wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase RFWD3 (EC 2.3.2.27) (RING finger and WD repeat domain-containing protein 3) (RING finger protein 201) (Q6PCD5)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. Plays a key role in RPA-mediated DNA damage signaling and repair. Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination. Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53.
Subcellular location: Nucleus {ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:28575657, ECO:0000269|PubMed:28691929}. Nucleus, PML body {ECO:0000269|PubMed:21558276}. Cytoplasm {ECO:0000269|PubMed:21558276, ECO:0000269|PubMed:28691929}. Note=In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies (PubMed:21558276). In response to replication block, such as that caused by hydroxyurea treatment, or to DNA damage caused by ionizing radiations or doxorubicin, recruited to the nucleus, to stalled replication forks or to sites of DNA repair (PubMed:21504906, PubMed:28575657). This recruitment depends upon RPA2 (PubMed:21504906). {ECO:0000269|PubMed:21504906, ECO:0000269|PubMed:28575657}.
Interaction partners:
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 14 kDa subunit
- Replication protein A 32 kDa subunit
- DNA-directed primase/polymerase protein
- E3 ubiquitin-protein ligase Mdm2
- Fanconi anemia group I protein
- DNA repair protein RAD51 homolog 1
- Mixed lineage kinase domain-like protein
- Fanconi anemia group D2 protein
- Fanconi anemia group A protein
Sequence:
MAHEAMEYDVQVQLNHAEQQPAPAGMASSQGGPALLQPVPADVVSSQGVPSILQPAPAEVISSQATPPLLQPAPQLSVDLTEVEVLGEDTVENINPRTSEQHRQGSDGNHTIPASSLHSMTNFISGLQRLHGMLEFLRPSSSNHSVGPMRTRRRVSASRRARAGGSQRTDSARLRAPLDAYFQVSRTQPDLPATTYDSETRNPVSEELQVSSSSDSDSDSSAEYGGVVDQAEESGAVILEEQLAGVSAEQEVTCIDGGKTLPKQPSPQKSEPLLPSASMDEEEGDTCTICLEQWTNAGDHRLSALRCGHLFGYRCISTWLKGQVRKCPQCNKKARHSDIVVLYARTLRALDTSEQERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDKCTRLQRRVQDLQKLTSHQSQNLQQPRGSQAWVLSCSPSSQGQHKHKYHFQKTFTVSQAGNCRIMAYCDALSCLVISQPSPQASFLPGFGVKMLSTANMKSSQYIPMHGKQIRGLAFSSYLRGLLLSASLDNTIKLTSLETNTVVQTYNAGRPVWSCCWCLDEANYIYAGLANGSILVYDVRNTSSHVQELVAQKARCPLVSLSYMPRAASAAFPYGGVLAGTLEDASFWEQKMDFSHWPHVLPLEPGGCIDFQTENSSRHCLVTYRPDKNHTTIRSVLMEMSYRLDDTGNPICSCQPVHTFFGGPTCKLLTKNAIFQSPENDGNILVCTGDEAANSALLWDAASGSLLQDLQTDQPVLDICPFEVNRNSYLATLTEKMVHIYKWE
Protein: Rap guanine nucleotide exchange factor 5 isoform 1 (A0A0S2Z5S1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGSSRLRVFDPHLERKDSAAALSDRELPLPTFDVPYFKYIDEEDEDDEWSSRSQSSTEDDSVDSLLSDRYVVVSGTPEKILEHLLNDLHLEEVQDKETETLLDDFLLTYTVFMTTDDLCQALLRHYSAKKYQGKEENSDVPRRKRKVLHLVSQWIALYKDWLPEDEHSKMFLKTIYRNVLDDVYEYPILEKELKEFQKILGMHRRHTVDEYSPQKKNKALFHQFSLKENWLQHRGTVTETEEIFCHVYITEHSYVSVKAKVSSIAQEILLCSQLGKRVQLVKKFIKIAAHCKAQRNLNSFFAIVMGLNTASVSRLSQTWEKIPGKFKKLFSELESLTDPSLNHKAYRDAFKKMKPPKIPFMPLLLKDVTFIHEGNKTFLDNLVNFEKLHMIADTVRTLRHCRTNQFGDLSPKEHQELKSYVNHLYVIDSQQALFELSHRIEPRV
Protein: Signal recognition particle subunit SRP72 (SRP72) (Signal recognition particle 72 kDa protein) (P33731)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity). Binds the signal recognition particle RNA (7SL RNA) in presence of SRP68. Can bind 7SL RNA with low affinity (By similarity). The SRP complex possibly participates in the elongation arrest function (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O76094}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76094}.
