O00499 (BIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myc box-dependent-interacting protein 1

Alternative name(s):
Amphiphysin II
Amphiphysin-like protein
Box-dependent myc-interacting protein 1
Bridging integrator 1

Gene names

Name:	BIN1
Synonyms:	AMPHL

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	593 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation.
Subunit structure	Heterodimer with AMPH. Binds SH3GLB1 By similarity. Interacts (via SH3 domain) with SYNJ1. Interacts (via SH3 domain) with DNM1. Isoform IIA interacts with CLTC. Isoform IIB does not interact with CLTC. Isoform IIC1 does not interact with CLTC. Isoform IIC2 does not interact with CLTC. Interacts with AP2A2. Interacts with AP2B1. Interacts with MYC (via N-terminal transactivation domain); the interaction requires the integrity of the conserved MYC box regions 1 and 2. Interacts with BIN2. Interacts (SH3 domain) with HCV NS5A. Ref.5 Ref.14 Ref.17
Subcellular location	Isoform BIN1: Nucleus. Isoform IIA: Cytoplasm.
Tissue specificity	Ubiquitous. Highest expression in the brain and muscle. Isoform IIA is expressed only in the brain where it is concentrated in axon initial segments and nodes of Ranvier. Isoform BIN1 is widely expressed with highest expression in skeletal muscle. Ref.14
Post-translational modification	Phosphorylated by protein kinase C By similarity. Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Involvement in disease	Defects in BIN1 are the cause of centronuclear myopathy autosomal recessive (ARCNM) [MIM:255200]; also known as autosomal recessive myotubular myopathy. Centronuclear myopathies are congenital muscle disorders characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. Ref.23
Sequence similarities	Contains 1 BAR domain. Contains 1 SH3 domain.
Sequence caution	The sequence AAC23441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Differentiation Endocytosis Host-virus interaction
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Tumor suppressor
Domain	Coiled coil SH3 domain
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell proliferation Traceable author statement. Source: ProtInc endocytosis Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	actin cytoskeleton Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BIN2	Q9UBW5	2	EBI-719094,EBI-2042570
DLGAP4	Q9Y2H0	4	EBI-719094,EBI-722139
FBP1	P09467	4	EBI-719094,EBI-712740
XRCC4	Q13426	4	EBI-719094,EBI-717592

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform IIA (identifier: O00499-1)

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 IIB (identifier: O00499-2)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     378-421: Missing.

Isoform IIC1 (identifier: O00499-3)

The sequence of this isoform differs from the canonical sequence as follows:
     335-421: Missing.

Isoform IIC2 (identifier: O00499-4)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     335-421: Missing.

Isoform IID (identifier: O00499-5)

The sequence of this isoform differs from the canonical sequence as follows:
     335-377: Missing.

Isoform II2 (identifier: O00499-6)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     378-457: Missing.

Isoform II3 (identifier: O00499-7)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     335-457: Missing.

Isoform BIN1 (identifier: O00499-8)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     285-285: P → PRKKSKLFSRLRRKKN
     335-457: Missing.

Isoform BIN1-10-13 (identifier: O00499-9)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     335-487: Missing.

Isoform BIN1-13 (identifier: O00499-10)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     285-285: P → PRKKSKLFSRLRRKKN
     335-487: Missing.

Isoform BIN1+12A (identifier: O00499-11)

The sequence of this isoform differs from the canonical sequence as follows:
     174-204: Missing.
     285-285: P → PRKKSKLFSRLRRKKN
     378-457: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 593

593

Myc box-dependent-interacting protein 1

PRO_0000192951

Regions

Domain

29 – 276

248

BAR

Domain

520 – 592

73

SH3

Region

1 – 122

122

Interaction with BIN2

Region

378 – 421

44

Clathrin-binding

Coiled coil

15 – 42

28

Potential

Coiled coil

193 – 267

75

Potential

Amino acid modifications

Modified residue

296

1

Phosphoserine Ref.15 Ref.16 Ref.19 Ref.21 Ref.22

Modified residue

298

1

Phosphoserine Ref.15 Ref.16 Ref.18 Ref.21 Ref.22

Modified residue

303

1

Phosphoserine Ref.15 Ref.16 Ref.21 Ref.22

Modified residue

307

1

Phosphothreonine Ref.20 Ref.21

Modified residue

323

1

Phosphothreonine Ref.21

Modified residue

331

1

Phosphoserine Ref.16 Ref.21

Natural variations

Alternative sequence

174 – 204

31

Missing in isoform IIB, isoform IIC2, isoform II2, isoform II3, isoform BIN1, isoform BIN1+12A, isoform BIN1-10-13 and isoform BIN1-13.

