entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
P01034 | CYTC_HUMAN | Cystatin-C (Cystatin-3) (Gamma-trace) (Neuroendocrine basic polypeptide) (Post-gamma-globulin) | MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA | As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity. |
P01036 | CYTS_HUMAN | Cystatin-S (Cystatin-4) (Cystatin-SA-III) (Salivary acidic protein 1) | MARPLCTLLLLMATLAGALASSSKEENRIIPGGIYDADLNDEWVQRALHFAISEYNKATEDEYYRRPLQVLRAREQTFGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWEDRMSLVNSRCQEA | This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively. |
P01037 | CYTN_HUMAN | Cystatin-SN (Cystain-SA-I) (Cystatin-1) (Salivary cystatin-SA-1) | MAQYLSTLLLLLATLAVALAWSPKEEDRIIPGGIYNADLNDEWVQRALHFAISEYNKATKDDYYRRPLRVLRARQQTVGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWENRRSLVKSRCQES | Human saliva appears to contain several cysteine proteinase inhibitors that are immunologically related to cystatin S but that differ in their specificity due to amino acid sequence differences. Cystatin SN, with a pI of 7.5, is a much better inhibitor of papain and dipeptidyl peptidase I than is cystatin S, although b... |
P01040 | CYTA_HUMAN | Cystatin-A (Cystatin-AS) (Stefin-A) [Cleaved into: Cystatin-A, N-terminally processed] | MIPGGLSEAKPATPEIQEIVDKVKPQLEEKTNETYGKLEAVQYKTQVVAGTNYYIKVRAGDNKYMHLKVFKSLPGQNEDLVLTGYQVDKNKDDELTGF | This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis. |
P01041 | CYTB_RAT | Cystatin-B (Cystatin-beta) (Liver thiol proteinase inhibitor) (Stefin-B) | MMCGAPSATMPATTETQEIADKVKSQLEEKANQKFDVFKAISFRRQVVAGTNFFIKVDVGEEKCVHLRVFEPLPHENKPLTLSSYQTDKEKHDELTYF | This is an intracellular thiol proteinase inhibitor. |
P01042 | KNG1_HUMAN | Kininogen-1 (Alpha-2-thiol proteinase inhibitor) (Fitzgerald factor) (High molecular weight kininogen) (HMWK) (Williams-Fitzgerald-Flaujeac factor) [Cleaved into: Kininogen-1 heavy chain; T-kinin (Ile-Ser-Bradykinin); Bradykinin (Kallidin I); Lysyl-bradykinin (Kallidin II); Kininogen-1 light chain; Low molecular weight... | MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFID... | Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombo... |
P01044 | KNG1_BOVIN | Kininogen-1 (Kininogen I) (Thiol proteinase inhibitor) [Cleaved into: Kininogen-1 heavy chain; Bradykinin (Kallidin I); Lysyl-bradykinin (Kallidin II); Kininogen-1 light chain] | MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGECTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQRQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPVKDFVQPPTRLCAGCPKPIPVDSPDLEEPLSHSIAKLNAEHDGAFYFKIDTVKKATVQVVAGLKYSIVF... | Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombo... |
P01045 | KNG2_BOVIN | Kininogen-2 (Kininogen II) (Thiol proteinase inhibitor) [Cleaved into: Kininogen-2 heavy chain; Bradykinin (Kallidin I); Lysyl-bradykinin (Kallidin II); Kininogen-2 light chain] | MKLITILFLCSRLLPSLTQESSQEIDCNDQDVFKAVDAALTKYNSENKSGNQFVLYRITEVARMDNPDTFYSLKYQIKEGDCPFQSNKTWQDCDYKDSAQAATGQCTATVAKRGNMKFSVAIQTCLITPAEGPVVTAQYECLGCVHPISTKSPDLEPVLRYAIQYFNNNTSHSHLFDLKEVKRAQKQVVSGWNYEVNYSIAQTNCSKEEFSFLTPDCKSLSSGDTGECTDKAHVDVKLRISSFSQKCDLYPGEDFLPPMVCVGCPKPIPVDSPDLEEALNHSIAKLNAEHDGTFYFKIDTVKKATVQVVGGLKYSIVFIA... | (1) Kininogens are inhibitors of thiol proteases (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes (4) the active peptide bradykinin that ... |
P01048 | KNT1_RAT | T-kininogen 1 (Alpha-1-MAP) (Major acute phase protein) (T-kininogen I) (Thiostatin) [Cleaved into: T-kininogen 1 heavy chain (T-kininogen I heavy chain); T-kinin; T-kininogen 1 light chain (T-kininogen I light chain)] | MKLITILLLCSRLLPSLAQEEGAQELNCNDETVFQAVDTALKKYNAELESGNQFVLYRVTEGTKKDGAETLYSFKYQIKEGNCSVQSGLTWQDCDFKDAEEAATGECTTTLGKKENKFSVATQICNITPGKGPKKTEEDLCVGCFQPIPMDSSDLKPVLKHAVEHFNNNTKHTHLFALREVKSAHSQVVAGMNYKIIYSIVQTNCSKEDFPSLREDCVPLPYGDHGECTGHTHVDIHNTIAGFSQSCDLYPGDDLFELLPKNCRGCPREIPVDSPELKEALGHSIAQLNAQHNHIFYFKIDTVKKATSQVVAGVIYVIEF... | Kininogens are plasma glycoproteins with a number of functions: (1) as precursor of the active peptide bradykinin they effect smooth muscle contraction, induction of hypotension and increase of vascular permeability. (2) They play a role in blood coagulation by helping to position optimally prekallikrein and factor XI ... |
P01050 | HIRV1_HIRME | Hirudin variant-1 (Hirudin-1) (Hirudin-I) (Lepirudin) | VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ | Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen. |
P01083 | IAA2_WHEAT | Alpha-amylase inhibitor 0.28 (CIII) (WMAI-1) | MWMKTVFWGLLVFMLVATTMAVEYGARSHNSGPWSWCNPATGYKVSALTGCRAMVKLQCVGSQVPEAVLRDCCQQLADINNEWCRCGDLSSMLRSVYQELGVREGKEVLPGCRKEVMKLTAASVPEVCKVPIPNPSGDRAGVCYGDWAAYPDV | Alpha-amylase inhibitor. |
P01089 | 2SS_RICCO | 2S seed storage albumin protein (2S albumin) (allergen Ric c 1/3) [Cleaved into: Allergen Ric c 3 small chain (4.7 kDa napin-like protein small chain) (CB-1A small chain) (RS1A); Allergen Ric c 3 large chain (CB-1A large chain) (RL1); Allergen Ric c 1 small chain (2S albumin small chain) (4 kDa napin-like protein small... | MAKLIPTIALVSVLLFIIANASFAYRTTITTIEIDESKGEREGSSSQQCRQEVQRKDLSSCERYLRQSSSRRSPGEEVLRMPGDENQQQESQQLQQCCNQVKQVRDECQCEAIKYIAEDQIQQGQLHGEESERVAQRAGEIVSSCGVRCMRQTRTNPSQQGCRGQIQEQQNLRQCQEYIKQQVSGQGPRRSDNQERSLRGCCDHLKQMQSQCRCEGLRQAIEQQQSQGQLQGQDVFEAFRTAANLPSMCGVSPTECRF | 2S seed storage proteins. |