Interaction partners:
- Signal recognition particle subunit SRP54
- Signal recognition particle 19 kDa protein
- Signal recognition particle 9 kDa protein
- Signal recognition particle subunit SRP68
- Signal recognition particle 14 kDa protein
- Signal recognition particle receptor subunit alpha
- SRP receptor subunit beta.
- Large ribosomal subunit protein uL13
- Uncharacterized protein.
- Ribosomal protein L5.
Sequence:
MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLYRLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEKVVPENLGLQEGTHELCYNAACALIGQGQLSQAMKILQKAEDLCRRSLSEDSDGTEEDPQAELAIIHGQMAYILQLQGRTEEALQLYNQIIKLKPTDVGLLAVIANNIITINKDQNVFDSKKKVKLTNAEGVEFKLSKKQLQAIEFNKALLAMYTNQAEQCRKISASLQSQSPEHLLPVLIQAAQLCREKQHTKAIELLQEFSDQHPENAAEIKLTMAQLKISQGNISKACLILRSIEELKHKPGMVSALVTMYSHEEDIDSAIEVFTQAIQWYQNHQPKSSAHLSLIREAANFKLKYGRKKEAISDLEQLWKQNPKDIHTLAQLISAYSLVDPEKAKALSKHLPSSDSMSLKVDVEALENSPGATYIRKKGGKVAGDSQPKEQGQGDLKKKKKKKKGKLPKNYDPKVTPDPERWLPMRERSYYRGRKKGKKKDQIGKGTQGATAGASSELDASKTVSSPPTSPRPGSAATASASTSNIIPPRHQKPAGAPATKKKQQQKKKKGGKGGW
Protein: Noggin-2 (Q9W740)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Inhibitor of bone morphogenetic proteins (BMP) signaling.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein 4.
- Bone morphogenetic protein 7
- Chordin
- Bone morphogenetic protein 2
- Bone morphogenetic protein 2a.
- Noggin-1
- Noggin-3
- Bone morphogenetic protein 6.
- Growth differentiation factor 5
- Follistatin 2
Sequence:
MGSITRALPLLLLLLLCAHGTASQHHLRLRPLPSEGLPVPDLIENPDPEHDPREQDLSEKTLLKKLGSNFDANFMSIHLPAQLNASAPPELPRLPMPAELKKLDLTETPYGRRVKVGKKARRKFLQWLWMYTHCPVLYTWKDLGLRFWPRYIKEGNCFSERSCSFPEGMSCKPVKAVTKTFLRWYCQGFMRQKYCTWIQVQYPIISQCKCSC
Protein: Protein IQ-DOMAIN 6 (AtIQD6) (O64852)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:28115582}. Nucleus, nuclear body {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582}. Cell membrane {ECO:0000269|PubMed:28115582}.
