wanglab/gogpt-training-data huggingface dataset:
Protein: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (EC 2.3.1.168) (Branched-chain alpha-keto acid dehydrogenase complex component E2) (Dihydrolipoamide branched-chain transacylase E2) (Q23571)
Organism: Caenorhabditis elegans
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2) (By similarity). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component (By similarity). Required for the catabolism of branched-chain amino acids and the subsequent synthesis of monomethyl branched-chain fatty acids, which are important for regulating postembryonic growth.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P11181}. Cytoplasm, cytosol {ECO:0000269|PubMed:26683372}. Cell projection, dendrite {ECO:0000269|PubMed:26683372}. Cell projection, cilium {ECO:0000269|PubMed:26683372}. Note=Localizes to puncta within the cytosol which is consistent with its expected location in mitochondria. {ECO:0000269|PubMed:26683372}.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Isovaleryl-CoA dehydrogenase, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Probable methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
Sequence:
MMAARLLGTSSRIFKLNKHLHTSKVAFMPVVQFKLSDIGEGIAEVQVKEWYVKEGDTISQFDKVCEVQSDKAAVTISCRYDGIVKKLYHEVDGMARVGQALIDVEIEGNVEEPEQPKKEAASSSPEAPKSSAPKAPESAHSEGKVLATPAVRRIAIENKIKLAEVRGTGKDGRVLKEDVLKFLGQVPADHTSGSTNIRTTHQAPQPSSKSYEPLKEDVAVPIRGYTRAMVKTMTEALKIPHFGYNDEINVDSLVKYRAELKEFAKERHIKLSYMPFFIKAASLALLEYPSLNSTTDEKMENVIHKASHNICLAMDTPGGLVVPNIKNCEQRSIFEIAQELNRLLEAGKKQQIKREDLIDGTFSLSNIGNIGGTYASPVVFPPQVAIGAIGKIEKLPRFDKHDNVIPVNIMKVSWCADHRVVDGATMARFSNRWKFYLEHPSAMLAQLK
Protein: Dynein regulatory complex subunit 5 (Flagellar-associated protein 155) (A8HMZ4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. May play a role in the assembly of N-DRC.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A6H639}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}. Note=Detected along the length of the sperm flagellum. {ECO:0000250|UniProtKB:A6H639}.
Interaction partners:
Sequence:
MAAPNLITPLRDICVKVVAANFEGCPTFGPLPDKYVKRIIDILPLDLPLELVGSLIADEDYWRRRSQARWKNCEVAAHGYSWKQLFFERNLMEFLEQYDPAVTDLSSLKRLLTYSRRFVQTVHIRQLPSHLDLQILFECMVNTPSSLALSYNLKEVGMDYDRSLFGMKLSDCRALAKALEHTETLTHLDLSNNSLDDDKVRMLASGLVENLSITHLNLSHNKIADRGVRALAKLLDGHSVISLLELHDNQIHTEGAESLARAFKSNQCLLSVNLRLNRMGDEGCKAVVESVRGSPTLQRLNISANAAGPGTAAAVVALLRLNNTLTELDVSCNQFGEDACGNVRRALEQNGSVRLMDVRMTGINPDDEMAIAENLRARQERVDKARVLGK
Protein: Pigment epithelium-derived factor (PEDF) (Serpin F1) (Q95121)
Organism: Bos taurus (Bovine)
Function: Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.
Subcellular location: Secreted. Melanosome {ECO:0000250}.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Low-density lipoprotein receptor-related protein
- Fibromodulin
- Peptidyl-prolyl cis-trans isomerase FKBP10
- Cartilage-associated protein
- Trimeric intracellular cation channel type B
Sequence:
MQALVLLLWTGALLGFGRCQNAGQEAGSLTPESTGAPVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSGESPTANVLLSPLSVATALSALSLGAEQRTESNIHRALYYDLISNPDIHGTYKDLLASVTAPQKNLKSASRIIFERKLRIKASFIPPLEKSYGTRPRILTGNSRVDLQEINNWVQAQMKGKVARSTREMPSEISIFLLGVAYFKGQWVTKFDSRKTSLEDFYLDEERTVKVPMMSDPQAVLRYGLDSDLNCKIAQLPLTGSTSIIFFLPQKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTIPKLKLSYEGELTKSVQELKLQSLFDAPDFSKITGKPIKLTQVEHRVGFEWNEDGAGTNSSPGVQPARLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGT
Protein: Kinesin-II 85 kDa subunit (KRP-85/95 85 kDa subunit) (P46872)
Organism: Strongylocentrotus purpuratus (Purple sea urchin)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-associated protein 3
- Uncharacterized protein.