P01094 | IPA3_YEAST | Protease A inhibitor 3 (Proteinase inhibitor I(A)3) (Proteinase yscA-inhibitor) (Saccharopepsin inhibitor) | MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE | Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. |
P01096 | ATIF1_BOVIN | ATPase inhibitor, mitochondrial (ATP synthase F1 subunit epsilon) (Inhibitor of F(1)F(o)-ATPase) (IF(1)) (IF1) | MAATALAARTRQAVWSVWAMQGRGFGSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIERLQKEIERHKQSIKKLKQSEDDD | Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts... |
P01097 | ATIF_YEAST | F(1)-ATPase inhibitor IF(1), mitochondrial (ATPase inhibitory factor 1) (IF(1)) (IF1) | MLPRSALARSLQLQRGVAARFYSEGSTGTPRGSGSEDSFVKRERATEDFFVRQREKEQLRHLKEQLEKQRKKIDSLENKIDSMTK | Endogenous ATPase inhibitor, which inhibits specifically the reverse ATPase reaction of mitochondrial F(1)F(0)-type ATP synthase. It limits ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(0)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix... |
P01100 | FOS_HUMAN | Protein c-Fos (Cellular oncogene fos) (Fos proto-oncogene, AP-1 transcription factor subunit) (G0/G1 switch regulatory protein 7) (Proto-oncogene c-Fos) (Transcription factor AP-1 subunit c-Fos) | MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATEL... | Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding s... |
P01101 | FOS_MOUSE | Protein c-Fos (Cellular oncogene fos) (FBJ osteosarcoma oncogene) (Transcription factor AP-1 subunit c-Fos) | MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTQSAGAYARAGMVKTVSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEASTPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPDVDLSGSFYAADWEPLHSNSLGMGPMVTEL... | Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By similarity). Has a critical function in regulating the dev... |
P01106 | MYC_HUMAN | Myc proto-oncogene protein (Class E basic helix-loop-helix protein 39) (bHLHe39) (Proto-oncogene c-Myc) (Transcription factor p64) | MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTH... | Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, contro... |
P01108 | MYC_MOUSE | Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64) | MDFLWALETPQTATTMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTH... | Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, contro... |
P01109 | MYC_CHICK | Myc proto-oncogene protein (c-Myc) | MASLRLAAGALEEPAAAAAMPLSASLPSKNYDYDYDSVQPYFYFEEEEENFYLAAQQRGSELQPPAPSEDIWKKFELLPTPPLSPSRRSSLAAASCFPSTADQLEMVTELLGGDMVNQSFICDPDDESFVKSIIIQDCMWSGFSAAAKLEKVVSEKLATYQASRREGGPAAASRPGPPPSGPPPPPAGPAASAGLYLHDLGAAAADCIDPSVVFPYPLSERAPRAAPPGANPAALLGVDTPPTTSSDSEEEQEEDEEIDVVTLAEANESESSTESSTEASEEHCKPHHSPLVLKRCHVNIHQHNYAAPPSTKVEYPAAKR... | Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. |
P01111 | RASN_HUMAN | GTPase NRas (EC 3.6.5.2) (Transforming protein N-Ras) | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM | Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. |
P01112 | RASH_HUMAN | GTPase HRas (EC 3.6.5.2) (H-Ras-1) (Ha-Ras) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed] | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS | Involved in the activation of Ras protein signal transduction. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. |
P01116 | RASK_HUMAN | GTPase KRas (EC 3.6.5.2) (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed] | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM | Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the regulation of cell proliferation. Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner. |
P01119 | RAS1_YEAST | Ras-like protein 1 (EC 3.6.5.2) | MQGNKSTIREYKIVVVGGGGVGKSALTIQFIQSYFVDEYDPTIEDSYRKQVVIDDKVSILDILDTAGQEEYSAMREQYMRTGEGFLLVYSVTSRNSFDELLSYYQQIQRVKDSDYIPVVVVGNKLDLENERQVSYEDGLRLAKQLNAPFLETSAKQAINVDEAFYSLIRLVRDDGGKYNSMNRQLDNTNEIRDSELTSSATADREKKNNGSYVLDNSLTNAGTGSSSKSAVNHNGETTKRTDEKNYVNQNNNNEGNTKYSSNGNGNRSDISRGNQNNALNSRSKQSAEPQKNSSANARKESSGGCCIIC | The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP. |
P01120 | RAS2_YEAST | Ras-like protein 2 (EC 3.6.5.2) | MPLNKSNIREYKLVVVGGGGVGKSALTIQLTQSHFVDEYDPTIEDSYRKQVVIDDEVSILDILDTAGQEEYSAMREQYMRNGEGFLLVYSITSKSSLDELMTYYQQILRVKDTDYVPIVVVGNKSDLENEKQVSYQDGLNMAKQMNAPFLETSAKQAINVEEAFYTLARLVRDEGGKYNKTLTENDNSKQTSQDTKGSGANSVPRNSGGHRKMSNAANGKNVNSSTTVVNARNASIESKTGLAGNQATNGKTQTDRTNIDNSTGQAGQANAQSANTVNNRVNNNSKAGQVSNAKQARKQQAAPGGNTSEASKSGSGGCCI... | The S.cerevisiae Ras proteins modulate the activity of the adenylate cyclase catalytic subunit and therefore affect the biosynthesis of cyclic-AMP. |
P01123 | YPT1_YEAST | GTP-binding protein YPT1 (Protein YP2) (Rab GTPase YPT1) (Transport GTPase YPT1) | MNSEYDYLFKLLLIGNSGVGKSCLLLRFSDDTYTNDYISTIGVDFKIKTVELDGKTVKLQIWDTAGQERFRTITSSYYRGSHGIIIVYDVTDQESFNGVKMWLQEIDRYATSTVLKLLVGNKCDLKDKRVVEYDVAKEFADANKMPFLETSALDSTNVEDAFLTMARQIKESMSQQNLNETTQKKEDKGNVNLKGQSLTNTGGGCC | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsi... |
