wanglab/gogpt-training-data huggingface dataset:
Protein: ATP synthase mitochondrial F1 complex assembly factor 2 (Q91YY4)
Organism: Mus musculus (Mouse)
Function: May play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8N5M1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N5M1}.
Interaction partners:
- ATP synthase F
- ATP synthase mitochondrial F1 complex assembly factor 1
- ATP synthase F
- Transmembrane protein 70
- ATP synthase F
Sequence:
MWRIYPRLRDRWRGLLDRRLSDPTVSVWPGPAPQPPARAYVPPTERKRFYQNVSISQGEGGFEINLDHRKLKTPQAKLFTVPSEALAIAVATEWDSQQDTIKFYTMHLTTLCNTSLDNPTQRSKDQLIRAAVKFLDTDTICYRVEEPETLVELQKNEWDPVIEWAEKRYGMEIGSSTSIMGPSIPTQTREVLTSHLSSYNMWALQGIEFVVAQLKSMLLTLGLIDLRLTVEQAVLLSRLEEEYQIQKWGNIEWAHDYELQELRARTAAGTLFVHLCSESSTVKHKLLQE
Protein: Proteasome subunit alpha type-3 (Macropain subunit C8) (Multicatalytic endopeptidase complex subunit C8) (Proteasome component C8) (Proteasome subunit K) (Proteasome subunit alpha-7) (alpha-7) (O70435)
Organism: Mus musculus (Mouse)
Function: 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). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P25788}. Nucleus {ECO:0000250|UniProtKB:P25788}. 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:P25788}.
Interaction partners:
- Proteasome subunit beta type-10
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-9
- Proteasome subunit beta type-7
- Proteasome subunit beta type-3
- Proteasome subunit beta type-5
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
Sequence:
MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSANDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDVVKEVAKIIYIVHDEVKDKAFELELSWVGELTKGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM
Protein: Chorismate mutase (CM) (EC 5.4.99.5) (Monofunctional chorismate mutase AroQ(f)) (Q57696)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the conversion of chorismate into prephenate via a Claisen rearrangement.
Interaction partners:
- Small ribosomal subunit protein eS17
- 4-hydroxy-tetrahydrodipicolinate synthase
- Chorismate synthase
- Probable arogenate/prephenate dehydrogenase
- Elongation factor 1-beta
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein eS6
- Prephenate dehydratase
- Large ribosomal subunit protein eL37
- Small ribosomal subunit protein uS3
Sequence:
MIEKLAEIRKKIDEIDNKILKLIAERNSLAKDVAEIKNQLGIPINDPEREKYIYDRIRKLCKEHNVDENIGIKIFQILIEHNKALQKQYLEETQNKNKK
Protein: Target of Nesh-SH3 variant 3 (Q59IW8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLSSLGCLLLCGSIALALGNAQKLPKGKKPSLKVHINTTSDSILLKFLRPNANVKLEGFLLGYGSNVSPNQYFPLPTEGKFTEAVVDAEPKYLIVVRPAPPPSQKKSCSGKSRPRKPLQLVVGTLTPSSVFLSWGFLINPHHDWTLPSHCPSDRFYTIRYREKDKEKKWIFQLCPATETIVENLKPNTVYEFGVKDNIEGGIWSKIFNHKTIVGSKNKVNGKIQSTYDQVHSVPVPRKLIPLTIIKQVIQNVTHRASTKSPDKTPFGGTILVHQIIPGLNESTVKLPTSIMLEISDALKAQLAKNETLALPAESKTPEVEKLAGQPVTVTPESVSRSTKPTLSSALDTAETALAPRQTTSMPPKLKTPHSRMPAKEPVPKEPLHTTSKPKMPPSPEVADTTSAPLETRGIPLIPVISPRPSQEELQTAMEETDQSTQELFTTKIPRTTELAKTTQAPHRLHTAPVRPRIPGRPHGRPALNKTTTRPDKTKPRGTSHKNGVGTGTKQAPKPPSPGRNASVDSHATRKPGSVSGTRRPPIPHRHSSTRPVSPERRPLPPNNVTGKPGRAGIVSSSRVTSPPLKATLHPIGTATARPGAEQKEPTAPASEEEFGTTTDFSSSPTKETDPLGKPRFIGPHVRYIPKPENKPCSITDSVRRFPTEEATEGNATSPPQNPPTNLTVVTVEGCPSFVILDWEKPLNDTVTEYEVISRENGSFSGKNKSIQITNQTFSTVENLKPDTSYEFQVKPKNPLGEGPASNTVAFSTESADPRVSEPISAGRDAIWTERPFNSDSYSECKGKQYVKRTWYKKFVGVQLCNSLRYKIYLSDSLTGKFYNIGDQRGHGEDHCQFVDSFLDGRTGQQLTSEQLPTKEGYFRAVRQEPVQFGEIGGHTQINYVQWYECGTTIPGKW
