Q62261 (SPTB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin beta chain, non-erythrocytic 1

Alternative name(s):
Beta-II spectrin
Embryonic liver fodrin
Fodrin beta chain

Gene names

Name:	Sptbn1
Synonyms:	Elf, Spnb-2, Spnb2, Sptb2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2363 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.
Subunit structure	Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers. Interacts with ANK2. Ref.5
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › M line. Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes. Ref.2 Isoform 2: Cell membrane; Peripheral membrane protein; Cytoplasmic side Ref.2.
Tissue specificity	Isoform 2 is present in brain, heart, kidney and liver (at protein level). Ref.2 Ref.5
Developmental stage	Isoform 2 is expressed in brain, heart and liver throughout embryonic development. Isoform 1 is mainly expressed in neonatal developing ventricular cardiomyocytes. Ref.2
Post-translational modification	Isoform 2 is phosphorylated on Ser-8 and Ser-10.
Sequence similarities	Belongs to the spectrin family. Contains 2 CH (calponin-homology) domains. Contains 1 PH domain. Contains 17 spectrin repeats.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding Calmodulin-binding
Molecular function	Actin capping
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi to plasma membrane protein transport Inferred from electronic annotation. Source: Compara SMAD protein import into nucleus Inferred from direct assay PubMed 12543979. Source: MGI actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW common-partner SMAD protein phosphorylation Inferred from direct assay PubMed 12543979. Source: MGI cytokinesis after mitosis Inferred from electronic annotation. Source: Compara membrane assembly Inferred from electronic annotation. Source: Compara protein targeting to plasma membrane Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL
Cellular_component	M band Inferred from direct assay Ref.5. Source: BHF-UCL axolemma Inferred from direct assay PubMed 21966409. Source: BHF-UCL cuticular plate Inferred from direct assay PubMed 18796539. Source: MGI nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay PubMed 12543979. Source: MGI spectrin Inferred from electronic annotation. Source: InterPro
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q62261-1)

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: Q62261-2)

Also known as: Elf3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MTTTVATDYD...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
     2140-2246: MAGTMETSEM...KDAKSAASGI → VSYRSQTYQNYKNFNSRRTASDHSWSGM
     2247-2363: Missing.

Note: Contains a phosphoserine at position 14 (By similarity). Contains a phosphoserine at position 8. Contains a phosphoserine at position 10.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2363

