O00213 (APBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amyloid beta A4 precursor protein-binding family B member 1

Alternative name(s):
Protein Fe65

Gene names

Name:	APBB1
Synonyms:	FE65, RIR

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

General annotation (Comments)

Function	Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Ref.6 Ref.8 Ref.9 Ref.10 Ref.11
Subunit structure	Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts (via PID domain 2) with APP (with the intracellular domain of the beta-amyloid precursor protein). Interacts (via PID domain 2) with RASD1/DEXRAS1; impairs the trancription activation activity. Interacts (via PID domain 1) with KAT5/TIP60. Interacts (via the WW domain) with the proline-rich region of APBB1IP. Interacts with TSHZ1 and TSHZ2 By similarity. Interacts (via the WW domain) with histone H2AX (when phosphorylated on 'Tyr-142') and the proline-rich region of ENAH. Interacts with MAPK8. Interacts (via PID domain 1) with TSHZ3 (via homeobox domain). Interacts with SET. Found in a trimeric complex with HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Interacts (via WWW domain) with NEK6. Interacts (via WWW domain) with ABL1. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Subcellular location	Cell membrane. Cytoplasm. Nucleus. Cell projection › growth cone By similarity. Nucleus speckle. Note: Colocalizes with TSHZ3 in axonal growth cone By similarity. In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP. Following exposure to DNA damaging agents, it is released from cell membrane and translocates to the nucleus. Nuclear translocation is under the regulation of APP. Colocalizes with TSHZ3 in the nucleus. Co-localizes with NEK6 at the nuclear speckles. Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Tissue specificity	Highly expressed in brain; strongly reduced in post-mortem elderly subjects with Alzheimer disease. Ref.11
Post-translational modification	Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus By similarity. Phosphorylated following nuclear translocation. Phosphorylation at Tyr-547 by ABL1 enhances transcriptional activation activity and reduces the affinity for RASD1/DEXRAS1. Ref.6 Ref.9
Sequence similarities	Contains 2 PID domains. Contains 1 WW domain.

Ontologies

Keywords
Biological process	Apoptosis DNA damage Transcription Transcription regulation
Cellular component	Cell membrane Cell projection Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Activator Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axonogenesis Non-traceable author statement. Source: UniProtKB cell cycle arrest Inferred from sequence or structural similarity. Source: UniProtKB histone H4 acetylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of S phase of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of thymidylate synthase biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.11. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay Ref.8. Source: UniProtKB signal transduction Non-traceable author statement Ref.1. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB growth cone Inferred from direct assay. Source: UniProtKB lamellipodium Inferred from direct assay. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.8. Source: UniProtKB synapse Inferred from direct assay. Source: UniProtKB
Molecular function	beta-amyloid binding Inferred from physical interaction Ref.8. Source: UniProtKB chromatin binding Inferred from direct assay Ref.11. Source: UniProtKB histone binding Inferred from physical interaction Ref.10. Source: UniProtKB proline-rich region binding Inferred from physical interaction Ref.12. Source: UniProtKB transcription factor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	5	EBI-81694,EBI-77613

Alternative products

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

Isoform 1 (identifier: O00213-1)

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 2 (identifier: O00213-2)

The sequence of this isoform differs from the canonical sequence as follows:
     462-463: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 710

710

Amyloid beta A4 precursor protein-binding family B member 1

PRO_0000076049

Regions

Domain

253 – 285

33

WW

Domain

370 – 509

140

PID 1

Domain

542 – 699

158

PID 2

Compositional bias

158 – 171

14

Glu-rich

Amino acid modifications

Modified residue

547

1

Phosphotyrosine; by ABL1 Ref.6 Ref.9

Modified residue

610

1

Phosphoserine; by SGK1 By similarity

Natural variations

Alternative sequence

462 – 463

2

Missing in isoform 2.

VSP_011658

Natural variant

327

1

M → V.
Corresponds to variant rs1800423 [ dbSNP | Ensembl ].

VAR_014444

Natural variant

396

1

N → S.
Corresponds to variant rs1800425 [ dbSNP | Ensembl ].

VAR_014445

Experimental info

Mutagenesis

117

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

234

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

269 – 271

3

YYW → AAA: Impairs transcriptional activation and inhibits binding to ABL1. Ref.6

Mutagenesis

269

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

270

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

403

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

467

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

546

1

Y → F: No effect on phosphorylation by ABL1. Ref.6

Mutagenesis

547

1

Y → F: Abrogates phosphorylation and stimulation of transcription by ABL1, and increases the interaction with RASD1/DEXRAS1. Ref.6 Ref.9

Mutagenesis

658

1

Y → F: No effect on phosphorylation by ABL1.