Protein: Macrophage receptor MARCO (Macrophage receptor with collagenous structure) (Scavenger receptor class A member 2) (Q9UEW3)
Organism: Homo sapiens (Human)
Function: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria. Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9468508}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Toll-like receptor 2
- Secretoglobin family 3A member 2
Sequence:
MRNKKILKEDELLSETQQAAFHQIAMEPFEINVPKPKRRNGVNFSLAVVVIYLILLTAGAGLLVVQVLNLQARLRVLEMYFLNDTLAAEDSPSFSLLQSAHPGEHLAQGASRLQVLQAQLTWVRVSHEHLLQRVDNFTQNPGMFRIKGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENSVSVRIVGSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYKVGAGTGQIWLDNVQCRGTESTLWSCTKNSWGHHDCSHEEDAGVECSV
Protein: 5,7-dihydroxy-2-methylchromone synthase (EC 2.3.1.216) (Pentaketide chromone synthase) (PCS) (Q58VP7)
Organism: Aloe arborescens (Kidachi aloe)
Function: Catalyzes the iterative condensations of 5 molecules of malonyl-CoA to produce a pentaketide 5,7-dihydroxy-2-methylchromone.
Interaction partners:
Sequence:
MSSLSNSLPLMEDVQGIRKAQKADGTATVMAIGTAHPPHIFPQDTYADVYFRATNSEHKVELKKKFDHICKKTMIGKRYFNYDEEFLKKYPNITSYDEPSLNDRQDICVPGVPALGTEAAVKAIEEWGRPKSEITHLVFCTSCGVDMPSADFQCAKLLGLHANVNKYCIYMQGCYAGGTVMRYAKDLAENNRGARVLVVCAELTIMMLRAPNETHLDNAIGISLFGDGAAALIIGSDPIIGVEKPMFEIVCTKQTVIPNTEDVIHLHLRETGMMFYLSKGSPMTISNNVEACLIDVFKSVGITPPEDWNSLFWIPHPGGRAILDQVEAKLKLRPEKFRAARTVLWDYGNMVSASVGYILDEMRRKSAAKGLETYGEGLEWGVLLGFGPGITVETILLHSLPLM
Protein: IML2-like protein YKR018C (P36114)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MFKVFGFGAKEEIPELSQEEKTKAILKQAHDFEQALRAMDYVLDDNADEGLALLDESDAKEASDQTINALARGVIEFLEATLGFEAEEMKKASATLAKAEALSLKSRERAQKIGLKSSSLYPPGTVYAVTYTESCLLHALLMIFSESMMEAAKAILKLRKSYYMLQEILETIKAANKAKKLKITSGSEDKESTPATFITGGDAFNSVDIPYELTPEEQKDKDLLQFAEQIHSMRTERLSGAHIGNSPAINRLRGELGLQAMEDLPEEEITDHKVLSDDIDLSQATIDEFVHSGVNLCFGILQVVISLLPPAIGAVLSVVGFRGSREEGLRLVWKATKQRNVHGCIGLLALMFYYDGPFQFTDDDFDIPAAVKDSSNSEDSEDEEMDGPTLLHPGKILEDALLQSRALFPNSALWLLNEARMLSGKGRLEEAVALMDSIDVSKIRMRQVKSLMIFDRAITLIHLHQYDRAAEDILSLLDISDWSHAFYTYFAGCCYLENWRMCEMGLMKSDKKDEYQKKAEELIFTSVNLLGKKTFKSKNLPLDRFILRKVEQFKAKKEELGVENPLDGIATSPVHEIAYFYNGYNRMSEEHLELTKKMLTEYRNPAIEALDSDQELIKDLLVSLTLRRLGHIQEGCDILDEKVLPKFFSIQNGKVKYIKKTEDPWAYPTALYERALFTWKLEGMDGLPESKEWLLRAQGYADDYELSTRVGMKIKAAIDRVDHSL
Protein: COMM domain-containing protein 4 (Q9H0A8)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. Down-regulates activation of NF-kappa-B.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21778237}. Nucleus {ECO:0000269|PubMed:21778237}.
