wanglab/gogpt-training-data huggingface dataset:
Protein: Cellulose synthase A catalytic subunit 8 [UDP-forming] (AtCesA8) (EC 2.4.1.12) (Protein IRREGULAR XYLEM 1) (AtIRX1) (Protein LEAF WILTING 2) (Q8LPK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the secondary cell wall formation. Required for the xylem cell wall thickening.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cellulose synthase A catalytic subunit 7
- Beta-1,4-xylosyltransferase IRX9
- Cellulose synthase A catalytic subunit 4
- COBRA-like protein 4
- Probable galacturonosyltransferase 12
- Transcription factor MYB46
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Beta-1,4-xylosyltransferase IRX14
- Probable glucuronoxylan glucuronosyltransferase IRX7
- Chitinase-like protein 2
Sequence:
MMESRSPICNTCGEEIGVKSNGEFFVACHECSFPICKACLEYEFKEGRRICLRCGNPYDENVFDDVETKTSKTQSIVPTQTNNTSQDSGIHARHISTVSTIDSELNDEYGNPIWKNRVESWKDKKDKKSKKKKKDPKATKAEQHEAQIPTQQHMEDTPPNTESGATDVLSVVIPIPRTKITSYRIVIIMRLIILALFFNYRITHPVDSAYGLWLTSVICEIWFAVSWVLDQFPKWSPINRETYIDRLSARFEREGEQSQLAAVDFFVSTVDPLKEPPLITANTVLSILALDYPVDKVSCYVSDDGAAMLSFESLVETADFARKWVPFCKKYSIEPRAPEFYFSLKIDYLRDKVQPSFVKERRAMKRDYEEFKIRMNALVAKAQKTPEEGWTMQDGTSWPGNNTRDHPGMIQVFLGYSGARDIEGNELPRLVYVSREKRPGYQHHKKAGAENALVRVSAVLTNAPFILNLDCDHYVNNSKAVREAMCFLMDPVVGQDVCFVQFPQRFDGIDKSDRYANRNIVFFDVNMRGLDGIQGPVYVGTGTVFRRQALYGYSPPSKPRILPQSSSSSCCCLTKKKQPQDPSEIYKDAKREELDAAIFNLGDLDNYDEYDRSMLISQTSFEKTFGLSTVFIESTLMENGGVPDSVNPSTLIKEAIHVISCGYEEKTEWGKEIGWIYGSITEDILTGFKMHCRGWRSIYCMPLRPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPLWYGCSGGRLKLLQRLAYINTIVYPFTSLPLVAYCTLPAICLLTGKFIIPTLSNLASMLFLGLFISIILTSVLELRWSGVSIEDLWRNEQFWVIGGVSAHLFAVFQGFLKMLAGLDTNFTVTSKTADDLEFGELYIVKWTTLLIPPTSLLIINLVGVVAGFSDALNKGYEAWGPLFGKVFFAFWVILHLYPFLKGLMGRQNRTPTIVILWSILLASVFSLVWVRINPFVSKTDTTSLSLNCLLIDC
Protein: Zinc finger protein 213 (Putative transcription factor CR53) (Zinc finger protein with KRAB and SCAN domains 21) (O14771)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger protein 397
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger and SCAN domain-containing protein 20
- PiggyBac transposable element-derived protein 1
- Zinc finger and SCAN domain-containing protein 1
Sequence:
MAAPLEAQDQAPGEGEGLLIVKVEDSSWEQESAQHEDGRDSEACRQRFRQFCYGDVHGPHEAFSQLWELCCRWLRPELRTKEQILELLVLEQFLTVLPGEIQGWVREQHPGSGEEAVALVEDLQKQPVKAWRQDVPSEEAEPEAAGRGSQATGPPPTVGARRRPSVPQEQHSHSAQPPALLKEGRPGETTDTCFVSGVHGPVALGDIPFYFSREEWGTLDPAQRDLFWDIKRENSRNTTLGFGLKGQSEKSLLQEMVPVVPGQTGSDVTVSWSPEEAEAWESENRPRAALGPVVGARRGRPPTRRRQFRDLAAEKPHSCGQCGKRFRWGSDLARHQRTHTGEKPHKCPECDKSFRSSSDLVRHQGVHTGEKPFSCSECGKSFSRSAYLADHQRIHTGEKPFGCSDCGKSFSLRSYLLDHRRVHTGERPFGCGECDKSFKQRAHLIAHQSLHAKMAQPVG
Protein: BZIP domain-containing protein (A7S7R0)
Organism: Nematostella vectensis (Starlet sea anemone)
Interaction partners:
- Polyribonucleotide 5'-hydroxyl-kinase Clp1 P-loop domain-containing protein
- Uncharacterized protein
- WD repeat-containing protein 18
- Pre-rRNA-processing protein Ipi1 N-terminal domain-containing protein
Sequence:
MLEPTDVGLAEYLLNFPGVNCSQTPGIQEEKHDYFDHIEDPFEFDLNASSFHENHSENIMELPETGKSTSKKKNLTKISKRDEKANQKTTPASKRLKGKTVAKGERRQAAKVSMRSSQTRTLSTTLDDNKMTLKSETTKSKCSKECKKRINEKSNGKTVKENQFDDHTTSPNPTTTSTKGIKNKGKAMHNEGLVGDVDKVKTITVMKCLDANVSPTQLDMDRYVSDEGINRQAIMAKINREKKKQYVQELEGSVEEYKSKNAVLQKDCEDMKGLVKDLQMEIAYLKGVLANESQLAGLLKNIGNTDGVEFVGSVDKVNTLKRKASTTKESVKPSKISRPNGDTDYVNAAGVCLHVKSGKVSLEFCSKCNMSSSSDE
Protein: (-)-beta-phellandrene synthase 2, chloroplastic (EC 4.2.3.52) (Terpene synthase TPS-Phel-2) (PsTPS-Phel-2) (C0PTH8)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-phellandrene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAIVSSVPLASKSCLHKSLISSIHKLKPFCRTIPTLGMSRPGKYVMPSMSMSSPVSDDGVQRRTGGYHSNLWNDDIIQFLSTTYGEPAYRERGERLIDEVKNMFNSISMEDVEFSPLNDLIQRLWIVDSVERLGIDRHFKNEIKSTLDYVYSYWTQKGIGCGIESVVPDLNSTALGLRTLRLHGYPVSAEVLKHFQNQNGQFACSPSETEGEMRSIVNLYRASLIAFPGEKVMEEAEIFSTKYLKEALQKIPVSSLSREIGDVLEQDWHTNLPRLEARNYIDVFGQDTKDTKLYMKTEKLLELAKLEFNIFQSLQKTELDSLLRWWKDSGFHHITFSRHLHVEYYTLASCIAIEPQHSRFRLGFAKACHVITILDDMYDVFGTIDELELFTAQIKRWDPSATDCLPKYMKRMYMILYDMVNEMSREAETAQGRDTLNYARQAWEDFIDSYMQEAKWIATGYLPTFDEYFENGKVSSGHRVAALQPILTMDIPFPHDILKEVDFPSKLNDLASAILRLRGDTRCYKADRARGEEASCISCYMKDNPGATEEDALSHINAVISDVIKGLNWELLNPNSSVPISSKKHVFDVSRALHYGYKYRDGYSVSNIETKSLVMRTLLESVPF
Protein: Small integral membrane protein 20 (Mitochondrial translation regulation assembly intermediate of cytochrome c oxidase protein of 7 kDa) (MITRAC7) [Cleaved into: Phoenixin-14 (PNX-14); Phoenixin-20 (PNX-20)] (Q8N5G0)
Organism: Homo sapiens (Human)
Function: Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. Promotes the progression of complex assembly after the association of MT-CO1/COX1 with COX4I1 and COX6C. Chaperone-like assembly factor required to stabilize newly synthesized MT-CO1/COX1 and to prevent its premature turnover.
