ID RIP_HUMAN STANDARD; PRT; 671 AA. AC Q13546; Q13180; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE SERINE/THREONINE PROTEIN KINASE RIP (EC 2.7.1.-) (CELL DEATH PROTEIN DE RIP) (RECEPTOR INTERACTING PROTEIN). GN RIP. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; OC Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=UMBILICAL VEIN ENDOTHELIAL CELLS; RX MEDLINE; 96200892. RA HSU H., HUANG J., SHU H.-B., BAICHWAL V.R., GOEDDEL D.V.; RT "TNF-dependent recruitment of the protein kinase RIP to the TNF RT receptor-1 signaling complex."; RL Immunity 4:387-396(1996). RN [2] RP SEQUENCE OF 300-671 FROM N.A. RX MEDLINE; 95277838. RA STANGER B.Z., LEDER P., LEE T.-H., KIM E., SEED B.; RT "RIP: a novel protein containing a death domain that interacts with RT Fas/APO-1 (CD95) in yeast and causes cell death."; RL Cell 81:513-523(1995). CC -!- FUNCTION: INTERACTS WITH THE DEATH DOMAIN OF FAS AND TRADD AND CC INITIATES APOPTOSIS. IT IS RECRUITED BY TRADD TO TNFR1 IN A TNF- CC DEPENDENT PROCESS. REQUIRED FOR TNFR1 ACTIVATION OF NF-KAPPA B. CC -!- SIMILARITY: WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR- CC PROTEIN KINASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U50062; G1236943; -. DR EMBL; U25994; AAC50137.1; -. DR HSSP; P11362; 1FGI. DR MIM; 603453; -. DR PFAM; PF00069; pkinase; 1. DR PFAM; PF00531; death; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50017; DEATH_DOMAIN; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW Apoptosis. FT DOMAIN 17 289 PROTEIN KINASE. FT NP_BIND 23 31 ATP (BY SIMILARITY). FT BINDING 49 49 ATP (BY SIMILARITY). FT ACT_SITE 138 138 BY SIMILARITY. FT DOMAIN 583 669 DEATH DOMAIN. FT DOMAIN 411 414 POLY-ARG. FT CONFLICT 514 514 T -> S (IN REF. 2). SQ SEQUENCE 671 AA; 76032 MW; E27E74FD CRC32; MQPDMSLNVI KMKSSDFLES AELDSGGFGK VSLCFHRTQG LMIMKTVYKG PNCIEHNEAL LEEAKMMNRL RHSRVVKLLG VIIEEGKYSL VMEYMEKGNL MHVLKAEMST PLSVKGRIIW EIIEGMCYLH GKGVIHKDLK PENILVDNDF HIKIADLGLA SFKMWSKLNN EEHNELREVD GTAKKNGGTL YYMAPEHLND VNAKPTEKSD VYSFAVVLWA IFANKEPYEN AICEQQLIMC IKSGNRPDVD DITEYCPREI ISLMKLCWEA NPEARPTFPG IEEKFRPFYL SQLEESVEED VKSLKKEYSN ENAVVKRMQS LQLDCVAVPS SRSNSATEQP GSLHSSQGLG MGPVEESWFA PSLEHPQEEN EPSLQSKLQD EANYHLYGSR MDRQTKQQPR QNVAYNREEE RRRRVSHDPF AQQRPYENFQ NTEGKGTVYS SAASHGNAVH QPSGLTSQPQ VLYQNNGLYS SHGFGTRPLD PGTAGPRVWY RPIPSHMPSL HNIPVPETNY LGNTPTMPFS SLPPTDESIK YTIYNSTGIQ IGAYNYMEIG GTSSSLLDST NTNFKEEPAA KYQAIFDNTT SLTDKHLDPI RENLGKHWKN CARKLGFTQS QIDEIDHDYE RDGLKEKVYQ MLQKWVMREG IKGATVGKLA QALHQCSRID LLSSLIYVSQ N //