Interaction partners:
- COMM domain-containing protein 2
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 3
- COMM domain-containing protein 1
- COMM domain-containing protein 9
- COMM domain-containing protein 5
- COMM domain-containing protein 6
- COMM domain-containing protein 8
- COMM domain-containing protein 10
- COMM domain-containing protein 7
Sequence:
MRFRFCGDLDCPDWVLAEISTLAKMSSVKLRLLCSQVLKELLGQGIDYEKILKLTADAKFESGDVKATVAVLSFILSSAAKHSVDGESLSSELQQLGLPKEHAASLCRCYEEKQSPLQKHLRVCSLRMNRLAGVGWRVDYTLSSSLLQSVEEPMVHLRLEVAAAPGTPAQPVAMSLSADKFQVLLAELKQAQTLMSSLG
Protein: C-type natriuretic peptide (CNP) [Cleaved into: Venom peptide 1; Venom peptide 2; Venom peptide 3; Venom peptide 4; Venom peptide 5; Venom peptide 6; Venom peptide 7; Venom peptide 8; Venom peptide 9; Venom peptide 10; Venom peptide 11; C-type natriuretic peptide 39 (ovCNP-39)] (P84715)
Organism: Ornithorhynchus anatinus (Duckbill platypus)
Function: Venom component with vasorelaxant activity. In vitro stimulates the production of cGMP in rat aortic smooth muscle cells and histamine release from rat peritoneal mast cells. Induces relaxation of isolated rat uterus. Induces local edema following subplantar injection into rat hind paw. Forms voltage-dependent cation channels which are weakly selective for potassium relative to sodium, and whose conductance decreases with increasing dehydration energy of the monovalent cation. The activity of the fast cation channels is calcium dependent and is characterized by short bursts of current separated by long periods of inactivation.
Subcellular location: Secreted {ECO:0000269|PubMed:7597719, ECO:0000269|PubMed:9663691, ECO:0000269|PubMed:9827022}.
Interaction partners:
- Guanylate cyclase
- ANF_receptor domain-containing protein.
- Natriuretic peptide receptor 3
- Guanylate cyclase
- Guanylate cyclase.
- Guanylate cyclase.
- Guanylate cyclase
- Guanylate cyclase
- Uncharacterized protein.
Sequence:
MHLSHLLAWALLLTLLSLRAEAKPPSPQPQVPRSPGDEASEAVAANGGGKKGDKEPKGDRPRLLRELRLDTRSRGSRGVWTRLLHDHPNPRKYKPANKKGLSKGCFGLKLDRIGSTSGLGC
Protein: Actin-related protein 2/3 complex subunit 4 (Arp2/3 complex 20 kDa subunit) (p20-ARC) (O96625)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 3
- SPIN90/Ldb17 leucine-rich domain-containing protein
- Wiscott-Aldrich syndrome protein
- WASP-related protein
- Protein BRICK1
Sequence:
MSTAQVPYLNCIRNTLTASMCLQNFGSQIVERHNKPEVEVKTSKELVLNPVIIARNKNERVLIETSINSIRISVSIKKSDEVDVILAKKFVRFLQQRAENFIILRRKPVEGYDISFLVTNFHTENMFKHKLVDFIIQFMEDIDREISDLKLTLNARGRIVASEYLKNFA
Protein: Translocation protein sec62 (O13787)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and bip1 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to sec61 and sec62. sec62 and sec63 are required for interactions between sec61 and translocating polypeptides. sec62 may affect sec61-polypeptide interactions by increasing the affinity of targeting pathways for sec61 and/or by modifying sec61 to allow more efficient polypeptide interaction. A cycle of assembly and disassembly of Sec62/63 complex from sec61 may govern the activity of the translocon (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Translocation protein sec63
- ER protein translocation subcomplex subunit sec67
- Translocation protein sec66
- Protein transport protein sec61 subunit beta
- Protein transport protein sec61 subunit alpha
- Probable protein transport protein Sec61 subunit gamma
- Uncharacterized protein C19G7.17
- Protein transport protein sec73
- Calnexin homolog
Sequence:
MDSSNVPVLKDEDKCKFSMRFTNFLKSRPELKTKPAILNGKRVYYFRVKRVLRFLTSEAYTPKKYKGFPEISSREEAIEVLKLLIMNSMLVRVDKLPPKQRKQKLVELQINRNQDFQDDMHYVWLYEPLPKRVMALAVLFALVVLALVLFPLWPMFMRKGAWYLSMGGLGVIGLFFVLVILRFFLFCITAVIVRPGIWLFPNLLADVGFCDSFKPLWSWHNSKSEVKKTRKSKKLSKKATSPAASATPEKSSTSTTSLKNLRHRNPTVEEVSE
Protein: Tetratricopeptide repeat protein 29 (TbTTC29) (Q57ZB2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:31735292, ECO:0000269|PubMed:37934199}.
