wanglab/gogpt-training-data huggingface dataset:
Protein: Sorting nexin-24 (Q9Y343)
Organism: Homo sapiens (Human)
Function: May be involved in several stages of intracellular trafficking.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Sorting nexin-22
- GTPase-activating protein and VPS9 domain-containing protein 1
- Casein kinase I isoform alpha
- Casein kinase I isoform epsilon
- Testis-specific serine/threonine-protein kinase 1
Sequence:
MEVYIPSFRYEESDLERGYTVFKIEVLMNGRKHFVEKRYSEFHALHKKLKKCIKTPEIPSKHVRNWVPKVLEQRRQGLETYLQAVILENEELPKLFLDFLNVRHLPSLPKAESCGSFDETESEESSKLSHQPVLLFLRDPYVLPAASDFPNVVIEGVLHGIFYPHLQPR
Protein: Shikimate transporter (Shikimate permease) (P76350)
Organism: Escherichia coli (strain K12)
Function: Involved in the uptake of shikimate, an intermediate in the aromatic amino acid biosynthetic pathway.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Superoxide dismutase
Sequence:
MDSTLISTRPDEGTLSLSRARRAALGSFAGAVVDWYDFLLYGITAALVFNREFFPQVSPAMGTLAAFATFGVGFLFRPLGGVIFGHFGDRLGRKRMLMLTVWMMGIATALIGILPSFSTIGWWAPILLVTLRAIQGFAVGGEWGGAALLSVESAPKNKKAFYSSGVQVGYGVGLLLSTGLVSLISMMTTDEQFLSWGWRIPFLFSIVLVLGALWVRNGMEESAEFEQQQHYQAAAKKRIPVIEALLRHPGAFLKIIALRLCELLTMYIVTAFALNYSTQNMGLPRELFLNIGLLVGGLSCLTIPCFAWLADRFGRRRVYITGTLIGTLSAFPFFMALEAQSIFWIVFFSIMLANIAHDMVVCVQQPMFTEMFGASYRYSGAGVGYQVASVVGGGFTPFIAAALITYFAGNWHSVAIYLLAGCLISAMTALLMKDSQRA
Protein: UDP-glycosyltransferase 72B1 (EC 2.4.1.-) (Arbutin synthase) (Probable hydroquinone glucosyltransferase) (EC 2.4.1.218) (Q9M156)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional O-glycosyltransferase and N-glycosyltransferase that can detoxify xenobiotics. Possesses high activity to metabolize the persistent pollutants 2,4,5-trichlorophenol (TCP) and 3,4-dichloroaniline (DCA). Also active on benzoates and benzoate derivatives in vitro.
Interaction partners:
- Mucin-like protein
- Hydroxyproline-rich glycoprotein family protein
- F-box/kelch-repeat protein At1g55270
Sequence:
MEESKTPHVAIIPSPGMGHLIPLVEFAKRLVHLHGLTVTFVIAGEGPPSKAQRTVLDSLPSSISSVFLPPVDLTDLSSSTRIESRISLTVTRSNPELRKVFDSFVEGGRLPTALVVDLFGTDAFDVAVEFHVPPYIFYPTTANVLSFFLHLPKLDETVSCEFRELTEPLMLPGCVPVAGKDFLDPAQDRKDDAYKWLLHNTKRYKEAEGILVNTFFELEPNAIKALQEPGLDKPPVYPVGPLVNIGKQEAKQTEESECLKWLDNQPLGSVLYVSFGSGGTLTCEQLNELALGLADSEQRFLWVIRSPSGIANSSYFDSHSQTDPLTFLPPGFLERTKKRGFVIPFWAPQAQVLAHPSTGGFLTHCGWNSTLESVVSGIPLIAWPLYAEQKMNAVLLSEDIRAALRPRAGDDGLVRREEVARVVKGLMEGEEGKGVRNKMKELKEAACRVLKDDGTSTKALSLVALKWKAHKKELEQNGNH
