wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase RNF34 (EC 2.3.2.27) (Phafin-1) (RING finger protein 34) (RING-type E3 ubiquitin transferase RNF34) (Q99KR6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells. Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q969K3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q969K3}. Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus {ECO:0000250|UniProtKB:Q969K3}. Nucleus speckle {ECO:0000250|UniProtKB:Q969K3}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q969K3}.
Interaction partners:
Sequence:
MKAGATSMWASCCGLLNEVMGTGAVRGQQAGFPGSTGPFRFTPSSDFPTYPPAATEGPNIVCKACGLSFSVFRKKHVCCDCKKDFCSLCSVSQENLRRCSTCHLLQETAFQRPQLMRLKVKDLRQYLLLRNIPTDTCREKEDLVDLVLCHRGLGSGDDLDSSSLNSSRSQTSSFFTQSLFSNYTPPSATVSSFQGELMDRDGAFRSEVLAQVQSEIASANTDDDDDDDDDDDDDEDDDDEQEEEEQNPGLSKKKARASLSDLSSLEEVEGMSVRQLKEILARNFVNYSGCCEKWELVEKVNRLYKENEENQKSYGERMQLQDEEDDSLCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICRQYVVRAVHVFKS
Protein: Proteasome subunit beta type-1 (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain) (Proteasome subunit beta-6) (beta-6) (O09061)
Organism: Mus musculus (Mouse)
Function: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus {ECO:0000250|UniProtKB:P20618}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P20618}.
Interaction partners:
- 26S proteasome regulatory subunit 6A
- Proteasome subunit beta type-7
- Proteasome subunit beta type-3
- Proteasome subunit beta type-5
- Proteasome subunit beta type-2
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-1
- 26S proteasome non-ATPase regulatory subunit 2
- Proteasome subunit beta type-10
Sequence:
MLSTAAYRDVERELGMGPHGSAGPVQLRFSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLTLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD
Protein: Transcriptional regulatory protein GAT1 (Q5A432)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcriptional regulator of nitrogen utilization required for nitrogen catabolite repression and utilization of isoleucine, tyrosine and tryptophan as nitrogen sources. Controls expression of the MEP2 ammonium permease, the DUR1,2 urea amidolyase, and the transcription factor STP1, which in turn mediates SAP2 expression, a long-known virulence attribute of C.albicans. Influences the filamentation process depending upon the nitrogen sources available. Required for virulence in a mouse systemic infection model.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Importin subunit alpha
Sequence:
MYYRARHSLPYQKRMENLTWRMMYINNKSIFTNTNNAPKEIFEQSLDPEIDDFDYVAHIKKIGQFNQQKTQQQQDHLQSNLDNHNSIFADNTGFSNNNDRGSSGGGMTSISSLSKKRPAPFSPMIQPEKTTIIPTATNTMSQLSQQLNEFNKFNHPSQTSNFNDVNHHMEISTSHIAPTSSAFEFSLDPLAFEGPNQNFQPEPHHDFNTNSFDSMTSSYERPLFDDFLPRDHHNIQSSSVPTSASSFSTIVPKNTQFSTSASITSPTSTFSNQGNNSSNFHRLNSTVSITATPGNLLRQESMVSLPDYANHLRSMSQTPTMNSSNAPFSHSFNDGGSYFMNNFTGITLPSQPSPQPIHFDNKPKDDHFNTSLSVSQQQPSAKKSKRKSTITKSKKKAASPETTITSTGSTITTKSTNSNSTGKGTATGPAASNTGVSCTNCGTKTTPLWRRNPQGQPLCNACGLFLKLHGVVRPLSLKTDVIKKRQRGNNNGSGNSSGTTNNSNNYNNKSISKKNEIDDGDDLNPTSITNNTGLTNNNNSKSPAKSKKKSNFDNNSNSALNNLDKSKLKINTNEITNISETTSNSSSPVINLNHGGRSSGVFGNTPDYLNGITSPAVSLVKSEIDNPHQLNNSNSNGMLMTMHQSSHQSSLSTTFDHEVESNNEGSNSSGVNTSTANNQDWDWLNMNY
Protein: Spectrin repeat containing nuclear envelope protein 2 (A0A669KB22)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVEGTTPPIEADTLDSSDAQGGLEPRVEKTRPEPTEVLHACKTQVAELELWLQQANVAVEPETLNADMQQVLEQQLVGCQAMLTEIEHKVAFLLETCKDQGLGDNGATQHEAEALSLKLKTVKCNLEKVQMMLQEKHSEDQVLELKPMEQKDFIKFIEFNAKKMWPQYCQHDNDTTQESSASNQASSPENDVPDSILSPQGQNGDKWQYLHHELSSKIKLPLPQLVEPQVSLYLHGANSLFIFENPTSIH