VSP_000246

Alternative sequence

285

1

P → PRKKSKLFSRLRRKKN in isoform BIN1, isoform BIN1+12A and isoform BIN1-13.

VSP_000247

Alternative sequence

335 – 487

153

Missing in isoform BIN1-10-13 and isoform BIN1-13.

VSP_000251

Alternative sequence

335 – 457

123

Missing in isoform II3 and isoform BIN1.

VSP_000250

Alternative sequence

335 – 421

87

Missing in isoform IIC1 and isoform IIC2.

VSP_000249

Alternative sequence

335 – 377

43

Missing in isoform IID.

VSP_000248

Alternative sequence

378 – 457

80

Missing in isoform II2 and isoform BIN1+12A.

VSP_000253

Alternative sequence

378 – 421

44

Missing in isoform IIB.

VSP_000252

Natural variant

35

1

K → N in ARCNM; abolishes membrane tubulation. Ref.23

VAR_037425

Natural variant

151

1

D → N in ARCNM; abolishes membrane tubulation. Ref.23

VAR_037426

Experimental info

Sequence conflict

474

1

A → P in AAB63263. Ref.2

Sequence conflict

481

1

A → S in AAC24126. Ref.10

Sequence conflict

481

1

A → S in AAC23750. Ref.10

Sequence conflict

481

1

A → S in AAC23751. Ref.10

Sequence conflict

510

1

S → C in AAC23440. Ref.7

Sequence conflict

510

1

S → C in AAC23441. Ref.7

Sequence conflict

528

1

Q → H in AAC23440. Ref.7

Sequence conflict

528

1

Q → H in AAC23441. Ref.7

Sequence conflict

576

1

E → K in AAC23440. Ref.7

Sequence conflict

576

1

E → K in AAC23441. Ref.7

Secondary structure

1

.

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593

Helix Strand Turn

Details...

