P49418 (AMPH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amphiphysin

Gene names

Name:	AMPH
Synonyms:	AMPH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	695 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.
Subunit structure	Heterodimer with BIN1. Binds SH3GLB1 and AP2A2 By similarity. Interacts with AP2B1. Ref.8
Subcellular location	Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton.
Tissue specificity	Neurons, certain endocrine cell types and spermatocytes.
Miscellaneous	Antibodies against AMPH are detected in patients with stiff-man syndrome, a rare disease of the central nervous system characterized by progressive rigidity of the body musculature with superimposed painful spasms.
Sequence similarities	Contains 1 BAR domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil SH3 domain
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	actin cytoskeleton Traceable author statement. Source: ProtInc cell junction Inferred from electronic annotation. Source: UniProtKB-KW synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49418-1)

Also known as: 128 kDa;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P49418-2)

Also known as: 108 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     425-466: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 695

695

Amphiphysin

PRO_0000192947

Regions

Domain

24 – 240

217

BAR

Domain

622 – 695

74

SH3

Coiled coil

10 – 83

74

Potential

Coiled coil

144 – 191

48

Potential

Amino acid modifications

Modified residue

6

1

Phosphothreonine Ref.9

Modified residue

250

1

Phosphoserine By similarity

Modified residue

295

1

Phosphoserine By similarity

Modified residue

297

1

Phosphothreonine By similarity

Modified residue

506

1

Phosphoserine By similarity

Natural variations

Alternative sequence

425 – 466

42

Missing in isoform 2.

VSP_000245

Natural variant

218

1

K → E.
Corresponds to variant rs35166354 [ dbSNP | Ensembl ].

VAR_053004

Natural variant

376

1

M → I.
Corresponds to variant rs17171345 [ dbSNP | Ensembl ].

VAR_053005

Natural variant

496

1

K → T. Ref.7
Corresponds to variant rs35024632 [ dbSNP | Ensembl ].

VAR_053006

Secondary structure

1

.

.

.

695

Helix Strand Turn

Details...

Helix

382 – 384

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (128 kDa) [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 78B4F75AB75BA357	FASTA	695	76,257
	10 20 30 40 50 60 MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL 70 80 90 100 110 120 RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT 130 140 150 160 170 180 LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF 190 200 210 220 230 240 EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD 250 260 270 280 290 300 KAFTIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG 310 320 330 340 350 360 PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET LLDLDFDPFK 370 380 390 400 410 420 PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF NGFTQPQDTS LFTMQTDQSM 430 440 450 460 470 480 ICNLAESEQA PPTEPKAEEP LAAVTPAVGL DLGMDTRAEE PVEEAVIIPG ADADAAVGTL 490 500 510 520 530 540 VSAAEGAPGE EAEAEKATVP AGEGVSLEEA KIGTETTEGA ESAQPEAEEL EATVPQEKVI 550 560 570 580 590 600 PSVVIEPASN HEEEGENEIT IGAEPKETTE DAAPPGPTSE TPELATEQKP IQDPQPTPSA 610 620 630 640 650 660 PAMGAADQLA SAREASQELP PGFLYKVETL HDFEAANSDE LTLQRGDVVL VVPSDSEADQ 670 680 690 DAGWLVGVKE SDWLQYRDLA TYKGLFPENF TRRLD
	Isoform 2 (108 kDa) [UniParc]. Checksum: 44C1115E3E70B6A9	FASTA	653	71,929
	10 20 30 40 50 60 MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL 70 80 90 100 110 120 RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT 130 140 150 160 170 180 LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF 190 200 210 220 230 240 EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD 250 260 270 280 290 300 KAFTIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG 310 320 330 340 350 360 PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET LLDLDFDPFK 370 380 390 400 410 420 PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF NGFTQPQDTS LFTMQTDQSM 430 440 450 460 470 480 ICNLIIPGAD ADAAVGTLVS AAEGAPGEEA EAEKATVPAG EGVSLEEAKI GTETTEGAES 490 500 510 520 530 540 AQPEAEELEA TVPQEKVIPS VVIEPASNHE EEGENEITIG AEPKETTEDA APPGPTSETP 550 560 570 580 590 600 ELATEQKPIQ DPQPTPSAPA MGAADQLASA REASQELPPG FLYKVETLHD FEAANSDELT 610 620 630 640 650 LQRGDVVLVV PSDSEADQDA GWLVGVKESD WLQYRDLATY KGLFPENFTR RLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Autoimmunity in stiff-man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161." David C., Solimena M., de Camilli P. FEBS Lett. 351:73-79(1994) [PubMed: 8076697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Cerebellum.
[2]	"Primary structure of human amphiphysin, the dominant autoantigen of paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to chromosome 7p13-p14." Yamamoto R., Li X., Winter S., Francke U., Kilimann M.W. Hum. Mol. Genet. 4:265-268(1995) [PubMed: 7757077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer." Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V. Mol. Med. 4:29-39(1998) [PubMed: 9513187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Mammary gland.
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-496. Tissue: Brain.
[8]	"Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly." Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T. PLoS Biol. 4:E262-E262(2006) [PubMed: 16903783] [Abstract] Cited for: INTERACTION WITH AP2B1.
[9]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"Accessory protein recruitment motifs in clathrin-mediated endocytosis." Brett T.J., Traub L.M., Fremont D.H. Structure 10:797-809(2002) [PubMed: 12057195] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 322-330 IN COMPLEX WITH AP2A2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U07616 mRNA. Translation: AAA21865.1.
X81438 mRNA. Translation: CAA57197.1.
AF034996 mRNA. Translation: AAC02977.1.
AC011309 Genomic DNA. Translation: AAS07391.1.
AC012490 Genomic DNA. Translation: AAS07563.1.
AC007245 Genomic DNA. Translation: AAS07541.1.
CH236951 Genomic DNA. Translation: EAL23989.1.
CH236951 Genomic DNA. Translation: EAL23990.1.
CH471073 Genomic DNA. Translation: EAW94110.1.
CH471073 Genomic DNA. Translation: EAW94111.1.
BC034376 mRNA. Translation: AAH34376.1.