Subcellular location: [Small integral membrane protein 20]: Mitochondrion inner membrane {ECO:0000269|PubMed:26321642}; Single-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Phoenixin-14]: Secreted {ECO:0000250|UniProtKB:C0HLM6}.; SUBCELLULAR LOCATION: [Phoenixin-20]: Secreted {ECO:0000250|UniProtKB:C0HLM6}.
Interaction partners:
- Probable G-protein coupled receptor 173
- Cytochrome c oxidase assembly factor 3 homolog, mitochondrial
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin I, cardiac muscle
- Troponin I, slow skeletal muscle
- Troponin I, fast skeletal muscle
Sequence:
MSRNLRTALIFGGFISLIGAAFYPIYFRPLMRLEEYKKEQAINRAGIVQEDVQPPGLKVWSDPFGRK
Protein: Integrin beta (E9PEE8)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
Interaction partners:
Sequence:
MITYKNFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDC
Protein: Keratin-associated protein 23-1 (A1A580)
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:
MSYNCCCGNFSSHSCEGYLCYSGYSRGGSSYPSNLVYSTEPLISQHLPAGFLSLQGLSGDLLGNP
Protein: X-box-binding protein 1 (Q4H2M1)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Interaction partners:
Sequence:
MMIGDKKRISMLEHEQDDGYADVDEKELRKKLRNRESAQRARDRQKARMQWLEHEVSMLQVRNLTLTRENNLLRNLLAIGAQKKEPCDVVTSCNDAVASCNDGVTSEAEDDRLTNETRTSPKRSHEEPEAMSKRSRYEVSEKQDHLDLNGRRSLSDSEVEKPNFDGSALLTKTSAMLGQIINPLLCGRHSSFDIFNPRLQFNQPDDSTTGVDEETNPPALIYPYLLPTFPLRSWPVKQ
Protein: DNA-directed RNA polymerase I subunit RPA34 (A34.5) (Antisense to ERCC-1 protein) (ASE-1) (CD3-epsilon-associated protein) (CD3E-associated protein) (DNA-directed RNA polymerase I subunit G) (RNA polymerase I-associated factor PAF49) (O15446)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Isoform 1 is involved in UBTF-activated transcription, presumably at a step following PIC formation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:9426281}. Chromosome {ECO:0000269|PubMed:9426281}. Note=Found at the fibrillar centers of the nucleolus in interphase and during cell division it is localized to the nucleolus organizer regions of the chromosomes.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA43
Sequence:
MEEPQAGDAARFSCPPNFTAKPPASESPRFSLEALTGPDTELWLIQAPADFAPECFNGRHVPLSGSQIVKGKLAGKRHRYRVLSSCPQAGEATLLAPSTEAGGGLTCASAPQGTLRILEGPQQSLSGSPLQPIPASPPPQIPPGLRPRFCAFGGNPPVTGPRSALAPNLLTSGKKKKEMQVTEAPVTQEAVNGHGALEVDMALGSPEMDVRKKKKKKNQQLKEPEAAGPVGTEPTVETLEPLGVLFPSTTKKRKKPKGKETFEPEDKTVKQEQINTEPLEDTVLSPTKKRKRQKGTEGMEPEEGVTVESQPQVKVEPLEEAIPLPPTKKRKKEKGQMAMMEPGTEAMEPVEPEMKPLESPGGTMAPQQPEGAKPQAQAALAAPKKKTKKEKQQDATVEPETEVVGPELPDDLEPQAAPTSTKKKKKKKERGHTVTEPIQPLEPELPGEGQPEARATPGSTKKRKKQSQESRMPETVPQEEMPGPPLNSESGEEAPTGRDKKRKQQQQQPV
Protein: Epididymis secretory protein Li 108 (V9HW56)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAGLNSLEAVKRKIQALQQQADEAEDRAQGLQRELDGERERREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELNCI
Protein: Cholecystokinin receptor type A (CCK-A receptor) (CCK-AR) (Cholecystokinin-1 receptor) (CCK1-R) (P30551)
Organism: Rattus norvegicus (Rat)
Function: Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Cholecystokinin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Gastrin
- Gastrin/cholecystokinin type B receptor
- Guanine nucleotide-binding protein subunit alpha
- C-C motif chemokine
- Guanine nucleotide-binding protein G
