wanglab/gogpt-training-data huggingface dataset:
Protein: FI21273p1 (Kinesin-like protein at 59D (EC 3.6.1.3)) (Q9W1U1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- FI06030p
- GH14206p
- AT20903p
- non-specific serine/threonine protein kinase
- inositol-phosphate phosphatase
- Kinesin-like protein Klp59C
- Kinesin-like protein Klp10A
- IP09476p
- Dynein regulatory complex protein 10
- MORN repeat-containing protein 5
Sequence:
MDRIKIGEQLLFQRSDGRVHQVVCTAKNLERDSITGEWTEGTVVKGKEVPLSTLIGINHHIFAENQPPISKPPSSLLPKPRGSSPTGGPKTHTGNPYAERMRVQDGRSKIATRKTDPAAVGAGNHELGRAHTPRVPAGRPDRDASPTQGRKSQGGNNSNQRFSSVVREVNRMKEQREKRRARQAEQLQEKDALRRNNPGNPNWEVSVMLRQYRSTLIFSPLRCLDPNGGTVQQITVCVRKRPMSRKEENSKNLDIITVPSADSLIVHELRLKVDLTKFLEHHKFRFDYTFDEECSNALVYDHTARPLIRTMFEGGNATCFAYGQTGSGKTHTMGGEFFGKVQDCGTGIYAMAARDVFEEVSRPEYRQMGAKITCSFFEIYGTKVFDLLLPNKPMLRVLEDARQQVVVVGLTEMPVTKVEDVLRLIEHGSKERTSGQTSANAKSSRSHAVFQIALHFPDSWGPHGKCSFVDLAGNERGADTQSADRQTRIEGAEINKSLLALKECIRALSRQSSHLPFRGSKLTQVLRDSFVGGKKNKTCMIAMISPSMSCVENTLNTLRYADRVKELIAKEDEHLQSVEGDGEKSPDLNEESEPEMMADEEGDEEPEDEDNQHLTISSEEASSYNNMSYDMSFNHTLNILGPSRNVDIQEVAEQHALLVENLETYAHNFRQLKTDKEIEQYTQNSESALMKLLAMVNRTRDVTHNYNTQKLLKEENQNAYKKGELDESE
Protein: Cyclin dependent kinase like 5 (A0A1B0GUM4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKIPNIGNVMNKFEILGVVGEGAYGVVLKCRHKETHEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEKNMLELLEEMPNGVPPEKVKSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGNNANYTEYVATRWYRSPELLLGAPYGKSVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPSEQMKLFYSNPRFHGLRFPAVNHPQSLERRYLGILNSVLLDLMKNLLKLDPADRYLTEQCLNHPTFQTQRLLDRSPSRSAKRKPYHVESSTLSNRNQAGKSTALQSHHRSNSKDIQNLSVGLPRADEGLPANESFLNGNLAGASLSPLHTKTYQASSQPGSTSKDLTNNNIPHLLSPKEAKSKTEFDFNIDPKPSEGPGTKYLKSNSRSQQNRHSFMESSQSKAGTLQPNEKQSRHSYIDTIPQSSRSPSYRTKAKSHGALSDSKSVSNLSEARAQIAEPSTSRYFPSSCLDLNSPTSPTPTRHSDTRTLLSPSGRNNRNEGTLDSRRTTTRHSKTMEELKLPEHMDSSHSHSLSAPHESFSYGLGYTSPFSSQQRPHRHSMYVTRDKVRAKGLDGSLSIGQGMAARANSLQLLSPQPGEQLPPEMTVARSSVKETSREGTSSFHTRQKSEGGVYHDPHSDDGTAPKENRHLYNDPVPRRVGSFYRVPSPRPDNSFHENNVSTRVSSLPSESSSGTNHSKRQPAFDPWKSPENISHSEQLKEKEKQGFFRSMKKKKKKSQTVPNSDSPDLLTLQKSIHSASTPSSRPKEWRPEKISDLQTQGLTQSLRLECSGKIMAHCSLDLLGSSHSPISASRVTGTTGTRHHTWPVF
Protein: Cell division cycle protein 27 homolog (Anaphase-promoting complex subunit 3) (APC3) (CDC27 homolog) (CDC27Hs) (H-NUC) (P30260)
Organism: Homo sapiens (Human)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Subcellular location: Nucleus {ECO:0000269|PubMed:18445686}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}.