Protein: LD24434p (NC2alpha) (Q9GSP1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPSKKKKYNARFPAGRIKKIMQSDEEIGKVAQAVPVIISRTLELFVESLLTKTLRITNARNAKTLSPSHMRQCIVSEKRFDFLKELVRNIPDISVAEEAAYNEDDVLRSSPEEQYPDSDTPYDLSLPSTSMRSQANGTAAYMRSMSLNNGAGSGGGAAATKRQFQSQHSTQETPTTSTTLPAKLARSGSMPAYTPRGRPPNHLKKHSVQLDTAIPAPICNYELNKPIVKIDYSHVQMPTANLCTPDASDSGSGSGAGSGAFNFDIAAPVINIDLTNIVAGGAPGSGVPPASIGLPAATPGDNNNVNQMAGKSSAPIIPKATAASATPTETVFELDEDYDNI
Protein: Protein FAF-like, chloroplastic (Q0V865)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- RING finger protein
- Uncharacterized protein
- Uncharacterized protein At2g34110
- adenylate kinase
- Nonsense-mediated mRNA decay-like protein
- PsbP domain-containing protein 7, chloroplastic
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 2, mitochondrial
- Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 3, mitochondrial
- Protein RECOGNITION OF PERONOSPORA PARASITICA 7
Sequence:
MMACGLSKSLGLSSSLKKQQGIVSILGGISSNTSSAPSLRRTFSADLSSKTWVSQNGFSPMKRISSSEKLRPDEEEAEEESRSGVDIWAQIQQDKNDKKKEEEIEPGQSDVWSSILSEKKKTESSKDTVPPPYVHPLMKRASSLSEKSLEICTESLGSETGCDGFSSHASSETGDAEIEIHDETNLVVNVTETKVEEITETEIVVEQESSIIVPNHIIELPPGSFPPPIRSLSSQSGSSLHMKTRRDNGRLVLEAVSMPSHNNFSAKRQDGRLLLTFAEISNEPNYDKEDEIDSEVQWFDEEEEEEEEEEDEEEEAPDEFAYKPNGLLYKMAQKPIPITVHRLAHKPIGVPKRNSRWPMADEFDTKSDLSTPVVHSLPPRPRVAQLARSTKPPSTVDDTVGAACFNTCDYSWKSTNTESFGPNTKTQFQAQNFVNKSMGDGWINGCKDRRRSLLSVEPFCIAT
Protein: Tryparedoxin (Q57WB4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Thioredoxin
- protein disulfide-isomerase
- Trypanothione reductase
- Glutathione peroxidase
- Glutathione peroxidase
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- Thioredoxin-like protein
- Monothiol glutaredoxin, putative
- Glutathione peroxidase
Sequence:
MSGLAKYLPGATNLLSKSGEVSLGSLVGKTVFLYFSASWCPPCRGFTPVLAEFYEKHHVAKNFEVVLISWDENESDFHDYYGKMPWLALPFDQRSTVSELGKTFGVESIPTLITINADTGAIIGTQARTRVIEDPDGANFPWPN
Protein: Defensin alpha 4 (Defensin-related cryptdin-4) (P28311)
Organism: Mus musculus (Mouse)
Function: Host-defense peptide that has antimicrobial activity. Exhibits activity against Gram-negative E.coli (in vitro). Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q01523}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:10569786}.
Interaction partners:
Sequence:
MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSISFGGQEGSALHEKSLRGLLCYCRKGHCKRGERVRGTCGIRFLYCCPRR
Protein: Rap guanine nucleotide exchange factor (RA-GEF) (PDZ-domain-containing exchange factor) (G5EDB9)
Organism: Caenorhabditis elegans
Function: Acts as a guanine nucleotide exchange factor for small G protein GTPases like rap-1 and rap-2. Required in the hypodermis, especially in the seam cells, for proper formation of the cuticle.
