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XSB2124 : amphiphysin isoform 2 [Homo sapiens]

[ CaMP Format ]

This entry is computationally expanded from SB0093

* Basic Information

OrganismHomo sapiens (human)
Protein NamesAmphiphysin; amphiphysin isoform 2; 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_647477 NM_139316 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: 653 aa

Average Mass: 71.929 kDa

Monoisotopic Mass: 71.885 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) ---
--- cleavage 489 ---
--- cleavage 567 ---
--- cleavage 551 ---
--- cleavage 485 ---
SH3_1 1. 58365224.10.00017

3. Sequence Information

Fasta Sequence: XSB2124.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

7 [sites]

Cleavage sites (±10aa)

[Site 1] SAQPEAEELE489-ATVPQEKVIP

Glu489 Ala

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ser480Ala481Gln482Pro483Glu484Ala485Glu486Glu487Leu488Glu489
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Ala490Thr491Val492Pro493Gln494Glu495Lys496Val497Ile498Pro499

Sequence conservation (by blast)

[Site 2] APAMGAADQL567-ASAREASQEL

Leu567 Ala

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ala558Pro559Ala560Met561Gly562Ala563Ala564Asp565Gln566Leu567
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Ala568Ser569Ala570Arg571Glu572Ala573Ser574Gln575Glu576Leu577

Sequence conservation (by blast)

[Site 3] 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 4] LATEQKPIQD551-PQPTPSAPAM

Asp551 Pro

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Leu542Ala543Thr544Glu545Gln546Lys547Pro548Ile549Gln550Asp551
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Pro552Gln553Pro554Thr555Pro556Ser557Ala558Pro559Ala560Met561

Sequence conservation (by blast)

[Site 5] EGAESAQPEA485-EELEATVPQE

Ala485 Glu

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Glu476Gly477Ala478Glu479Ser480Ala481Gln482Pro483Glu484Ala485
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Glu486Glu487Leu488Glu489Ala490Thr491Val492Pro493Gln494Glu495

Sequence conservation (by blast)

[Site 6] 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 7] 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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