Interaction partners:
- Cell division cycle protein 16 homolog
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 13
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 20 homolog
- G2/mitotic-specific cyclin-B1
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 16
- Anaphase-promoting complex subunit 2
Sequence:
MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSNCLPNSCTTQVPNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSAVISPDTVPLGTGTSILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQNYTNTPPVIDVPSTGAPSKKSVARIGQTGTKSVFSQSGNSREVTPILAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGITQPNINDSLEITKLDSSIISEGKISTITPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF
Protein: Protein transport protein Sec23A (SEC23-related protein A) (Q01405)
Organism: Mus musculus (Mouse)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (By similarity). Required for the translocation of insulin-induced glucose transporter SLC2A4/GLUT4 to the cell membrane.
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q15436}. Note=Enriched at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000250|UniProtKB:Q15436}.
Interaction partners:
- SEC24 homolog B, COPII coat complex component)
- Protein transport protein Sec31A
- Protein SEC13 homolog
- Protein transport protein Sec31B
- Vesicle-trafficking protein SEC22b
- Protein transport protein Sec24A
- Small COPII coat GTPase SAR1B
- SEC24 homolog C, COPII coat complex component
- SEC24 homolog D, COPII coat complex component)
- Protein transport protein Sec16A
Sequence:
MTTYLEFIQQNEERDGVRFSWNVWPSSRLEATRMVVPVAALFTPLKERPDLPPIQYEPVLCSRTTCRAVLNPLCQVDYRAKLWACNFCYQRNQFPPTYAGISELNQPAELLPQFSSIEYVVLRGPQMPLIFLYVVDTCIEDEDLQALKESMQMSLSLLPPTALVGLITFGRMVQVHELGCEGISKSYVFRGTKDLSAKQLQEMLGLSKVPVTQATRGPQVQQPPPSNRFLQPVQKIDMNLTDLLGELQRDPWPVPQGKRPLRSSGVALSIAVGLLECTFPNTGARIMMFIGGPATQGPGMVVGDELKTPIRSWHDIEKDNAKYVKKGTKHFEALANRAATTGHVIDIYACALDQTGLLEMKCCPNLTGGYMVMGDSFNTSLFKQTFQRVFTKDIHGQFKMGFGGTLEIKTSREIKISGAIGPCVSLNSKGPCVSENEIGTGGTCQWKICGLSPTTTLAIYFEVVNQHNAPIPQGGRGAVQFVTQYQHSSGQRRIRVTTIARNWADAQTQIQNIAASFDQEAAAILMARLAIYRAETEEGPDVLRWLDRQLIRLCQKFGEYHKDDPNSFRFSETFSLYPQFMFHLRRSPFLQVFNNSPDESSYYRHHFMRQDLTQSLIMIQPILYAYSFSGPPEPVLLDSSSILADRILLMDTFFQILIYHGETIAQWRKSGYQDMPEYENFRHLLQAPVDDAQEILHSRFPMPRYIDTEHGGSQARFLLSKVNPSQTHNNMYAWGQESGAPILTDDVSLQVFMDHLKKLAVSSAA
Protein: rRNA-processing protein fcf2 (O42877)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-rRNA processing and 40S ribosomal subunit assembly. Required for the early cleavage steps of 35S rRNA at the A(0), A(1), and A(2) sites (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- rRNA-processing protein fcf1