Sequence:
MSHSPARQHLVESSRMDVVDSLLMNGSNITPPCELGLENETLFCLDQPQPSKEWQSALQILLYSIIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICRPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSNLVPFTKNNNQTANMCRFLLPSDAMQQSWQTFLLLILFLLPGIVMVVAYGLISLELYQGIKFDASQKKSAKEKKPSTGSSTRYEDSDGCYLQKSRPPRKLELQQLSSGSGGSRLNRIRSSSSAANLIAKKRVIRMLIVIVVLFFLCWMPIFSANAWRAYDTVSAEKHLSGTPISFILLLSYTSSCVNPIIYCFMNKRFRLGFMATFPCCPNPGPPGVRGEVGEEEDGRTIRALLSRYSYSHMSTSAPPP
Protein: HTH-type transcriptional activator RhaS (L-rhamnose operon regulatory protein RhaS) (P09377)
Organism: Escherichia coli (strain K12)
Function: Activates expression of the rhaBAD and rhaT operons.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01534}.
Interaction partners:
- L-rhamnose-proton symporter
- RNA polymerase sigma factor RpoD
- Melibiose operon regulatory protein
- L-Rhamnulokinase
- HTH-type transcriptional activator RhaR
- Uncharacterized HTH-type transcriptional regulator YidL
- Arabinose operon regulatory protein
- L-rhamnose isomerase
- Multiple antibiotic resistance protein MarA
- Right origin-binding protein
Sequence:
MTVLHSVDFFPSGNASVAIEPRLPQADFPEHHHDFHEIVIVEHGTGIHVFNGQPYTITGGTVCFVRDHDRHLYEHTDNLCLTNVLYRSPDRFQFLAGLNQLLPQELDGQYPSHWRVNHSVLQQVRQLVAQMEQQEGENDLPSTASREILFMQLLLLLRKSSLQENLENSASRLNLLLAWLEDHFADEVNWDAVADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLMKARHLLRHSEASVTDIAYRCGFSDSNHFSTLFRREFNWSPRDIRQGRDGFLQ
Protein: Junction plakoglobin (Q6P0K8)
Organism: Rattus norvegicus (Rat)
Function: Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity).
Subcellular location: Cell junction, adherens junction {ECO:0000250|UniProtKB:P14923}. Cell junction, desmosome {ECO:0000269|PubMed:21617128, ECO:0000269|PubMed:26858265}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P14923}. Cell membrane {ECO:0000250|UniProtKB:P14923}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14923}. Cytoplasm {ECO:0000250|UniProtKB:Q9PVF7}. Cell junction {ECO:0000250|UniProtKB:Q9PVF7}. Nucleus {ECO:0000250|UniProtKB:Q9PVF7}. Note=Cytoplasmic in a soluble and membrane-associated form. Colocalizes with DSG4 at desmosomes (By similarity). {ECO:0000250|UniProtKB:P14923}.
Interaction partners:
- Desmoplakin
- Cadherin-1
- Desmoglein 2
- Catenin beta-1
- Cadherin-2
- Desmocollin 2
- Cadherin-5
- Cadherin 3
- Lymphoid enhancer-binding factor 1
- Transcription factor 7 like 1
Sequence:
MEVMNLIEQPIKVTEWQQTYTYDSGIHSGVNTCVPSVSSKGLLDEDDTCGRQYTLKKTTTYTQGVPQSQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQTTNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQGLVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLENVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYADDMDATYRPMYSSDVPLDPLDMHMDMDGDYPMDTYSDGLRPPYPAADHMLA
Protein: Kallikrein related-peptidase 6 (H3BKZ6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPMKMLTMKMLALCLVLAKSAWSEEQEKVVHGGPCLKDSHPFQAALYTSGHLLCGGVLIDPQWVLTAAHCKKPNLQVILGKHNLRQTETFQRQISVDRTIVHPRYNPETHDNDIMMVHLKNPVKFSKKI
Protein: Riboflavin-binding protein (RBP) [Cleaved into: Riboflavin-binding protein, plasma form; Riboflavin-binding protein, yolk major form; Riboflavin-binding protein, yolk minor form] (P02752)
Organism: Gallus gallus (Chicken)
Function: Required for the transport of riboflavin to the developing oocyte.