- Uncharacterized protein.
- Kinesin light chain
- WD_REPEATS_REGION domain-containing protein.
- Kinesin heavy chain
- Kinesin-II 95 kDa subunit
Sequence:
MPGGSSGNDNVRVVVRCRPLNSKETGQGFKSVVKMDEMRGTVQVTNPNAPSGEPPKSFTFDTVFAPGAKQTDVYNQTARPIVDAIIEGYNGTIFAYGQTGTGKTFTMEGVRSQPELRGIIPNSFAHIFGHIAKEQENVRFLVRVSYLEIYNEEVKDLLGKDQQHRLEVKERPDVGVYVKDLSAFVVNNADDMDRIMTLGNKNRSVGATNMNESSSRSHAIFTITLERSDMGLDKEQHVRVGKLHMVDLAGSERQTKTGATGQRLKEATKINLSLSTLGNVISSLVDGKSTHIPYRNSKLTRLLQDSLGGNAKTVMCANIGPAEYNYDETISTLRYANRAKNIKNKAKINEDPKDALLREFQKEIEELKKQISESGEGLDDDEESGSEESGDEEAGEGGVKKKRKGKNPKRKLSPEIMAAMQKKIDEEKKALEEKKDMVEEDRNTVHRELQRRESELHKAQDDQKILNEKLNAIQKKLIVGGVDLLAKSEEQEQLLEQSALEMKERMAKQESMRKMMEEREQERMDIEEKYSSLQDEAHGKTKKLKKVWTMLMQAKSEVADMQAEHQREMEALLENVRELSRELRLSMLIIDSFIPQEFQEMIEQYVHWNEDIGEWQLKCVAYTGNNMRKQTPVADKDKSLAYGEADLSNVFLTYNLEGGGMKYKPSQGKSGRPKTSSGRPKTGKKKQASMASSIDALLQ
Protein: CD79b molecule (A0A8J8XPU7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKLPSRVPGEMVPPLGLNLHGRKGPNGEEVERRKVAARADTQLHVLPQTLLGLRDRAVTMATLVLSPVPCHWLMFLLLLLSGEPVPAMTKSDQPPIFQGSPCSKIWQHPRFAAKKRSSMVKFHCHTDYSGVMTWFRQKGNQRPQELFPEDGHISQTRNGSVYTLTLQNIQYEDNGIYFCQQKCNSTEPDVTDGCGTELLVLGFSTLDQLKRRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLNIDQTATYEDIVTLRTGEVKWSVGEHPGQE
Protein: Probable integral membrane protein (O33248)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Possible conserved membrane protein
- Outer membrane channel protein CpnT
- DAPG hydrolase PhiG domain-containing protein
- Transcriptional repressor Mce3R
Sequence:
MSLSVRRPPAARAAAIVEAESWFLKRGLPSVLTMRGRCRRLWPRSAPMLAAWAVVEGCLMAVFFVTDGGEVFISATPTTAQWVILALLAVALPLASLVGWLVSQISSGRGQAAVATMAVAFAAASDVIESGPIQLLRTAVVVGLVLLQTGCGVGSVLGWAVRMTLEHLATVGTLAVRALPIVLLTALVFFNTYVWLMAANINGERLTLAMVFLLAIAGAFVVSKTVERVRPLLRSTTVMPQGSQSLAGTPFATMGDPSPGFPLTRAERLNVVFLLAASQLVEILVVASVGAAIYLVLGMIILTPPLLREWTHYDSMTTTVLGMTFPAPDSLIRMCLFLGALTFMYISARAVDDAEYRAMFLDPLIDDLHTALLARNRYRNNVVTAPCAGVDAGHVDD
Protein: BRCA1-associated RING domain protein 1 (BARD-1) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BARD1) (Q99728)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.