P01127 | PDGFB_HUMAN | Platelet-derived growth factor subunit B (PDGF subunit B) (PDGF-2) (Platelet-derived growth factor B chain) (Platelet-derived growth factor beta polypeptide) (Proto-oncogene c-Sis) (Becaplermin) | MNRCWALFLSLCCYLRLVSAEGDPIPEELYEMLSDHSIRSFDDLQRLLHGDPGEEDGAELDLNMTRSHSGGELESLARGRRSLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVTRSPGGSQEQRAKTPQTRVTIRTVRVRRPPKGKHRKFKHTHDKTALKETLGA | Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous syste... |
P01129 | CDC10_SCHPO | Start control protein cdc10 | MASANFIRQFELGNDSFSYQKRPEDEPSQPLSNRNINKLNDSSTLKDSSSRIFINSQVLRDGRPVELYAVECSGMKYMELSCGDNVALRRCPDSYFNISQILRLAGTSSSENAKELDDIIESGDYENVDSKHPQIDGVWVPYDRAISIAKRYGVYEILQPLISFNLDLFPKFSKQQQIESSSISKNLNTSSFNTRSPLRNHNFSNPSKSSKNGVHTINNMQSSPSPSSSFLLPLTQIDSQNVKRSNNYLSTSPPILEQRLKRHRIDVSDEDLHPSSQLNDNEASSLFPDTPRLNHSLSFVSLVSSLPPLDQNIMQDYHTS... | Major component of the cell cycle transcription factor complex MBF (MCB binding factor, also known as DSC1), that controls G1-S phase specific gene expression. Involved in the control of rRNA production, via interaction with pol5. May be involved in the transcriptional regulation of the cdc22 and cdt1 genes. In fission... |
P01130 | LDLR_HUMAN | Low-density lipoprotein receptor (LDL receptor) | MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLD... | Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct ... |
P01131 | LDLR_BOVIN | Low-density lipoprotein receptor (LDL receptor) | MRLAGWGLRWAIALLIAVGEAAVEDNCGRNEFQCQDGKCISYKWVCDGTAECQDGSDESQETCKSVTCKMGDFSCGGRVNRCISGSWRCDGQVDCENGSDEEGCSPKTCSQDEFRCNDGKCIAPKFVCDLDLDCLDGSDEASCPMPTCGPANFQCNSSMCIPQLWACDGDPDCDDGSDEWPKHCGTPHPSGPLQDNNPCSALEFHCGSGECIHSSWHCDHDPDCKDKSDEENCAVATCRPDEFQCSDGTCIHGSRQCDREPDCKDLSDELGCVNVTLCEGPNKFKCQSGECISLDKVCNSVRDCRDWSDEPLKDCGTNEC... | Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. |
P01132 | EGF_MOUSE | Pro-epidermal growth factor (EGF) [Cleaved into: Epidermal growth factor] | MPWGRRPTWLLLAFLLVFLKISILSVTAWQTGNCQPGPLERSERSGTCAGPAPFLVFSQGKSISRIDPDGTNHQQLVVDAGISADMDIHYKKERLYWVDVERQVLLRVFLNGTGLEKVCNVERKVSGLAIDWIDDEVLWVDQQNGVITVTDMTGKNSRVLLSSLKHPSNIAVDPIERLMFWSSEVTGSLHRAHLKGVDVKTLLETGGISVLTLDVLDKRLFWVQDSGEGSHAYIHSCDYEGGSVRLIRHQARHSLSSMAFFGDRIFYSVLKSKAIWIANKHTGKDTVRINLHPSFVTPGKLMVVHPRAQPRTEDAAKDPD... | EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By similarity). |
P01133 | EGF_HUMAN | Pro-epidermal growth factor (EGF) [Cleaved into: Epidermal growth factor (Urogastrone)] | MLLTLIILLPVVSKFSFVSLSAPQHWSCPEGTLAGNGNSTCVGPAPFLIFSHGNSIFRIDTEGTNYEQLVVDAGVSVIMDFHYNEKRIYWVDLERQLLQRVFLNGSRQERVCNIEKNVSGMAINWINEEVIWSNQQEGIITVTDMKGNNSHILLSALKYPANVAVDPVERFIFWSSEVAGSLYRADLDGVGVKALLETSEKITAVSLDVLDKRLFWIQYNREGSNSLICSCDYDGGSVHISKHPTQHNLFAMSLFGDRIFYSTWKMKTIWIANKHTGKDMVRINLHSSFVPLGELKVVHPLAQPKAEDDTWEPEQKLCKL... | EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite... |
P01134 | TGFA_RAT | Protransforming growth factor alpha [Cleaved into: Transforming growth factor alpha (TGF-alpha) (EGF-like TGF) (ETGF) (TGF type 1)] | MVPAAGQLALLALGILVAVCQALENSTSPLSDSPVAAAVVSHFNKCPDSHTQYCFHGTCRFLVQEEKPACVCHSGYVGVRCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALVCRHEKPSALLKGRTACCHSETVV | TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar. |
P01135 | TGFA_HUMAN | Protransforming growth factor alpha [Cleaved into: Transforming growth factor alpha (TGF-alpha) (EGF-like TGF) (ETGF) (TGF type 1)] | MVPSAGQLALFALGIVLAACQALENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVCHSGYVGARCEHADLLAVVAASQKKQAITALVVVSIVALAVLIITCVLIHCCQVRKHCEWCRALICRHEKPSALLKGRTACCHSETVV | TGF alpha is a mitogenic polypeptide that is able to bind to the EGF receptor/EGFR and to act synergistically with TGF beta to promote anchorage-independent cell proliferation in soft agar. |
P01136 | VGF_VACCW | Pro-Viral epidermal growth factor (Pro-VGF) [Cleaved into: Viral epidermal growth factor (VGF) (Secreted epidermal growth factor-like)] | MSMKYLMLLFAAMIIRSFADSGNAIETTSPEITNATTDIPAIRLCGPEGDGYCLHGDCIHARDIDGMYCRCSHGYTGIRCQHVVLVDYQRSENPNTTTSYIPSPGIMLVLVGIIIITCCLLSVYRFTRRTKLPIQDMVVP | [Viral epidermal growth factor]: Stimulates cellular proliferation (hyperplasia)and mobility around infected cells to promote rapid and efficient spread of infection. This effect is beneficial for virus replication in vivo, because poxviruses replicate possibly better in proliferating cells than in quiescent cells. Act... |
P01137 | TGFB1_HUMAN | Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)] | MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. [Latency-associated peptide]: Required to maintain the Transforming growth factor be... |
P01138 | NGF_HUMAN | Beta-nerve growth factor (Beta-NGF) | MSMLFYTLITAFLIGIQAEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNITVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRSSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA | Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable). The immature NGF precursor (proNG... |
P01139 | NGF_MOUSE | Beta-nerve growth factor (Beta-NGF) | MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG | Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems. Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival. The immature NGF precursor (proNGF) function... |