Helix

43 – 89

47

Helix

97 – 121

25

Helix

123 – 131

9

Helix

133 – 161

29

Helix

171 – 268

98

Beta strand

523 – 527

5

Beta strand

535 – 537

3

Beta strand

546 – 549

4

Helix

555 – 557

3

Beta strand

562 – 567

6

Helix

568 – 572

5

Helix

573 – 579

7

Beta strand

582 – 585

4

Helix

586 – 588

3

Beta strand

589 – 591

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform IIA [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 0FF1956F0C7E3B50	FASTA	593	64,699
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK 190 200 210 220 230 240 AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN 250 260 270 280 290 300 TFQSIAGLEE NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP 310 320 330 340 350 360 DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQLRKGPP VPPPPKHTPS KEVKQEQILS 370 380 390 400 410 420 LFEDTFVPEI SVTTPSQFEA PGPFSEQASL LDLDFDPLPP VTSPVKAPTP SGQSIPWDLW 430 440 450 460 470 480 EPTESPAGSL PSGEPSAAEG TFAVSWPSQT AEPGPAQPAE ASEVAGGTQP AAGAQEPGET 490 500 510 520 530 540 AASEAASSSL PAVVVETFPA TVNGTVEGGS GAGRLDLPPG FMFKVQAQHD YTATDTDELQ 550 560 570 580 590 LKAGDVVLVI PFQNPEEQDE GWLMGVKESD WNQHKELEKC RGVFPENFTE RVP
	Isoform IIB [UniParc]. Checksum: 9BEF82FC2C28C845	FASTA	518	56,499
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS 310 320 330 340 350 360 PSQLRKGPPV PPPPKHTPSK EVKQEQILSL FEDTFVPEIS VTTPSQPTES PAGSLPSGEP 370 380 390 400 410 420 SAAEGTFAVS WPSQTAEPGP AQPAEASEVA GGTQPAAGAQ EPGETAASEA ASSSLPAVVV 430 440 450 460 470 480 ETFPATVNGT VEGGSGAGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD VVLVIPFQNP 490 500 510 EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVP
	Isoform IIC1 [UniParc]. Checksum: F3EA5A2EF666CE59	FASTA	506	55,175
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK 190 200 210 220 230 240 AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN 250 260 270 280 290 300 TFQSIAGLEE NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP 310 320 330 340 350 360 DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQPTESPA GSLPSGEPSA AEGTFAVSWP 370 380 390 400 410 420 SQTAEPGPAQ PAEASEVAGG TQPAAGAQEP GETAASEAAS SSLPAVVVET FPATVNGTVE 430 440 450 460 470 480 GGSGAGRLDL PPGFMFKVQA QHDYTATDTD ELQLKAGDVV LVIPFQNPEE QDEGWLMGVK 490 500 ESDWNQHKEL EKCRGVFPEN FTERVP
	Isoform IIC2 [UniParc]. Checksum: 876B8A866F96BA14	FASTA	475	51,737
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS 310 320 330 340 350 360 PSQPTESPAG SLPSGEPSAA EGTFAVSWPS QTAEPGPAQP AEASEVAGGT QPAAGAQEPG 370 380 390 400 410 420 ETAASEAASS SLPAVVVETF PATVNGTVEG GSGAGRLDLP PGFMFKVQAQ HDYTATDTDE 430 440 450 460 470 LQLKAGDVVL VIPFQNPEEQ DEGWLMGVKE SDWNQHKELE KCRGVFPENF TERVP
	Isoform IID [UniParc]. Checksum: 99FC3F5471E1926B	FASTA	550	59,937
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK 190 200 210 220 230 240 AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN 250 260 270 280 290 300 TFQSIAGLEE NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP 310 320 330 340 350 360 DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQFEAPGP FSEQASLLDL DFDPLPPVTS 370 380 390 400 410 420 PVKAPTPSGQ SIPWDLWEPT ESPAGSLPSG EPSAAEGTFA VSWPSQTAEP GPAQPAEASE 430 440 450 460 470 480 VAGGTQPAAG AQEPGETAAS EAASSSLPAV VVETFPATVN GTVEGGSGAG RLDLPPGFMF 490 500 510 520 530 540 KVQAQHDYTA TDTDELQLKA GDVVLVIPFQ NPEEQDEGWL MGVKESDWNQ HKELEKCRGV 550 FPENFTERVP
	Isoform II2 [UniParc]. Checksum: DF00A44348B6F1BF	FASTA	482	53,020
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS 310 320 330 340 350 360 PSQLRKGPPV PPPPKHTPSK EVKQEQILSL FEDTFVPEIS VTTPSQPAEA SEVAGGTQPA 370 380 390 400 410 420 AGAQEPGETA ASEAASSSLP AVVVETFPAT VNGTVEGGSG AGRLDLPPGF MFKVQAQHDY 430 440 450 460 470 480 TATDTDELQL KAGDVVLVIP FQNPEEQDEG WLMGVKESDW NQHKELEKCR GVFPENFTER VP
	Isoform II3 [UniParc]. Checksum: 350E429F13AF49C6	FASTA	439	48,258
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS 310 320 330 340 350 360 PSQPAEASEV AGGTQPAAGA QEPGETAASE AASSSLPAVV VETFPATVNG TVEGGSGAGR 370 380 390 400 410 420 LDLPPGFMFK VQAQHDYTAT DTDELQLKAG DVVLVIPFQN PEEQDEGWLM GVKESDWNQH 430 KELEKCRGVF PENFTERVP
	Isoform BIN1 [UniParc]. Checksum: 7E2ADD14E9D56D9E	FASTA	454	50,185
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPRKKSKL FSRLRRKKNS DNAPAKGNKS PSPPDGSPAA TPEIRVNHEP 310 320 330 340 350 360 EPAGGATPGA TLPKSPSQPA EASEVAGGTQ PAAGAQEPGE TAASEAASSS LPAVVVETFP 370 380 390 400 410 420 ATVNGTVEGG SGAGRLDLPP GFMFKVQAQH DYTATDTDEL QLKAGDVVLV IPFQNPEEQD 430 440 450 EGWLMGVKES DWNQHKELEK CRGVFPENFT ERVP
	Isoform BIN1-10-13 [UniParc]. Checksum: 08C5B23D79252350	FASTA	409	45,563
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS 310 320 330 340 350 360 PSQSSLPAVV VETFPATVNG TVEGGSGAGR LDLPPGFMFK VQAQHDYTAT DTDELQLKAG 370 380 390 400 DVVLVIPFQN PEEQDEGWLM GVKESDWNQH KELEKCRGVF PENFTERVP
	Isoform BIN1-13 [UniParc]. Checksum: 1C86B9D4C8C204C6	FASTA	424	47,491
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPRKKSKL FSRLRRKKNS DNAPAKGNKS PSPPDGSPAA TPEIRVNHEP 310 320 330 340 350 360 EPAGGATPGA TLPKSPSQSS LPAVVVETFP ATVNGTVEGG SGAGRLDLPP GFMFKVQAQH 370 380 390 400 410 420 DYTATDTDEL QLKAGDVVLV IPFQNPEEQD EGWLMGVKES DWNQHKELEK CRGVFPENFT ERVP
	Isoform BIN1+12A [UniParc]. Checksum: 55E3246DD05172AA	FASTA	497	54,948