Interaction partners:
- Ras protein let-60
- GTP binding protein
- GTP binding protein
- Tyrosine-protein phosphatase 1
- small monomeric GTPase
- PDZ domain-containing protein
- PDZ domain-containing protein
- Ras-related protein Rap-1
- PDZ domain-containing protein
- General receptor for phosphoinositides 1-associated scaffold protein 1 homolog
Sequence:
MDPRKPRQDPVNDARFYESLIKPPHLRTPDDIRNVYEQLRQLDTFSNLFIGPLKALCKTARYERHPAQYILFRDGDVARSWYILLSGSVFIENQIYMPYGCFGKRTGQNHRRTHNCLLLQESEMIVIDYPTEPQSNGMSPRTPPRGIHHSGEPVHQKTPRKSAPNMSVDSIAMPPPPVPPRPLRLPQTAAKGPAPLPPRGLPRTYPLDFPVDIPTTSSSSSNTSYNDQHRSQVYLNGLSADEDTLVRVKHRREKSNSVGGQAQNGISTARRLRGRSTASSTTTEGETASNEGADSDEDEGSMPSQESSSGGFMDLRDSVRECLEKEPSERNSEDLAVLLDFMQHMSAFAALPMSIKRQLCLKMVFAVVNDAGTVVLAHNEKLDSWSVIVNGCVEVVKPSGERVEYKLGDSFGAEPTPATQIHIGEMRTMVDDCEFVLVEHRDFCSIMSTIGDHIEKDRDGLTGEVVSEVERRTVGTHCGQVLIKGKPDKLIHHLVDERDHNVDPHYVDDFLLTYRVFIRDPTTIFEKLMLWFADSIYRDKVARLVLLWVNNHFNDFETNDEMWNLLERFEGALERDGMHSQLSLLNIACSVKAKPRQVILTRRKDDKMMMRLVGGQESGNSVYVAEVFPDTSAAREGVKRADEMLEVNQQSAKYLSAKKAEDLLTGSLSLTLMLKNNVLGYKETIGKIEHNKPKNGTSRSGAGIPMVIPVHKTSITGKKSSTTSSKSGMMEKLMTILKSSKEDSMDFTDEAKISSADLRPSRSNPDITSISQYYGPVRSECPEHVLKIYRNDQTFKYLPVYKETSAQNVVQLALQEFNMTAEGSPEWSLCECTVTIDGVIKQRRLPPQMENLAERIALNSRYYLKNNSRSEPLVPDELAPELLKEAQTQLLSLNAQVVAAQLTLQDFSVFSAIEPTEFLDNLFKLDSKYGSPKLEEFEQLFNREMWWVATEICTERHVQKRAKLIKKFIKVARYCRDLRNFNSMFAIMSGLDKPAVRRLHSSWERVSSKYIRMLDEIHQLVDPSRNMSKYRQHLAEVAQEPPVVPIYPVIKKDLTFAHDGNATYSEKLINFEKLRLIAKSIRGVMKLSSAPYEIASMAERSGGVVMDALLHMNSFENSNVATMRKGMSGKQNQPRKKVYEQALMVRKVKSYLEGLHVVDNEMELDSMSYDIEPQVQTAHRGANSSSTANIRRVPSPTPSSLSSQSAGSADQSSRHRLLFNGTGSISSAGGGSKFGVESPQAVQKMLSLVQNSKVKGAPPQITSPSTSARSSLQRNMPRVTGRQATSSAQGPVQLNEETSTVTTYYQSDNGRRQRSGSEGRFDNIPPSTFYLTSDGLTVSPRQSLSVVIPTHPHGHSPTSPRCRSRSPASSGCSSFSTIASIAATSMAAAPSAFVSNPYQHHQTVRGHVIGHRPMPIVTSGSATLPNHVSPRGLPPKSRPTILPGSHTNSSSRMGTIKEATFLTSEQVSRV
Protein: DnaJ homolog subfamily B member 11 (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (Liver regeneration-related protein LRRGT00084) (Q6TUG0)
Organism: Rattus norvegicus (Rat)
Function: As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A4
- Protein disulfide-isomerase A6
- Hypoxia up-regulated protein 1
- Stromal cell-derived factor 2-like 1
- Stromal cell derived factor 2
- Endoplasmic reticulum protein 44.
- Peptidyl-prolyl cis-trans isomerase B
- Mesencephalic astrocyte-derived neurotrophic factor
Sequence:
MAPQNLSTFCLLLLYLIGAVIAGRDFYKILGVPRSASIKDIKKAYRKLALQLHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSSHGDIFSHFFGDFGFMFGGAPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFVEVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHRIFERRGDDLYTNVTVSLVEALVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAKEGIKQLLKQGPVQKVYNGLQGY
Protein: Aldehyde dehydrogenase family 2 member B7, mitochondrial (ALDH2b) (EC 1.2.1.3) (Q8S528)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses activity on acetaldehyde and glycolaldehyde in vitro.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:25732537}.