P01143 | CRF_RAT | Corticoliberin (Corticotropin-releasing factor) (CRF) (Corticotropin-releasing hormone) | MRLRLLVSAGMLLVALSPCLPCRALLSRGSVSGAPRAPQPLNFLQPEQPQQPQPILIRMGEEYFLRLGNLNRSPAARLSPNSTPLTAGRGSRPSHDQAAANFFRVLLQQLQMPQRPLDSSTELAERGAEDALGGHQGALERERRSEEPPISLDLTFHLLREVLEMARAEQLAQQAHSNRKLMEIIGK | Hormone regulating the release of corticotropin from pituitary gland. Induces NLRP6 in intestinal epithelial cells, hence may influence gut microbiota profile (By similarity). |
P01148 | GON1_HUMAN | Progonadoliberin-1 (Progonadoliberin I) [Cleaved into: Gonadoliberin-1 (Gonadoliberin I) (Gonadorelin) (Gonadotropin-releasing hormone I) (GnRH-I) (Luliberin I) (Luteinizing hormone-releasing hormone I) (LH-RH I); GnRH-associated peptide 1 (GnRH-associated peptide I)] | MKPIQKLLAGLILLTWCVEGCSSQHWSYGLRPGGKRDAENLIDSFQEIVKEVGQLAETQRFECTTHQPRSPLRDLKGALESLIEEETGQKKI | Stimulates the secretion of gonadotropins it stimulates the secretion of both luteinizing and follicle-stimulating hormones. |
P01150 | TRH_RAT | Pro-thyrotropin-releasing hormone (Pro-TRH) (Prothyroliberin) [Cleaved into: Thyrotropin-releasing hormone (TRH) (Protirelin) (TSH-releasing factor) (Thyroliberin) (Thyrotropin-releasing factor) (TRF)] | MPGPWLLLALALIFTLTGIPESCALPEAAQEEGAVTPDLPGLENVQVRPERRFLWKDLQRVRGDLGAALDSWITKRQHPGKREEEEKDIEAEERGDLGEGGAWRLHKRQHPGRRANQDKYSWADEEDSDWMPRSWLPDFFLDSWFSDVPQVKRQHPGRRSFPWMESDVTKRQHPGRRFIDPELQRSWEEKEGEGVLMPEKRQHPGKRALGHPCGPQGTCGQTGLLQLLGDLSRGQETLVKQSPQVEPWDKEPLEE | Functions as a regulator of the biosynthesis of TSH in the anterior pituitary gland and as a neurotransmitter/ neuromodulator in the central and peripheral nervous systems. |
P01160 | ANF_HUMAN | Natriuretic peptides A (Atrial natriuretic factor prohormone) (proANF) (Atrial natriuretic peptide prohormone) (preproANP) (proANP) (Atriopeptigen) (Cardiodilatin) (CDD) (preproCDD-ANF) [Cleaved into: Long-acting natriuretic peptide (LANP) (Long-acting natriuretic hormone) (LANH) (Pro atrial natriuretic factor 1-30) (p... | MSSFSTTTVSFLLLLAFQLLGQTRANPMYNAVSNADLMDFKNLLDHLEEKMPLEDEVVPPQVLSEPNEEAGAALSPLPEVPPWTGEVSPAQRDGGALGRGPWDSSDRSALLKSKLRALLTAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRY | [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism. Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biol... |
P01161 | ANF_RAT | Natriuretic peptides A (Atrial natriuretic factor prohormone) (preproANF) (proANF) (Atrial natriuretic peptide prohormone) (preproANP) (proANP) (Atriopeptigen) (Cardiodilatin) (CDD) (preproCDD-ANF) [Cleaved into: Long-acting natriuretic peptide (LANP) (Long-acting natriuretic hormone) (LANH) (Pro atrial natriuretic fac... | MGSFSITKGFFLFLAFWLPGHIGANPVYSAVSNTDLMDFKNLLDHLEEKMPVEDEVMPPQALSEQTDEAGAALSSLSEVPPWTGEVNPSQRDGGALGRGPWDPSDRSALLKSKLRALLAGPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR | [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that dr... |
P01165 | 7B2_PIG | Neuroendocrine protein 7B2 (Secretogranin V) (Secretogranin-5) (Secretory granule endocrine protein I) [Cleaved into: N-terminal peptide; C-terminal peptide] | MVSTMLSGLVLWLTFGWTPALAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNTPKDFSEDQGYPDPPNPCPIGKTDDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE | Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also requir... |
P01175 | NEU1_BOVIN | Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] | MAGSSLACCLLGLLALTSACYIQNCPLGGKRAVLDLDVRTCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCSPDGCHEDPACDPEAAFSQH | Neurophysin 1 specifically binds oxytocin. Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (By similarity). |
P01178 | NEU1_HUMAN | Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] | MAGPSLACCLLGLLALTSACYIQNCPLGGKRAAPDLDVRKCLPCGPGGKGRCFGPNICCAEELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEATFSQR | Neurophysin 1 specifically binds oxytocin. Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR). |
P01179 | NEU1_RAT | Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] | MACPSLACCLLGLLALTSACYIQNCPLGGKRAALDLDMRKCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCATAGICCSPDGCRTDPACDPESAFSER | Neurophysin 1 specifically binds oxytocin. Oxytocin causes contraction of the smooth muscle of the uterus and of the mammary gland. Acts by binding to oxytocin receptor (OXTR) (By similarity). |
P01180 | NEU2_BOVIN | Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Arg-vasopressin (Arginine-vasopressin); Neurophysin 2 (Neurophysin-II); Copeptin] | MPDATLPACFLSLLAFTSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCNDESCVTEPECREGVGFPRRVRANDRSNATLLDGPSGALLLRLVQLAGAPEPAEPAQPGVY | Neurophysin 2 specifically binds vasopressin. Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). |
P01183 | NEU2_PIG | Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Lys-vasopressin; Neurophysin 2 (Neurophysin-I/-III); Copeptin] | MPDATLPACFLGLLALTSACYFQNCPKGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCGDELGCFVGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCNDESCVTEPECREGASFLRRARASDRSNATLLDGPSGALLLRLVQLAGAPEPAEPAQPGVY | Neurophysin 2 specifically binds vasopressin. Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). |
