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Protein Page:
FREM1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
FREM1 Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development. Defects in FREM1 are the cause of bifid nose with or without anorectal and renal anomalies (BNAR). A bifid nose is a rare congenital deformity due to failure of the paired nasal processes to fuse to a single midline organ during early gestation. BNAR is an autosomal recessive disorder and patients usually present a bifid nose associated with renal and anorectal malformations. Defects in FREM1 are the cause of Manitoba oculotrichoanal syndrome (MOTA). MOTA is a rare condition defined by eyelid colobomas, cryptophthalmos, and anophthalmia/microphthalmia, an aberrant hairline, a bifid or broad nasal tip, and gastrointestinal anomalies such as omphalocele and anal stenosis. Defects in FREM1 are the cause of trigonocephaly type 2 (TRIGNO2). TRIGNO2 is a keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head. Belongs to the FRAS1 family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted
Cellular Component: integral to membrane; basement membrane
Molecular Function: metal ion binding; carbohydrate binding
Biological Process: cell-matrix adhesion; cell communication
Reference #:  Q5H8C1 (UniProtKB)
Alt. Names/Synonyms: BNAR; C9orf143; C9orf145; C9orf154; extracellular matrix protein QBRICK; FLJ25461; FRAS1 related extracellular matrix 1; FRAS1-related extracellular matrix protein 1; FREM1; Protein QBRICK; QBRICK; RP11-439N12.3
Gene Symbols: FREM1
Molecular weight: 244,154 Da
Basal Isoelectric point: 5.55  Predict pI for various phosphorylation states
Select Structure to View Below

FREM1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S43-p KGHSAFLsGDDLKFA
0 1 T112-p KLRLYRFtERDTFIE
0 1 Y163-p KNLLRFDyDRMASLE
0 1 S950-p GVTVDQFsQRDVISE
0 1 S1223-p QKHAPVHsFSMELLK
0 1 S1306-p LSAIDEDsPREKIyY
0 1 Y1312-p DsPREKIyYVFERLP
0 1 Q1570 LQHNFTQQDVDSKNV
0 1 Y1768-p LEIIRRGysMDsAFV
0 1 S1769-p EIIRRGysMDsAFVG
0 1 S1772-p RRGysMDsAFVGIKV
0 1 S1858-p KGGQCHPsySSNQSK
0 1 Y1859-p GGQCHPsySSNQSKH
0 1 S1900-p ERRPLPSsMQLAVIR
0 1 T1910-p LAVIRGDtLRGFDST
0 1 T1943-p SSVYRNGtDIIYNYH
0 1 S1954-p YNYHGIVsLKLEDDS
0 1 T1964-p LEDDSFPtHKRKAKV
0 1 S2142-p TNGRRGPsQRSKLGK
  mouse

 
S49 KGSSAFLSGDHLRVA
T118 KLRLYRFTETDTFME
Y169 KNLLQFDYDRTASLD
S975 GLHVDRFSQGDVISG
S1242 QLQHEIHSFSVDLLK
S1325 LSATDKDSPREKIHY
H1331 DSPREKIHYVFERLP
R1588-m1 LQHNFTQrDVDSGGV
Y1786 LEVTRRGYPMDSAFV
P1787 EVTRRGYPMDSAFVG
S1790 RRGYPMDSAFVGVEV
S1876 KGGRCHPSNSFNQSK
N1877 GGRCHPSNSFNQSKH
- gap
A1922 PSFTSGDALQGFGLT
T1955 SSVCRNGTDTIYNYH
S1966 YNYHGIVSLKLEGDR
A1976 LEGDRFSAHKRKAKI
P2154 TNWRRGAPLHPKPGK
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