Interaction partners:
- ER membrane protein complex subunit 6
- Peptidyl-prolyl cis-trans isomerase CYP21-4
- Heptahelical transmembrane protein 4
- Rop guanine nucleotide exchange factor 5
- Kinesin-like protein KIN-12C
- GATA transcription factor 20
Sequence:
MGASGKWVKSIIGLKKLEKDEIEKGNGKNKKWKLWRTTSVDSWKGFRGKHRSDSDGVDSSTVYSAAVATVLRAPPKDFKAVREEWAAIRIQTAFRGFLARRALRALKGIVRLQALVRGRQVRKQAAVTLRCMQALVRVQARVRARRVRMTVEGQAVQKLLDEHRTKSDLLKEVEEGWCDRKGTVDDIKSKLQQRQEGAFKRERALAYALAQKQWRSTTSSNLKTNSSISYLKSQEFDKNSWGWSWLERWMAARPWETRLMDTVDTAATPPPLPHKHLKSPETADVVQVRRNNVTTRVSAKPPPHMLSSSPGYEFNESSGSSSICTSTTPVSGKTGLVSDNSSSQAKKHKPSYMSLTESTKAKRRTNRGLRQSMDEFQFMKNSGMFTGELKTSPSSDPFVSFSKPLGVPTRFEKPRG
Protein: F-box protein At1g47340 (Q0V7S0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Guanylate kinase 2
- SKP1-like protein 1B
Sequence:
MLKKTAPNSPKRRRCSSFAAVDLVGSANRTFMVSVSLPKELILEILKRLPAKSVKRFHCVSKQWASMLSCPHFRELFLTRSSSAQPRLLFAIEKHNQWSLFSLPQRLTPYEKSSSSSVVVTPEFHMKFPPDGMLIYPRHDRRFSFGYASGLMYFYGMWINEHDYDGVPVICNPLTGRYASLPFLERYRKAFSFFGFDPIEKQYKVLFMAYPSGPDHHTVLTFGTGEMSWRKIECSVKHDIVSDGICINGVMYYLGDTSEFMTAFVVVCFDVRSETFSFIYPGSYCEVINYKGKLGLVFCDDYTDDAIELRLWVLEDKEKIEWSKYAYKLKDEKFSAHYVSIVGVSAAGEIVLSMADFTSKQPFYVFYYNPERNTLQCTEIQGFEEHHGTFDRRSRVRVFVDDCSSFYRFADHVEYLNVDEPKLLKSKIYDGPNAKIEWEEEEEEDEDEDQEKEEEDQWS
Protein: Catenin alpha-3 (Alpha T-catenin) (Cadherin-associated protein) (Q9UI47)
Organism: Homo sapiens (Human)
Function: May be involved in formation of stretch-resistant cell-cell adhesion complexes.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q65CL1}. Note=Localizes to intercalated disks of cardiomyocytes and in peritubular myoid cells of testis, and colocalizes with CTNNA1 and CTNNA2. Colocalizes with PKP2 at intercalated disks in the heart (By similarity). {ECO:0000250|UniProtKB:Q65CL1, ECO:0000269|PubMed:11590244}.
Interaction partners:
- Catenin beta-1
- Plakophilin-2
- Cadherin-1
- Vinculin
- Catenin alpha-1
- Tight junction protein 1
- Catenin alpha-2
- 14-3-3 protein gamma
- Afadin
- Alpha-actinin-4
Sequence:
MSAETPITLNIDPQDLQVQTFTVEKLLEPLIIQVTTLVNCPQNPSSRKKGRSKRASVLLASVEEATWNLLDKGEKIAQEATVLKDELTASLEEVRKESEALKVSAERFTDDPCFLPKREAVVQAARALLAAVTRLLILADMIDVMCLLQHVSAFQRTFESLKNVANKSDLQKTYQKLGKELENLDYLAFKRQQDLKSPNQRDEIAGARASLKENSPLLHSICSACLEHSDVASLKASKDTVCEEIQNALNVISNASQGIQNMTTPPEPQAATLGSALDELENLIVLNPLTVTEEEIRPSLEKRLEAIISGAALLADSSCTRDLHRERIIAECNAIRQALQDLLSEYMNNAGKKERSNTLNIALDNMCKKTRDLRRQLRKAIIDHVSDSFLDTTVPLLVLIEAAKNGREKEIKEYAAIFHEHTSRLVEVANLACSMSTNEDGIKIVKIAANHLETLCPQIINAALALAARPKSQAVKNTMEMYKRTWENHIHVLTEAVDDITSIDDFLAVSESHILEDVNKCIIALRDQDADNLDRAAGAIRGRAARVAHIVTGEMDSYEPGAYTEGVMRNVNFLTSTVIPEFVTQVNVALEALSKSSLNVLDDNQFVDISKKIYDTIHDIRCSVMMIRTPEELEDVSDLEEEHEVRSHTSIQTEGKTDRAKMTQLPEAEKEKIAEQVADFKKVKSKLDAEIEIWDDTSNDIIVLAKNMCMIMMEMTDFTRGKGPLKHTTDVIYAAKMISESGSRMDVLARQIANQCPDPSCKQDLLAYLEQIKFYSHQLKICSQVKAEIQNLGGELIMSALDSVTSLIQAAKNLMNAVVQTVKMSYIASTKIIRIQSPAGPRHPVVMWRMKAPAKKPLIKREKPEETCAAVRRGSAKKKIHPLQVMSEFRGRQIY
Protein: Kinetochore protein NDC80 (Q9VYB1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|RuleBase:RU368072}. Nucleus {ECO:0000256|RuleBase:RU368072}.