Interaction partners:
- Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Polyamine oxidase 3
- Probable polyamine oxidase 4
- Nitrilase 2
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 3 member F1
Sequence:
MASRRVSSLLSRSFMSSSRSIFSLRGMNRGAQRYSNLAAAVENTITPPVKVEHTQLLIGGRFVDAVSGKTFPTLDPRNGEVIAQVSEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSKILFRFADLIEKHNDEIAALETWDNGKPYEQSAQIEVPMLARVFRYYAGWADKIHGMTMPGDGPHHVQTLHEPIGVAGQIIPWNFPLLMLSWKLGPALACGNTVVLKTAEQTPLSALLVGKLLHEAGLPDGVVNIVSGFGATAGAAIASHMDVDKVAFTGSTDVGKIILELASKSNLKAVTLELGGKSPFIVCEDADVDQAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRNVGDPFKSGIEQGPQVDSEQFNKILKYIKHGVEAGATLQAGGDRLGSKGYYIQPTVFSDVKDDMLIATDEIFGPVQTILKFKDLDEVIARANNSRYGLAAGVFTQNLDTAHRLMRALRVGTVWINCFDVLDASIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTSLKNPAWL
Protein: AGAMOUS-like 58 (F3M18.11) (Q9SGP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- At5g26880
- AGAMOUS-like 48
- Leucine-rich repeat protein FLOR 1
- Agamous-like MADS-box protein AGL65
- Receptor-like protein kinase HSL1
- AGAMOUS-like 95
Sequence:
MNPKKTKGKQKINIKKIEKDEDRSVTLSKRLNAIYTMIIELSILCGVEVAFIGYSCSGKPYTFGSPSFQAVVERFLNGEASSSSSSSLQRSVKNAHKQAKIQELCKRYNRLVEELKVDEVKVKKAAALAETRAVNKDAWWKADPNDVKDHEKAKKMMEKYQELKEKLREEVALRIKRGHDENNNK
Protein: Nuclear pore complex protein Nup88 (88 kDa nuclear pore complex protein) (Nucleoporin Nup88) (Protein members only) (dNup88) (Q9GYU8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of nuclear pore complex. Required for the anchoring of Nup214 and emb on the nuclear envelope and thereby attenuates nuclear export signal (NES)-mediated nuclear export. Together with Nup214, required for the nuclear import of the Rel family transcription factors dorsal (dl) and Dorsal-related immunity factor (Dif) and the activation of an immune response.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10921908}. Nucleus membrane {ECO:0000269|PubMed:10921908, ECO:0000269|PubMed:17032737}; Peripheral membrane protein {ECO:0000269|PubMed:10921908}; Cytoplasmic side {ECO:0000269|PubMed:10921908}. Chromosome {ECO:0000269|PubMed:20144761}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20144761}. Note=Is recruited to non-active chromatin sites (PubMed:20144761). Localization to the nuclear rim is promoted by Nup214 (PubMed:17032737). {ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:20144761}.
Interaction partners:
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup154
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup107
- Nuclear pore protein
- Nucleoporin Nup35
- Nuclear pore complex protein Nup75
- Nucleoporin 43kD
Sequence:
MSLTDVLELNKTELFAKIRNGLPVVQRTQNLLDCKDDLLFAWHAKDSCLLVRNWRSSLAAKVNIQFQTLIPSSLVSLEVDRVLASNEGSLVALSGPRGVVIMELPRRWGPDGYYKDGKPVITCRTFGLDTQLFLKNPHLEVRQVRWHPHSVSDSTLLVLLNNNTIRVYNHSKLRHVWQVGPPVLRSGANNSLCDFGELAVDFDIAPAAKPRVTEPETAGNNETTLDKSNKTLVAAKSLPKQERIEWPMVVLRENGNIYILMTGVDSENTRLQGPVTITPQAHDNYGLESCALMIIPSLPPTIVIAESNGKLHHALLMEAEATEHSFNEVDDSVLIEPAEYVVHVLETVELELGISAPATGKEGGNCPIYLKRDLINELRYFAYHNAGLHAVTVSFIAELQRYLESESDEDRLELAVSASAEYILCTKFDSSETVNAVFGLALLQIPAGIVLLLGSGQVISLKLVIDAQLLVTPNENKPVDSEVSQQESGPPFVDTIKSLLQRSVNQPILADKLSSPSAQESFELLNQAIEVLREQYLKRHDLVRAAFTRHINQIQLKKEQQLQEIQDLEQERELISERAHKLAERFEEISYNQELLVRKCNALMQRANASLPNSVIAEREFSQEVIRLNKVTQSLAAGLETAKKTFNKQRYHIAQSQEDLKKNAYELPEKQHRTITEILTQLTGEIDRQITDVKRINKIVGI
Protein: Histone deacetylase (EC 3.5.1.98) (Q38C74)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR037913}.