Subcellular location: Nucleus. Note=During S phase of the cell cycle, colocalizes with BRCA1 into discrete subnuclear foci. Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.
Interaction partners:
- BRCA1-A complex subunit RAP80
- DNA repair protein RAD51 homolog 1
- DNA endonuclease RBBP8
- Breast cancer type 2 susceptibility protein
- Double-strand break repair protein MRE11
- BRCA1-A complex subunit Abraxas 1
- Breast cancer type 1 susceptibility protein
- BRISC and BRCA1-A complex member 2
- Fanconi anemia group J protein
- Lys-63-specific deubiquitinase BRCC36
Sequence:
MPDNRQPRNRQPRIRSGNEPRSAPAMEPDGRGAWAHSRAALDRLEKLLRCSRCTNILREPVCLGGCEHIFCSNCVSDCIGTGCPVCYTPAWIQDLKINRQLDSMIQLCSKLRNLLHDNELSDLKEDKPRKSLFNDAGNKKNSIKMWFSPRSKKVRYVVSKASVQTQPAIKKDASAQQDSYEFVSPSPPADVSERAKKASARSGKKQKKKTLAEINQKWNLEAEKEDGEFDSKEESKQKLVSFCSQPSVISSPQINGEIDLLASGSLTESECFGSLTEVSLPLAEQIESPDTKSRNEVVTPEKVCKNYLTSKKSLPLENNGKRGHHNRLSSPISKRCRTSILSTSGDFVKQTVPSENIPLPECSSPPSCKRKVGGTSGRKNSNMSDEFISLSPGTPPSTLSSSSYRRVMSSPSAMKLLPNMAVKRNHRGETLLHIASIKGDIPSVEYLLQNGSDPNVKDHAGWTPLHEACNHGHLKVVELLLQHKALVNTTGYQNDSPLHDAAKNGHVDIVKLLLSYGASRNAVNIFGLRPVDYTDDESMKSLLLLPEKNESSSASHCSVMNTGQRRDGPLVLIGSGLSSEQQKMLSELAVILKAKKYTEFDSTVTHVVVPGDAVQSTLKCMLGILNGCWILKFEWVKACLRRKVCEQEEKYEIPEGPRRSRLNREQLLPKLFDGCYFYLWGTFKHHPKDNLIKLVTAGGGQILSRKPKPDSDVTQTINTVAYHARPDSDQRFCTQYIIYEDLCNYHPERVRQGKVWKAPSSWFIDCVMSFELLPLDS
Protein: Probable acetyltransferase Rv3034c (EC 2.3.1.-) (Peroxisome homeostasis protein Rv3034c) (O53281)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May be involved in the biosynthesis of 6-O-methylglucosyl-containing lipopolysaccharides (MGLP).