- Probable U3 small nucleolar RNA-associated protein 11
- Probable U3 small nucleolar RNA-associated protein 7
- Ribosome biogenesis protein bms1
- Protein bfr2
- Uncharacterized protein C1604.06c
- Uncharacterized protein C3B8.09
- Uncharacterized protein C18B11.06
- U3 small nucleolar ribonucleoprotein protein mpp10
- U3 small nucleolar ribonucleoprotein protein imp4
Sequence:
MTEIGLSVDLATISKLLESAKSTLQEKQASDDDKHGQQKLLTKIPKIISSSFELPSYFEKKFVMGLKKDELVENSESYINDASFEPTVPIYESHVSAPGISKKKKNIKDTAGSNWFDMPATELTESVKRDIQLLKMRNALDPKRHYRRENTKSMPKYFQVGSIVEGPQDFYSSRIPTRERKETIVDELLHDSERRSYFKKKYLELQKSKMSGRKGQYKKLQQRRKPSYLK
Protein: Myosin heavy chain type IIa (Q0GC40)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSDSEMAVFGEAAPYLRKSEKERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSKDAGKVTVKTEAGATLTVKEDQIFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCV
Protein: Probable 2' cyclic ADP-D-ribose synthase TcpB (2'cADPR synthase TcpB) (EC 3.2.2.-) (Brucella TIR-containing protein 1) (Btp1) (NAD(+) hydrolase TcpB) (EC 3.2.2.6) (TIR domain-containing protein in Brucella) (TcpB) (Q8YF53)
Organism: Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M)
Subcellular location: Secreted {ECO:0000305|PubMed:19196716}. Host cell membrane {ECO:0000269|PubMed:19196716}. Note=Translocated into the host cell via the type IV secretion system (T4SS) (Probable). Upon overexpression in HEK or HeLa cells forms tubular networks that colocalize with microtubules; nocodazole treatment decreases the thickness of the network but does not disrupt it (PubMed:19196716). {ECO:0000269|PubMed:19196716, ECO:0000305|PubMed:27311859}.
Interaction partners:
Sequence:
MSKEKQAQSKAHKAQQAISSAKSLSTQKSKMSELERATRDGAAIGKKRADIAKKIADKAKQLSSYQAKQFKADEQAVKKVAQEQKRLSDERTKHEAFIKQSLSSMRTTASATMEAEEEYDFFISHASEDKEAFVQDLVAALRDLGAKIFYDAYTLKVGDSLRRKIDQGLANSKFGIVVLSEHFFSKQWPARELDGLTAMEIGGQTRILPIWHKVSYDEVRRFSPSLADKVALNTSLKSVEEIAKELHSLI
Protein: E3 ubiquitin-protein ligase RNF216 (EC 2.3.2.27) (RING finger protein 216) (RING-type E3 ubiquitin transferase RNF216) (Triad domain-containing protein 3) (Ubiquitin-conjugating enzyme 7-interacting protein 1) (Zinc finger protein inhibiting NF-kappa-B) (Q9NWF9)
Organism: Homo sapiens (Human)
Function: Isoform 1 acts as an E3 ubiquitin ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Promotes degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of antiviral responses. Down-regulates activation of NF-kappa-B, IRF3 activation and IFNB production. Isoform 3 inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis.
Subcellular location: Cytoplasm. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:24945773}.