Protein: DNA-dependent RNA polymerases, putative (EC 2.7.7.6) (Q384D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase I subunit RPA1
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- Plastid-encoded RNA polymerase subunit alpha
- RNA polymerase III subunit Rpc25 domain-containing protein
Sequence:
MSFHPRDAFILHQEYIQRLNEGDEVDTSAEQKVELNLQRHADSESAATVTFSHEDHTLGNPLRHVIMEDPSVTSAGYAIPHPLEAKMQLHVQSSEYAVETVAKGLERLAAICDETLKSFNACVEAISAEDPEGH
Protein: Baculoviral IAP repeat-containing protein 5 (Apoptosis inhibitor survivin) (E3SCZ8)
Organism: Cavia porcellus (Guinea pig)
Function: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (By similarity). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (By similarity). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (By similarity). May counteract a default induction of apoptosis in G2/M phase (By similarity). The acetylated form represses STAT3 transactivation of target gene promoters (By similarity). May play a role in neoplasia. Inhibitor of CASP3 and CASP7 (By similarity). Essential for the maintenance of mitochondrial integrity and function (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Nucleus {ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000269|PubMed:20727954}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20727954}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O15392}. Midbody {ECO:0000269|PubMed:20727954}. Note=Localizes at the centromeres from prophase to metaphase, at the spindle midzone during anaphase and a the midbody during telophase and cytokinesis. Accumulates in the nucleus upon treatment with leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor (PubMed:20727954). Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes (By similarity). {ECO:0000250|UniProtKB:O15392, ECO:0000269|PubMed:20627126, ECO:0000269|PubMed:20727954, ECO:0000269|PubMed:21364656}.
Interaction partners:
- Inner centromere protein
- Borealin
- non-specific serine/threonine protein kinase
- ATP synthase subunit beta
- Diablo IAP-binding mitochondrial protein
- non-specific serine/threonine protein kinase
- Ubiquitin-conjugating enzyme E2 C
- Mitotic spindle assembly checkpoint protein MAD2A
- non-specific serine/threonine protein kinase
- Serine/threonine-protein kinase PLK
Sequence:
MGAPSLPRAWQLYLKEHRVSTFKNWPFVNGCSCTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHKKHSSGCAFLSVKKQFEELTLSEFLKLDKERAKNKIAKETNSKQKEFEETAAKVRQAMEQLAALE
Protein: Actin filament-associated protein 1-like 2 (AFAP1-like protein 2) (Q8N4X5)
Organism: Homo sapiens (Human)
Function: May play a role in a signaling cascade by enhancing the kinase activity of SRC. Contributes to SRC-regulated transcription activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17412687}.
Interaction partners:
Sequence:
MERYKALEQLLTELDDFLKILDQENLSSTALVKKSCLAELLRLYTKSSSSDEEYIYMNKVTINKQQNAESQGKAPEEQGLLPNGEPSQHSSAPQKSLPDLPPPKMIPERKQLAIPKTESPEGYYEEAEPYDTSLNEDGEAVSSSYESYDEEDGSKGKSAPYQWPSPEAGIELMRDARICAFLWRKKWLGQWAKQLCVIKDNRLLCYKSSKDHSPQLDVNLLGSSVIHKEKQVRKKEHKLKITPMNADVIVLGLQSKDQAEQWLRVIQEVSGLPSEGASEGNQYTPDAQRFNCQKPDIAEKYLSASEYGSSVDGHPEVPETKDVKKKCSAGLKLSNLMNLGRKKSTSLEPVERSLETSSYLNVLVNSQWKSRWCSVRDNHLHFYQDRNRSKVAQQPLSLVGCEVVPDPSPDHLYSFRILHKGEELAKLEAKSSEEMGHWLGLLLSESGSKTDPEEFTYDYVDADRVSCIVSAAKNSLLLMQRKFSEPNTYIDGLPSQDRQEELYDDVDLSELTAAVEPTEEATPVADDPNERESDRVYLDLTPVKSFLHGPSSAQAQASSPTLSCLDNATEALPADSGPGPTPDEPCIKCPENLGEQQLESLEPEDPSLRITTVKIQTEQQRISFPPSCPDAVVATPPGASPPVKDRLRVTSAEIKLGKNRTEAEVKRYTEEKERLEKKKEEIRGHLAQLRKEKRELKETLLKCTDKEVLASLEQKLKEIDEECRGEESRRVDLELSIMEVKDNLKKAEAGPVTLGTTVDTTHLENVSPRPKAVTPASAPDCTPVNSATTLKNRPLSVVVTGKGTVLQKAKEWEKKGAS