Interaction partners:
- Probable S-adenosylmethionine-dependent methyltransferase Rv3030
- Glycogen synthase
- Diglucosylglycerate octanoyltransferase
- Probable 1,4-alpha-glucan branching enzyme Rv3031
- Glucosyl-3-phosphoglycerate synthase
- Uncharacterized S-adenosylmethionine-dependent methyltransferase Rv3037c
- Conserved protein
- Polyketide cyclase / dehydrase and lipid transport
Sequence:
MNVLSLGSSSGVVWGRVPITAPAGAATGVTSRADAHSQMRRYAQTGPTAKLSSAPMTTMWGAPLHRRWRGSRLRDPRQAKFLTLASLKWVLANRAYTPWYLVRYWRLLRFKLANPHIITRGMVFLGKGVEIHATPELAQLEIGRWVHIGDKNTIRAHEGSLRFGDKVVLGRDNVINTYLDIEIGDSVLMADWCYICDFDHRMDDITLPIKDQGIIKSPVRIGPDTWIGVKVSVLRGTTIGRGCVLGSHAVVRGAIPDYSIAVGAPAKVVKNRQLSWEASAAQRAELAAALADIERKKAAR
Protein: Teleost multiple tissue opsin 2a (Teleost multiple tissue opsin-1a) (R9R6C7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MFPEETNMSYISNGTDDDLLSALEDWSDTPAEKLSRTGHNVVAVILGSILIFGTLNNLVVLVLFCKFKTLRTPVNMLLLNISVSDMLVCLFGTTLSFAASIRGRWLVGRHGCMWYGFVNSCFGIVSLISLAILSYDRYSTLTVYNKRAPDYSKPLLAVGGSWLYSLFWTVPPLLGWSSYGLEGAGTSCSVTWTANTPQSHSYIICLFIFCLGIPVLVMVYCYSRLICAVKQVGRIRKTAARRREYHILFMVITTVVCYLLCWMPYGVVAMMATFGRPGIISPIASVVPSLLAKSSTVINPLIYILMNKQFYRCFLILIHCKHSSLENGQSSMPSRTTGIQLNRRPYSNPVADNAPPSIDLQNDCSTPVSG
Protein: Neuromedin-B receptor (NMB-R) (Neuromedin-B-preferring bombesin receptor) (P24053)
Organism: Rattus norvegicus (Rat)
Function: Receptor for neuromedin-B. Contributes to the maintenance of basal sigh rate through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity. Contributes to the induction of sneezing following exposure to chemical irritants or allergens which causes release of NMB by nasal sensory neurons and activation of NMBR-expressing neurons in the sneeze-evoking region of the brainstem (By similarity). These in turn activate neurons of the caudal ventral respiratory group, giving rise to the sneezing response (By similarity). Contributes to induction of acute itch, possibly through its activation on dorsal root ganglion neurons by the NMB peptide (By similarity). Plays a role in the innate immune response to influenza A virus infection by enhancing interferon alpha expression and reducing expression of IL6 (By similarity). Plays a role in CSF1-induced proliferation of osteoclast precursors by contributing to the positive regulation of the expression of the CSF1 receptor CSF1R (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuromedin B
- Gastrin-releasing peptide
- Toll-like receptor 4
Sequence:
MPPRSLPNLSLPTEASESELEPEVWENDFLPDSDGTTAELVIRCVIPSLYLIIISVGLLGNIMLVKIFLTNSTMRSVPNIFISNLAAGDLLLLLTCVPVDASRYFFDEWVFGKLGCKLIPAIQLTSVGVSVFTLTALSADRYRAIVNPMDMQTSGVVLWTSLKAVGIWVVSVLLAVPEAVFSEVARIGSSDNSSFTACIPYPQTDELHPKIHSVLIFLVYFLIPLVIISIYYYHIAKTLIRSAHNLPGEYNEHTKKQMETRKRLAKIVLVFVGCFVFCWFPNHILYLYRSFNYKEIDPSLGHMIVTLVARVLSFSNSCVNPFALYLLSESFRKHFNSQLCCGQKSYPERSTSYLLSSSAVRMTSLKSNAKNVVTNSVLLNGHSTKQEIAL
Protein: Dual specificity protein kinase (Eurofung) (C8VU80)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MSTPSTATATHPVTHHHQHYGFPHHQTYLPNPSYPTTSSPHLNSTVYPYAVPSTTAALPYTQSPHSAAAASTATSTAAMPQPPKPASTGVSTQNGRRKKPDWGEFYKNGIPKEVIVIDDTPPPDQSAAASRTYPTASTAQVANGNTAQPAGKRRRTGIETAYDLGYFDRPSFSTNPQHYGEESSAGSLSTDRTASLHTTAPTSLSQGSSGASNGAYYEDANVGQKRKRVATRKSVRDQQKKLEQETATDAFLSYIPPPKPPIKAKDVPVPVVRSYANRGEKYDDDDGHYIVNPNTPITDRYSIIKLLGQGTFGKVVEAYDKQRKARCAIKIIRSIQKYRDASRIELRVLSTLASNDKHNRNKCIHLRDCFDFRNHICIVTDLLGQSVFDFLKGNGFVPFPSSQIQSFARQLFTSVAFLHDLNLIHTDLKPENILLVKNAYQTFTYNRTIPSSSTAISRNARQRRVLLDSEIRLIDFGSATFDDEYHSSVVSTRHYRAPEIILNLGWSFPCDIWSIGCILVEFFTGDALFQTHDNLEHLAMMEAVIGERIDPKLVRQVMQGGRNGNQNQAAKYFVRNRLDYPNEETTRASKKYVQAMRRLTSFMPTNTKFYRLFLDLLQRIFVYDPKQRITAKDALKHPWFKEPITDDGTEALRIGQQLQQRNNGQQR
