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UniProtKB - O75533 (SF3B1_HUMAN)

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Protein

Splicing factor 3B subunit 1

Gene

SF3B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (PubMed:15146077).4 Publications

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • mRNA splicing, via spliceosome Source: UniProtKB
  • positive regulation of gene expression, epigenetic Source: Reactome
  • RNA splicing, via transesterification reactions Source: UniProtKB
  • spliceosomal complex assembly Source: GO_Central
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway
SIGNORiO75533

Names & Taxonomyi

Protein namesi
Recommended name:
Splicing factor 3B subunit 1
Alternative name(s):
Pre-mRNA-splicing factor SF3b 155 kDa subunit
Short name:
SF3b155
Spliceosome-associated protein 155
Short name:
SAP 155
Gene namesi
Name:SF3B1
Synonyms:SAP155
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000115524.15
HGNCiHGNC:10768 SF3B1
MIMi605590 gene
neXtProtiNX_O75533

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi200W → A: Abolishes interaction with RBM39; when associated with A-218; A-232; A-254; A-293; A-310 and A-338. 1 Publication1
Mutagenesisi218W → A: Abolishes interaction with RBM39; when associated with A-200; A-232; A-254; A-293; A-310 and A-338. 1 Publication1
Mutagenesisi223T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi227T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi232W → A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-254; A-293; A-310 and A-338. 1 Publication1
Mutagenesisi235T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi244T → A: Slight inhibition of interaction with PPP1R8. 1 Publication1
Mutagenesisi248T → A: Slight inhibition of interaction with PPP1R8. 1 Publication1
Mutagenesisi254W → A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-293; A-310 and A-338. 1 Publication1
Mutagenesisi257T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi261T → A: Slight inhibition of interaction with PPP1R8. 1 Publication1
Mutagenesisi267T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi273T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi278T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi293W → A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-310 and A-338. 1 Publication1
Mutagenesisi296T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi303T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi310W → A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-293 and A-338. 1 Publication1
Mutagenesisi313T → A: No effect on interaction with PPP1R8. 1 Publication1
Mutagenesisi338W → A: Abolishes interaction with RBM39; when associated with A-200; A-218; A-232; A-254; A-293 and A-310. 1 Publication1
Mutagenesisi700K → E: Does not affect the stability of the SF3B complex interaction with U2AF65. Does not decrease the affinity to RNA. 1 Publication1

Organism-specific databases

DisGeNETi23451
MalaCardsiSF3B1
OpenTargetsiENSG00000115524
Orphaneti75564 Acquired idiopathic sideroblastic anemia
PharmGKBiPA35686

Polymorphism and mutation databases

BioMutaiSF3B1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001743231 – 1304Splicing factor 3B subunit 1Add BLAST1304

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei125PhosphothreonineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei141N6-acetyllysineCombined sources1
Modified residuei142PhosphothreonineCombined sources1
Modified residuei157CitrullineBy similarity1
Modified residuei194PhosphoserineCombined sources1
Modified residuei203PhosphothreonineCombined sources1
Modified residuei207PhosphothreonineCombined sources1
Modified residuei211PhosphothreonineCombined sources1
Modified residuei214N6-acetyllysine; alternateBy similarity1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei223PhosphothreonineCombined sources1
Modified residuei227PhosphothreonineCombined sources1
Modified residuei229PhosphoserineBy similarity1
Modified residuei235PhosphothreonineCombined sources1
Modified residuei244Phosphothreonine1 Publication1
Modified residuei248Phosphothreonine1 Publication1
Modified residuei257PhosphothreonineCombined sources1
Modified residuei261PhosphothreonineCombined sources1
Modified residuei267PhosphothreonineCombined sources1
Modified residuei273PhosphothreonineCombined sources1
Modified residuei278PhosphothreonineCombined sources1
Modified residuei287PhosphoserineCombined sources1
Modified residuei296PhosphothreonineCombined sources1
Modified residuei299PhosphothreonineCombined sources1
Modified residuei303PhosphothreonineCombined sources1
Modified residuei313PhosphothreonineCombined sources1
Modified residuei322PhosphoserineCombined sources1
Modified residuei326PhosphothreonineCombined sources1
Modified residuei328PhosphothreonineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei341PhosphothreonineCombined sources1
Modified residuei344PhosphoserineCombined sources1
Modified residuei349PhosphoserineCombined sources1
Modified residuei350PhosphothreonineCombined sources1
Modified residuei354PhosphothreonineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Cross-linki413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki413Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei426PhosphothreonineCombined sources1
Cross-linki430Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei434PhosphothreonineCombined sources1
Modified residuei436PhosphothreonineCombined sources1
Modified residuei488PhosphoserineCombined sources1
Modified residuei554N6-acetyllysineCombined sources1
Modified residuei562N6-acetyllysineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation occurs concomitantly with the splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis.2 Publications
Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75533
MaxQBiO75533
PaxDbiO75533
PeptideAtlasiO75533
PRIDEiO75533
ProteomicsDBi50072

