wanglab/gogpt-training-data huggingface dataset:
Protein: Fe(3+) dicitrate transport system permease protein FecC (Iron(III) dicitrate transport system permease protein FecC) (P15030)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2651410}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fe
- Fe
- Fe
- Fe
- Iron
- Ferric enterobactin transport ATP-binding protein FepC
- Vitamin B12-binding protein
- Iron
- Ferric citrate uptake sigma factor regulator FecR
- Vitamin B12 import ATP-binding protein BtuD
Sequence:
MTAIKHPVLLWGLPVAALIIIFWLSLFCYSAIPVSGADATRALLPGHTPTLPEALVQNLRLPRSLVAVLIGASLALAGTLLQTLTHNPMASPSLLGINSGAALAMALTSALSPTPIAGYSLSFIAACGGGVSWLLVMTAGGGFRHTHDRNKLILAGIALSAFCMGLTRITLLLAEDHAYGIFYWLAGGVSHARWQDVWQLLPVVVTAVPVVLLLANQLNLLNLSDSTAHTLGVNLTRLRLVINMLVLLLVGACVSVAGPVAFIGLLVPHLARFWAGFDQRNVLPVSMLLGATLMLLADVLARALAFPGDLPAGAVLALIGSPCFVWLVRRRG
Protein: Uncharacterized protein YNL108C (P53929)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized vacuolar membrane protein YNL115C
- H/ACA ribonucleoprotein complex non-core subunit NAF1
Sequence:
MAIENIYIARHGYRSNWLPKGPYPPPPTGIDNDVPLSEHGVEQAHELANYISKLDVKPEMIFSSPFYRCLETSKPTVEALKIPLYVDRGVGEWYKPDRPIIPEPATHEVMSKFFPSMISPDWEPSIIPSNKGETEEDIFERCHKFWPVFIDRVERKFPNVKTIMIVTHAATKSALGMNLLKFSSAKEPIDNKGTFIRNGSCAIDKFELVKGENESIPFEEREWKLTMNGNTSFLTNGEEMNWTFMNAFEAGSDADIKARRAAESGKLKME
Protein: Caveolae-associated protein 2 (Cavin-2) (Phosphatidylserine-binding protein) (Serum deprivation-response protein) (Q63918)
Organism: Mus musculus (Mouse)
Function: Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (By similarity). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:19546242}.
Interaction partners:
- Caveolin-1
- Caveolae-associated protein 4
- EH domain-containing protein 2
Sequence:
MGEDAAQAEKFQHPNTDMLQEKPSSPSPMPSSTPSPSLNLGSTEEAIRDNSQVNAVTVHTLLDKLVNMLDAVRENQHNMEQRQINLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVRERLERQCVQVKRLENNHAQLLRRNHFKVLIFQEESEIPASVFVKEPVPSAAEGKEELADENKSLEETLHNVDLSSDDELPRDEEALEDSAEEKMEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTPNHQKASSGKSSPFKVSPLSFGRKKVREGESSVENETKLEDQMQEDREEGSFTEGLSEASLPSGLMEGSAEDAEKSARRGNNSAVGSNADLTIEEDEEEEPVALQQAQQVRYESGYMLNSEEMEEPSEKQVQPAVLHVDQTA
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A0G2K897)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- [histone H3]-lysine
- Uncharacterized protein
- Histone deacetylase 1
- ATP synthase F
- [histone H3]-trimethyl-L-lysine
- RNA helicase
- LRRGT00139
Sequence:
MELGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEIVVEEGGYETICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKNLRKKDKEGPECPPTVVVKEELGGDVKMESASPKTFLEGKEELSHSPEPCTKMTMRLRRNHSNAQFIESYVCRMCSRGDEDDKLLLCDGCDDNYHIFCLLPPLPEIPKGVWRCPKCVMAECKRPPEAFGFEQATREYTLQSFGEMADSFKADYFNMPVHMVPTELVEKEFWRLVNSIEEDVTVEYGADIHSKEFGSGFPVSDSKRHLTPEEEEYATSGWNLNVMPVLEQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKKLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAACPEKLDLNLAAAVHKEMFIMVQEERRLRKALLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPAMLHKLKVRAESFDTWANKVRVALEVEDGRKRSLEELRALESEARERRFPNSELLQRLKNCLSEAEACVSRALGLVSGQEAGPDRVAGVQMTLAELQDFLGQMNNLPCAMHQIGDVKGILEQVEAYQTEAREALVSQPSSPGLLQSLLERGQQLGVEVPEAQQLQRQVEQARWLDEVKRTLAPSARRGTLAIMRGLLVAGASVAPSPAVDKAQAELQELLTIAERWEEKAHLCLEARQKHPPATLEAIIHEAENIPVHLPNIQSLKEALAKARAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKELGLYKSDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLASLTTNSSTASICVCGQVPAGVGALQCDLCQDWFHGRCVTVPRLLSSQRSSLTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAISWQGRARQVLASEEVTALLGRLAELRQRLQAESKPEESLAYSSDGGDGTGNMPKVQGLLENGDSVTSPEKVATEEGSDLELLSSLLPQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLKRVQTLLELEKAERHGSRTRGRALERRRRRKVDRGGEPDDPAREELEPKRVRSSGPEAEEVQEEEELEEETGGEVPPVPFPNNGSPSTQEDQDGLEPVLDAGSDTSAPFSTLTSRLLMSCPQQPSLQQL
Protein: Synaptotagmin-16 (Chr14Syt) (Synaptotagmin 14-like protein) (Synaptotagmin XIV-related protein) (Q17RD7)
Organism: Homo sapiens (Human)
Function: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
Interaction partners:
Sequence:
MVLAMASQDVQNFFQPFSSWISRVYEALQQAGDMLSASLVNISKQDSKLSDKLDQDLDNIQIQETYFEDEEQDNDWSQEDANSLFLEVDHFSCCNSDLQDSAQNSSPSLSQHAKDSCSTMSQWPNWASDDRKLPHVLSSIAEEEHHLEKQRSGLQHGFDSQLPGTLETVNGKKQVNSFGDDEELSTSSDSDEEVIKQFEISVSRSQSFRSVTSEKGKQTGLEQKPKFSRSLLTHGEDGTEVSACEDLDGASQRRYSENLSYGEDDHIPAHSQSPCERGDAKHHGTSHQESSVVQSLRRQSTEGSLEMETAFNSRGFEDSYATDSSSMWSPEEQDRTNLQVPSGVSEPISKCGDLDVIFEYRAASQKLTVTIVRAQGLPDKDRSGVNSWQVHVVLLPGKKHRGRTNIQRGPNPVFREKVTFAKLEPRDVAACAVRFRLYAARKMTRERMMGEKLFYLSHLHPEGEMKVTLVLEPRSNISSGGSPLSPSAVSHSDSTSSTQSLSHGGAPELLVGLSYNATTGRLSVEMIKGSHFRNLAVNRAPDTYGKLFLLNSVGQEMSRCKTSIRRGQPNPVYKETFVFQVALFQLSDVTLMISVYNRRTMKRKEMIGWIALGQNSSGEEEQDHWEEMKETKGQQICRWHTLLES
Protein: Speedy protein E4A (Rapid inducer of G2/M progression in oocytes E4A) (RINGO E4A) (mSpy/Ringo E4A) (Q5IBH6)
Organism: Mus musculus (Mouse)
Function: Promotes progression through the cell cycle via binding and activation of CDK1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5MJ70}.