Interaction partners:
- Polyubiquitin-C
- Receptor-interacting serine/threonine-protein kinase 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- TNF receptor-associated factor 3
Sequence:
MEEGNNNEEVIHLNNFHCHRGQEWINLRDGPITISDSSDEERIPMLVTPAPQQHEEEDLDDDVILTEDDSEDDYGEFLDLGPPGISEFTKPSGQTEREPKPGPSHNQAANDIVNPRSEQKVIILEEGSLLYTESDPLETQNQSSEDSETELLSNLGESAALADDQAIEEDCWLDHPYFQSLNQQPREITNQVVPQERQPEAELGRLLFQHEFPGPAFPRPEPQQGGISGPSSPQPAHPLGEFEDQQLASDDEEPGPAFPMQESQEPNLENIWGQEAAEVDQELVELLVKETEARFPDVANGFIEEIIHFKNYYDLNVLCNFLLENPDYPKREDRIIINPSSSLLASQDETKLPKIDFFDYSKLTPLDQRCFIQAADLLMADFKVLSSQDIKWALHELKGHYAITRKALSDAIKKWQELSPETSGKRKKRKQMNQYSYIDFKFEQGDIKIEKRMFFLENKRRHCRSYDRRALLPAVQQEQEFYEQKIKEMAEHEDFLLALQMNEEQYQKDGQLIECRCCYGEFPFEELTQCADAHLFCKECLIRYAQEAVFGSGKLELSCMEGSCTCSFPTSELEKVLPQTILYKYYERKAEEEVAAAYADELVRCPSCSFPALLDSDVKRFSCPNPHCRKETCRKCQGLWKEHNGLTCEELAEKDDIKYRTSIEEKMTAARIRKCHKCGTGLIKSEGCNRMSCRCGAQMCYLCRVSINGYDHFCQHPRSPGAPCQECSRCSLWTDPTEDDEKLIEEIQKEAEEEQKRKNGENTFKRIGPPLEKPVEKVQRVEALPRPVPQNLPQPQMPPYAFAHPPFPLPPVRPVFNNFPLNMGPIPAPYVPPLPNVRVNYDFGPIHMPLEHNLPMHFGPQPRHRF
Protein: Importin-5 (Imp5) (Importin subunit beta-3) (Karyopherin beta-3) (Ran-binding protein 5) (RanBP5) (Q8BKC5)
Organism: Mus musculus (Mouse)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17143267}. Nucleus {ECO:0000269|PubMed:17143267}.
Interaction partners:
- Importin-7
- Importin subunit beta-1
- Importin-9
- Exportin-1
- Interferon regulatory factor 3
- Importin subunit alpha-4
- Importin-8
- Importin-4
- Exportin-2
- Importin-13
Sequence:
MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGRSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKICDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNMGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTNLNNMQRQLALEVIVTLSETAAAMLRKHTSLIAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPQRPWPDRQWGLCIFDDIVEHCSPASFKYAEYFISPMLQYVCDNSPEVRQAAAYGLGVMAQFGGDNYRPFCTDALPLLVRVIQAPEAKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFSYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA
Protein: DNA-dependent metalloprotease WSS1 homolog 2 (EC 3.4.24.-) (DNA damage response protein WSS1 homolog 2) (O94580)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Metalloendopeptidase that acts selectively on DNA-binding proteins. DNA is needed to bring the protease and substrates together to enable proteolysis. Involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesions or DPCs induced by reactive compounds such as formaldehyde.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA-dependent metalloprotease WSS1 homolog
- Uncharacterized peptidase C18A7.01