P01185 | NEU2_HUMAN | Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Arg-vasopressin (Arginine-vasopressin); Neurophysin 2 (Neurophysin-II); Copeptin] | MPDTMLPACFLGLLAFSSACYFQNCPRGGKRAMSDLELRQCLPCGPGGKGRCFGPSICCADELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAAFGVCCNDESCVTEPECREGFHRRARASDRSNATQLDGPAGALLLRLVQLAGAPEPFEPAQPDAY | [Neurophysin 2]: Specifically binds vasopressin. [Arg-vasopressin]: Has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2). |
P01186 | NEU2_RAT | Vasopressin-neurophysin 2-copeptin (AVP-NPII) [Cleaved into: Arg-vasopressin (Arginine-vasopressin); Neurophysin 2 (Neurophysin-I); Copeptin] | MLAMMLNTTLSACFLSLLALTSACYFQNCPRGGKRATSDMELRQCLPCGPGGKGRCFGPSICCADELGCFLGTAEALRCQEENYLPSPCQSGQKPCGSGGRCAAAGICCSDESCVAEPECREGFFRLTRAREQSNATQLDGPARELLLRLVQLAGTQESVDSAKPRVY | Neurophysin 2 specifically binds vasopressin. Vasopressin has a direct antidiuretic action on the kidney, it also causes vasoconstriction of the peripheral vessels. Acts by binding to vasopressin receptors (V1bR/AVPR1B, V1aR/AVPR1A, and V2R/AVPR2) (By similarity). |
P01189 | COLI_HUMAN | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Potential peptide; Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-L... | MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPMFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSSGSSGAGQKREDVSAGEDCGPLPEGGPEPRSDGAKPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRLREGDGPDGPADDGAGAQADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production... |
P01190 | COLI_BOVIN | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gam... | MPRLCSSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLACIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNGSSSSGVGGAAQKREEEVAVGEGPGPRGDDAETGPREDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEFKRELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Beta-endorphin]: Endogenous orexigenic opiate. [Met-enkephalin]: Endogenous opiate. |
P01191 | COLI_SHEEP | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gam... | MPRLCSSRSGALLLVLLLQASMEVRGWCLESSQCQDLTTESNLLACIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNGSSSFGAGGAAQKREEEVAVGEGPGPRGDGAETGPREDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAQAFPLEFKRELTGERLEQARGPEAQAESAAARAELEYGLVAEAEAAEKKDSGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production... |
P01192 | COLI_PIG | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gam... | MPRLCGSRSGALLLTLLLQASMGVRGWCLESSQCQDLSTESNLLACIRACKPDLSAETPVFPGNGDAQPLTENPRKYVMGHFRWDRFGRRNGSSSGGGGGGGGAGQKREEEEVAAGEGPGPRGDGVAPGPRQDKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDELAEAFPLEFRRELAGAPPEPARDPEAPAEGAAARAELEYGLVAEAEAAEKKDEGPYKMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIVKNAHKKGQ | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production... |
P01193 | COLI_MOUSE | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-LPH); Lipotropin gam... | MPRFCYSRSGALLLALLLQTSIDVWSWCLESSQCQDLTTESNLLACIRACKLDLSLETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGPRNSSSAGSAAQRRAEEEAVWGDGSPEPSPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNVAENESAEAFPLEFKRELEGERPLGLEQVLESDAEKDDGPYRVEHFRWSNPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAHKKGQ | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production... |
P01194 | COLI_RAT | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Potential peptide; Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-L... | MPRFCNSRSGALLLALLLQTSIDVWSWCLESSQCQDLTTESNLLACIRACRLDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGPRNSSSAGGSAQRRAEEETAGGDGRPEPSPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNVAENESAEAFPLEFKRELEGEQPDGLEQVLEPDTEKADGPYRVEHFRWGNPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNVHKKGQ | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production... |
P01201 | COLI_MACNE | Pro-opiomelanocortin (POMC) (Corticotropin-lipotropin) [Cleaved into: NPP; Melanotropin gamma (Gamma-MSH); Potential peptide; Corticotropin (Adrenocorticotropic hormone) (ACTH); Melanocyte-stimulating hormone alpha (Alpha-MSH) (Melanotropin alpha); Corticotropin-like intermediary peptide (CLIP); Lipotropin beta (Beta-L... | MPRSCCSRSGALLLALLLQASMEVRGWCLESSQCQDLTTESNLLECIRACKPDLSAETPVFPGNGDEQPLTENPRKYVMGHFRWDRFGRRNSSSGSAHQKREDVAAGEDRGLLPEGGPEPRGDGAGPGPREGKRSYSMEHFRWGKPVGKKRRPVKVYPNGAEDESAEAFPLEFKRELTGQRPRAGDGPDGPADDGAGPRADLEHSLLVAAEKKDEGPYRMEHFRWGSPPKDKRYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGQ | [Corticotropin]: Stimulates the adrenal glands to release cortisol. [Melanocyte-stimulating hormone alpha]: Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes. [Melanocyte-stimulating hormone beta]: Increases the pigmentation of skin by increasing melanin production... |
P01210 | PENK_HUMAN | Proenkephalin-A [Cleaved into: Synenkephalin; Met-enkephalin (Opioid growth factor) (OGF); PENK(114-133); PENK(143-183); Met-enkephalin-Arg-Gly-Leu; Leu-enkephalin; PENK(237-258); Met-enkephalin-Arg-Phe] | MARFLTLCTWLLLLGPGLLATVRAECSQDCATCSYRLVRPADINFLACVMECEGKLPSLKIWETCKELLQLSKPELPQDGTSTLRENSKPEESHLLAKRYGGFMKRYGGFMKKMDELYPMEPEEEANGSEILAKRYGGFMKKDAEEDDSLANSSDLLKELLETGDNRERSHHQDGSDNEEEVSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEALPSDEEGESYSKEVPEMEKRYGGFMRF | [Met-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. [Leu-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of phy... |