2363

Spectrin beta chain, non-erythrocytic 1

PRO_0000073462

Regions

Domain

1 – 275

275

Actin-binding

Domain

54 – 158

105

CH 1

Domain

173 – 275

103

CH 2

Repeat

276 – 384

109

Spectrin 1

Repeat

385 – 498

114

Spectrin 2

Repeat

499 – 608

110

Spectrin 3

Repeat

609 – 714

106

Spectrin 4

Repeat

715 – 819

105

Spectrin 5

Repeat

820 – 925

106

Spectrin 6

Repeat

926 – 1032

107

Spectrin 7

Repeat

1033 – 1139

107

Spectrin 8

Repeat

1140 – 1245

106

Spectrin 9

Repeat

1246 – 1350

105

Spectrin 10

Repeat

1351 – 1462

112

Spectrin 11

Repeat

1463 – 1562

100

Spectrin 12

Repeat

1563 – 1668

106

Spectrin 13

Repeat

1669 – 1775

107

Spectrin 14

Repeat

1776 – 1881

106

Spectrin 15

Repeat

1882 – 1987

106

Spectrin 16

Repeat

1988 – 2132

145

Spectrin 17

Domain

2196 – 2306

111

PH

Region

1563 – 2093

531

Interaction with ANK2 By similarity

Amino acid modifications

Modified residue

90

1

N6-acetyllysine By similarity

Modified residue

257

1

Phosphoserine Ref.13

Modified residue

817

1

Phosphoserine By similarity

Modified residue

999

1

Phosphothreonine Ref.7

Modified residue

1057

1

Phosphoserine By similarity

Modified residue

1447

1

Phosphoserine By similarity

Modified residue

1805

1

Phosphotyrosine Ref.10

Modified residue

1815

1

N6-acetyllysine By similarity

Modified residue

1913

1

N6-acetyllysine By similarity

Modified residue

1918

1

Phosphoserine Ref.6

Modified residue

1989

1

N6-acetyllysine By similarity

Modified residue

2102

1

Phosphoserine Ref.7 Ref.9 Ref.13

Modified residue

2115

1

Phosphoserine Ref.6

Modified residue

2127

1

Phosphoserine Ref.11

Modified residue

2137

1

Phosphoserine Ref.6 Ref.11 Ref.13

Modified residue

2159

1

Phosphoserine By similarity

Modified residue

2160

1

Phosphoserine By similarity

Modified residue

2163

1

Phosphoserine By similarity

Modified residue

2164

1

Phosphoserine Ref.7 Ref.14

Modified residue

2168

1

Phosphoserine Ref.6 Ref.7 Ref.14

Modified residue

2186

1

Phosphothreonine By similarity

Modified residue

2194

1

Phosphothreonine Ref.7 Ref.11

Modified residue

2318

1

Phosphoserine By similarity

Modified residue

2319

1

Phosphothreonine By similarity

Modified residue

2327

1

Phosphothreonine Ref.13

Modified residue

2339

1

Phosphoserine By similarity

Modified residue

2340

1

Phosphoserine By similarity

Modified residue

2357

1

Phosphoserine Ref.13

Glycosylation

2323

1

O-linked (GlcNAc) Ref.8

Natural variations

Alternative sequence

1 – 49

49

MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2.

VSP_026057

Alternative sequence

2140 – 2246

107

MAGTM…AASGI → VSYRSQTYQNYKNFNSRRTA SDHSWSGM in isoform 2.

VSP_026058

Alternative sequence

2247 – 2363

117

Missing in isoform 2.

VSP_026059

Experimental info

Sequence conflict

252

1

D → A in BAE41221. Ref.4

Sequence conflict

309

1

S → T in AAD01616. Ref.2

Sequence conflict

368

1

T → A in AAD01616. Ref.2

Sequence conflict

737

1

K → I in AAC42040. Ref.1

Sequence conflict

796

1

Y → C in AAD01616. Ref.2

Sequence conflict

846

1

Q → R in AAC42040. Ref.1

Sequence conflict

970

1

W → C in AAD01616. Ref.2

Sequence conflict

996

1

R → C in AAD01616. Ref.2

Sequence conflict

1401 – 1403

3

SQI → KPGF in AAC42040. Ref.1

Sequence conflict

1414 – 1455

42

SVNIL…KSTDE → QSQYSSEKGNRRRRIRWKFG RKRSRNCRPSPGSSRGRAQM R in AAC42040. Ref.1

Sequence conflict

1508

1

A → R in AAC42040. Ref.1

Sequence conflict

1619 – 1624

6

EKAKDE → KRPRMK in AAC42040. Ref.1

Sequence conflict

1898

1

D → G in AAC42040. Ref.1

Sequence conflict

2171

1

L → S in AAC42040. Ref.1

Sequence conflict

2345 – 2346

2

EK → AE in AAC42040. Ref.1

Sequence conflict

2356 – 2358

3

FSL → STV in AAC42040. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2363

Helix Strand Turn

Details...