Interaction partners:
- Cyclin-dependent kinase 1
- Cyclin-dependent kinase 2
- M-phase inducer phosphatase 3
Sequence:
MGEGTPGVDSARVQEEGGRDQSLGFVEGRIQVGRIVTAGQLSLCSEEQSPQPGITRPSPGVVVDGESSGLAEPRVEATPQPPSSIQKRKRDESLDSEDDLAELFEPDPQPVWSVEMLCGLRMRLKRRRVSTVRPEHHKVFTKLLEDPVVKKFLTWDKMLRVSDKYLLSMVIAYFSRAGLFSWQYRPIHFFLALYLANDMEEDNQAPKQDIFYFLYGKSYAQRPMFHKLRFQFIRSMGWKIWVSREECEEIQAYNPDLWVWARDRTNLT
Protein: Gastrin-releasing peptide receptor isoform A (X5D7H2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASRYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHSTGRSTTCMTSLKSTNPSVATFSLINGNICHERYV
Protein: Endoplasmic reticulum junction formation protein lunapark (ER junction formation factor lunapark) (P38878)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in tubular endoplasmic reticulum network formation and maintenance. Works in conjunction with the ER shaping proteins (reticulons RTN1 and RTN2, YOP1), and in antagonism to SEY1 to maintain the network in a dynamic equilibrium. May counterbalance SEY1-directed polygon formation by promoting polygon loss through ring closure.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22729086}; Multi-pass membrane protein {ECO:0000269|PubMed:22729086}. Note=Localizes to three-way ER tubule junctions. This localization is SEY1-dependent.
Interaction partners:
- Protein SEY1
- Reticulon-like protein 1
- Reticulon-like protein 2
- Protein YOP1
Sequence:
MFSALGKWVRGSRNDKDFVTKYTADLSQITSQIHQLDVALKKSQSILSQWQSNLTFYGIALTVLALSYTYWEYHGYRPYLVVTALLCIGSLILFKWALTKLYAFYNNNRLRKLAKLRAIHQKKLEKLKEETHYNATSSIIQRFSSGEDQNDDAMVLLDDELNAKYQELNNLKTELEKFKKESHVKGLKKEDSDAWFDKIISVLAGGNELDSTSSLSPFKKIICPQCHWKSNCYRLASKPIIFICPHCNHKIDEVKEREDAIEAKQPAQPSQSEKEKTK
Protein: Pogo transposable element derived with KRAB domain (Q5TIJ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MESTAYPLNLSLKEEEEEEEIQSRELEDGPADMQKVRICSEGGWVPALFDEVAIYFSDEEWEVLTEQQKALYREVMRMNYETVLSLEFPFPKPDMITRLEGEEESQNSDEWQLQGGTSAENEESDVKPPDWPNPMNATSQFPQPQHFDSFGLRLPRDITELPEWSEGYPFYMAMGFPGYDLSADDIAGKFQFSRGMRRSYDAGFKLMVV
Protein: AP-2 complex subunit mu (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (Mu2-adaptin) (Plasma membrane adaptor AP-2 50 kDa protein) (Protein dumpy-23) (P35603)
Organism: Caenorhabditis elegans
Function: Component of the adapter complexes which link clathrin to receptors in coated vesicles (By similarity). Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration (By similarity). AP50 is a subunit of the plasma membrane adapter (By similarity). Essential wnt/egl-20 signaling protein that functions in wnt/egl-20-producing cells. Required for the AP-2 complex-mediated endocytosis of membrane proteins including wntless homolog mig-14 in egl-20-producing cells. During development, regulates the migration of HSN neurons and the left and right Q neuroblasts (QL and QR, respectively) and their descendants, possibly through hox gene and wnt/egl-20 gene target mab-5, and plays a role in establishing ALM and PLM neuronal cell polarity. Regulates AWB sensory neuron cilia membrane expansion during development, potentially via localization of tub-1 and PtdIns(4,5)P2 to the ciliary base. Required for the asymmetric divisions of V5 cells.