P01211 | PENK_BOVIN | Proenkephalin-A [Cleaved into: Synenkephalin; Met-enkephalin (Opioid growth factor) (OGF); PENK(111-130); PENK(140-179); Met-enkephalin-Arg-Gly-Leu; Leu-enkephalin; Enkelytin; PENK(233-254); Met-enkephalin-Arg-Phe] | MARFLGLCTWLLALGPGLLATVRAECSQDCATCSYRLARPTDLNPLACTLECEGKLPSLKTWETCKELLQLTKLELPPDATSALSKQEESHLLAKKYGGFMKRYGGFMKKMDELYPLEVEEEANGGEVLGKRYGGFMKKDAEEDDGLGNSSNLLKELLGAGDQREGSLHQEGSDAEDVSKRYGGFMRGLKRSPHLEDETKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAEPLPSEEEGESYSKEVPEMEKRYGGFMRF | [Met-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. [Leu-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of phy... |
P01213 | PDYN_HUMAN | Proenkephalin-B (Beta-neoendorphin-dynorphin) (Preprodynorphin) [Cleaved into: Alpha-neoendorphin; Beta-neoendorphin; Big dynorphin (Big Dyn); Dynorphin A(1-17) (Dyn-A17) (Dynorphin A); Dynorphin A(1-13); Dynorphin A(1-8); Leu-enkephalin; Rimorphin (Dynorphin B) (Dyn-B) (Dynorphin B(1-13)); Leumorphin (Dynorphin B-29)] | MAWQGLVLAACLLMFPSTTADCLSRCSLCAVKTQDGPKPINPLICSLQCQAALLPSEEWERCQSFLSFFTPSTLGLNDKEDLGSKSVGEGPYSELAKLSGSFLKELEKSKFLPSISTKENTLSKSLEEKLRGLSDGFREGAESELMRDAQLNDGAMETGTLYLAEEDPKEQVKRYGGFLRKYPKRSSEVAGEGDGDSMGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQEDPNAYSGELFDA | Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 ... |
P01214 | PDYN_PIG | Proenkephalin-B (Beta-neoendorphin-dynorphin) (Preprodynorphin) [Cleaved into: Alpha-neoendorphin; Beta-neoendorphin; Big dynorphin (Big Dyn); Dynorphin A(1-17) (Dyn-A17) (Dynorphin A); Dynorphin A(1-13); Dynorphin A(1-8); Leu-enkephalin; Rimorphin (Dynorphin B) (Dyn-B) (Dynorphin B(1-13)); Leumorphin (Dynorphin B-29)] | MAWQGLLLAACLLVLPSTMADCLSGCSLCAVKTQDGPKPINPLICSLECQAALQPAEEWERCQGLLSFLAPLSLGLEGKEDLESKAALEEPSSELVKYMGPFLKELEKNRFLLSTPAEETSLSRSLVEKLRSLPGRLGEETESELMGDAQQNDGAMEAAALDSSVEDPKEQVKRYGGFLRKYPKRSSEVAGEGDGDRDKVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQEDPNAYYEELFDV | Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a typical opioid activity, it is 700 ... |
P01215 | GLHA_HUMAN | Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Choriogonadotropin alpha chain) (Chorionic gonadotrophin subunit alpha) (CG-alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin a... | MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS | Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. These hormones bind specific receptors on target cells that in turn activate downstream signaling pat... |
P01216 | GLHA_MOUSE | Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin alpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha) (Thyrotropin alpha... | MDYYRKYAAVILVMLSMFLHILHSLPDGDFIIQGCPECKLKENKYFSKLGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNARVENHTECHCSTCYYHKS | Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. |
P01222 | TSHB_HUMAN | Thyrotropin subunit beta (Thyroid-stimulating hormone subunit beta) (TSH-B) (TSH-beta) (Thyrotropin beta chain) (Thyrotropin alfa) | MTALFLMSMLFGLTCGQAMSFCIPTEYTMHIERRECAYCLTINTTICAGYCMTRDINGKLFLPKYALSQDVCTYRDFIYRTVEIPGCPLHVAPYFSYPVALSCKCGKCNTDYSDCIHEAIKTNYCTKPQKSYLVGFSV | Indispensable for the control of thyroid structure and metabolism. |
P01223 | TSHB_BOVIN | Thyrotropin subunit beta (Thyroid-stimulating hormone subunit beta) (TSH-B) (TSH-beta) (Thyrotropin beta chain) | MTATFLMSMIFGLACGQAMSFCIPTEYMMHVERKECAYCLTINTTVCAGYCMTRDVNGKLFLPKYALSQDVCTYRDFMYKTAEIPGCPRHVTPYFSYPVAISCKCGKCNTDYSDCIHEAIKTNYCTKPQKSYMVGFSI | Indispensable for the control of thyroid structure and metabolism. |
P01225 | FSHB_HUMAN | Follitropin subunit beta (Follicle-stimulating hormone beta subunit) (FSH-B) (FSH-beta) (Follitropin beta chain) | MKTLQFFFLFCCWKAICCNSCELTNITIAIEKEECRFCISINTTWCAGYCYTRDLVYKDPARPKIQKTCTFKELVYETVRVPGCAHHADSLYTYPVATQCHCGKCDSDSTDCTVRGLGPSYCSFGEMKE | Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and sperma... |
P01229 | LSHB_HUMAN | Lutropin subunit beta (Lutropin beta chain) (Luteinizing hormone subunit beta) (LH-B) (LSH-B) (LSH-beta) | MEMLQGLLLLLLLSMGGAWASREPLRPWCHPINAILAVEKEGCPVCITVNTTICAGYCPTMMRVLQAVLPPLPQVVCTYRDVRFESIRLPGCPRGVDPVVSFPVALSCRCGPCRRSTSDCGGPKDHPLTCDHPQLSGLLFL | Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. |
P01231 | LSHB_SHEEP | Lutropin subunit beta (Lutropin beta chain) (Interstitial cell-stimulating hormone) (Luteinizing hormone subunit beta) (LH-B) (LSH-B) (LSH-beta) [Cleaved into: LH beta-1; LH beta-2; LH beta-3] | MEMLQGLLLWLLLGVAGVWASRGPLRPLCQPINATLAAEKEACPVCITFTTSICAGYCLSMKRVLPVILPPMPQRVCTYHELRFASVRLPGCPPGVDPMVSFPVALSCHCGPCRLSSTDCGGPRTQPLACDHPPLPDILFL | Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. The LH alpha 3/LH beta 3 heterodimer was shown to have potent renotropic and weak gonadotropic activity. |
P01236 | PRL_HUMAN | Prolactin (PRL) | MNIKGSPWKGSLLLLLVSNLLLCQSVAPLPICPGGAARCQVTLRDLFDRAVVLSHYIHNLSSEMFSEFDKRYTHGRGFITKAINSCHTSSLATPEDKEQAQQMNQKDFLSLIVSILRSWNEPLYHLVTEVRGMQEAPEAILSKAVEIEEQTKRLLEGMELIVSQVHPETKENEIYPVWSGLPSLQMADEESRLSAYYNLLHCLRRDSHKIDNYLKLLKCRIIHNNNC | Prolactin acts primarily on the mammary gland by promoting lactation. |