Beta strand

2200 – 2209

10

Beta strand

2211 – 2213

3

Beta strand

2222 – 2229

8

Beta strand

2232 – 2238

7

Helix

2239 – 2244

6

Beta strand

2248 – 2250

3

Beta strand

2253 – 2255

3

Beta strand

2260 – 2263

4

Beta strand

2269 – 2277

9

Beta strand

2283 – 2287

5

Helix

2291 – 2303

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 16, 2006. Version 2. Checksum: 221362054E64BB8C	FASTA	2,363	274,223
	10 20 30 40 50 60 MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF 70 80 90 100 110 120 TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL 130 140 150 160 170 180 QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL 190 200 210 220 230 240 LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL 250 260 270 280 290 300 AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 310 320 330 340 350 360 EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG 370 380 390 400 410 420 NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL 430 440 450 460 470 480 EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA 490 500 510 520 530 540 VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI 550 560 570 580 590 600 MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG 610 620 630 640 650 660 YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI 670 680 690 700 710 720 LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII 730 740 750 760 770 780 YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ 790 800 810 820 830 840 SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL 850 860 870 880 890 900 RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 910 920 930 940 950 960 QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY 970 980 990 1000 1010 1020 HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE 1030 1040 1050 1060 1070 1080 KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR 1090 1100 1110 1120 1130 1140 TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL 1150 1160 1170 1180 1190 1200 RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 1210 1220 1230 1240 1250 1260 LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN 1270 1280 1290 1300 1310 1320 REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM 1330 1340 1350 1360 1370 1380 AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN 1390 1400 1410 1420 1430 1440 KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ 1450 1460 1470 1480 1490 1500 SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW 1510 1520 1530 1540 1550 1560 VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA 1570 1580 1590 1600 1610 1620 EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK 1630 1640 1650 1660 1670 1680 AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY 1690 1700 1710 1720 1730 1740 AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF 1750 1760 1770 1780 1790 1800 REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1810 1820 1830 1840 1850 1860 LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV 1870 1880 1890 1900 1910 1920 RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV 1930 1940 1950 1960 1970 1980 RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR 1990 2000 2010 2020 2030 2040 KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL 2050 2060 2070 2080 2090 2100 SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2110 2120 2130 2140 2150 2160 PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS 2170 2180 2190 2200 2210 2220 KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS 2230 2240 2250 2260 2270 2280 WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD 2290 2300 2310 2320 2330 2340 GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS 2350 2360 PGKREKDKEK DKEKRFSLFG KKK
	Isoform 2 (Elf3) [UniParc]. Checksum: 5128A840C3FD28AC	FASTA	2,154	251,156
	10 20 30 40 50 60 MELQRTSSIS GPLSPAYTGQ VPYNYNQLEG RFKQLQDERE AVQKKTFTKW VNSHLARVSC 70 80 90 100 110 120 RITDLYTDLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL ENVDKALQFL KEQRVHLENM 130 140 150 160 170 180 GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS VETEDNKEKK SAKDALLLWC QMKTAGYPNV 190 200 210 220 230 240 NIHNFTTSWR DGMAFNALIH KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP 250 260 270 280 290 300 EDISVDHPDE KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD 310 320 330 340 350 360 LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE VLLFTIQSKM 370 380 390 400 410 420 RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE LIRQEKLEQL ARRFDRKAAM 430 440 450 460 470 480 RETWLSENQR LVSQDNFGFD LPAVEAATKK HEAIETDIAA YEERVQAVVA VARELEAENY 490 500 510 520 530 540 HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLLLS 550 560 570 580 590 600 QDYGKHLLGV EDLLQKHALV EADIAIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV 610 620 630 640 650 660 AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEKILSS DDYGKDLTSV 670 680 690 700 710 720 MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE KIRERIIYIR EQWANLEQLS 730 740 750 760 770 780 AIRKKRLEEA SLLHQFQADA DDIDAWMLDI LKIVSSNDVG HDEYSTQSLV KKHKDVAEEI 790 800 810 820 830 840 TNYRPTIDTL HEQASALPQA HAESPDVKGR LAGIEERCKE MAELTRLRKQ ALQDTLALYK 850 860 870 880 