Interaction partners:
- Trans sialidase, putative
- C2H2-type domain-containing protein
- Guanine nucleotide-binding beta subunit-like protein
- Uncharacterized protein
- Histone-binding protein RBBP4-like N-terminal domain-containing protein
- Uncharacterized protein
- Histone H2A
- Structural maintenance of chromosomes protein
- Histone deacetylase, putative
- histone deacetylase
Sequence:
MNEDGDCRRVALIDTSCYSADCTLSALVPQHAMKPYRLLVTMELIASLGLKRFCRTVVPPPIGIKELLTYHAEDYILNLGLHSNRSWLWNTEVSKVTFSGDCPPVEGIVEYSLSTVSGSLMAAVLLNSGAVDTAIHWGGGMHHAKCGECSGFCYVNDIVIAIIELLKCHDRVLYVDLDMHHGDGVDEAFCRSRRVFTLSLHKFGESFFPGTGHPRDVGIGNGRHYTMNLAMWDGVDDFYYTTVFERALRSIVKRFNPNVVVLQCGADSLAGDRLGHFNLSSWGHGKCVEEVKKLGLPMLVVGGGGYTLRNVAKLWAYETSILCGKRLPLNTVIPLHRMPLSGWLFEESPQLLVSQDEENKPLPGVNVQRSFRVIIEQIDKHCPNIMTV
Protein: MKIAA4236 protein (Q5DTF8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
TALPHCDCTSAFSLKVGRFSGPAPRSACIADMEEMLSFRDVAVDFSAEEWECLEPAQWNLYRDVMLENYSHLVFLGLAFSKPYLVTFLEQRQEPLNEKRQVATTMHPDIKPYKCKECGKACDWNSLLLEHQRTNPGENAYKCEECGQASGSYSVIPEHHINDTEEKACKCEECGKVICTCSENSSYQRICIGENPYKCEECGKAFSSHSCLAQHEVEHTGQQFYNCEECGKLFYCPSHLTEHQKIHSQENLFKIEVCSEVFCAPIELSKDQNFCTEEKPYRYEEYVKAFSACSVLSEHPTIHPGEKAFKCEECGNAFCTLHSVSKMKIHYEVKSYKCEECGKAFATHLSLIQHKIGHTREKPYQCEECGKMFYCSSNLKQHQITHSQEKPYKCEVCGKVFRTCWQLSKHLRIHSGEKPYKCEECGKAFYTLSYLTQHKLGHTGEKPYKCEECGKTFYYPSVLKEHLAIHSGEKPYRCDECGKDFCTRSGRSRHQRIHTGEKPYKCEQCGKAFSTHSYLSHHKIVHTGHKPYKCEECGKKFYYPSRLKEHQRIHSQENPYKCEICGKAFYTHSYFTQHKLGHTGEKPYKCEECGKTFYYPSILKEHLAIHSGKKPYRCEECGKDFCTRSGRSRHQRIHTGEKPHKCEECGKVFSTHSYLTQHKVVHSGEKPYKCEECGKKFYYPSRLKEHQRIHSQENPYKCEICGNVFCTPKGLSKHQRFHTGEKPYKCEECGKMFYYPSRLKEHQRIHSQENPYKCEICGKAFYTHSYLTQHKLGHTGEKPYKCEECGKTFYYPSILKEHLAIHSGKKPYRCEECGKDFCTRSGRSRHQRIHTGEKPYKCEQCGKAFSTHSYLSQHKVVHSGEKPYKCEECGKMFYYPSRLKEHQRIHSQENPYKCEVCGKVFSAHLELATHLSIHSG
Protein: Immunoglobulin kappa variable 1-39 (Ig kappa chain V-I region DEE) (Ig kappa chain V-I region Hau) (Ig kappa chain V-I region Mev) (Ig kappa chain V-I region OU) (Ig kappa chain V-I region Walker) (P01597)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMRVPAQLLGLLLLWLRGARCDIQMTQSPSSLSASVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSYSTP
Protein: Large ribosomal subunit protein uL11 (50S ribosomal protein L11) (P36238)
Organism: Thermus thermophilus
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Interaction partners:
Sequence:
MKKVVAVVKLQLPAGKATPAPPVGPALGQHGANIMEFVKAFNAATANMGDAIVPVEITIYADRSFTFVTKTPPASYLIRKAAGLEKGAHKPGREKVGRITWEQVLEIAKQKMPDLNTTDLEAAARMIAGSARSMGVEVVGAPEVKDA
Protein: Carboxysome shell protein CcmK1 (Carbon dioxide-concentrating mechanism protein CcmK1) (Q8DKB3)
Organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Function: One of the shell proteins of the carboxysome, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. Assembles into hexamers which make sheets that form the facets of the polyhedral carboxysome. The hexamer central pore probably regulates metabolite flux.