PTM databases

iPTMnetiO75533
PhosphoSitePlusiO75533
SwissPalmiO75533

Miscellaneous databases

PMAP-CutDBiO75533

Expressioni

Gene expression databases

BgeeiENSG00000115524
CleanExiHS_SF3B1
ExpressionAtlasiO75533 baseline and differential
GenevisibleiO75533 HS

Organism-specific databases

HPAiHPA050275

Interactioni

Subunit structurei

Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (PubMed:16603771). Identified in the spliceosome C complex (PubMed:11991638). Component of the U11/U12 snRNPs that are part of the U12-type spliceosome (PubMed:15146077). Component of splicing factor SF3B complex which is composed of at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42 (PubMed:12234937, PubMed:12738865, PubMed:28541300, PubMed:27720643). SF3B associates with the splicing factor SF3A and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts directly with the splicing factor U2AF (PubMed:12234937). Within the SF3B complex interacts directly (via HEAT domain) with SF3B3, SF3B5 and (via HEAT domain) with PHF5A (PubMed:27720643). Interacts directly with SF3B6 (PubMed:16432215, Ref. 36, PubMed:21062891). The SF3B complex composed of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2 (PubMed:27720643). Phosphorylated form interacts with PPP1R8 (PubMed:12105215). Interacts with PQBP1 (PubMed:23512658). Interacts with RBM17 (PubMed:17589525). Interacts with RBM39 (PubMed:24795046). Interacts with SETX (PubMed:21700224). Interacts with RBM15 (PubMed:26575292).16 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei469Interaction with RNA1 Publication1
Sitei587Interaction with RNA1 Publication1
Sitei592Interaction with PHF5A1 Publication1
Sitei602Interaction with SF3B31 Publication1
Sitei677Interaction with SF3B31 Publication1
Sitei1035Interaction with RNA1 Publication1
Sitei1049Interaction with RNA1 Publication1
Sitei1141Interaction with RNA1 Publication1
Sitei1205Interaction with SF3B31 Publication1

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi117017, 201 interactors
ComplexPortaliCPX-1099 B-WICH chromatin remodelling complex
CORUMiO75533
DIPiDIP-29411N
ELMiO75533
IntActiO75533, 64 interactors
MINTiO75533
STRINGi9606.ENSP00000335321

Structurei

Secondary structure

11304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi380 – 394Combined sources15
Helixi401 – 406Combined sources6
Beta strandi410 – 414Combined sources5
Helixi469 – 471Combined sources3
Helixi472 – 475Combined sources4
Helixi476 – 478Combined sources3
Helixi491 – 498Combined sources8
Helixi500 – 505Combined sources6
Helixi509 – 521Combined sources13
Helixi523 – 526Combined sources4
Helixi528 – 540Combined sources13
Helixi546 – 562Combined sources17
Helixi568 – 570Combined sources3
Helixi571 – 578Combined sources8
Helixi579 – 583Combined sources5
Helixi587 – 603Combined sources17
Helixi606 – 613Combined sources8
Turni615 – 618Combined sources4
Helixi622 – 639Combined sources18
Helixi641 – 651Combined sources11
Helixi658 – 675Combined sources18
Helixi676 – 682Combined sources7
Helixi683 – 690Combined sources8
Helixi691 – 695Combined sources5
Helixi699 – 716Combined sources18
Helixi722 – 724Combined sources3
Helixi725 – 737Combined sources13
Helixi741 – 753Combined sources13
Helixi754 – 756Combined sources3
Helixi759 – 775Combined sources17
Helixi776 – 778Combined sources3
Helixi782 – 795Combined sources14
Beta strandi798 – 801Combined sources4
Helixi803 – 809Combined sources7
Helixi811 – 817Combined sources7
Helixi821 – 823Combined sources3
Helixi827 – 844Combined sources18
Helixi846 – 854Combined sources9
Helixi855 – 858Combined sources4
Helixi862 – 879Combined sources18
Helixi886 – 901Combined sources16
Helixi908 – 921Combined sources14
Helixi922 – 928Combined sources7
Helixi929 – 940Combined sources12
Helixi948 – 963Combined sources16
Turni964 – 966Combined sources3
Helixi968 – 979Combined sources12
Turni980 – 983Combined sources4
Helixi987 – 1001Combined sources15
Helixi1013 – 1020Combined sources8
Helixi1021 – 1025Combined sources5
Helixi1029 – 1045Combined sources17
Helixi1047 – 1049Combined sources3
Helixi1052 – 1062Combined sources11
Helixi1063 – 1067Combined sources5
Helixi1071 – 1088Combined sources18
Helixi1109 – 1122Combined sources14
Turni1125 – 1128Combined sources4
Helixi1129 – 1134Combined sources6
Beta strandi1137 – 1139Combined sources3
Helixi1141 – 1158Combined sources18
Helixi1159 – 1164Combined sources6
Helixi1166 – 1177Combined sources12
Beta strandi1178 – 1180Combined sources3
Helixi1182 – 1199Combined sources18
Helixi1205 – 1215Combined sources11
Helixi1216 – 1219Combined sources4
Helixi1224 – 1241Combined sources18
Helixi1243 – 1250Combined sources8
Helixi1252 – 1254Combined sources3
Helixi1259 – 1274Combined sources16
Turni1277 – 1279Combined sources3
Helixi1280 – 1282Combined sources3
Helixi1299 – 1301Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F9DX-ray2.50P/Q373-415[»]
2F9JX-ray3.00P/Q380-415[»]
2FHONMR-A379-424[»]
2PEHX-ray2.11C/D333-342[»]
3LQVX-ray2.38P/Q377-415[»]
4OZ1X-ray1.74C333-342[»]
5IFEX-ray3.10C1-1304[»]
5O9Zelectron microscopy4.50v1-1304[»]
5ZD5electron microscopy3.95C1-1304[»]
ProteinModelPortaliO75533
SMRiO75533
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75533