Interaction partners:
- Folate_rec domain-containing protein.
- Clusterin
- Ovomucoid
- Ovostatin
- WD repeat and SOCS box containing 2.
- Ovomucoid
Sequence:
MLRFAITLFAVITSSTCQQYGCLEGDTHKANPSPEPNMHECTLYSESSCCYANFTEQLAHSPIIKVSNSYWNRCGQLSKSCEDFTKKIECFYRCSPHAARWIDPRYTAAIQSVPLCQSFCDDWYEACKDDSICAHNWLTDWERDESGENHCKSKCVPYSEMYANGTDMCQSMWGESFKVSESSCLCLQMNKKDMVAIKHLLSESSEESSSMSSSEEHACQKKLLKFEALQQEEGEERR
Protein: Ankyrin repeat domain-containing protein 12 (Ankyrin repeat-containing cofactor 2) (GAC-1 protein) (Q6UB98)
Organism: Homo sapiens (Human)
Function: May recruit HDACs to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation.
Subcellular location: Nucleus {ECO:0000269|PubMed:15184363, ECO:0000269|Ref.2}.
Interaction partners:
Sequence:
MPKSGFTKPIQSENSDSDSNMVEKPYGRKSKDKIASYSKTPKIERSDVSKEMKEKSSMKRKLPFTISPSRNEERDSDTDSDPGHTSENWGERLISSYRTYSEKEGPEKKKTKKEAGNKKSTPVSILFGYPLSERKQMALLMQMTARDNSPDSTPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDESYTDSEEAQSVNPSSVDENIDSETEKDSLICESKQILPSKTPLPSALDEYEFKDDDDEEINKMIDDRHILRKEQRKENEPEAEKTHLFAKQEKAFYPKSFKSKKQKPSRVLYSSTESSDEEALQNKKISTSCSVIPETSNSDMQTKKEYVVSGEHKQKGKVKRKLKNQNKNKENQELKQEKEGKENTRITNLTVNTGLDCSEKTREEGNFRKSFSPKDDTSLHLFHISTGKSPKHSCGLSEKQSTPLKQEHTKTCLSPGSSEMSLQPDLVRYDNTESEFLPESSSVKSCKHKEKSKHQKDFHLEFGEKSNAKIKDEDHSPTFENSDCTLKKMDKEGKTLKKHKLKHKEREKEKHKKEIEGEKEKYKTKDSAKELQRSVEFDREFWKENFFKSDETEDLFLNMEHESLTLEKKSKLEKNIKDDKSTKEKHVSKERNFKEERDKIKKESEKSFREEKIKDLKEERENIPTDKDSEFTSLGMSAIEESIGLHLVEKEIDIEKQEKHIKESKEKPEKRSQIKEKDIEKMERKTFEKEKKIKHEHKSEKDKLDLSECVDKIKEKDKLYSHHTEKCHKEGEKSKNTAAIKKTDDREKSREKMDRKHDKEKPEKERHLAESKEKHLMEKKNKQSDNSEYSKSEKGKNKEKDRELDKKEKSRDKESINITNSKHIQEEKKSSIVDGNKAQHEKPLSLKEKTKDEPLKTPDGKEKDKKDKDIDRYKERDKHKDKIQINSLLKLKSEADKPKPKSSPASKDTRPKEKRLVNDDLMQTSFERMLSLKDLEIEQWHKKHKEKIKQKEKERLRNRNCLELKIKDKEKTKHTPTESKNKELTRSKSSEVTDAYTKEKQPKDAVSNRSQSVDTKNVMTLGKSSFVSDNSLNRSPRSENEKPGLSSRSVSMISVASSEDSCHTTVTTPRPPVEYDSDFMLESSESQMSFSQSPFLSIAKSPALHERELDSLADLPERIKPPYANRLSTSHLRSSSVEDVKLIISEGRPTIEVRRCSMPSVICEHTKQFQTISEESNQGSLLTVPGDTSPSPKPEVFSNVPERDLSNVSNIHSSFATSPTGASNSKYVSADRNLIKNTAPVNTVMDSPVHLEPSSQVGVIQNKSWEMPVDRLETLSTRDFICPNSNIPDQESSLQSFCNSENKVLKENADFLSLRQTELPGNSCAQDPASFMPPQQPCSFPSQSLSDAESISKHMSLSYVANQEPGILQQKNAVQIISSALDTDNESTKDTENTFVLGDVQKTDAFVPVYSDSTIQEASPNFEKAYTLPVLPSEKDFNGSDASTQLNTHYAFSKLTYKSSSGHEVENSTTDTQVISHEKENKLESLVLTHLSRCDSDLCEMNAGMPKGNLNEQDPKHCPESEKCLLSIEDEESQQSILSSLENHSQQSTQPEMHKYGQLVKVELEENAEDDKTENQIPQRMTRNKANTMANQSKQILASCTLLSEKDSESSSPRGRIRLTEDDDPQIHHPRKRKVSRVPQPVQVSPSLLQAKEKTQQSLAAIVDSLKLDEIQPYSSERANPYFEYLHIRKKIEEKRKLLCSVIPQAPQYYDEYVTFNGSYLLDGNPLSKICIPTITPPPSLSDPLKELFRQQEVVRMKLRLQHSIEREKLIVSNEQEVLRVHYRAARTLANQTLPFSACTVLLDAEVYNVPLDSQSDDSKTSVRDRFNARQFMSWLQDVDDKFDKLKTCLLMRQQHEAAALNAVQRLEWQLKLQELDPATYKSISIYEIQEFYVPLVDVNDDFELTPI
Protein: fructose-bisphosphatase (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (O97193)
Organism: Leishmania major
Interaction partners:
- Transketolase
- Fructose-bisphosphate aldolase
- Transaldolase
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- mannose-6-phosphate isomerase
- Pyruvate kinase
- Pyruvate kinase
Sequence:
MDVRRTPTPTTLTQYIIKSQPPHSRGDFTLLMMAIQTSVKVIEKNIRRAGMKGMLGYIAGQSANATGDHQAKLDVISNIAFKAYLLSSTSVCVLGSEEEEQMIIAESGRRGDYLIFFDPLDGSSNIDANVSVGSIWGVWRLPKDTTINSVEDANAVIRMLKGTDMVSAGYAVYGSATNLVLTSGHGVDGFTLDPNIGEFILTHPHISIPKKRSIYSVNEGNYGKWEPWFKEYIDYLKMNKTTRYSARYIGSMVGDIHRTLLYGGIFCYPKDANQVEGKLRLLYEAAPMAMIVEQAGGKAVGSNGRILEQSITRLHQRTPVYFGSRQEVDLCMAFRDRNVKTEALAPTSSKL
Protein: Rifin (Q8I0E0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLNILEHNKNEPHTTPNHTQTTRSLCECDIYTSIYDNDPQMKAVMENYNRQTSDRFKEYDERMKTTRQKCKDKCDKEIQKIVLKDKMEKQMAQQLTTLETKITTEDIPTCICEKSLADKTEKFCLNCGVNVGGGVTLSSGVLGGIGAVAVNAWKDAAIIAAKEAAIAKGAAAGKIAGEAKGVDVVIYYLKGLGVEELIPRISESIGKTIPYTNAGKISDIIYGKYTTTCMGLNNRGPPAACNSFNIKFGLFNTRGKPIGSPPSSAIPTKVREAVDKATRSAKAAAEAKSTTVTAEITEKQTALIEAGFNSSITSINASIIAILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Hairy/enhancer-of-split related with YRPW motif protein 1 (XHey-1) (Hairy and enhancer of split-related protein 1) (Hesr-1) (Hairy-related transcription factor 1) (HRT-1) (XHRT1) (xHRT-1) (Protein xbc8) (Q9I8A3)
Organism: Xenopus laevis (African clawed frog)
Function: Downstream effector of Notch signaling. Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Acts as a suppressor of neurogenesis by antagonizing proneural gene function. Functions during floorplate development. Plays a role in pronephros formation in the inhibition of distal tubule and duct cell fates and the promotion of glomus and proximal tubule formation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14648848}.