IPI

IPI00305486.
IPI00386245.

PIR

S62400.

RefSeq

NP_001626.1. NM_001635.3.
NP_647477.1. NM_139316.2.

UniGene

Hs.592182.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KY7	X-ray	2.15	P	322-331	[»]
1UTC	X-ray	2.30	P/Q	379-387	[»]
3SOG	X-ray	2.30	A	34-236	[»]
4A3A	X-ray	1.78	A	1-242	[»]

ProteinModelPortal

P49418.

SMR

P49418. Positions 36-235, 614-694.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-109264.

STRING

P49418.

PTM databases

PhosphoSite

P49418.

Polymorphism databases

DMDM

1351924.

Proteomic databases

PRIDE

P49418.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356264; ENSP00000348602; ENSG00000078053.

GeneID

273.

KEGG

hsa:273.

UCSC

uc003tgu.1. human.
uc003tgv.1. human.

Organism-specific databases

CTD

273.

GeneCards

GC07M038423.

H-InvDB

HIX0006613.

HGNC

HGNC:471. AMPH.

HPA

CAB008559.
HPA019828.
HPA019829.

MIM

600418. gene.

neXtProt

NX_P49418.

PharmGKB

PA24779.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG713912.

HOVERGEN

HBG004224.

OMA

MICNLAE.

PhylomeDB

P49418.

Gene expression databases

ArrayExpress

P49418.

Bgee

P49418.

CleanEx

HS_AMPH.

Genevestigator

P49418.

GermOnline

ENSG00000078053. Homo sapiens.

Family and domain databases

InterPro

IPR003005. Amphiphysin.
IPR003017. Amphiphysin_1.
IPR004148. BAR_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

KO

K12562.

Pfam

PF03114. BAR. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR01251. AMPHIPHYSIN.
PR01252. AMPHIPHYSIN1.
PR00452. SH3DOMAIN.

SMART

SM00721. BAR. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS51021. BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1081.

PMAP-CutDB

P49418.

SOURCE

Search...

Entry information

Entry name

AMPH_HUMAN

Accession

Primary (citable) accession number: P49418
Secondary accession number(s): A4D1X8 , A4D1X9, O43538, Q75MJ8, Q75MK5, Q75MM3, Q8N4G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.