Interaction partners:
Sequence:
MASVGPVKTKTVTLKELTPPIPSPEKSACKGAKPDSNHMALVPVKPSQPGSGKLITRTRLQRDSLISQQQRDALVVSSFGIGTTRHGQPDNTTSSIKDGFSTAAGGVNCASVVVAQSEKDSVRFHLCVDALAEGCVNTFIHLFHLSHRDPVCVDQLAQTLFTIPDEKLVWVKSQLAAVEVLRRQSEFRDVCERCQLLADYFESERDCDEAAWHYDVALRIAMESLDRPLEQEVRLSFGAFFERHKQLRKAIALFEEVYHLAMALNDVETAVEANYRLIRTYLSLSAELKDTNPKEAISFLERALDMSQRVKSSKDEADSLHALGNIYESMGDFRRALEYQKRFFEVARAANLVEREKRASLCVASMQERMNMTDEAVHSLQCALELSEKAADIEGVYRATMQLGQAYDSSGDHEKALMSYRANFGAARKLNNSDLTDQARVALGFALGEHYLKHAGGGRGYVPIVCDDVKAQLEWMSNGIL
Protein: DNA topoisomerase I (EC 5.6.2.1) (DNA topoisomerase 1) (E5RIC7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLDHEYTTKEVFRKNFFNDWRKEMAVEEREVIKSLDKCDFTEIHRYFVDKAAARKVLSREEKQKLKEEAEKLQQEFGYCILDGHQEKIGNFKIEPPGLFRGRGDHPKMGMLKRRITPEDVVINCSRDSKIPEPPAGHQWKEVRSDNTVTWLAAWTESVQNSIKYIMLNPCSKLKGETAWQKFETARRLRGFVDEIRSQYRADWKSREMKTRQRAVALYFIDKLALRAGNEKEDGEAADTVGCCSLRVEHVQLHPEADGCQHVVEFDFLGKDCIRYYNRVPVEKPVYKNLQLFMENKDPRDDLFDRLTVSWDGPAKPRNYRDHFPPQTTSLNKHLQELMDGLTAKVFRTYNASITLQEQLRALTRAEDSIAAKILSY
Protein: Radial spoke head protein 4 homolog A (Radial spoke head-like protein 3) (Q8BYM7)
Organism: Mus musculus (Mouse)
Function: Component of the axonemal radial spoke head which plays an important role in ciliary motility. Essential for triplet radial spokes (RS1, RS2 and RS3) head assembly in the motile cilia.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:32203505, ECO:0000269|PubMed:34871179}.
Interaction partners:
- Radial spoke head protein 9 homolog
- Radial spoke head 1 homolog
- Dynein axonemal intermediate chain 1
- Radial spoke head protein 3 homolog B
- Dynein axonemal heavy chain 5
- Dynein axonemal intermediate chain 2
- E3 SUMO-protein ligase RanBP2
- Coiled-coil domain-containing protein 39
- Outer dynein arm-docking complex subunit 1
- Dynein axonemal assembly factor 1
Sequence:
MENSTSLKQEKENQEPGEAERLWQGESDVSPQEPGPPSPEYREEEQRTDTEPAPRMSPSWSHQSRVSLSTGDLTAGPEVSSSPPPPPLQFHSTPLNTETTQDPVAASPTEKTANGIADTGTPYSDPWESSSAAKQSTSHYTSHAEESTFPQSQTPQPDLCGLRDASRNKSKHKGLRFDLLQEEGSDSNCDPDQPEVGASEAAQSMLEVAIQNAKAYLLSTSSKSGLNLYDHLSKVLTKILDERPADAVDIIENISQDVKMAHFNKKLDTLHNEYEMLPAYEIAETQKALFLQGHLEGADSELEEEMAESSLPNVMESAYYFEQAGVGLGTDETYRVFLALKQLTDTHPIQRCRFWGKILGLEMNYIVAEVEFRDGEDEEEVEEEGIAEERDNGGSEAGEEEEEELPKSLYKAPQVIPKEESRTGANKYVYFVCNVPGRPWVRLPSVTPAQIVTARKIKKFFTGRLDAAVISYPPFPGNESNYLRAQIARISAGTHVSPLGFYQFGEEEGEEEEVEGGRDSYEENPDFEGIQVIDLVESLSNWVHHVQYILPQGRCNWFNPIQKDEDEEEEEEEDEEKGEEPDYIEQEVGPPLLTPISEDLGIQNIPSWTTQLSSNLIPQYAIAVLRSNLWPGAYAFSNGKKFENFYIGWGHKYCVENYTPPSPPPVYQEYPSGPEITEMNDPSVEEEQAFRMTQEPVALSTEENEGTEDEDEDDED
Protein: G protein-coupled receptor kinase (EC 2.7.11.-) (A0A2R8QPB8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Presynapse {ECO:0000256|ARBA:ARBA00034106}.