	10 20 30 40 50 60 MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 70 80 90 100 110 120 LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD 130 140 150 160 170 180 QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK 190 200 210 220 230 240 AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE 250 260 270 280 290 300 KQHGSNTFTV KAQPRKKSKL FSRLRRKKNS DNAPAKGNKS PSPPDGSPAA TPEIRVNHEP 310 320 330 340 350 360 EPAGGATPGA TLPKSPSQLR KGPPVPPPPK HTPSKEVKQE QILSLFEDTF VPEISVTTPS 370 380 390 400 410 420 QPAEASEVAG GTQPAAGAQE PGETAASEAA SSSLPAVVVE TFPATVNGTV EGGSGAGRLD 430 440 450 460 470 480 LPPGFMFKVQ AQHDYTATDT DELQLKAGDV VLVIPFQNPE EQDEGWLMGV KESDWNQHKE 490 LEKCRGVFPE NFTERVP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a nerve terminal-enriched amphiphysin isoform." Ramjaun A.R., Micheva K.D., Bouchelet I., McPherson P.S. J. Biol. Chem. 272:16700-16706(1997) [PubMed: 9195986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIA). Tissue: Brain.
[2]	"Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of Ranvier in brain and around T tubules in skeletal muscle." Butler M.H., David C., Ochoa G.-C., Freyberg Z., Daniell L., Grabs D., Cremona O., De Camilli P. J. Cell Biol. 137:1355-1367(1997) [PubMed: 9182667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIA AND BIN1). Tissue: Brain and Skeletal muscle.
[3]	"BIN1 is a novel Myc-interacting protein with features of a tumour suppressor." Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C. Nat. Genet. 14:69-76(1996) [PubMed: 8782822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIN1). Tissue: Skeletal muscle.
[4]	Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[5]	"Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites." Ramjaun A.R., McPherson P.S. J. Neurochem. 70:2369-2376(1998) [PubMed: 9603201] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIB; IIC1; IIC2 AND IID), INTERACTION WITH CLTC. Tissue: Brain.
[6]	"cDNA cloning of a novel amphiphysin isoform and tissue-specific expression of its multiple splice variants." Tsutsui K., Maeda Y., Tsutsui K., Seki S., Tokunaga A. Biochem. Biophys. Res. Commun. 236:178-183(1997) [PubMed: 9223448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS II2 AND II3). Tissue: Brain.
[7]	"Structural analysis of the human BIN1 gene. Evidence for tissue-specific transcriptional regulation and alternate RNA splicing." Wechsler-Reya R.J., Sakamuro D., Zhang J., Duhadaway J., Prendergast G.C. J. Biol. Chem. 272:31453-31458(1997) [PubMed: 9395479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS II3; II3; BIN1-10-13; BIN1-13 AND BIN1+12A). Tissue: Fibroblast.
[8]	Zhang J., Du W., Wechsler-Reya R.J., Duhadaway J., Sakamuro D., Prendergast G.C. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM II2).
[9]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA). Tissue: Brain.
[10]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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].
[12]	Yu W., Gibbs R.A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-593. Tissue: Brain.
[13]	"A role for the putative tumor suppressor Bin1 in muscle cell differentiation." Wechsler-Reya R.J., Elliott K.J., Prendergast G.C. Mol. Cell. Biol. 18:566-575(1998) [PubMed: 9418903] [Abstract] Cited for: CHARACTERIZATION. Tissue: Skeletal muscle.
[14]	"Bin2, a functionally nonredundant member of the BAR adaptor gene family." Ge K., Prendergast G.C. Genomics 67:210-220(2000) [PubMed: 10903846] [Abstract] Cited for: INTERACTION WITH BIN2, TISSUE SPECIFICITY.
[15]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 AND SER-303, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303 AND SER-331, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"The SH3 binding motif of HCV NS5A protein interacts with Bin1 and is important for apoptosis and infectivity." Nanda S.K., Herion D., Liang T.J. Gastroenterology 130:794-809(2006) [PubMed: 16530520] [Abstract] Cited for: INTERACTION WITH HCV NS5A.
[18]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, MASS SPECTROMETRY. Tissue: T-cell.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-303; THR-307; THR-323 AND SER-331, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 AND SER-303, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[23]	"Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy." Nicot A.-S., Toussaint A., Tosch V., Kretz C., Wallgren-Pettersson C., Iwarsson E., Kingston H., Garnier J.-M., Biancalana V., Oldfors A., Mandel J.-L., Laporte J. Nat. Genet. 39:1134-1139(2007) [PubMed: 17676042] [Abstract] Cited for: VARIANTS ARCNM ASN-35 AND ASN-151, CHARACTERIZATION OF VARIANTS ARCNM ASN-35 AND ASN-151.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF004015 mRNA. Translation: AAC51345.1.
AF070576 mRNA. Translation: AAC28646.1.
AF001383 mRNA. Translation: AAB61363.1.
U68485 mRNA. Translation: AAC17461.1.
AF043898 mRNA. Translation: AAC39710.1.
AF043899 mRNA. Translation: AAC39711.1.
AF043900 mRNA. Translation: AAC39712.1.
AF043901 mRNA. Translation: AAC39713.1.
U87558 mRNA. Translation: AAB63263.1.
AF068914 mRNA. Translation: AAC24126.1.
AF068915 mRNA. Translation: AAC24127.1.
AF068916 mRNA. Translation: AAC24128.1.
AF068917 mRNA. Translation: AAC23750.1.
AF068918 mRNA. Translation: AAC23751.1.
U84004 , U83999, U84001, U84002, U84003 Genomic DNA. Translation: AAC23440.1.
U84004 , U83999, U84001, U84002, U84003 Genomic DNA. Translation: AAC23441.1. Different initiation.
AL713697 mRNA. Translation: CAD28496.1.
AC012508 Genomic DNA. Translation: AAY24328.1.
CH471103 Genomic DNA. Translation: EAW95302.1.