Secondary structure

1

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710

Helix Strand Turn

Details...

Beta strand

259 – 263

5

Beta strand

268 – 272

5

Turn

273 – 275

3

Beta strand

278 – 281

4

Beta strand

368 – 379

12

Helix

382 – 385

4

Turn

387 – 389

3

Helix

390 – 401

12

Beta strand

421 – 427

7

Beta strand

430 – 434

5

Turn

436 – 438

3

Beta strand

441 – 446

6

Helix

447 – 449

3

Beta strand

452 – 455

4

Beta strand

464 – 470

7

Turn

472 – 474

3

Beta strand

477 – 486

10

Helix

488 – 504

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1998. Version 2. Checksum: FD4A2EF7E8D8E884	FASTA	710	77,244
	10 20 30 40 50 60 MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL RSAMGEGGGP 70 80 90 100 110 120 EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEPEMAPLGP KGLIHLYSEL 130 140 150 160 170 180 ELSAHNAANR GLRGPGLIIS TQEQGPDEGE EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP 190 200 210 220 230 240 EPLESVEAPP RPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT 250 260 270 280 290 300 DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL 310 320 330 340 350 360 TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP LPQEEEKLPP 370 380 390 400 410 420 RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMSGGWGEGK 430 440 450 460 470 480 DLLLQLEDET LKLVEPQSQA LLHAQPIISI RVWGVGRDSG RERDFAYVAR DKLTQMLKCH 490 500 510 520 530 540 VFRCEAPAKN IATSLHEICS KIMAERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV 550 560 570 580 590 600 QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV 610 620 630 640 650 660 LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK 670 680 690 700 710 CLDARSQAST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGAHTP
	Isoform 2 [UniParc]. Checksum: FC578B7688BCC1A0	FASTA	708	76,959
	10 20 30 40 50 60 MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL RSAMGEGGGP 70 80 90 100 110 120 EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEPEMAPLGP KGLIHLYSEL 130 140 150 160 170 180 ELSAHNAANR GLRGPGLIIS TQEQGPDEGE EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP 190 200 210 220 230 240 EPLESVEAPP RPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT 250 260 270 280 290 300 DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL 310 320 330 340 350 360 TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP LPQEEEKLPP 370 380 390 400 410 420 RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMSGGWGEGK 430 440 450 460 470 480 DLLLQLEDET LKLVEPQSQA LLHAQPIISI RVWGVGRDSG RDFAYVARDK LTQMLKCHVF 490 500 510 520 530 540 RCEAPAKNIA TSLHEICSKI MAERRNARCL VNGLSLDHSK LVDVPFQVEF PAPKNELVQK 550 560 570 580 590 600 FQVYYLGNVP VAKPVGVDVI NGALESVLSS SSREQWTPSH VSVAPATLTI LHQQTEAVLG 610 620 630 640 650 660 ECRVRFLSFL AVGRDVHTFA FIMAAGPASF CCHMFWCEPN AASLSEAVQA ACMLRYQKCL 670 680 690 700 DARSQASTSC LPAPPAESVA RRVGWTVRRG VQSLWGSLKP KRLGAHTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein." Bressler S.L., Gray M.D., Sopher B.L., Hu Q., Hearn M.G., Pham D.G., Dinulos M.B., Fukuchi K., Sisodia S.S., Miller M.A., Disteche C.M., Martin G.M. Hum. Mol. Genet. 5:1589-1598(1996) [PubMed: 8894693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type." Hu Q., Kukull W.A., Bressler S.L., Gray M.D., Cam J.A., Larson E.B., Martin G.M., Deeb S.S. Hum. Genet. 103:295-303(1998) [PubMed: 9799084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Tissue: Brain.
[3]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 2). Tissue: Uterus.
[6]	"The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling." Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L., Ward M., McLoughlin D.M., Miller C.C. J. Biol. Chem. 279:22084-22091(2004) [PubMed: 15031292] [Abstract] Cited for: FUNCTION, INTERACTION WITH ABL1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-547 BY ABL1, MUTAGENESIS OF TYR-117; TYR-234; TYR-269; TYR-270; TYR-403; TYR-467; 269-TYR--TRP-271; TYR-546 AND TYR-547.
[7]	"Human NIMA-related kinase 6 is one of the Fe65 WW domain binding proteins." Lee E.J., Hyun S.H., Chun J., Kang S.S. Biochem. Biophys. Res. Commun. 358:783-788(2007) [PubMed: 17512906] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
[8]	"Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells." Nakaya T., Kawai T., Suzuki T. J. Biol. Chem. 283:19119-19131(2008) [PubMed: 18468999] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APP.
[9]	"Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription." Lau K.-F., Chan W.-M., Perkinton M.S., Tudor E.L., Chang R.C.C., Chan H.-Y., McLoughlin D.M., Miller C.C.J. J. Biol. Chem. 283:34728-34737(2008) [PubMed: 18922798] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-547, INTERACTION WITH RASD1, MUTAGENESIS OF TYR-547.
[10]	"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions." Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G. Nature 458:591-596(2009) [PubMed: 19234442] [Abstract] Cited for: FUNCTION, INTERACTION WITH H2AX AND MAPK8.
[11]	"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4." Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D. PLoS ONE 4:E5071-E5071(2009) [PubMed: 19343227] [Abstract] Cited for: FUNCTION, INTERACTION WITH SET AND TSHZ3, IDENTIFICATION IN A TRIMERIC COMPLEX WITH HDAC1 AND TSHZ3, CHROMATIN-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"Structural basis for polyproline recognition by the FE65 WW domain." Meiyappan M., Birrane G., Ladias J.A.A. J. Mol. Biol. 372:970-980(2007) [PubMed: 17686488] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 253-289 IN COMPLEX WITH ENAH.
[13]	"Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2." Radzimanowski J., Simon B., Sattler M., Beyreuther K., Sinning I., Wild K. EMBO Rep. 9:1134-1140(2008) [PubMed: 18833287] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 534-667 IN COMPLEX WITH APP.
[14]	"Crystal structure of the human Fe65-PTB1 domain." Radzimanowski J., Ravaud S., Schlesinger S., Koch J., Beyreuther K., Sinning I., Wild K. J. Biol. Chem. 283:23113-23120(2008) [PubMed: 18550529] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 366-505.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77864 mRNA. Translation: AAB93631.1.
AF029234, AF047835 Genomic DNA. Translation: AAC79942.1.
AC068733 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68723.1.
CH471064 Genomic DNA. Translation: EAW68724.1.
BC010854 mRNA. Translation: AAH10854.1.