Interaction partners:
- Kinetochore protein Spc25
- Bub1-related kinase
- Aurora kinase B
- Nuf2
- Monopolar spindle 1, isoform B
- Bub1 kinase, isoform A
- Protein mini spindles
- Mis12
- CG1558-RA protein
- Nnf1b
Sequence:
MSHLMPRRTSEFRGDVLEERGTADKRQTRATKRSAATHTPSSSQAAPRRPSASRLPQPLNLERDRASQMGVTPKRGHRFVPSTAERAIAPHSDKKWVAERAQQILEYLHGIQNSEAPTGLIADLFSRPGGLRHMTIKQFVSILNFMFHHIWRNRVTVGQNHVEDITSAMQKLQYPYQVNKSWLVSPTTQHSFGHVIVLLDFLMDFLPPLPSSDVVEEEFPFMETMEQPSSYLNSMHCESTTIMSTTQAHAIQLDEDVNGLLFEEASKCIALWDQELTNEEAKLQAETRDQVISKKCDLPDRKALDQLIGDLKTKLQQLENKLHDPSEDNKLNKLERLTKEHDQLAQQLAASEEELIKKLKLYEQLSAQVEEKQSNLRQQMKYEKRLEQAVNRQKFSAQQLKELQMKCDDMENYSKAYERQVKEVSELELHQQVMLSRAKQKQLDSVEVFNSHVRHLSMDPVICGLIKSGIGQQSDLTLPLNPNQEDISERVQCLELLGKLLQQHRQQNIDRRQMLDKQVAKVKSDSIELDTEIATMDSQLRAQKQRLTKMEASYRTKRDMQAQHRQQLLEDQYDQTARLDELEKREKQALEKLEASKQRNEDLLTAAEQFQEQDLKARQDRLEKCEQKLAKAEDQLLAVESKVNATQAKLNEVEQKVYSAKLPSFQPVLDAIKNH
Protein: Integrase (EC 2.7.7.-) (EC 3.1.-.-) (P03700)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome.
Interaction partners:
Sequence:
MGRRRSHERRDLPPNLYIRNNGYYCYRDPRTGKEFGLGRDRRIAITEAIQANIELFSGHKHKPLTARINSDNSVTLHSWLDRYEKILASRGIKQKTLINYMSKIKAIRRGLPDAPLEDITTKEIAAMLNGYIDEGKAASAKLIRSTLSDAFREAIAEGHITTNHVAATRAAKSEVRRSRLTADEYLKIYQAAESSPCWLRLAMELAVVTGQRVGDLCEMKWSDIVDGYLYVEQSKTGVKIAIPTALHIDALGISMKETLDKCKEILGGETIIASTRREPLSSGTVSRYFMRARKASGLSFEGDPPTFHELRSLSARLYEKQISDKFAQHLLGHKSDTMASQYRDDRGREWDKIEIK
Protein: Neurogenic differentiation factor 4 (NeuroD4) (Class A basic helix-loop-helix protein 4) (bHLHa4) (Protein atonal homolog 3) (ATH-3) (Atoh3) (Q9HD90)
Organism: Homo sapiens (Human)
Function: Probably acts as a transcriptional activator. Mediates neuronal differentiation. Required for the regulation of amacrine cell fate specification in the retina (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Forkhead box protein N4
- Achaete-scute homolog 1
- Insulin gene enhancer protein ISL-1
- LIM/homeobox protein Lhx3
Sequence:
MSKTFVKSKEMGELVNTPSWMDKGLGSQNEVKEEESRPGTYGMLSSLTEEHDSIEEEEEEEEDGEKPKRRGPKKKKMTKARLERFRARRVKANARERTRMHGLNDALDNLRRVMPCYSKTQKLSKIETLRLARNYIWALSEVLETGQTPEGKGFVEMLCKGLSQPTSNLVAGCLQLGPQSVLLEKHEDKSPICDSAISVHNFNYQSPGLPSPPYGHMETHLLHLKPQVFKSLGESSFGSHLPDCSTPPYEGPLTPPLSISGNFSLKQDGSPDLEKSYSFMPHYPSSSLSSGHVHSTPFQAGTPRYDVPIDMSYDSYPHHGIGTQLNTVFTE
Protein: Telomere repeats-binding bouquet formation protein 1 (Coiled-coil domain-containing protein 79) (Q8NA31)
Organism: Homo sapiens (Human)