Protein: Uncharacterized derlin-like protein C1687.17c (O94458)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase hrd1
- Ubiquitin fusion degradation protein 1
- Nuclear protein localization protein 4
- Cell division cycle protein 48
- Protein OS-9 homolog
- Uncharacterized derlin-like protein C365.08c
- ER-derived vesicles protein 41
- Putative ERAD-associated E3 ubiquitin-protein ligase component
- Uncharacterized Sel1-like repeat-containing protein C1B3.10c
- Endoplasmic reticulum chaperone BiP
Sequence:
MAILPEFISQTPPVTRYIVLGTLFTTLAVNFGYVSDLKIFFNWKLFLAKGEYWRAITTFLYVGPFGLELILYLSFLLRFMSMLERSSPPPQTQSFLKTVLIVWFSLLVTSYFSYMPFAASYFSFTMLYIWSWKHPLYRISILGLFDVKAPYVPWVMVLLRWLRTGIFPLLDLISALIGHVYFFVTDFSTV
Protein: Geko (RE30284p) (Q9VVN7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALIDTAWRCRLMIFVIVSLLLVGDLFGYGGGMKSNHPNPHSVRSARGAVPGGAPTGPAAAAASKFQTKNAEIDITEEHDFNELSAAAQSLKPGMAVVTGASLKTKSQLTDAIKESCLPKMLCELASKADYQLSEKERELLRLIRSPTMPWMMNMPPSKWYFAAHMGELMRHTGDNLSGPMGCANLWPNCPISSKKLMKLSYKVRV
Protein: Potassium channel toxin alpha-KTx 9.5 (Kbot1) (P84744)
Organism: Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus)
Function: Blocks voltage-gated potassium channels Kv1.1/KCNA1 (IC(50)=145 nM), Kv1.2/KCNA2 (IC(50)=2.5 nM), and Kv1.3/KCNA3 (IC(50)=15). Also inhibits calcium-activated potassium channels (KCa/KCNN).
Subcellular location: Secreted {ECO:0000269|PubMed:15165720}.
Interaction partners:
Sequence:
VGCEECPMHCKGKHAVPTCDDGVCNCNV
Protein: BURP domain protein USPL1 (Unknown seed protein-like protein 1) (AtUSPL1) (Q9XI99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Associated with the protein storage vacuole formation.
Subcellular location: Protein storage vacuole {ECO:0000269|PubMed:19639386}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:19639386}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19639386}. Prevacuolar compartment {ECO:0000269|PubMed:19639386}.
Interaction partners:
- AT-hook motif nuclear-localized protein 17
- At2g44380
- Cation/H
- Ubiquitin carboxyl-terminal hydrolase 7
- PPPDE putative thiol peptidase family protein
- At1g16880
- Cation/H
- VQ motif-containing protein 10
- Coilin
Sequence:
MASTFRLSISFLTLILFSLWVVEAHTSRKLISIKEKEGQDISHLLKDGEFDDPSLYMYFTLNDLKLGTKLLIYFYKNDLQKLPPLLTRQQADLIPFTKSKLDFLLDHFSITKDSPQGKAIKETLGHCDAKAIEGEHKFCGTSLESLIDLVKKTMGYNVDLKVMTTKVMVPAQNSISYALHNYTFVEAPKELVGIKMLGCHRMPYPYAVYYCHGHKGGSRVFEVNLVTDDGRQRVVGPAVCHMDTSTWDADHVAFKVLKMEPRSAPVCHFFPLDNIVWVTK
Protein: Uncharacterized protein (Q8BVB9)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
DSSVPLPNTDSTCPAEQDVGQKGCSERNPVFYTHSLLYRGTLKCNHSSETTSLEQCNIAQSSPCKIESPIPNPSGTESGTYFTDFQLPLPRIKEEPGQHSSGQENTVKNATQVPKENIRKHSQPRSFDLKTYKPMGFESSFLKFIQESEEKDDDFDDWEPSEHLTLNNSSHPSNDLTGNVVADTIVNESAPQVDIPHSSSDPPVSENLTAVPPLVVAEATAVPSLENLRVVLDKALTDCGELALKQLHYLRPVVVLERSKFSTPILDLFPTKKTDELCVGSS
Protein: BRISC and BRCA1-A complex member 1 (Mediator of RAP80 interactions and targeting subunit of 40 kDa) (New component of the BRCA1-A complex) (Q9NWV8)
Organism: Homo sapiens (Human)
Function: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:24075985}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000269|PubMed:19261746, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19261749, ECO:0000269|PubMed:21282113}.