Interaction partners:
Sequence:
MKRGHDYSSSDSELDENIEVEKESADENGNLSSMSPSTSSQILARKRRRGIIEKRRRDRINNSLSELRRLVPSAFEKQGSAKLEKAEILQMTVDHLKMLHTAGGKGYFDAHALAMDYRSLGFRECLAEVARYLSIIEGMETADPLRVRLVSHLNNYASQREAASTAHTSIGHIPWGGTFAHHPHLSHPLLLAQTAHTNSTSSSTEAHHHNRLRGSPHAESSSLRVAPNGNIASVLPVVASSKLSPPLLSSMASLSAFPFSFGSFHLLSPNSLSPTTPTPSGKPYRPWGTEIGAF
Protein: High mobility group protein I (HMG-I) (High mobility group AT-hook protein 1) (High mobility group protein A1) (cHMG1) (Q23794)
Organism: Chironomus tentans (Midge) (Camptochironomus tentans)
Function: Binds preferentially to the minor groove of A+T rich regions in double-stranded DNA via the second and third DBA-binding domains. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions.
Subcellular location: Nucleus, nucleolus. Chromosome. Note=In chromosomal puffs. {ECO:0000269|PubMed:7806532, ECO:0000269|PubMed:9087379}.
Interaction partners:
Sequence:
MSDSPVKKGRGRPAKAKPEETASPKAAKKEEKKVEEVPKKIEESTKPENGAAPKKGRGRPSKGDKAAPKRPASGKGRGRPAKNAKKVDDADTEEVNSSD
Protein: Frizzled-1 (Fz-1) (hFz1) (FzE1) (Q9UP38)
Organism: Homo sapiens (Human)
Function: Receptor for Wnt proteins. Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B. Contradictory results showing activation by WNT7B have been described for mouse (By similarity). Functions in the canonical Wnt/beta-catenin signaling pathway. The canonical Wnt/beta-catenin signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10557084}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein Wnt-3a
- Low-density lipoprotein receptor-related protein 5
- Proto-oncogene Wnt-1
- Protein Wnt-5a
- Protein Wnt-11
- Segment polarity protein dishevelled homolog DVL-1
- Low-density lipoprotein receptor-related protein 6
- Tyrosine-protein kinase RYK
- Protein Wnt-2
- Protein Wnt-7b
Sequence:
MAEEEAPKKSRAAGGGASWELCAGALSARLAEEGSGDAGGRRRPPVDPRRLARQLLLLLWLLEAPLLLGVRAQAAGQGPGQGPGPGQQPPPPPQQQQSGQQYNGERGISVPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGHRGGFPGGAGASERGKFSCPRALKVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGIWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYTAVAVAYIAGFLLEDRVVCNDKFAEDGARTVAQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAIKTITILALGQVDGDVLSGVCFVGLNNVDALRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLEKLMVRIGVFSVLYTVPATIVIACYFYEQAFRDQWERSWVAQSCKSYAIPCPHLQAGGGAPPHPPMSPDFTVFMIKYLMTLIVGITSGFWIWSGKTLNSWRKFYTRLTNSKQGETTV