Protein: Protein myomaker (Myoblast fusion maker) (Transmembrane protein 8C) (Q9D1N4)
Organism: Mus musculus (Mouse)
Function: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers. Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of MYMX. Acts independently of MYMX. Involved in skeletal muscle regeneration in response to injury by mediating the fusion of satellite cells, a population of muscle stem cells, with injured myofibers. Also involved in skeletal muscle hypertrophy, probably by mediating the fusion of satellite cells with myofibers.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23868259, ECO:0000269|PubMed:28860190}; Multi-pass membrane protein {ECO:0000269|PubMed:23868259}. Golgi apparatus membrane {ECO:0000269|PubMed:28860190}; Multi-pass membrane protein {ECO:0000269|PubMed:28860190}. Note=Localizes on the plasma membrane of myoblasts, where it mediates myoblasts fusion (PubMed:23868259, PubMed:28860190). Also localizes in the Golgi apparatus and post-Golgi following palmitoylation; the role of Golgi localization is unclear (PubMed:28860190). {ECO:0000269|PubMed:23868259, ECO:0000269|PubMed:28860190}.
Interaction partners:
- Protein myomixer
- Myogenin
- Myoblast determination protein 1
- Myosin-3
- Myogenic factor 5
Sequence:
MGTVVAKLLLPTLSSLAFLPTVSIATKRRFYMEAMVYLFTMFFVAFSHACDGPGLSVLCFMRRDILEYFSIYGTALSMWVSLMALADFDEPQRSTFTMLGVLTIAVRTFHDRWGYGVYSGPIGTATLIIAVKWLKKMKEKKGLYPDKSIYTQQIGPGLCFGALALMLRFFFEEWDYTYVHSFYHCALAMSFVLLLPKVNKKAGNAGAPAKLTFSTLCCTCV
Protein: Isoprenyl transferase (EC 2.5.1.-) (Q97SR4)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Interaction partners:
Sequence:
MFGFFKKDKAVEVEVPTQVPAHIGIIMDGNGRWAKKRMQPRVFGHKAGMEALQTVTKAANKLGVKVITVYAFSTENWTRPDQEVKFIMNLPVEFYDNYVPELHANNVKIQMIGETDRLPKQTFEALTKAEELTKNNTGLILNFALNYGGRAEITQALKLISQDVLDAKINPGDITEELIGNYLFTQHLPKDLRDPDLIIRTSGELRLSNFLPWQGAYSELYFTDTLWPDFDEAALQEAILAYNRRHRRFGGV
Protein: Musashi RNA binding protein 2 (cDNA FLJ56904, highly similar to RNA-binding protein Musashi homolog 2) (B4DHE8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSVLNSYSAQPNFGAPASPAGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIATAFTNGYH
Protein: Cytochrome P450 2F1 (EC 1.14.14.1) (CYPIIF1) (P24903)
Organism: Homo sapiens (Human)
Function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:10383923}; Peripheral membrane protein {ECO:0000305|PubMed:10383923}. Microsome membrane {ECO:0000269|PubMed:10383923}; Peripheral membrane protein {ECO:0000269|PubMed:10383923}.
Interaction partners:
- Epoxide hydrolase 1
- Peptidyl-prolyl cis-trans isomerase G
- Endoplasmic reticulum resident protein 29
- Glutathione S-transferase P
- Glutathione S-transferase Mu 1
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase A5
- Glutathione S-transferase theta-2B
- Glutathione S-transferase A3
- Microsomal glutathione S-transferase 1
Sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
Protein: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit N) (NDH subunit N) (NDH-N) (NADH-plastoquinone oxidoreductase subunit N) (Q9LVM2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q9CAC5}; Peripheral membrane protein {ECO:0000305}; Stromal side {ECO:0000305}.