Interaction partners:
- BRCA1-A complex subunit RAP80
- BRCA1-A complex subunit Abraxas 1
- BRISC and BRCA1-A complex member 2
- Breast cancer type 1 susceptibility protein
- BRISC complex subunit Abraxas 2
- Lys-63-specific deubiquitinase BRCC36
- BRCA1-associated RING domain protein 1
- Serine hydroxymethyltransferase, mitochondrial
- Poly [ADP-ribose] polymerase tankyrase-1
- Poly [ADP-ribose] polymerase tankyrase-2
Sequence:
MEVAEPSSPTEEEEEEEEHSAEPRPRTRSNPEGAEDRAVGAQASVGSRSEGEGEAASADDGSLNTSGAGPKSWQVPPPAPEVQIRTPRVNCPEKVIICLDLSEEMSLPKLESFNGSKTNALNVSQKMIEMFVRTKHKIDKSHEFALVVVNDDTAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDVVYIHNGTEEKEEEMSWKDMFAFMGSLDTKGTSYKYEVALAGPALELHNCMAKLLAHPLQRPCQSHASYSLLEEEDEAIEVEATV
Protein: Small monomeric GTPase (H2L0Q6)
Organism: Caenorhabditis elegans
Interaction partners:
- Ral guanine nucleotide dissociation stimulator-like 1
- Raf homolog serine/threonine-protein kinase
- Rho-GAP domain-containing protein
- Exocyst component Exo84 C-terminal domain-containing protein
- Protein shank
- Exocyst complex component 2
- V-type proton ATPase 116 kDa subunit a 2
- Afadin
- Exocyst complex component 6
- Exocyst complex component 4
Sequence:
MDKVSHVLRNGWNWIKLKFLALWHFLFRRKSDEPEFYDPEAMASKKASGTLPPQQQVVHKVIMVGTGGVGKSALTLQFMYDEFVEEYEPTKADSYRKKVVLDGEECSIDILDTAGQEDYSAIRDNYYRSGEGFICVFSILDMESFEATNEFREQILRVKNSDSSVPIVLVGNKGDMRDQRVVSAELCRQRAEQWGCHYVETSAKRRENVDKVFYDLMREMKRRKGGSQAQTGIDASASSGRKKRSGIKKHCTIL
Protein: Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)] (P27090)
Organism: Mus musculus (Mouse)
Function: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Transforming growth factor beta receptor type 3
- Latent-transforming growth factor beta-binding protein 1
- Latent-transforming growth factor beta-binding protein 3
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 2
- Integrin alpha-V
- Transforming growth factor beta-3 proprotein
- Thrombospondin-1
Sequence:
MHYCVLSTFLLLHLVPVALSLSTCSTLDMDQFMRKRIEAIRGQILSKLKLTSPPEDYPEPDEVPPEVISIYNSTRDLLQEKASRRAAACERERSDEEYYAKEVYKIDMPSHLPSENAIPPTFYRPYFRIVRFDVSTMEKNASNLVKAEFRVFRLQNPKARVAEQRIELYQILKSKDLTSPTQRYIDSKVVKTRAEGEWLSFDVTDAVQEWLHHKDRNLGFKISLHCPCCTFVPSNNYIIPNKSEELEARFAGIDGTSTYASGDQKTIKSTRKKTSGKTPHLLLMLLPSYRLESQQSSRRKKRALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIHEPKGYNANFCAGACPYLWSSDTQHTKVLSLYNTINPEASASPCCVSQDLEPLTILYYIGNTPKIEQLSNMIVKSCKCS
Protein: E3 ubiquitin-protein ligase NEURL1B (EC 2.3.2.27) (Neuralized-2) (NEUR2) (Neuralized-like protein 1B) (Neuralized-like protein 2) (Neuralized-like protein 3) (RING-type E3 ubiquitin transferase NEURL1B) (Q0MW30)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase involved in regulation of the Notch pathway through influencing the stability and activity of several Notch ligands.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19723503}.