Function: Meiosis-specific telomere-associated protein involved in meiotic telomere attachment to the nucleus inner membrane, a crucial step for homologous pairing and synapsis. Component of the MAJIN-TERB1-TERB2 complex, which promotes telomere cap exchange by mediating attachment of telomeric DNA to the inner nuclear membrane and replacement of the protective cap of telomeric chromosomes: in early meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA and the shelterin/telosome complex. During prophase, the complex matures and promotes release of the shelterin/telosome complex from telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably mediates association with the shelterin/telosome complex via interaction with TERF1, promoting priming telomeric DNA attachment'. Promotes telomere association with the nuclear envelope and deposition of the SUN-KASH/LINC complex. Also recruits cohesin to telomeres to develop structural rigidity.
Subcellular location: Chromosome, telomere {ECO:0000250|UniProtKB:Q8C0V1}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q8C0V1}. Note=Localizes to telomeres during meiotic prophase. In leptotene spermatocytes, localizes to telomeres that localize to the nucleus inner membrane. {ECO:0000250|UniProtKB:Q8C0V1}.
Interaction partners:
- Telomere repeats-binding bouquet formation protein 2
- Telomeric repeat-binding factor 1
- Membrane anchored junction protein
- SUN domain-containing protein 1
- Leucine-rich repeat and death domain-containing protein 1
- Protein KASH5
- Proton-coupled amino acid transporter 3
- SUN domain-containing protein 2
- Speedy protein A
- HORMA domain-containing protein 2
Sequence:
MESEDTKKTQEMKTDLNLLLECLKYQMDNAFSQKEALVTIHSICQQNSNASVYFREIGGLMFVKNLAKSSEHSMVKEAALYTLGAIAEKNVYCQQTLCTSELFEDLTWFLSNDSNINLKRMSVYVILVLVSNNRTGQTLVRETGCITVLSRLFRTVISKHELDLSDKNVFQSYQLWSSVCSTLCVCVNNPQNDENQMFCCSLFPHANEWLKNCTTPEIIRPICSFIGLTLANNTYVQKYFVSVGGLDVLSQVLMQLESDSHETLSSAKLAVVVTKTVDACIADNPTFGIVLSKYHIVSKLLALLLHESLDSGEKFSIMLTLGHCTEDCEENQYDLFKNNGLPLMIQALTESQNEELNKAATFVLHNCKKITEKLSLSLGEYPFDENETQQLKDISVKENNLEEHWRKAKEILHRIEQLEREGNEEEIQRENYQDNISSMNISIQNTWKHLHADRIGRGSKAEDEDKSHSRQLQSYKSHGVMSKACTNDDQMKTPLKSANPVHACYRESEQNKTLYKAKSSCNQNLHEETTFEKNFVSQSSDHVFKHPVHIAKNIKQQLPVTDPFTLCSDIINKEVVSFLATPSCSEMLTYRCSGCIAVEKSLNSRNFSKLLHSCPYQCDRHKVIVEAEDRYKSELRKSLICNKKILLTPRRRQRLSNESTTPGGIKKRRIRKNFTEEEVNYLFNGVKKMGNHWNSILWSFPFQQGRKAVDLAHKYHKLTKHPTCAAS
Protein: Collagen alpha-2(V) chain (Q3U962)
Organism: Mus musculus (Mouse)
Function: Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Lumican
- Fibrillin-1
- Collagen alpha-1
- Collagen alpha-1
- Serpin H1
- von Willebrand factor A domain-containing protein 1
Sequence:
MMANWVGARPLLILSVLLGYCVSIKAQEQENDEYDEEIACTQHGQMYLNRDIWKPSPCQICVCDNGAILCDKIECPEVLNCANPITPTGECCPVCPQTGGGDTSFGRGRKGQKGEPGLVPVVTGIRGRPGPAGPPGSQGPRGDRGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGMSRPFSAQMAGLDEKSGLGSQVGLMPGSVGPVGPRGPQGLQGQQGGVGPAGPPGEPGEPGPMGPIGSRGPEGPPGKPGEDGEPGRNGNTGEVGFSGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEIGAPGAKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGKRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPAGSQGLPGAVGTDGTPGAKGPTGSAGTSGPPGLAGPPGSPGPQGSTGPQGIRGQSGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPMGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGGQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDLGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKAGDQGVPGEPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGNPGPTGTIGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPHGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPAGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGSPGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGEPGSRGPVGPPGRAGKRGLPGPQGPRGDKGDNGDRGDRGQKGHRGFTGLQGLPGPPGPNGEQGSAGIPGPFGPRGPPGPVGPSGKEGNPGPLGPIGPPGVRGSVGEAGPEGPPGEPGPPGPPGPPGHLTAALGDIMGHYDENMPDPLPEFTEDQAAPDDTNKTDPGIHVTLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHPTKQSGEYWIDPNQGSAEDAIKVYCNMETGETCISANPASVPRKTWWASKSPDNKPVWYGLDMNRGSQFTYGDYQSPNTAITQMTFLRLLSKEASQNLTYICRNTVGYMDDQAKNLKKAVVLKGSNDLEIKGEGNIRFRYTVLQDTCSKRNGNVGKTIFEYRTQNVARLPIIDVGPVDIGNADQEFGLDIGPVCFM
Protein: Septin-7 (CDC10 protein homolog) (Q16181)
Organism: Homo sapiens (Human)
Function: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18460473}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18460473}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18460473}. Cleavage furrow {ECO:0000269|PubMed:18460473}. Midbody {ECO:0000269|PubMed:18460473}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:25588830}. Note=Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase. Associated with actin stress fibers (By similarity). Found in the sperm annulus (PubMed:25588830). {ECO:0000250, ECO:0000269|PubMed:25588830}.
Interaction partners:
- Septin-6
- Septin-2
- Septin-11
- Septin-9
- Uncharacterized protein C17orf47
- Septin-5
- Septin-12
- Septin-8
- Neuronal-specific septin-3
- Septin-10
Sequence:
MSVSARSAAAEERSVNSSTMVAQQKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNGVDNNKNKGQLTKSPLAQMEEERREHVAKMKKMEMEMEQVFEMKVKEKVQKLKDSEAELQRRHEQMKKNLEAQHKELEEKRRQFEDEKANWEAQQRILEQQNSSRTLEKNKKKGKIF