Subcellular location: Carboxysome {ECO:0000255|HAMAP-Rule:MF_00854, ECO:0000305|PubMed:22748766}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000269|PubMed:22748766}.
Interaction partners:
- Carboxysome shell vertex protein CcmL
- Carboxysome assembly protein CcmM
- Carboxysome shell protein CcmK2
- Carbon dioxide concentrating mechanism protein
- Tlr0311 protein
Sequence:
MAIAVGMIETLGFPAVVEAADAMVKAARVTLVGYEKIGSGRVTVIVRGDVSEVQASVAAGVENVKRVNGGQVLSTHIIARPHENLEYVLPIRYTEAVEQFRESVSGIRPMGRP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I5Y728)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFVSHRQAKAGLGDWTGQALTHKARVTWWGAGLPLNGRYELDSVSDVTGVPEPLVSSHLGIDRACRHGGQGPGKAPPPARWERTWRGLQSLLCTYGQWMALAGPSAALIAVCILLFLLCISQVVALSEASLASLDPIRVASLFLVIGPWVLLGSSVSLF
Protein: Integrin alpha chain (Q7LZ57)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
SNVDVKNAMTFSGPLEDMXVLIGSPLVGQPEKGLVQYSPNLXGEQIGSYFGGVITXIDIVYVYALXKNEPCGARFGTAIAXVDVTIGGLGGAALFWSRFYVLPK
Protein: Chloride channel protein (F4JN11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
Interaction partners:
Sequence:
MAATLPLCAALRSPVSSRRFAPIHKTDVPFQFNVVLSPFFGSVAIGGRIFPRLPAAKQETDQDEVGFDQQPSQELAIASACLVGVLTGVSVVLFNNCVHLLRDFSWDGIPDRGASWLREAPIGSNWLRVILVPTIGGLVVSILNQLRESAGKSTGDSHSSLDRVKAVLRPFLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFNAAVAGCFFAVESVLWPSSSTDSSTSLPNTTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLLLGALCGLVSLALSRCTSSMTSAVDSLNKDAGIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLEKRPFVKGLSADLLLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLALAQNPDFNLSILEVASPQAYGLVGMAATLAGVCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWITSGQSKRQETRETKETRKRKSQEAVQSLTSSDDESSTNNLCEVESSLCLDDSLNQSEELPKSIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKEGNNRPKDIFVNDICSRSGGKCKVPWTVTPDMDLLAAQTIMNKHELSHVAVVSGSIDAPRIHPVGVLDRECITLTRRFPTLDVVEVKLVKKNYLQLFVCSSEERSESQSPGSSNQNVPPKFAVSVNGLAL
Protein: Hemoglobin subunit alpha-A (Alpha-A-globin) (Hemoglobin alpha-A chain) (P01994)
Organism: Gallus gallus (Chicken)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
- Hemoglobin subunit rho
- Hemoglobin subunit beta
- Hemoglobin subunit epsilon
- Beta-H globin
- NPR3 like, GATOR1 complex subunit.
- Transmembrane protein 8A.
- Hemoglobin subunit pi
- LUC7 like.
Sequence:
MVLSAADKNNVKGIFTKIAGHAEEYGAETLERMFTTYPPTKTYFPHFDLSHGSAQIKGHGKKVVAALIEAANHIDDIAGTLSKLSDLHAHKLRVDPVNFKLLGQCFLVVVAIHHPAALTPEVHASLDKFLCAVGTVLTAKYR
Protein: Uncharacterized mitochondrial carrier YPR011C (Q12251)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}.