Subcellular location: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Interaction partners:
- AP complex subunit sigma
- AP complex subunit beta
- AP-2 complex subunit alpha
- Probable clathrin heavy chain 1
- NECAP PHear domain-containing protein
- FCH domain only protein 2
- AP-1 complex subunit gamma
- Serine/threonine-protein kinase sel-5
- AP-3 complex subunit delta
- Phosphatidylinositol-binding clathrin assembly protein unc-11
Sequence:
MIGGLFVYNHKGEVLISRIYRDDVTRNAVDAFRVNVIHARQQVRSPVTNMARTSFFHVKRGNVWICAVTRQNVNAAMVFEFLKRFADTMQSYFGKLNEENVKNNFVLIYELLDEILDFGYPQNTDPGVLKTFITQQGVRTADAPVPVTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVIEYVNLLMNQQGQVLSAHVAGKVAMKSYLSGMPECKFGINDKITIEGKSKPGSDDPNKASRAAVAIDDCQFHQCVKLTKFETEHAISFIPPDGEYELMRYRTTKDIQLPFRVIPLVREVSRNKMEVKVVVKSNFKPSLLAQKLEVRIPTPPNTSGVQLICMKGKAKYKAGENAIVWKIKRMAGMKESQISAEIDLLSTGNVEKKKWNRPPVSMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGLYETRC
Protein: Keratin-associated protein 13-4 (Q3LI77)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MSYNCCSRNFSSRSFGGYLYYPGSYPSSLVYSTALCSPSTCQLRSSLYRDCQKTCWEPASCQKSCYRPRTSILCCPCQTTCSGSLGFRSSSCRSQGYGSRCCYSLGNGSSGFRFLKYGGCGFPSLSYGSRFCYPNYLASGAWQSSCYRPICGSRFYQFTC
Protein: dolichyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.18) (Q9XZ53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- GH11935p
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- DSec61alpha
- Mannosyl-oligosaccharide glucosidase
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
Sequence:
MNRTPKMLNSKVAGYSSLITFAILLIAWLAGFSSRLFAVIRFESIIHEFDPWFNYRATAYMVQNGWYNFLNWFDERAWYPLGRIVGGTVYPGLMITSGGIHWLLHVLNIPVHIRDICVFLAPIFSGLTSISTYLLTKELWSAGAGLFAASFIAIVPGYISRSVAGSYDNEGIAIFALQFTYFLWVRSVKTGSVFWSAAAALSYFYMVSAWGGYVFIINLIPLHVFVLLIMGRYSPRLLTSYSTFYILGLLFSMQIPFVGFQPIRTSEHMAALGVFVLLMAVATLRHLQSVLSRNEFRKLFIVGGLLVGVGVFVAVVVLTMLGVVAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWFSFFFDLHILVCAFPVGVWYCIKQINDERVFVVLYAISAVYFAGVMVRLMLTLTPVVCMLAGVAFSGLLDVFLQEDSSKRMGTAISAATEVDEAEDSIEKKTLYDKAGKLKHRTKHDAQQDTGVSSNLKSIVILAVLMLLMMFAVHCTWVTSNAYSSPSIVLAFHNSQDGSRNILDDFREAYYWLSQNTADDARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSTEEKSYEIMTSLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIKESDYFTDRGEFRVDAEGAPALLNCLMYKLSYYRFGELKLDYRGPSGYDRTRNAVIGNKDFDLTYLEEAYTTEHWLVRIYRVKKPHEFNRPSLKTKERTIPPANFISRKNSKRRKGYIRNRPVVVKGKRTLK
Protein: Protein E7 (P06933)
Organism: Bovine papillomavirus type 1
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04004}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04004}. Note=Predominantly found in the host nucleus. {ECO:0000255|HAMAP-Rule:MF_04004}.