P01237 | PRL_RAT | Prolactin (PRL) | MNSQVSARKAGTLLLLMMSNLLFCQNVQTLPVCSGGDCQTPLPELFDRVVMLSHYIHTLYTDMFIEFDKQYVQDREFIAKAINDCPTSSLATPEDKEQAQKVPPEVLLNLILSLVHSWNDPLFQLITGLGGIHEAPDAIISRAKEIEEQNKRLLEGIEKIISQAYPEAKGNEIYLVWSQLPSLQGVDEESKDLAFYNNIRCLRRDSHKVDNYLKFLRCQIVHKNNC | Prolactin acts primarily on the mammary gland by promoting lactation. |
P01238 | PRL_PIG | Prolactin (PRL) | MDNRGSSQKGSLLLLLLLVSNLFLCKSVASLPICPSGAVNCQVSLRDLFDRAVILSHYIHNLSSEMFNEFDKRYAQGRGFITKAINSCHTSSLSTPEDKEQAQQIHHEVLLNLILRVLRSWNDPLYHLVTEVRGMQEAPDAILSRAIEIEEQNKRLLEGMEKIVGQVHPGIKENEVYSVWSGLPSLQMADEDTRLFAFYNLLHCLRRDSHKIDNYLKLLKCRIIYDSNC | Prolactin acts primarily on the mammary gland by promoting lactation. |
P01239 | PRL_BOVIN | Prolactin (PRL) | MDSKGSSQKGSRLLLLLVVSNLLLCQGVVSTPVCPNGPGNCQVSLRDLFDRAVMVSHYIHDLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGAPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARYSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC | Prolactin acts primarily on the mammary gland by promoting lactation. |
P01240 | PRL_SHEEP | Prolactin (PRL) | MDSKGSAQKGSRLLLLLVVSNLLLCQGVVSTPVCPNGPGNCQVSLRDLFDRAVMVSHYIHNLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGVPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARHSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC | Prolactin acts primarily on the mammary gland by promoting lactation, mammogenesis, mitogenesis and osmoregulation. |
P01241 | SOMA_HUMAN | Somatotropin (Growth hormone) (GH) (GH-N) (Growth hormone 1) (Pituitary growth hormone) | MATGSRTSLLLAFGLLCLPWLQEGSAFPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. |
P01242 | SOM2_HUMAN | Growth hormone variant (GH-V) (Growth hormone 2) (Placenta-specific growth hormone) | MAAGSRTSLLLAFGLLCLSWLQEGSAFPTIPLSRLFDNAMLRARRLYQLAYDTYQEFEEAYILKEQKYSFLQNPQTSLCFSESIPTPSNRVKTQQKSNLELLRISLLLIQSWLEPVQLLRSVFANSLVYGASDSNVYRHLKDLEEGIQTLMWRLEDGSPRTGQIFNQSYSKFDTKSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. |
P01244 | SOMA_RAT | Somatotropin (Growth hormone) | MAADSQTPWLLTFSLLCLLWPQEAGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKEEAQQRTDMELLRFSLLLIQSWLGPVQFLSRIFTNSLMFGTSDRVYEKLKDLEEGIQALMQELEDGSPRIGQILKQTYDKFDANMRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFAESSCAF | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. |
P01246 | SOMA_BOVIN | Somatotropin (Growth hormone) | MMAAGPRTSLLLAFALLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDGTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. |
P01248 | SOMA_PIG | Somatotropin (Growth hormone) | MAAGPRTSALLAFALLCLPWTREVGAFPAMPLSSLFANAVLRAQHLHQLAADTYKEFERAYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILKQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF | Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues. |
P01256 | CALCA_RAT | Calcitonin gene-related peptide 1 (Alpha-type CGRP) (Calcitonin gene-related peptide I) (CGRP-I) | MGFLKFSPFLVVSILLLYQACGLQAVPLRSTLESSPGMAATLSEEEARLLLAALVQNYMQMKVRELEQEQEAEGSSVTAQKRSCNTATCVTHRLAGLLSRSGGVVKDNFVPTNVGSEAFGRRRRDLQA | CGRP induces vasodilation. It dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role. |
P01257 | CALC_RAT | Calcitonin | MGFLKFSPFLVVSILLLYQACGLQAVPLRSTLESSPGMATLSEEEARLLAALVQNYMQMKVRELEQEEEQEAEGSSLDSPRSKRCGNLSTCMLGTYTQDLNKFHTFPQTSIGVGAPGKKRDMAKDLETNHHPYFGN | Causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones. |
P01258 | CALC_HUMAN | Calcitonin [Cleaved into: Calcitonin; Katacalcin (Calcitonin carboxyl-terminal peptide) (CCP) (PDN-21)] | MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN | Calcitonin causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones. Katacalcin is a potent plasma calcium-lowering peptide. |
P01266 | THYG_HUMAN | Thyroglobulin (Tg) | MALVLEIFTLLASICWVSANIFEYQVDAQPLRPCELQRETAFLKQADYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLSFCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRCPRSCEIRNRRLLHGVGDKSPPQCSAEGEFMPVQCKFVNTTDMMIFDLVHSYNRFPDAFVTFSSFQRRFPEVSGYCHCADSQGRELAETGLELLLDEIYDTIFAGLDLPSTFTETTLYRILQRRFLAVQSVISGRFRCPTKCEVERFTATSFGHPYVPSCR... | Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling in the thyroid follicle lumen. Following TG re-internalization and lysosoma... |
P01267 | THYG_BOVIN | Thyroglobulin (Tg) | MALALWVFGLLDLICLASANIFEYQVDAQPLRPCELQRERAFLKREDYVPQCAEDGSFQTVQCGKDGASCWCVDADGREVPGSRQPGRPAACLSFCQLQKQQILLSSYINSTATSYLPQCQDSGDYSPVQCDLRRRQCWCVDAEGMEVYGTRQQGRPARCPRSCEIRNRRLLHGVGDRSPPQCSPDGAFRPVQCKLVNTTDMMIFDLVHSYSRFPDAFVTFSSFRSRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDLASTFAETTLYRILQRRFLAVQLVISGRFRCPTKCEVERFAATSFRHPYVPSCH... | Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization and lysoso... |
P01269 | PTHY_PIG | Parathyroid hormone (PTH) (Parathyrin) | MMSAKDTVKVMVVMLAICFLARSDGKPIKKRSVSEIQLMHNLGKHLSSLERVEWLRKKLQDVHNFVALGASIVHRDGGSQRPRKKEDNVLVESHQKSLGEADKAAVDVLIKAKPQ | PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells (By similarity). |
