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XSB2082 : amphiphysin isoform 1 [Homo sapiens]

[ CaMP Format ]

This entry is computationally expanded from SB0093

* Basic Information

OrganismHomo sapiens (human)
Protein NamesAmphiphysin; amphiphysin isoform 1; Stiff-Man syndrome with breast cancer 128kDa autoantigen; amphiphysin (Stiff-Mann syndrome with breast cancer 128kD autoantigen)
Gene NamesAMPH; AMPH1; amphiphysin
Gene Locus7p14-p13; chromosome 7
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001626 NM_001635 273 P49418 600418 471 N/A hsa:273

* Information From OMIM

Function: David et al. (1994) found that the N- and C-terminal domains of the amphiphysin protein are highly conserved between chicken and human. Autoantibodies from patients with the stiff-man syndrome show a dominant autoepitope located in the C-terminal region, which contains an SH3 domain.

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* Structure Information

1. Primary Information

Length: 695 aa

Average Mass: 76.257 kDa

Monoisotopic Mass: 76.210 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
BAR 1. 13233288.11.9e-83
Drf_FH1 1. 250397-40.24.3
--- cleavage 333 (inside Drf_FH1 250..397) ---
--- cleavage 392 (inside Drf_FH1 250..397) ---
--- cleavage 377 (inside Drf_FH1 250..397) ---
Ribosomal_60s 1. 431508-34.96.9
--- cleavage 454 (inside Ribosomal_60s 431..508) ---
--- cleavage 478 (inside Ribosomal_60s 431..508) ---
--- cleavage 531 ---
--- cleavage 609 ---
--- cleavage 593 ---
--- cleavage 527 ---
SH3_1 1. 62569424.10.00017

3. Sequence Information

Fasta Sequence: XSB2082.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1KY7 (X-ray; 215 A; P=322-331), 1UTC (X-ray; 230 A; P/Q=379-387)

* Cleavage Information

9 [sites]

Cleavage sites (±10aa)

[Site 1] TPAVGLDLGM454-DTRAEEPVEE

Met454 Asp

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Thr445Pro446Ala447Val448Gly449Leu450Asp451Leu452Gly453Met454
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Asp455Thr456Arg457Ala458Glu459Glu460Pro461Val462Glu463Glu464

Sequence conservation (by blast)

[Site 2] SAQPEAEELE531-ATVPQEKVIP

Glu531 Ala

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ser522Ala523Gln524Pro525Glu526Ala527Glu528Glu529Leu530Glu531
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Ala532Thr533Val534Pro535Gln536Glu537Lys538Val539Ile540Pro541

Sequence conservation (by blast)

[Site 3] APAMGAADQL609-ASAREASQEL

Leu609 Ala

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ala600Pro601Ala602Met603Gly604Ala605Ala606Asp607Gln608Leu609
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Ala610Ser611Ala612Arg613Glu614Ala615Ser616Gln617Glu618Leu619

Sequence conservation (by blast)

[Site 4] PGADADAAVG478-TLVSAAEGAP

Gly478 Thr

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Pro469Gly470Ala471Asp472Ala473Asp474Ala475Ala476Val477Gly478
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Thr479Leu480Val481Ser482Ala483Ala484Glu485Gly486Ala487Pro488

Sequence conservation (by blast)

[Site 5] FEDNFVPEIS333-VTTPSQNEVP

Ser333 Val

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Phe324Glu325Asp326Asn327Phe328Val329Pro330Glu331Ile332Ser333
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Val334Thr335Thr336Pro337Ser338Gln339Asn340Glu341Val342Pro343

Sequence conservation (by blast)

[Site 6] LATEQKPIQD593-PQPTPSAPAM

Asp593 Pro

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Leu584Ala585Thr586Glu587Gln588Lys589Pro590Ile591Gln592Asp593
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Pro594Gln595Pro596Thr597Pro598Ser599Ala600Pro601Ala602Met603

Sequence conservation (by blast)

[Site 7] EGAESAQPEA527-EELEATVPQE

Ala527 Glu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Glu518Gly519Ala520Glu521Ser522Ala523Gln524Pro525Glu526Ala527
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Glu528Glu529Leu530Glu531Ala532Thr533Val534Pro535Gln536Glu537

Sequence conservation (by blast)

[Site 8] DLWTTSTDLV392-QPASGGSFNG

Val392 Gln

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Asp383Leu384Trp385Thr386Thr387Ser388Thr389Asp390Leu391Val392
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Gln393Pro394Ala395Ser396Gly397Gly398Ser399Phe400Asn401Gly402

Sequence conservation (by blast)

[Site 9] SAGVTHSPMS377-QTLPWDLWTT

Ser377 Gln

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ser368Ala369Gly370Val371Thr372His373Ser374Pro375Met376Ser377
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Gln378Thr379Leu380Pro381Trp382Asp383Leu384Trp385Thr386Thr387

Sequence conservation (by blast)

* References

[PubMed ID: 18206907] Hou T, Zhang W, Case DA, Wang W, Characterization of domain-peptide interaction interface: a case study on the amphiphysin-1 SH3 domain. J Mol Biol. 2008 Feb 29;376(4):1201-14. Epub 2008 Jan 3.

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