890 900 MFSEADACEL WIDEKEQWLN NMQIPEKLED LEVIQHRFES LEPEMNNQAS RVAVVNQIAR 910 920 930 940 950 960 QLMHNGHPSE KEIRAQQDKL NTRWSQFREL VDRKKDALLS ALSIQNYHLE CNETKSWIRE 970 980 990 1000 1010 1020 KTKVIESTQD LGNDLAGVMA LQRKLTGMER DLVAIEAKLS DLQKEAEKLE SEHPDQAQAI 1030 1040 1050 1060 1070 1080 LSRLAEISDV WEEMKTTLKN REASLGEASK LQQFLRDLDD FQSWLSRTQT AIASEDMPNT 1090 1100 1110 1120 1130 1140 LTEAEKLLTQ HENIKNEIDN YEEDYQKMRD MGEMVTQGQT DAQYMFLRQR LQALDTGWNE 1150 1160 1170 1180 1190 1200 LHKMWENRQN LLSQSHAYQQ FLRDTKQAEA FLNNQEYVLA HTEMPTTLEG AEAAIKKQED 1210 1220 1230 1240 1250 1260 FMTTMDANEE KINAVVETGR RLVSDGNINS DRIQEKVDSI DDRHRKNREA ASELLMRLKD 1270 1280 1290 1300 1310 1320 NRDLQKFLQD CQELSLWINE KMLTAQDMSY DEARNLHSKW LKHQAFMAEL ASNKEWLDKI 1330 1340 1350 1360 1370 1380 EKEGMQLISE KPETEAVVKE KLTGLHKMWE VLESTTQTKA QRLFDANKAE LFTQSCADLD 1390 1400 1410 1420 1430 1440 KWLHGLESQI QSDDYGKDLT SVNILLKKQQ MLENQMEVRK KEIEELQSQA QALSQEGKST 1450 1460 1470 1480 1490 1500 DEVDSKRLTV QTKFMELLEP LSERKHNLLA SKEIHQFNRD VEDEILWVGE RMPLATSTDH 1510 1520 1530 1540 1550 1560 GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNIIT DSSSLNAEAI RQRLADLKQL 1570 1580 1590 1600 1610 1620 WGLLIEETEK RHRRLEEAHK AQQYYFDAAE AEAWMSEQEL YMMSEEKAKD EQSAVSMLKK 1630 1640 1650 1660 1670 1680 HQILEQAVED YAETVHQLSK TSRALVADSH PESERISMRQ SKVDKLYAGL KDLAEERRGK 1690 1700 1710 1720 1730 1740 LDERHRLFQL NREVDDLEQW IAEREVVAGS HELGQDYEHV TMLQERFREF ARDTGNIGQE 1750 1760 1770 1780 1790 1800 RVDTVNNMAD ELINSGHSDA ATIAEWKDGL NEAWADLLEL IDTRTQILAA SYELHKFYHD 1810 1820 1830 1840 1850 1860 AKEIFGRIQD KHKKLPEELG RDQNTVETLQ RMHTTFEHDI QALGTQVRQL QEDAARLQAA 1870 1880 1890 1900 1910 1920 YAGDKADDIQ KRENEVLEAW KSLLDACEGR RVRLVDTGDK FRFFSMVRDL MLWMEDVIRQ 1930 1940 1950 1960 1970 1980 IEAQEKPRDV SSVELLMNNH QGIKAEIDAR NDSFTACIEL GKSLLARKHY ASEEIKEKLL 1990 2000 2010 2020 2030 2040 QLTEKRKEMI DKWEDRWEWL RLILEVHQFS RDASVAEAWL LGQEPYLSSR EIGQSVDEVE 2050 2060 2070 2080 2090 2100 KLIKRHEAFE KSAATWDERF SALERLTTLE LLEVRRQQEE EERKRRPPSP DPNTKVSEEA 2110 2120 2130 2140 2150 ESQQWDTSKG DQVSQNGLPA EQGSPRVSYR SQTYQNYKNF NSRRTASDHS WSGM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete amino acid sequence for brain beta spectrin (beta fodrin): relationship to globin sequences." Ma Y., Zimmer W.E., Riederer B.M., Goodman S.R. Brain Res. Mol. Brain Res. 18:87-99(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c.
[2]	"Elf3 encodes a novel 200-kD beta-spectrin: role in liver development." Mishra L., Cai T., Yu P., Monga S.P., Mishra B. Oncogene 18:353-364(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION. Strain: C57BL/6. Tissue: Liver.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-399 (ISOFORM 2). Strain: C57BL/6J. Tissue: Thymus.
[5]	"Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes." Mohler P.J., Yoon W., Bennett V. J. Biol. Chem. 279:40185-40193(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ANK2, TISSUE SPECIFICITY.
[6]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1918; SER-2115; SER-2137 AND SER-2168, MASS SPECTROMETRY. Tissue: Forebrain.
[7]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-999; SER-2102; SER-2164; SER-2168 AND THR-2194, MASS SPECTROMETRY. Tissue: Brain.
[8]	"O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry." Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-2323, MASS SPECTROMETRY. Tissue: Brain.
[9]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1805, MASS SPECTROMETRY. Tissue: Brain.
[11]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2127; SER-2137 AND THR-2194, MASS SPECTROMETRY. Tissue: Brain cortex.
[12]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-10 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Liver.
[13]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-2102; SER-2137; THR-2327 AND SER-2357, MASS SPECTROMETRY. Tissue: Melanoma.
[14]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2164 AND SER-2168, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[15]	"Structure of the pleckstrin homology domain from beta-spectrin." Macias M.J., Musacchio A., Ponstingl H., Nilges M., Saraste M., Oschkinat H. Nature 369:675-677(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2199-2304.
[16]	"Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin." Nilges M., Macias M.J., O'Donoghue S.I., Oschkinat H. J. Mol. Biol. 269:408-422(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2199-2304.
[17]	"Structure of the binding site for inositol phosphates in a PH domain." Hyvoenen M., Macias M.J., Nilges M., Oschkinat H., Saraste M., Wilmanns M. EMBO J. 14:4676-4685(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2199-2304.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74773 mRNA. Translation: AAC42040.1.
AF017112 mRNA. Translation: AAD01616.1.
AL731792, AL672225 Genomic DNA. Translation: CAI24366.1.
AL731792, AL672225 Genomic DNA. Translation: CAI24367.1.
AL672225, AL731792 Genomic DNA. Translation: CAI25429.1.
AL672225, AL731792 Genomic DNA. Translation: CAI25430.1.
AL731792, AL672225 Genomic DNA. Translation: CAM16973.1.
AL672225, AL731792 Genomic DNA. Translation: CAM22716.1.
AK169544 mRNA. Translation: BAE41221.1.