Interaction partners:
Sequence:
MVQGPNTHRNLDDSPAGPLLILSPCAGTPTRSPAAPDAPDFRLPCHFGRPTRKRGPTTPPLSSPGKLCATGPRRVYSVTVCCGNCGKELTFAVKTSSTSLLGFEHLLNSDLDLLCPRCESRERHGKR
Protein: 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) (Q97R25)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
Interaction partners:
Sequence:
MSYQDLKKCKIITAFITPFHEDGSINFDAIPALIEHLLAHHTDGILLAGTTAESPTLTHDEELELFAAVQKVVNGRVPLIAGVGTNDTRDSIEFVKEVAEFGGFAAGLAIVPYYNKPSQEGMYQHFKTIADASDLPIIIYNIPGRVVVELTPETMLRLADHPNIIGVKECTSLANMAYLIEHKPEEFLIYTGEDGDAFHAMNLGADGVISVASHTNGDEMHEMFTAIAESDMKKAAAIQRKFIPKVNALFSYPSPAPVKAILNYMGFEAGPTRLPLVPAPEEDAKRIIKVVVDGDYEATKATVTGVLRPDY
Protein: RAB6-interacting golgin (N-terminal kinase-like-binding protein 1) (NTKL-BP1) (NTKL-binding protein 1) (hNTKL-BP1) (SCY1-like 1-binding protein 1) (SCYL1-BP1) (SCYL1-binding protein 1) (Q5T7V8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15781263}. Golgi apparatus {ECO:0000269|PubMed:18997784}.
Interaction partners:
- N-terminal kinase-like protein
- Ras-related protein Rab-6A
- RING finger and CHY zinc finger domain-containing protein 1
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- ADP-ribosylation factor 5
- V-type proton ATPase 116 kDa subunit a 2
Sequence:
MAQGWAGFSEEELRRLKQTKDPFEPQRRLPAKKSRQQLQREKALVEQSQKLGLQDGSTSLLPEQLLSAPKQRVNVQKPPFSSPTLPSHFTLTSPVGDGQPQGIESQPKELGLENSHDGHNNVEILPPKPDCKLEKKKVELQEKSRWEVLQQEQRLMEEKNKRKKALLAKAIAERSKRTQAETMKLKRIQKELQALDDMVSADIGILRNRIDQASLDYSYARKRFDRAEAEYIAAKLDIQRKTEIKEQLTEHLCTIIQQNELRKAKKLEELMQQLDVEADEETLELEVEVERLLHEQEVESRRPVVRLERPFQPAEESVTLEFAKENRKCQEQAVSPKVDDQCGNSSSIPFLSPNCPNQEGNDISAALAT
Protein: Chromosome 20 open reading frame 129 (Family with sequence similarity 83 member D) (A0A087WXK8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARACLIQRLPIKRDCTPVFVRGLSSPSAAMALLSEGLDEVPAACLSPCGPPNPTELFSESRRLALEELVAGGPEAFAAFLRRERLARFLNPDEVHAILRAAERPGEEGAAAAAAAEDSFGSSHDCSSGTYFPEQSDLEPPLLELGWPAFYQGAYRGATRVETHFQPRGAGEGGPYGCKDALRQQLRSAREVIAVVMDVFTDIDIFRDLQEICRKQGVAVYILLDQALLSQFLDMCMDLKVHPEQEKLMTVRTITGNIYYARSGTKIIGKVHEKFTLIDGIRVATGSYSFTWTDGKLNSSNLVILSGQVVEHFDLEFRILYAQSKPISPKLLSHFQSSNKFDHLTNRKPQSKELTLGNLLRMRLARLSSTPRKADLDPEMPAEGKAERKPHDCESSTVSEEDYFSSHRDELQSRKAIDAATQTEPGEEMPGLSVSEVGTQTSITTACAGTQTAVITRIASSQTTIWSRSTTTQTDMDENILFPRGTQSTEGSPVSKMSVSRSSSLKSSSSVSSQGSVASSTGSPASIRTTDFHNPGYPKYLGTPHLELYLSDSLRNLNKERQFHFAGIRSRLNHMLAMLSRRTLFTENHLGLHSGNFSRVNLLAVRDVALYPSYQ
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) (Q3UI43)
Organism: Mus musculus (Mouse)
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:0000250|UniProtKB:Q9NWV8}. Nucleus {ECO:0000250|UniProtKB:Q9NWV8}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NWV8}.
