYSFDILAFFLTFITKESGQDLPFTKSLSRRRTYLTRIAQSSSLRQFLQLSTRPNIRILGGNGQGTGNSNYPEFTNASSVISPKLRASPLLERRASKICYAITKLLYRLECHPIGMALLKKYLHNQLREAYLESKRHFISKKGDSTNTSSTIASSSFAGASVPLSSNESGMLNGLKQINEQQESTLETTQKED
Protein: Nuclear export mediator factor (A0A8I6ARH7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTESFASTKSMIYYMFRFCSLLGMRVNNVYDVDNKTYLIRLQKPDFKATLLLESGIRIHTTEFEWPKNMMPSSFAMKCRKHLKSRRLVSAKQLGVDRIVDFQFGSDEAAYHLIIELYDRGNIVLTDYEYLILNILRFRTDEADDVKFAVRERYPIDHARAAEPLLTLERLTEVIARAPRGELLKRVLNPLLPYGPALIEHCLIENGFSGNVKVDEKLESKDIEKILVCVQRAEDYLEKTANFNGKGYIIQKREVKPSLDANKPAEDILTYEEFHPFLFSQHLQCPYIEFESFDKAVDEFYSKIEGQKIDLKALQQEKQALKKLDNVRKDHENRLEALQQAQEIDKLKGELIEMNLQIVDRAIQVVRSALANQIDWTEIGVIVKEAQAQGDPVASAIKELKLQTNHITMLLRNPYLLSEEEDGDGDGSIENSDAEAPKGKKKKQKNKQLQKPQKNKPLLVDVDLSLSAYANAKKYYDHKRYAAKKTQRTVEAAEKAFKSAEKKTKQTLKEVQTVTSIQKARKVYWFEKFLWFISSENYLIIGGRDQQQNEIIVKRYLTPGDIYVHADLHGATSCVIKNPTGDPIPPRTLTEAGTMALCYSAAWDARVITSAWWVHHHQVSKTAPTGEYLTTGSFMIRGKKNFLPPSYLMMGFSFLFKVDESCVWRHRGERKVRVQDEDMETLTSCTSELMSEEMEQLEGGDSSEEETEELRGTTEEVELRTQADPEDIAAHSGREELSSEDGEAIKTATKDEEPIGEVREEEEEPFEYPDTTIDLSHLQSQRPLQKLTPREESFNSSDSKSQSRRHLSAKERREMKKKKLPCDSGDLEVIEEKDKEKESAVHSEADQNTSKNVAAGQPMKRGQKSKMKKMKEKYKDQDDEDRELIMKLLASAGSNKEEKGKKGKKGKTKDEPVKKNPQKPRGGQRVLDVVKETPSLQASTPDLQDFAVDEPHDDKEEHDLDQQGNEENLFDSLTGQPHPEDVLMFAIPICAPYTIMTNYKYKVKLTPGVQKKGKAAKTALNSFMHSKEATAREKDLFRSVKDTDLSRNIPGKVKVSAPNLLHVKRK