Interaction partners:
- Protein smoothened
- Beta-arrestin-1
- Arrb2b protein
- Arrestin, beta 2a.
- non-specific serine/threonine protein kinase
- Casein kinase I isoform gamma-1
- non-specific serine/threonine protein kinase
- Casein kinase I isoform delta-B
- Casein kinase I isoform delta-A
- non-specific serine/threonine protein kinase
Sequence:
MADLEAVLADVSYLMAMEKSKSTPAARASKKIILPEPSIRSVMQKYLEERDELAFDKIFNQKIGFLLFKDFCMNEIDEAVPQLKFYEEIKEYEKLDSEEERLTRSRQIYDVYIMKELLSCSHPFSKKAVDHVQTHLAKKQVPPNLFQPYIVEICDSLRGNIFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNGGDLHYHLSQHGVFSEKDMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMNVELPDSFTPELKSLLEGLLQRDVAKRLGCLGRGASEVKEHVFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYKNFPLVISERWQQEVAETVYEAVNSDTDKNEARKRAKNKQQGHEEDYALGKDCIMHGYMLKLGNPFLTQWQRRYFYLFPNRVEWRGEGESRECWTKTLKKHKFKQNLLTMEHIVTVEETQIKDKKCILLRVKGGKQFVLQCESDPEFVQWKKELTEAFTEAQKLLRRAPKVIGKGRTNVVELSKPPLTHRNSNGL
Protein: Keratin-associated protein 4-6 (Keratin-associated protein 4-15) (Keratin-associated protein 4.15) (Keratin-associated protein 4.6) (Ultrahigh sulfur keratin-associated protein 4.15) (Q9BYQ5)
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:
MVSSCCGSVCSDQGCGLETCCRPSCCQTTCCRTTCCRPSCCVSSCCRPQCCQSVCCQPTCCRPSCCPSCCQTTCCRTTCCRPSCCVSSCCRPQCCQSVCCQPTCCRPSCSISSCCRPSCCVSRCCRSQCCQSVCCQPTCCRPSCCISSCCRPSCCESSCCRPCCCRPCCCLRPVCGRVSCHTTCYRPTCVISTCPRPLCCASSCC
Protein: Sorcin (A0A8I5ZWU9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MHCGGAPGGPVFPGHTQDPLYGYFAAVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFSEFRELWTVLSGWRQHFISFDSDRSGTVDPQELQKALTTMGFRLSPQTVNSVAKRYSTSGKITFDDYIACCVKLRALTDSFRRRDSGQQGVVNFSYDDFIQCVMTV
Protein: Arginyl-tRNA--protein transferase 1 (Arginyltransferase 1) (R-transferase 1) (EC 2.3.2.8) (Arginine-tRNA--protein transferase 1) (O14133)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31B fusion protein
- Enolase-phosphatase E1
- Probable UDP-N-acetylglucosamine pyrophosphorylase
- Bax inhibitor 1
- Putative enoyl reductase C646.07c
Sequence:
MVLDKLLYTGYNVSTECGYCKSGRKTEHFGLLAEKLSCEDYQRLIDLGWRRSGHYLYKPNGKTSCCSLYTIRLDSYNFKIAKEQKKAIKKWVKYVNGKPLKPMKSEISTDYLNNAFQTIESLGAEKYSVTMEPCTYTDEKFEVFKKYQMQVHLEKEEEITKKGFSRFLCNSPLFNEDKGIKYGSYHQMYRFQGRLVAVGVLDLLPHGVSSVYLFYDPDMSKFSLGRISACREIWLALECGYRYYYMGYYIHTCPKMKYKATYSPSYLLNPGTNKWIPIENFTSLWNTGAPKYISFGDENNSDIQTAVDYDSSEDSSQNEDDYTLFNRQLPGILSVNVAESLVSENFANIGNSTFPTRHVLSYFPQVKHWFVEINAAVGEEVAKSYTLVLSS
Protein: DNA-binding transcriptional regulator NtrC (Nitrogen regulation protein NR(I)) (Nitrogen regulator I) (NRI) (P03029)
Organism: Klebsiella pneumoniae
Function: Member of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. Phosphorylated NtrC binds directly to DNA and stimulates the formation of open promoter-sigma54-RNA polymerase complexes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0AFB8}.