Interaction partners:
- E3 ubiquitin-protein ligase MIB2
- E3 ubiquitin-protein ligase MIB1
Sequence:
MGNTVHRTLPDSSPPARLLATRPCYGPGPERRAVLGEAPRFHAQAKGKNVRLDGHSRRATRRNSFCNGVTFTQRPIRLYEQVRLRLVAVRPGWSGALRFGFTAHDPSLMSAQDIPKYACPDLVTRPGYWAKALPENLALRDTVLAYWADRHGRVFYSVNDGEPVLFHCGVAVGGPLWALIDVYGITDEVQLLESTFADTLTPLRLGQARLSACPPPGSHDAANFDNNELENNQVVAKLGHLALGRPDAAVPCVARERPRPASSPALLDAELRFHATRGPDVSLSADRRLACAPRPDGGRTLVFSERPLRPGESLCVEVGRPGLAAPAAVAFGITSCDPGALRPSELPADPAALLDRKEYWVVARAGPVPSGGDALSFTLRPGGDVLLAVNGRPRGRLLCVDTSQALWAFFAVRGGVAGQLRLLGTLQSSSETMTPSGSFSGSQDDSDSDMTFGVNQSSSASESSLVTAPSSPLSPPVSPAFSAPEPTGSRNGECTVCFDSEVDTVIYTCGHMCLCHGCGLRLRRQARACCPICRRPIKDVIKIYRP
Protein: tRNA pseudouridine synthase 4 (EC 5.4.99.25) (tRNA pseudouridine(55) synthase) (Psi55 synthase) (tRNA pseudouridylate synthase 4) (tRNA-uridine isomerase 4) (P48567)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. Also catalyzes pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3'.
Subcellular location: Nucleus {ECO:0000269|PubMed:9358157}. Mitochondrion {ECO:0000269|PubMed:9358157}.
Interaction partners:
- tRNA pseudouridine synthase 1
- H/ACA ribonucleoprotein complex subunit NOP10
- H/ACA ribonucleoprotein complex subunit GAR1
- Multisubstrate pseudouridine synthase 7
- tRNA pseudouridine
- tRNA
- tRNA pseudouridine
- tRNA pseudouridine
- tRNA
- H/ACA ribonucleoprotein complex subunit NHP2
Sequence:
MNGIFAIEKPSGITSNQFMLKLQHALTKSQVFSKEIQRATAERKQQYEKQTGKKASKRKLRKVSKVKMGHGGTLDPLASGVLVIGIGAGTKKLANYLSGTVKVYESEALFGVSTTSGDVEGEILSQNSVKHLNFDDLKTVEEKFVGQLKQTPPIYAALKMDGKPLHEYAREGKPLPRAIEPRQVTIYDLKVFSDSLKRDHDYPLLRPTTEEAVDTVKNLNANMLNDVLYFSKEYTEKHGLDSEVAKVEEPFPLSEQEEQEIQKEGDSYRAPKLHFKANVSSGTYIRSLVSDIGKSMRSSCYMVKLIRLQQQDWSLEKNNVFQLTDFTERDEKVWSKVLEKVLDEGATVDVIEELKKAEKEIPADVKECIVSSDQPGDEATAETIETANAEEHSNTLKRKIEQV