Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01464
Entry Name
UniProt Accession
Theoretical PI
7.23
Molecular Weight
67565.44
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Leucine zipper putative tumor suppressor 1
Protein Synonyms/Alias
PSD-Zip70;
Gene Name
Lzts1
Gene Synonyms/Alias
Created Date
13-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGSVSSLIS
[1]
N-Myristoylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Konno D, Ko JA, Usui S, Hori K, Maruoka H, Inui M, Fujikado T, Tano Y, Suzuki T, Tohyama K, Sobue K. The postsynaptic density and dendritic raft localizationof PSD-Zip70, which contains an N-myristoylation sequence and leucine-zippermotifs. J Cell Sci. 2002 Dec 1;115(Pt 23):4695-706.[PMID:12415013]
Functional Description
Involved in the regulation of cell growth. May stabilize the active CDC2-cyclin B1 complex and thereby contribute to the regulation of the cell cycle and the prevention of uncontrolled cell proliferation. May act as tumor suppressor (By similarity).
Sequence Annotation
Protein Length
601 AA.
Protein Sequence
(Canonical)
MGSVSSLISG HSLHSKHCRA SQYKLRKSSH LKKLNRYSDG LLRFGFSQDS GRGKSSSKMG  60
KSEDFFYIKV SQKARGSHRP DYTALSSGDM GGQTGVDFDP ATPPKLMPFS SQLEMSSDKA  120
AVRPTAFKPV LPRSGAILHS SPESTNHQLH PMPPDKPKEQ ELKPGLCSGA LSDSGRNSMS  180
SLPTHSTTSS YQLDPLVTPV GPTSRFGGSA HNITQGIILQ DSNMMSLKAL SFSDGGSKLA  240
HPGKVEKGSS CVRSPLSTDE CTIQELEQKL LQRETALQKL QRSFDEKEFA SGQTFEERPR  300
RTRDELECLE PKSKLKPASQ KSQRTQQVLQ LQVLQLQQEK RQLRQELESL MKEQDLLETK  360
LRSYEREKTN FAPALEETQW EVCQKSGEIS LLKQQLKESQ MEVNAKASEI LSLKAQLKDT  420
RGKLEGMELK TQDLESALRT KGLELEVCEN ELQRKKNEAE LLREKVNLLE QELLELRAQA  480
ALHRDAAPLG PPGIGLTFSE DIPALQRELD RLRAELKEER QGHDQMSSGF QHERLVWKEE  540
KEKVIQYQKQ LQQSYLAMYQ RNQRLEKALQ QLARGDIAGE PFEIDLEGAD IPYEDIIATE  600
I                                                                  601
FASTA
(Canonical)
>LipidDB-10116-01464|Q8CFC9
MGSVSSLISGHSLHSKHCRASQYKLRKSSHLKKLNRYSDGLLRFGFSQDSGRGKSSSKMG
KSEDFFYIKVSQKARGSHRPDYTALSSGDMGGQTGVDFDPATPPKLMPFSSQLEMSSDKA
AVRPTAFKPVLPRSGAILHSSPESTNHQLHPMPPDKPKEQELKPGLCSGALSDSGRNSMS
SLPTHSTTSSYQLDPLVTPVGPTSRFGGSAHNITQGIILQDSNMMSLKALSFSDGGSKLA
HPGKVEKGSSCVRSPLSTDECTIQELEQKLLQRETALQKLQRSFDEKEFASGQTFEERPR
RTRDELECLEPKSKLKPASQKSQRTQQVLQLQVLQLQQEKRQLRQELESLMKEQDLLETK
LRSYEREKTNFAPALEETQWEVCQKSGEISLLKQQLKESQMEVNAKASEILSLKAQLKDT
RGKLEGMELKTQDLESALRTKGLELEVCENELQRKKNEAELLREKVNLLEQELLELRAQA
ALHRDAAPLGPPGIGLTFSEDIPALQRELDRLRAELKEERQGHDQMSSGFQHERLVWKEE
KEKVIQYQKQLQQSYLAMYQRNQRLEKALQQLARGDIAGEPFEIDLEGADIPYEDIIATE
I
Gene Ontology
GO:0016324; C:apical plasma membrane; IDA:RGD
GO:0044297; C:cell body; IDA:RGD
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005737; C:cytoplasm; IEA:UniProtKB-KW
GO:0043198; C:dendritic shaft; IDA:RGD
GO:0043197; C:dendritic spine; IDA:RGD
GO:0043005; C:neuron projection; IDA:RGD
GO:0014069; C:postsynaptic density; IDA:RGD
GO:0045211; C:postsynaptic membrane; IDA:RGD
GO:0045202; C:synapse; IDA:RGD
GO:0007049; P:cell cycle; IEA:UniProtKB-KW
GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl
GO:0048814; P:regulation of dendrite morphogenesis; IMP:RGD
GO:0048167; P:regulation of synaptic plasticity; IMP:RGD
Interpro
Pfam
SMART
PROSITE
PRINTS