Interaction partners:
Sequence:
MQRGIAWIVDDDSSIRWVLERALTGAGLSCTTFESGNEVLDALTTKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVDRAISHYQEQQQPRNAPINSPTADIIGEAPAMQDVFRIIGRLSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTVRQGRFEQADGGTLFLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLELRVQEGKFREDLFHRLNVIRVHLPPLRERREDIPRLARHFLQIAARELGVEAKQLHPETEMALTRLAWPGNVRQLENTCRWLTVMAAGQEVLTQDLPSELFETAIPDNPTQMLPDSWATLLGQWADRALRSGHQNLLSEAQPEMERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME
Protein: Homeobox protein notochord (A8MTQ0)
Organism: Homo sapiens (Human)
Function: Transcription regulator acting downstream of both FOXA2 and Brachyury (T) during notochord development. Required for node morphogenesis. Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning; acts upstream of FOXJ1 and RFX3 in this process and is required for the expression of various components important for axonemal assembly and function. Plays a role in regulating axial versus paraxial cell fate. Activates the transcription of ciliary proteins C11orf97 homolog, FAM183B and SPACA9 in the embryonic ventral node (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Hepatocyte nuclear factor 3-beta
- T-box transcription factor T
- Putative solute carrier family 19 member 4
- Hepatocyte nuclear factor 3-alpha
- Transcriptional enhancer factor TEF-4
- Transcriptional coactivator YAP1
Sequence:
MPSPRPRGSPPPAPSGSRVRPPRSGRSPAPRSPTGPNTPRAPGRFESPFSVEAILARPDPCAPAASQPSGSACVHPAFWTAASLCATGGLPWACPTSWLPAYLSVGFYPVPGPRVAPVCGLLGFGVTGLELAHCSGLWAFPDWAPTEDLQDTERQQKRVRTMFNLEQLEELEKVFAKQHNLVGKKRAQLAARLKLTENQVRVWFQNRRVKYQKQQKLRAAVTSAEAASLDEPSSSSIASIQSDDAESGVDG
Protein: Adenosine transporter 2 (Q586N5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Heat shock 70 kDa protein, putative
Sequence:
MAMLGFESTAEFFVYLTFIFFGMSVMNVTNAIYSNYDYFSEYYKFAQRNADAISSNPSFWKHMFTYYNVVVFTMQVLLEAFMLTPLGRRIPISWRLIFGLTIPMVEIIVILVIPEVGGSEDGAIATMMIVAFVGGISKTLCDSSNAALAGPFPTKFYGAIVWGLAVSGLMTSFMSIVIKASMDSSFESKRVQSQIYFGLVMLLQVVACVLLVLLRKNPYAIKYAAEFRYAARKDGATGEEDDTDFKGRGPADENRYPDEKDDKNVLNADIDPDKMKDTDQVEGTTNAQQMLDASVMVVVKRIWPMLLSCFFVFFATLLVFPGVFFAVKGSMDLNNFWYFPVAIAMFNLGDFLSRLVLQFKQLHVSPRMVLIGSFARALLIIPLSLCVSGAIPGVGVPFTVSLLWGLTNGYFGGLSMIYGPRTGSLTTAGQRSLAAICINVALLMGLFAGAMFALAVKEGLPK
Protein: Hypocretin neuropeptide precursor (Hypocretin) (Orexin precursor) (Prepro-orexin) (Preprohypocretin) (Q0PIA1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Rough endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004427}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MDCTAKKLQVLVFMALLAHLARDAEGVASCCARAPGSCKLYEMLCRAGRRNDSSVARHLVHLNNDAAVGILTLGKRKVGESRVHDRLQQLLHNSRNQAAGILTMGKRLEEPAKFLIPTVPQDVDSYEKR