Interaction partners:
- NAD
- Photosynthetic NDH subunit of subcomplex B 1, chloroplastic
- NAD
- NAD
- Photosynthetic NDH subunit of subcomplex B 3, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 2, chloroplastic
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- NAD
- Photosynthetic NDH subunit of lumenal location 2, chloroplastic
- NAD
Sequence:
MGSRAICIQRVAPPCFEASQVKKIKTVGSFLVNTRSKRRRSTGVKCSSIADYIGGDLVKPDIGQWLQDVEEHKAIAIYAPHEGGYEGRYLNRLKMQGYYFLDISARGLGDPETTLLKNYPVCPAHLGKQPIARWYYPPEVDYRLAALPPSAKGLVVWVLEAKVLSKSELQFLALLPSLRPNVRVIAECGNWRKFVWKPLAEIANLAAQE
Protein: AT01548p (Q86NT3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
VAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGNLSPTHPSIMSLTPMRPGARMPLRTPIPREYDYFYDFFGFSDYRQGGSFGNNVSYYDDMYRWIDGDYNYYDYPNGGGGGSGGGGGSVSGGTVLPLSAGGSQNSPMASGQRSARGSASGPSASPSLMGVGRGHGITVPRGRVVGQRGSISRLGAQTVPQAAGAAAAAGQAAAAVAQRGATGQGAPAATGGFRGVLPTRPSARGTQHVKPLQNLPAGAAFKTFMEGN
Protein: Insulin (A3RID7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MVLWLQAASLLVLLALYPGADAAAAQHLCGSHLVDALYLVCGEKGFFYNPKRDVDPLTGFLFPKSSQENEVAEYPFKDQMDMIVKRGIVEQCCHKPCNIFDLQNYCN
Protein: E3 ubiquitin-protein ligase PPP1R11 (EC 2.3.2.27) (Hemochromatosis candidate gene V protein) (HCG V) (Protein phosphatase 1 regulatory subunit 11) (Protein phosphatase inhibitor 3) (O60927)
Organism: Homo sapiens (Human)
Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2. Inhibitor of protein phosphatase 1.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 7
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- UBX domain-containing protein 2B
- Protein phosphatase inhibitor 2
- HLA class I histocompatibility antigen, A alpha chain
- UBX domain-containing protein 2A
- Tripartite motif-containing protein 26
Sequence:
MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH
Protein: SLAM family member 8 (B-lymphocyte activator macrophage expressed) (CD antigen CD353) (Q9D3G2)
Organism: Mus musculus (Mouse)
Function: May play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
Sequence:
MWSLWSLLLFEALLPVVVVSVQVLSKVGDSELLVAECPPGFQVREAIWRSLWPSEELLATFFRGSLETLYHSRFLGRVQLYDNLSLELGPLKPGDSGNFSVLMVDTGGQTWTQTLYLKVYDAVPKPEVQVFTAAAEETQPLNTCQVFLSCWAPNISDITYSWRWEGTVDFNGEVRSHFSNGQVLSVSLGLGDKDVAFTCIASNPVSWDMTTVTPWESCHHEAASGKASYKDVLLVVVPITLFLILAGLFGAWHHGLCSGKKKDACTDGVLPETENALV
Protein: Cohesin subunit SA-3 (SCC3 homolog 3) (Stromal antigen 3) (Stromalin-3) (Q99M76)
Organism: Rattus norvegicus (Rat)
Function: Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750}. Chromosome {ECO:0000250}. Note=Associates with chromatin. In prophase I stage of meiosis, it is found along the axial elements of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. It however remains chromatin associated at the centromeres up to metaphase I. During anaphase I, it probably dissociates from centromeres, allowing chromosomes segregation (By similarity). {ECO:0000250}.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Meiotic recombination protein REC8 homolog