P01270 | PTHY_HUMAN | Parathyroid hormone (PTH) (Parathormone) (Parathyrin) | MIPAKDMAKVMIVMLAICFLTKSDGKSVKKRSVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNFVALGAPLAPRDAGSQRPRKKEDNVLVESHEKSLGEADKADVNVLTKAKSQ | PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells. |
P01272 | GLUC_BOVIN | Pro-glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)] | MKSLYFVAGLFVMLVQGSWQRSLQNTEEKSSSFPAPQTDPLGDPDQINEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVNIVEELRRRHADGSFSDEMNTVLDSLATRDFINWLLQTKITDRK | [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyp... |
P01274 | GLUC_PIG | Pro-glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)] | MKTIYFVAGLFVMLVQGSWQRSLQNTEEKSRSFPAPQTDPLDDPDQMTEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNKNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVTIVEELRRRHADGSFSDEMNTVLDNLATRDFINWLLHTKITDSL | [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyp... |
P01275 | GLUC_HUMAN | Pro-glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1) (Incretin hormone); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)] | MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK | [Glucagon]: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyp... |
P01282 | VIP_HUMAN | VIP peptides [Cleaved into: Intestinal peptide PHV-42 (Peptide histidine valine 42); Intestinal peptide PHM-27 (Peptide histidine methioninamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] | MDTRNKAQLLVLLTLLSVLFSQTSAWPLYRAPSALRLGDRIPFEGANEPDQVSLKEDIDMLQNALAENDTPYYDVSRNARHADGVFTSDFSKLLGQLSAKKYLESLMGKRVSSNISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGESPDFPEELEK | VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. PHM and PHV also cause vasodilation. PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitoni... |
P01283 | VIP_RAT | VIP peptides [Cleaved into: Intestinal peptide PHV-42; Intestinal peptide PHI-27 (Peptide histidine isoleucinamide 27); Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide)] | MESRSKPQFLAILTLFSVLFSQSLAWPLYGPPSSVRLDDRLQFEGAGDPDQVSLKADSDILQNALAENDTPYYDVSRNARHADGVFTSDYSRLLGQISAKKYLESLIGKRISSSISEDPVPVKRHSDAVFTDNYTRLRKQMAVKKYLNSILNGKRSSEGDSPDFLEELEK | VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder. PHM-27 is a potent agonist of the calcitonin receptor CALCR, with similar efficacy as calcitonin (By similarity). PHI also causes vas... |
P01286 | SLIB_HUMAN | Somatoliberin (Growth hormone-releasing factor) (GRF) (Growth hormone-releasing hormone) (GHRH) (Somatocrinin) (Somatorelin) (Sermorelin) | MPLWVFFFVILTLSNSSHCSPPPPLTLRMRRYADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQERGARARLGRQVDSMWAEQKQMELESILVALLQKHSRNSQG | GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone. |
P01289 | TKN1_BOVIN | Protachykinin-1 (PPT) [Cleaved into: Substance P; Neurokinin A (NKA) (Neuromedin L) (Substance K); Neuropeptide K (NPK); Neuropeptide gamma; C-terminal-flanking peptide] | MKILVAVAVIFFISTQLSAEEIGANDDFNYWSDWSDSDQIKEEMPEPFEHLLQRIARRPKPQQFFGLMGKRDADSSIEKQVALLKALYGHGQLSHKRHKTDSFVGLMGKRALNSVAYERSVMQDYERRRK | Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. |
P01297 | NMB_PIG | Neuromedin-B [Cleaved into: Neuromedin-B-32; Neuromedin-B-30; Neuromedin-B] | MTLRARGARLLGGLLFFTLLAAGAAPLSWDLPEPRSRAGKIRVHPRGNLWATGHFMGKKSLEPPNPSLLGTTHHISLRDQRLQLSHDLLRILLQKKALGLSLSGPASHTPYRRLLVQTLEK | Stimulates smooth muscle contraction. Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity). Contributes to the induction of sneezing following exposure to chemical irrit... |
P01298 | PAHO_HUMAN | Pancreatic polypeptide prohormone (PH) (Pancreatic polypeptide Y) (Obinepitide) [Cleaved into: Pancreatic polypeptide (HPP) (PP); Pancreatic icosapeptide (PI)] | MAAARLCLSLLLLSTCVALLLQPLLGAQGAPLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRYGKRHKEDTLAFSEWGSPHAAVPRELSPLDL | [Pancreatic polypeptide]: Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions probably by signaling through the G protein-coupled receptor NPY4R2. |
P01303 | NPY_HUMAN | Pro-neuropeptide Y [Cleaved into: Neuropeptide Y (Neuropeptide tyrosine) (NPY); C-flanking peptide of NPY (CPON)] | MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW | NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. |
P01304 | NPY_PIG | Pro-neuropeptide Y [Cleaved into: Neuropeptide Y (Neuropeptide tyrosine) (NPY); C-flanking peptide of NPY (CPON)] | VCLCALAEAYPSKPDNPGEDAPAEDLARYYSALRHYINLITRQRYGKRSSPETLISDLLMREGTENVPRTRLEDPS | NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. |
P01308 | INS_HUMAN | Insulin [Cleaved into: Insulin B chain; Insulin A chain] | MALWMRLLPLLALLALWGPDPAAAFVNQHLCGSHLVEALYLVCGERGFFYTPKTRREAEDLQVGQVELGGGPGAGSLQPLALEGSLQKRGIVEQCCTSICSLYQLENYCN | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. |
P01315 | INS_PIG | Insulin [Cleaved into: Insulin B chain; Insulin A chain] | MALWTRLLPLLALLALWAPAPAQAFVNQHLCGSHLVEALYLVCGERGFFYTPKARREAENPQAGAVELGGGLGGLQALALEGPPQKRGIVEQCCTSICSLYQLENYCN | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. |
P01317 | INS_BOVIN | Insulin [Cleaved into: Insulin B chain; Insulin A chain] | MALWTRLRPLLALLALWPPPPARAFVNQHLCGSHLVEALYLVCGERGFFYTPKARREVEGPQVGALELAGGPGAGGLEGPPQKRGIVEQCCASVCSLYQLENYCN | Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. |
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