Protein: LD33094p (Liprin-alpha, isoform A) (Liprin-alpha, isoform B) (Q9VM93)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWNMMCDVMPTISEDSISQRSSQFSGEDANFEQLMVSMLDERDKLMDSLREAQERLNETENKLRDVEKERDSLQRQINANLPQEFATLTKELTQARETLLERDEEIGELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAAAQSGVSSEVEVLKALKSLFEHHKALDEKVRERLRLSIEKNNMMEEELSSAKEELAQYKAGVVPAGVGSGSGAGSAATTAGGGGAENGLKEKMAGVGGSGGVNGEANELNDYAAKTHELQTIIEKQTSELSQWQRRVSDLNNKISELEENMSRVQKEHCKAQDQCAKLQRDLRENVAQKEDQEERITTLEKRYLNAQRESTSLHDLNEKLEQELRHKEAQLKLHEEKIGAIEEKLELSEQKLAQHAKLQPDMEEQLKARMEALTKAQERHGSAEDRIRGLETNLDEKTNEVVRLNQRLKMNEEHNLRLSSTVDKLLSESNERLQVHLKERMHALDEKNALTQELEKARKVAEELHHEKSEIMKELSKTRLEIENFKRQLLQQEIAYNIQQTEALTRSLSPSSVVDPSGAFSRSNSHASFETHSLRRQSKQRLSEENALVRSMAEQEWEKLQQAAHAQQQAYELASAADCDDSDVLYAAATDMMSPSGHTDAQTLAMMLQEQLDAINNEIRLIQEEKQSTEARAEELESRVGSLEHVNLLARGRSMDRQSPPMSGRSTPNSPQRDFMQKYHTLNLPVLSSDASREELHGGMSTTGDSSSGGAASPLTARSMRLERVAQALAHSQEELRRRSIGLNPNASVAPNHTGGHMPLSSHSYGLSPLSSRYGSQESLRHYNTMGSMSMLQTPTSGVSREAAAAAVQKKKGIKSSLGRFFSKKEKVKGVKDTLPDGSPSMMSIGNLSIGLSEVDSNYDAMSMTGGMMPRIASSQGSKISSVDYGRQKKEHDYRNDLLGEAMKAGTPFALWNGPTIVAWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPQTSRTTLAFGDMNHEWIGNYWLPGLGLPQYRTTFMECLVDARMLDHLTKKDLRGQLKMVDSFHRTSLQYGISMLKRLNYDRTELEHRRKMSENGLCDVLVWSNERVIRWVGSIGLKEYANNLLESGVHGGLMALDEGFDANAMGLALQIPTQNAQARQILDTEFNNLLQIATDRRPENEQRSAS
Protein: WW domain binding protein 1-like (Outcome predictor in acute leukemia 1 homolog) (Q8BGW2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPFLWGLRQDKEACVGTNNQSYICDTGHCCGQSQCCNYYYELWWFWLVWTVVIILSCCCVCHHRRAKHRLQAQQRQHEINLIAYREAHNYSALPFYFRFLPNSLLPPYEEVVNRPPTPPPPYSAFQLQQQQQLLPPPPQGGPPGGSPPGADPPPQGSQGAQSSPLSGPSRSSTRPPSVADPQSPEVPTDREATKASGTESGSPMAGHGELDPGAFLDQDSECKEELLKDSRSERGGVSPDSEDKTPGRHRRFTGDSGIEVCVCNRGHHDDDLKEFNTLIDDALDGPLDFCDSCHVRPPVDEEEGLCLSSEGQAREHGHPHLPRPPACLLLNTINEQDSPNSQHSGSPS
Protein: RuvB-like protein 2 (RUVBL2) (EC 3.6.4.12) (TIP49-homology protein 2) (TIP49b homolog) (Q12464)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:10787406, ECO:0000269|PubMed:11604509}.
Interaction partners:
- Actin-related protein 4
- TPR repeat-containing protein associated with Hsp90
- Chromatin-remodeling ATPase INO80
- Chromatin-remodeling complex subunit IES6
- Vacuolar protein sorting-associated protein 71
- TEL2-interacting protein 1
- RuvB-like protein 1
- Actin-related protein 5
- Actin-like protein ARP6
- Helicase SWR1
Sequence:
MSIQTSDPNETSDLKSLSLIAAHSHITGLGLDENLQPRPTSEGMVGQLQARRAAGVILKMVQNGTIAGRAVLVAGPPSTGKTALAMGVSQSLGKDVPFTAIAGSEIFSLELSKTEALTQAFRKSIGIKIKEETELIEGEVVEIQIDRSITGGHKQGKLTIKTTDMETIYELGNKMIDGLTKEKVLAGDVISIDKASGKITKLGRSFARSRDYDAMGADTRFVQCPEGELQKRKTVVHTVSLHEIDVINSRTQGFLALFTGDTGEIRSEVRDQINTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSFINRALEDEFAPIVMMATNRGVSKTRGTNYKSPHGLPLDLLDRSIIITTKSYNEQEIKTILSIRAQEEEVELSSDALDLLTKTGVETSLRYSSNLISVAQQIAMKRKNNTVEVEDVKRAYLLFLDSARSVKYVQENESQYIDDQGNVQISIAKSADPDAMDTTE