Sequence:
MELKFSCRGNVIALSFNENDTVLDAKEKLGQEIDVSPSLIKLLYKGNLSDDSHLQDVVKNESKIMCLIRQDKDIVNQAISQLKVPDYSTNTYSLKPKKPHTTPKPASIYTFNELVVLDYPHKDRALRYLERLRDDTGIKKIMDSHRWTVPLLSEMDPAEHTRHDSKTLGLNHNQGAHIELRLRTDRYDGFRDYKTVKSTLIHELTHNVHGEHDSSFWELFRQLTKEADAADLLGKPGSYVSDRASYTPQQDNDDEDQKNHRRDLLLAAAERRKQSGSKVQKE
Protein: Transcription factor jumonji (JmjC) domain-containing protein (F4JFK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDSVEEEGVVRVEEENGRGGLRRHRRVSTKLANYVDPPTDDEEDGGPKRKGKRGGNRAPKKTPKKDEEMQKNEIDEANRVTGLVKEKRAATKILNRKDSIIEVGEASGSMPKEVKGIRIGKRKGEIDGEIPTKPGKKPKTTVDPRIIGYRPDNMCHQCQKSDRIVERCQTCNSKRYCHPCLDTWYPLIAKEDVAKKCMFCSSTCNCRACLRLDTKLKGINSNLIVSEEEKVQASKFILQSLLPHLKGINDEQVAEKEVEAKIYGLKFEEVRPQDAKAFPDERLYCDICKTSIYDLHRNCKSCSFDICLSCCLEIRNGKALACKEDVSWNYINRGLEYEHGQEGKVIEKPANKLDDKLKDKLDGKPDDKPKGKPKGRPKGKPDDKPKGKLKGKQDDKPDDKPDEKPVNTDHMKYPSLWKANEAGIITCCCGAGELVLKRLLPDGWISELVNRVEKTAEAGELLNLPETVLERCPCSNSDRHIDIDSCNLLKAACREGSEDNYLYSPSVWDVQQDDLKHFQHHWVKGEPVIVRNVLEATSGLSWEPMVMHRACRQISHVQHGSLKDVVAVDCLDFCEVKVNLHEFFTGYTDGRYDRMGWPLVLKLKDWPPAKVFKDNLPRHAEEFLCSLPLKHYTHPVNGPLNLAVKLPQNCLKPDMGPKTYVASGFAQELGRGDSVTKLHCDMSDADLWTKLYPFNVSPSIAFLVLHRPGIRFLVLLMPNMQPGIGNLKKKHAEQDLKELYSSVANKEEMMEILENSRQQVQNVETDDGALWDIFRREDIPKLESYIEKHHKEFRHLYCCPVSQVVHPIHDQNFYLTRYHIMKLKEEYGIEPWTFNQKLGDAVLIPVGCPHQVRNLKSCNKVALDFVSPENVSECLRLTKQYRLLPPNHFAKEDKLGVKKMIVHAVDKALRDLSGEKSPEPEEKKQNMRGPKKGAAKAVAKALKDLSPSEKKSSEAAEEEISNGIVNAIDKGLKDLPPSEEKSSEAKVEISNGIVSAMDKDLEHISSSEKKSTEEEGVKRPNIVRTYERRKKLGSEVTNAYIDRLEMEKM
Protein: Tankyrase (E5RHD2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGQRLLNCLLRVMGLGAGSG
Protein: tRNA methyltransferase 10 homolog A (EC 2.1.1.221) (RNA (guanine-9-)-methyltransferase domain-containing protein 2) (tRNA (guanine(9)-N(1))-methyltransferase TRMT10A) (V9HVY8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSEMLPAFIETSNVDKKQGINEDQEESQKPRLGEGCEPISKRQMKKLIKQKQWEEQRELRKQKRKEKRKRKKLERQCQMEPNSDGHDRKRVRRDVVHSTLRLIIDCSFDHLMVLKDIKKLHKQIQRCYAENRRALHPVQFYLTSHGGQLKKNMDENDKGWVNWKDIHIKPEHYSELIKKEDLIYLTSDSPNILKELDESKAYVIGGLVDHNHHKGLTYKQASDYGINHAQLPLGNFVKMNSRKVLAVNHVFEIILEYLETRDWQEAFFTILPQRKGAVPTDKACESASHDNQSVRMEEGGSDSDSSEEEYSRNELDSPHEEKQDKENHTESTVNSLPH
Protein: MTA1 protein (Q9BRL8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGNMKKRLLMPSRGTYLGLANHGQTRHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED
Protein: LRR receptor-like serine/threonine-protein kinase SIK1 (EC 2.7.11.1) (ERECTA homolog 2) (ER homolog 2) (OsER2) (Stress-induced protein kinase 1) (OsSIK1) (Q658G7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Receptor kinase involved in salt drought stress responses. Acts as positive regulator of salt and drought tolerance. May promote salt and drought tolerance through the induction of the activities of antioxidative enzymes, such as peroxidase, superoxide dismutase and catalase. May be involved in the control of stomatal development in leaf epidermis. Possesses kinase activity in vitro. Does not seem to be involved in heat tolerance.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Epidermal patterning factor-like protein
- mitogen-activated protein kinase kinase kinase
- mitogen-activated protein kinase kinase kinase
- Epidermal patterning factor-like protein
- LRR receptor-like serine/threonine-protein kinase ER1
- LRR receptor-like serine/threonine-protein kinase ER2
- Os01g0623000 protein
Sequence:
MAAARAPWLWWWVVVVVGVAVAEAASGGGGGGDGEGKALMGVKAGFGNAANALVDWDGGADHCAWRGVTCDNASFAVLALNLSNLNLGGEISPAIGELKNLQFVDLKGNKLTGQIPDEIGDCISLKYLDLSGNLLYGDIPFSISKLKQLEELILKNNQLTGPIPSTLSQIPNLKTLDLAQNQLTGDIPRLIYWNEVLQYLGLRGNSLTGTLSPDMCQLTGLWYFDVRGNNLTGTIPESIGNCTSFEILDISYNQISGEIPYNIGFLQVATLSLQGNRLTGKIPDVIGLMQALAVLDLSENELVGPIPSILGNLSYTGKLYLHGNKLTGVIPPELGNMSKLSYLQLNDNELVGTIPAELGKLEELFELNLANNNLQGPIPANISSCTALNKFNVYGNKLNGSIPAGFQKLESLTYLNLSSNNFKGNIPSELGHIINLDTLDLSYNEFSGPVPATIGDLEHLLELNLSKNHLDGPVPAEFGNLRSVQVIDMSNNNLSGSLPEELGQLQNLDSLILNNNNLVGEIPAQLANCFSLNNLNLSYNNLSGHVPMAKNFSKFPMESFLGNPLLHVYCQDSSCGHSHGQRVNISKTAIACIILGFIILLCVLLLAIYKTNQPQPLVKGSDKPVQGPPKLVVLQMDMAIHTYEDIMRLTENLSEKYIIGYGASSTVYKCELKSGKAIAVKRLYSQYNHSLREFETELETIGSIRHRNLVSLHGFSLSPHGNLLFYDYMENGSLWDLLHGPSKKVKLNWDTRLRIAVGAAQGLAYLHHDCNPRIIHRDVKSSNILLDENFEAHLSDFGIAKCVPSAKSHASTYVLGTIGYIDPEYARTSRLNEKSDVYSFGIVLLELLTGKKAVDNESNLHQLILSKADDNTVMEAVDSEVSVTCTDMGLVRKAFQLALLCTKRHPSDRPTMHEVARVLLSLLPASAMTTPKTVDYSRLLASTTTAADMRGHDVTDIGDNSSSDEQWFVRFGEVISKHTM
Protein: Cyclic nucleotide gated channel beta 1 (A0A1D5RLH2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XVAVAKVNRPSSWMLSWFWRGMQKVVPQPVCSNGGQNLAAGERDPDQQGGAQIPEPCGTGDPGSAEASGTQDTEPSLWLLRWLEQNLEKVLPQPPPPSLAWKVEPEAAVLDPDPPGTPMQMEPTESPSQPNPGPLEPEEEPAAEPQPGFQSSSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPGCPGMCDVQTRATAAGGL
Protein: Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase (H7C2E4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQVRPSQPCLEAMEMWVGQSEPSAASTMALLTLQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
Protein: Kell blood group glycoprotein (EC 3.4.24.-) (CD antigen CD238) (P23276)
Organism: Homo sapiens (Human)
Function: Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference for EDN3.
Subcellular location: Cell membrane; Single-pass type II membrane protein. Note=Spans the erythrocyte membrane, and is attached to the underlying cytoskeleton.