Interaction partners:
- Lys-63-specific deubiquitinase BRCC36
- Breast cancer type 1 susceptibility protein homolog
- BRCA1-A complex subunit Abraxas 1
- BRCA1-A complex subunit RAP80
- BRISC complex subunit Abraxas 2
- BRISC and BRCA1-A complex member 2
- BRCA1-associated RING domain protein 1
- Lys-63-specific deubiquitinase BRCC36-like
- Serine hydroxymethyltransferase, mitochondrial
- E3 ubiquitin-protein ligase RNF8
Sequence:
MEVAEANSPTEEEEEEEEEGEETISEPRPHTRSNPEGAEDRALGAQASVGSRSEGEGEAATADGGAASVPGAGPKPWQVPASASEVQIRTPRVNCPEKVIICLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIVYIHNGTEEKEEDMSWKDMFAFMGSLDTKGASYKYEVALAGPALELHNCMAKLLAHPLQRPCQTHASYSLLEEDEEAGEEEATV
Protein: Proteasome subunit alpha 2 (20S proteasome alpha subunit 2) (Proteasome core protein PsmA 2) (Q9V2V5)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta-alpha2 proteasome is able to cleave oligopeptides after Tyr and thus displays chymotrypsin-like activity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
- Proteasome subunit beta
- Proteasome-activating nucleotidase 1
- Proteasome subunit alpha 1
- Proteasome-activating nucleotidase 2
- Glycerol kinase
- Probable metalloprotease HVO_1016
- Desampylase
- MOSC domain protein
- Large ribosomal subunit protein eL40
- Large ribosomal subunit protein eL15
Sequence:
MNRNDKQAYDRGTSLFSPDGRIYQVEYAREAVKRGAPVLGVRTADGVVLAALRSTPSELMEAESIEKLHKLDDALGAATAGHVADARKLVDFARTTAQREHLRYGEPIGVETLTKTITDNIQESTQSGGTRPYGASLLIGGVENGSGRLFATDPSGTPQEWKAVAIGGHREDVQAALEDGYAEDLSLEDGLALAVEALVAADEEIESDELNLVTVSEAGYEIVDEETIAELFADATADDESDETDEREE
Protein: Hypothetical alanine arginine proline rich protein (O05880)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MMASNQTAAQHSSATLQQAPRSIDDAGGCPLTISPIANSPGDTFAVTPVVEYEPPPRNIPPCGQSSHAARRPHTPQLARRQPIRPSGRAPAAVTSTAKSPRLRQAGTFADAALRRVLEVIDRRRPVGQLRPLLAPGLVDSVLAVSRTAAGHQQGAAMLRRIRLTPAGPDTADTAAEVFGTYSRGDRIHAIACRVEQRPAGNETRWLMVALHIG
Protein: Insulin gene enhancer protein ISL-2 (Islet-2) (P53410)
Organism: Gallus gallus (Chicken)
Function: Transcriptional factor that defines subclasses of motoneurons that segregate into columns in the spinal cord and select distinct axon pathways. Acts in conjunction with LIM-1, LIM-3 and ISL-1.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox domain-containing protein.
- Uncharacterized protein.
- POU domain, class 4, transcription factor 1
- LIM/homeobox protein Lhx3
- Visual system homeobox 2
- Oligodendrocyte transcription factor 2
- LIM homeobox 4.