IPI

IPI00010843.
IPI00783577.

RefSeq

NP_001155.1. NM_001164.2.
NP_663722.1. NM_145689.1.

UniGene

Hs.372840.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E45	NMR	-	A	241-290	[»]
2HO2	X-ray	1.33	A	253-289	[»]
2IDH	X-ray	2.28	A/B/C/D/E/F/G/H	253-289	[»]
2OEI	X-ray	1.35	A	253-289	[»]
3D8D	X-ray	2.20	A/B	366-505	[»]
3D8E	X-ray	2.80	A/B/C/D	366-505	[»]
3D8F	X-ray	2.70	A/B/C/D	366-505	[»]
3DXC	X-ray	2.10	A/C	534-667	[»]
3DXD	X-ray	2.20	A/C	534-667	[»]
3DXE	X-ray	2.00	A/C	534-667	[»]

ProteinModelPortal

O00213.

SMR

O00213. Positions 241-290, 366-666.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00213. 4 interactions.

MINT

MINT-1493266.

STRING

O00213.

PTM databases

PhosphoSite

O00213.

Proteomic databases

PRIDE

O00213.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389906; ENSP00000374556; ENSG00000166313.

GeneID

322.

KEGG

hsa:322.

UCSC

uc001mdb.1. human.
uc001mdc.1. human.

Organism-specific databases

CTD

322.

GeneCards

GC11M006414.

HGNC

HGNC:581. APBB1.

HPA

CAB022104.

MIM

602709. gene.

neXtProt

NX_O00213.

PharmGKB

PA24873.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000000002.

HOVERGEN

HBG050524.

Gene expression databases

ArrayExpress

O00213.

Bgee

O00213.

CleanEx

HS_APBB1.

Genevestigator

O00213.

GermOnline

ENSG00000166313. Homo sapiens.

Family and domain databases

InterPro

IPR011993. PH_type.
IPR006020. PTyr_interaction_dom.
IPR001202. WW_Rsp5_WWP.
[Graphical view]

Gene3D

G3DSA:2.20.70.10. G3DSA:2.20.70.10. 1 hit.
G3DSA:2.30.29.30. PH_type. 2 hits.

KO

K04529.

Pfam

PF00640. PID. 2 hits.
PF00397. WW. 1 hit.
[Graphical view]

SMART

SM00462. PTB. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]

SUPFAM

SSF51045. WW_Rsp5_WWP. 1 hit.

PROSITE

PS01179. PID. 2 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1319.

SOURCE

Search...

Entry information

Entry name

APBB1_HUMAN

Accession

Primary (citable) accession number: O00213
Secondary accession number(s): A6NH82 , A6NL69, D3DQT2, Q96A93

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 106 of the entry and version 2 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.