IPI

IPI00186966.
IPI00220586.
IPI00220587.
IPI00220996.
IPI00220997.
IPI00220998.
IPI00220999.
IPI00221000.
IPI00221001.
IPI00329733.
IPI00395680.

PIR

JC5593.

RefSeq

NP_004296.1. NM_004305.3.
NP_647593.1. NM_139343.2.
NP_647594.1. NM_139344.2.
NP_647595.1. NM_139345.2.
NP_647596.1. NM_139346.2.
NP_647597.1. NM_139347.2.
NP_647598.1. NM_139348.2.
NP_647599.1. NM_139349.2.
NP_647600.1. NM_139350.2.
NP_647601.1. NM_139351.2.

UniGene

Hs.193163.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MUZ	NMR	-	A	513-593	[»]
1MV0	NMR	-	B	513-593	[»]
1MV3	NMR	-	A	301-593	[»]
2FIC	X-ray	1.99	A/B	1-272	[»]
2RMY	NMR	-	A	1-33	[»]
2RND	NMR	-	A	1-33	[»]

ProteinModelPortal

O00499.

SMR

O00499. Positions 1-33, 40-271, 301-377, 455-593.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41480N.

IntAct

O00499. 7 interactions.

MINT

MINT-258326.

STRING

O00499.

PTM databases

PhosphoSite

O00499.

2D gel databases

UCD-2DPAGE

O00499.

Proteomic databases

PRIDE

O00499.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316724; ENSP00000316779; ENSG00000136717.

GeneID

274.

KEGG

hsa:274.

UCSC

uc002tns.1. human.
uc002tnt.1. human.
uc002tnu.1. human.
uc002tnv.1. human.
uc002tnw.1. human.
uc002tnx.1. human.
uc002tny.1. human.
uc002tnz.1. human.
uc002toa.1. human.
uc002tob.1. human.
uc002toc.1. human.

Organism-specific databases

CTD

274.

GeneCards

GC02M127898.

H-InvDB

HIX0002430.

HGNC

HGNC:1052. BIN1.

HPA

CAB001945.
HPA003894.
HPA005437.

MIM

255200. phenotype.
601248. gene.

neXtProt

NX_O00499.

Orphanet

169186. Autosomal recessive centronuclear myopathy.

PharmGKB

PA25355.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15217.

GeneTree

ENSGT00390000017588.

HOVERGEN

HBG004224.

InParanoid

O00499.

OMA

HEPEPAS.

PhylomeDB

O00499.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.

Gene expression databases

ArrayExpress

O00499.

Bgee

O00499.

Genevestigator

O00499.

GermOnline

ENSG00000136717. Homo sapiens.

Family and domain databases

InterPro

IPR003005. Amphiphysin.
IPR003023. Amphiphysin_2.
IPR004148. BAR_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

Pfam

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

PRINTS

PR01251. AMPHIPHYSIN.
PR01253. AMPHIPHYSIN2.
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

1087.

SOURCE

Search...

Entry information

Entry name

BIN1_HUMAN

Accession

Primary (citable) accession number: O00499
Secondary accession number(s): O00297 , O00545, O43867, O60552, O60553, O60554, O60555, O75514, O75515, O75516, O75517, O75518, Q659B7, Q92944, Q99688

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 130 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.