- Structural maintenance of chromosomes protein
- RAD21 cohesin complex component like 1
- Structural maintenance of chromosomes protein 1A
- RAD21 cohesin complex component
- Shugoshin 2
- Nipped-B protein
- Sister chromatid cohesion protein PDS5 homolog B
- Synaptonemal complex central element protein 1
Sequence:
MPTLWSPSTQHHGSSSGSMSSPLRKSVRCAQMALSPCSSNIQPCDDRDSQGTAEWDSSSTSEDSDFEDSLRRNVRKRAAKRPPKAIPVAKHPKKQSHIVPGGNDKNKSVPPTSDLFDAVKAARSCAQSLVDEWLENYKQDENAGFLELVNFFIRACGCKSTVTPEMFKTMSNSEIIQHLTEEFNEDSGDYPLTAPGPSWKKFQGSFCEFVKTLVCQCQYSLLFDGFPMDDLISLLIGLSDSQVRAFRHTSTLAAMKLMTSLVKVALQLSLHKDNNQRQYEAERNKGPEQRAPERLESLLEKRKEFQENQEEIEGMMNAIFRGVFVHRYRDILPEIRAVCIEEIGCWMQSYSTSFLNDSYLKYIGWTLHDKHKEVRLKCVKALAGLYSNQELSSRMELFTNRFKDRMVSMVMDRESEVAVEAIRLLTLILKNMEGVLTSADCEKIYSIVYISNRAMASSAGEFVYWKIFHPECGAKAVSGRERRRSPQAQRTFIYLLLAFFMESEHHDHAAYLVDSLWDCAGSYLKDWESLTSLLLQKDQNLGDMQERMLIEILVSSARQAAEGHPPVGRITGKKSLTAKERKLQAYDKVKLAEHLIPLLPQLLAKFSADAENVAPLLRLLSYFDLNIYCTQRLEKHLELLLQQLQEVVVKHVEPEVLEAAAHALYLLCKPEFTFFSRVDFARSQLVDLLTDRFQQELDDLMQSSFLDEDEVYSLTATLKRLSAFYNAHDLTRWEISEPCSRLLRKAVDTGEVPHQVILPALTLVYFSILWTVTHISESTSQKQLMSLKKRMVAFCELCQSCLSDVDPEIQEQAFVLLSDLLLIFSPQMVVGGRDFLRPLVFFPEATLQSELASFLMDHVFLQPGELGNGQSQEDHVQIELLHQRRRLLAGFCKLLLYGVLELDAASDVFKHYNKFYEDYGDIIKETLTRARQIDRCQCSRILLLSLKQLYTELIQEQGPQDLTELPAFIEMRDLARRFALSFGPQQLHNRDLVVMLHKEGIKFSLSELPPAGSSREPPNIAFLELLSEFSPRLFHQDKQLLLSYLEKCLQRVSMAPSHPWGPVTTYCHSLHLVENTAEASSQGPPHSKKRCIEVPRRLQEEESSSQGESLQLNSGPTTPTLTSTAVKRRQSPRTVGKRQKGGPGPGPGPGPGPGPGPGPGPGPGPGPELICSQQLSGTQRLKMSSAPCFQIRCDPSGSGLGKQMTRLSLMEEDEEEELRLLDEEWQCGDKLLHSPSSPSEHGLDLLDTTELNMEDF
Protein: Transcription factor (A0A1D8PJV0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transcriptional regulator
- G1/S-specific cyclin CLN3
- Transcription factor MBP1
- Hypha-specific G1 cyclin-related protein 1
- Transcription factor of morphogenesis MCM1
Sequence:
MSDSQIYSATYSNVPAFEFVTSEGPIMRRKKDSWINATHILKIAKFPKAKRTRILEKDVQTGIHEKVQGGYGKYQGTYVPLDLGAAIARNFGVYDVLKPIFEFQYIEGQTEVPPPAPKHNHASALNVAKRQASLLKKQKEKQVQPTLSDTSFGSSTSVPPTTVPKKRGRPKRATLSATPSLQRSDTTPINKSLIDFNANDHSAKSSFIGVVPSFARNDTEQDALQIMTNNMNLRQEDLASVETDDDEEYHNGSRGDGLQNDSFTTKRRKYPGGMTNGNGLESQADLLTSKELFGVSRTSFEKRANQQHNHYSPLQPYHQPSISLSQENQIYSDYFQSLLSYFLDDNNKIRSPIPDSLLSPPLPLSKIHIYQTIDSDGNTIFHWACSMGNLNMVEFLLKTFTHSLNPDVRNNNGETPLMFMVKFNNSFQLRNFPLILDLLKESVLLVDSNGKTVLHHIVDTDSKHKREKFAQYYLESLLEKIVDERQEQGDSNGHAMEDDLTKDELVTKFINHQDSDGNTAFHIAAHNLNKKCIKVFINYHRFINFGLRNLVSCTVEDYLASHNYVLRLDPVEHDQSNNSDGDEDIMEDYTNENQSFETQLHNSKMAINLQNTTANLLTEKMTQLAYAIDSELSEKDEVILKYFKVLSQINQIKLESQRKILSFFKLDHLIEELEQNKDDSQQQQQQVTDDDDPTSVHGNDLHLDFKRDHILQEEIYRLMNDLTYQELHQQDELDKVEHSYRMTKERLHEKVLDASSFVIDQTHQQGNVHEQLELAKQLQVEIIKRKKLVDEISKLTKNVPLPENPNAKTIIDTYPSTDKLYKYCKLISLSCGIPMDEIETSIDAMEESLVKK