Interaction partners:
- Large ribosomal subunit protein eL18A
- Uncharacterized mitochondrial carrier YFR045W
Sequence:
MAEVLTVLEQPNSIKDFLKQDSNIAFLAGGVAGAVSRTVVSPFERVKILLQVQSSTTSYNRGIFSSIRQVYHEEGTKGLFRGNGLNCIRIFPYSAVQFVVYEACKKKLFHVNGNNGQEQLTNTQRLFSGALCGGCSVVATYPLDLIKTRLSIQTANLSSLNRSKAKSISKPPGIWQLLSETYRLEGGLRGLYRGVWPTSLGVVPYVALNFAVYEQLREFGVNSSDAQPSWKSNLYKLTIGAISGGVAQTITYPFDLLRRRFQVLAMGGNELGFRYTSVWDALVTIGRAEGVSGYYKGLAANLFKVVPSTAVSWLVYEVVCDSVRNW
Protein: Type-1 angiotensin II receptor (Angiotensin II type-1 receptor) (AT1 receptor) (P30555)
Organism: Sus scrofa (Pig)
Function: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30556}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
Interaction partners:
- Angiotensinogen
- Angiotensin II receptor type 2
- Plasminogen activator inhibitor 1
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- G protein subunit alpha 12
- G protein subunit alpha 13
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 1
- Prothrombin
Sequence:
MILNSSTEDSIKRIQDDCPKAGRHNYIFVMIPTLYSIIFVVGIFGNSLVVIVIYFYMKLKTVASVFLLNLALADLCFLLTLPLWAVYTAMEYRWPFGNYLCKIASASVSFNLYASVFLLTCLSIDRYLAIVHPMKSRLRRTMLVAKVTCIIIWLLAGLASLPTIIHRNVFFIENTNITVCAFHYESQNSTLPVGLGLTKNILGFLFPFLIILTSYTLIWKALKKAYEIQKNKPRNDDIFKIIMAIVLFFFFSWVPHQIFTFLDVLIQLGIIHDCKIADIVDTAMPITICLAYFNNCLNPLFYGFLGKKFKKYFLQLLKYIPPKAKSHSSLSTKMSTLSYRPSENGSSSTKKSAPCTEVE
Protein: CROL BETA (Crooked legs, isoform B) (O61361)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQHVSAASSVPSVVTPVVTTGGTTITLGGPPPLPKSEHKEDGKPPHGIEMYKVNIEDISQLFTYHEVFGKIHGDVVNHQLAAAHGGQLPPPPPLPPQVTSHAASAAAAAAAASTNNAAVAAVMASANAAAAAAAAASAGGGLPPATSGNGGQQVTVTTTSSSTSSGGSTTSGGTTTTAGELLMPKMEGGIHGVDGSGNGGNGGGQNVALAPDGTPIATGTHVCDICGKMFQFRYQLIVHRRYHSERKPFMCQVCGQGFTTSQDLTRHGKIHIGGPMFTCIVCFNVFANNTSLERHMKRHSTDKPFACTICQKTFARKEHLDNHFRSHTGETPFRCQYCAKTFTRKEHMVNHVRKHTGETPHRCDICKKSFTRKEHYVNHYMWHTGQTPHQCDVCGKKYTRKEHLANHMRSHTNETPFRCEICGKSFSRKEHFTNHILWHTGETPHRCDFCSKTFTRKEHLLNHVRQHTGESPHRCSYCMKTFTRKEHLVNHIRQHTGETPFKCTYCTKAFTRKDHMVNHVRQHTGESPHKCTYCTKTFTRKEHLTNHVRQHTGDSPHRCSYCKKTFTRKEHLTNHVRLHTGDSPHKCEYCQKTFTRKEHLNNHMRQHSSDNPHCCNVCNKPFTRKEHLINHMSRCHTGDRPFTCETCGKSFPLKGNLLFHQRSHTKGQEMERPFACEKCPKNFICKVPHHSATTTMHTIQQITAGAAGGAGAVQLTPGLVPLVTSTLISHNAAAQQQSQKQQAAAAAAAQQQAAAAAAAQQQAAQQQAAAAHQQHQQQVAAQHQQQAAVAAHQQQQQQLQQQQQLLQLSIQQAAHHHQQEQHRQQQQQQHQQQQQQQHHQQQQQGHPQAPPPQQQQQPPPIALISDPSALARAAIQLQHLPANVEQHPVVY