Sequence:
FLLRVSPDLEWHVACLKCAECGQPLDETCTCFLRDGKAYCKRDYGRLFGIKCAQCRAAFSSSDLVMRARDHVYHLECFRCAACGRQLLPGDQFCLRERDLLCRADHGPPPDGAAARGPRSPAPPPAHLAEPVPGRPPGPRPQSHKAAEKTTRVRTVLNEKQLHTLRTCYAANPRPDALMKEQLVEMTGLSPRVIRVWFQNKRCKDKKKSILMKQLQQQQHSDKTSLQGLTGTPLVAGSPVRHESAVQGSAVEVQTYQPPWKALSDFALQSDLEPPAAFQQLVSFSESGSLGTSSGSDVTSLSSQLPDTPNSMVPSPAET
Protein: Cep170-like protein (CEP170 pseudogene 1) (Q96L14)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPTSSSFKHRIKEQEDYIRDWTAHREEIARISQDLALIAREINDVAGEIDSVTSSGTAPSTTLVDRVFDESLNFQKIPPLVHSKTPEGNNGRSGDPRPQAAEPPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSKKIRQSIDKTAGKIRILFKDKDRNWDDIESKLRAESEVPIVKTSSMEISSILQELKRVEKQLQAINAMIDPDGTLEALNNMGFPSAMLPSPPKQKSSPVNNHHSPGQTPTLGQPEARALHPAAVSAAAEFENAESEADFSIHFNRVNPDGEEEDVTVHK
Protein: Serine/threonine-protein kinase receptor (EC 2.7.11.30) (Q24229)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
Interaction partners:
Sequence:
MSKYDLLYLTAHVTLVCCLIGIHGSILPGSHGIIECEHFDEKMCNTTQQCETRIEHCKMEADKFPSCYVLWSVNETTGILRIKMKGCFTDMHECNQTECVTSAEPRQGNIHFCCCKGSRCNSNQKYIKSTTEATTQVPKEKTQDGSNLIYIYIGTSVFSVLMVIVGMGLLLYRRRKQAHFNEIPTHEAEITNSSPLLSNRPIQLLEQKASGRFGDVWQAKLNNQDVAVKIFRMQEKESWTTEHDIYKLPRMRHPNILEFLGVEKHMDKPEYWLISTYQHNGSLCDYLKSHTISWPELCRIAESMANGLAHLHEEIPASKTDGLKPSIAHRDFKSKNVLLKSDLTACIADFGLAMIFQPGKPCGDTHGQVGTRRYMAPEVLEGAINFNRDAFLRIDVYACGLVLWEMVSRCDFAGPVGEFQLPFEAELGLRPSLDEVQESVVMKKLRPRLLNSWRAHPGLNVFCDTMEECWDHDAEARLSSSCVMERFAQLNKYPSTQLLIKNHTNIDDAKESTNCL
Protein: Uncharacterized protein C17G8.02 (Q10314)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MTNTIDSFQKGSALENYNIWIDCDPGHDDVVALTLAACAGHCKILGVSTVHGNTTLEFTTKNALAVMELLNQDVDVHAGAAKPLMRESAFATHIHGTNGLAGISLLPDYPKKKATPDAVFAMYTTISNYPEPVTLVATGPLTNIALLLATYPSVTDNIERFIFMGGSTGIGNITSQAEFNVYADPEAARLVLETKSLIGKLFMVPLDVTHKVLLDANIIQLLRQHSNPFSSTLVELMTVFQQTYENVYGIRNGVPVHDVCAVALALWPSLWTSRSMYVTVSLDSLTLGRTVCDVWSQQNQYPANVHVVLEADVSLFWETFIGVIDRLNYL
Protein: UNC-76 (Q7JL62)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEAADLRVPDIPLASCDDDDIDSNKNLSNHSSDEKHHCNSNSDEERLHDEFSGSLEDLVGNFDEKIAACLKDHEVTTADIAPVQIRTQEEVMNESQTWWTLTGNFGNIQPLDFGTSSICKKMAAALDSDSLKDDASTRRSMTNSDDEDLLRQQMDVHQMIGHHHGSTDTGGETPPQTADQVIEEIDEMLQSCDFTGSMMTDRTMESVDSMYSSMRSPFPSSIQSSDADIKLRSAQALVSNPDNLQELSYSKLVTLCAEMEQLIRVYNESLVDELAHRDELDYEKEMKNSFISLLLAIQNKRRVYANDRKRKVGKASDASQLPQYLTATIPYNDHQHIDNASIASLIKILRAIHDDNTTVPTLLTDYILTHVCPKNISC