IPI

IPI00121892.
IPI00319830.

RefSeq

NP_033286.2. NM_009260.2.
NP_787030.2. NM_175836.2.

UniGene

Mm.123110.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BTN	X-ray	2.00	A	2199-2304	[»]
1MPH	NMR	-	A	2199-2304	[»]

ProteinModelPortal

Q62261.

SMR

Q62261. Positions 48-280, 299-2086, 2199-2304.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31558N.

IntAct

Q62261. 9 interactions.

PTM databases

PhosphoSite

Q62261.

Proteomic databases

PaxDb

Q62261.

PRIDE

Q62261.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000006629; ENSMUSP00000006629; ENSMUSG00000020315.
ENSMUST00000011877; ENSMUSP00000011877; ENSMUSG00000020315.
ENSMUST00000102838; ENSMUSP00000099902; ENSMUSG00000020315.
ENSMUST00000124231; ENSMUSP00000114841; ENSMUSG00000020315.

GeneID

20742.

KEGG

mmu:20742.

UCSC

uc007ihs.1. mouse.
uc007iht.1. mouse.

Organism-specific databases

CTD

6711.

MGI

MGI:98388. Sptbn1.

Phylogenomic databases

eggNOG

COG5069.

GeneTree

ENSGT00700000104022.

HOGENOM

HOG000007281.

HOVERGEN

HBG057912.

InParanoid

Q62261.

KO

K06115.

OMA

LWQFYWD.

OrthoDB

EOG4WWRHM.

Gene expression databases

ArrayExpress

Q62261.

Bgee

Q62261.

CleanEx

MM_SPNB2.

Genevestigator

Q62261.

GermOnline

ENSMUSG00000020315. Mus musculus.

Family and domain databases

Gene3D

1.10.418.10. 2 hits.
2.30.29.30. 1 hit.

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]

Pfam

PF00307. CH. 2 hits.
PF00169. PH. 1 hit.
PF00435. Spectrin. 17 hits.
[Graphical view]

PIRSF

PIRSF002297. Spectrin_beta_subunit. 1 hit.

PRINTS

PR00683. SPECTRINPH.

SMART

SM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q62261.

NextBio

299385.

SOURCE

Search...

Entry information

Entry name

SPTB2_MOUSE

Accession

Primary (citable) accession number: Q62261
Secondary accession number(s): A2AFU1 , Q3TEM7, Q5SQL8, Q5SQL9, Q9QWJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 16, 2006
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program