Interaction partners:
- Endoplasmic reticulum membrane adapter protein XK
- Endothelin-3
- XK-related protein 3
- XK-related protein 2
- Glycophorin-B
- Glycophorin-A
- Rh blood group D antigen
- Blood group Rh
- Prolactin-inducible protein
- Ammonium transporter Rh type A
Sequence:
MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVEGSRPWAVARRVLTAILILGLLLCFSVLLFYNFQNCGPRPCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEELGGWRISGKWTSLNFNRTLRLLMSQYGHFPFFRAYLGPHPASPHTPVIQIDQPEFDVPLKQDQEQKIYAQIFREYLTYLNQLGTLLGGDPSKVQEHSSLSISITSRLFQFLRPLEQRRAQGKLFQMVTIDQLKEMAPAIDWLSCLQATFTPMSLSPSQSLVVHDVEYLKNMSQLVEEMLLKQRDFLQSHMILGLVVTLSPALDSQFQEARRKLSQKLRELTEQPPMPARPRWMKCVEETGTFFEPTLAALFVREAFGPSTRSAAMKLFTAIRDALITRLRNLPWMNEETQNMAQDKVAQLQVEMGASEWALKPELARQEYNDIQLGSSFLQSVLSCVRSLRARIVQSFLQPHPQHRWKVSPWDVNAYYSVSDHVVVFPAGLLQPPFFHPGYPRAVNFGAAGSIMAHELLHIFYQLLLPGGCLACDNHALQEAHLCLKRHYAAFPLPSRTSFNDSLTFLENAADVGGLAIALQAYSKRLLRHHGETVLPSLDLSPQQIFFRSYAQVMCRKPSPQDSHDTHSPPHLRVHGPLSSTPAFARYFRCARGALLNPSSRCQLW
Protein: Phytanoyl-CoA dioxygenase, peroxisomal (EC 1.14.11.18) (Phytanic acid oxidase) (Phytanoyl-CoA alpha-hydroxylase) (PhyH) (O14832)
Organism: Homo sapiens (Human)
Function: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs.
Subcellular location: Peroxisome {ECO:0000269|PubMed:9326939}.
Interaction partners:
- Phytanoyl-CoA hydroxylase-interacting protein
- Peroxisomal targeting signal 2 receptor
- Peroxisomal targeting signal 1 receptor
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- Peroxisomal leader peptide-processing protease
- Peroxisomal membrane protein PEX13
- Peroxisomal ATPase PEX6
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisome biogenesis factor 10
- Peptidyl-prolyl cis-trans isomerase FKBP4
Sequence:
MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
Protein: Ribonuclease J (RNase J) (EC 3.1.-.-) (Pab-RNase J) (Q9V076)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: A highly processive 5'-3' exoribonuclease; no evidence has been seen for endonuclease activity. Prefers 5'-phosphate or 5'-hydroxyl ends; 5'-triphosphate substrates are very poorly degraded, does not degrade circular RNA. Does not degrade pre-tRNA(Trp) suggesting it is inhibited by strong secondary structures. Also degrades ssNDA but not dsDNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01492}.
Interaction partners:
- IdsA-like multifunctional short chain isoprenyl diphosphate synthase
- Metallo-beta-lactamase
- Membrane-associated metallopeptidase
- Ribonuclease Z
Sequence:
MWEEINMIKIYTLGGYEEVGKNMTAVEYNGEVVIVDMGIRLDRVLIHEDVEFQKMSSKDLRKLGAIPDDRPIRNKKVVAIALSHGHLDHIGAVGKLAPHYPDVPIYGTPYTIRLAKSEIKGEEYFEVTNPLYETNYGEIVQVSENLAIEFVQITHSIPQSSIVVIHTPEGAVVYACDYKFDNNHPYGERPDYKRLKELGKEGVKVLIAESTRVAEETKTPSEAVAKMLLEDFFLYEGMEADGLIATTFASHIARLQELIEIANKMGRQAIFIGRSLAKYTGIAKQLGLIKMKGSRVLRSPNAVSKVLKEVSQARENYLLIVTGHQGEPGAILTRMANGELYDIGPRDTVVFSAGVIPNPLNVAQRYALETKLRMKGVRMIKNLHVSGHASKEDHRYLIRMLNPEYIVPAHGEFRMLTHYAELAEEEGYMIGKEVFISRNGHVVEIPGSLEG