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati529 – 568HEAT 1Add BLAST40
Repeati569 – 603HEAT 2Add BLAST35
Repeati604 – 641HEAT 3Add BLAST38
Repeati643 – 677HEAT 4Add BLAST35
Repeati680 – 718HEAT 5Add BLAST39
Repeati763 – 801HEAT 6Add BLAST39
Repeati843 – 881HEAT 7Add BLAST39
Repeati1010 – 1048HEAT 8Add BLAST39
Repeati1052 – 1090HEAT 9Add BLAST39
Repeati1122 – 1160HEAT 10Add BLAST39
Repeati1163 – 1201HEAT 11Add BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 342U2AF homology region; mediates interaction with RBM391 PublicationAdd BLAST153
Regioni223 – 491Interaction with PPP1R81 PublicationAdd BLAST269
Regioni529 – 568Interaction with SF3B14Add BLAST40
Regioni547 – 550Interaction with PHF5A1 Publication4
Regioni1156 – 1157Interaction with PHF5A1 Publication2
Regioni1248 – 1304Interaction with SF3B3 and SF3B51 PublicationAdd BLAST57

Sequence similaritiesi

Belongs to the SF3B1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0213 Eukaryota
COG5181 LUCA
GeneTreeiENSGT00390000018393
HOGENOMiHOG000166737
HOVERGENiHBG079173
InParanoidiO75533
KOiK12828
OMAiYAVCPLL
OrthoDBiEOG091G00Q0
PhylomeDBiO75533
TreeFamiTF105680

Family and domain databases

Gene3Di1.25.10.10, 2 hits
InterProiView protein in InterPro
IPR011989 ARM-like
IPR016024 ARM-type_fold
IPR015016 SF3b_su1
IPR038737 SF3b_su1-like
PANTHERiPTHR12097 PTHR12097, 1 hit
PfamiView protein in Pfam
PF08920 SF3b1, 1 hit
SUPFAMiSSF48371 SSF48371, 3 hits

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75533-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR 
        60         70         80         90        100
FAGYVTSIAA TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ 
       110        120        130        140        150
YDPFAEHRPP KIADREDEYK KHRRTMIISP ERLDPFADGG KTPDPKMNAR 
       160        170        180        190        200
TYMDVMREQH LTKEEREIRQ QLAEKAKAGE LKVVNGAAAS QPPSKRKRRW 
       210        220        230        240        250
DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK GSETPGATPG 
       260        270        280        290        300
SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE 
       310        320        330        340        350
RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST 
       360        370        380        390        400
PVLTPGKTPI GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS 
       410        420        430        440        450
DEELDAMFPE GYKVLPPPAG YVPIRTPARK LTATPTPLGG MTGFHMQTED 
       460        470        480        490        500
RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV DVDESTLSPE EQKERKIMKL 
       510        520        530        540        550
LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM SPTLEDQERH 
       560        570        580        590        600
LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL 
       610        620        630        640        650
AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA 
       660        670        680        690        700
VCKSKKSWQA RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK 
       710        720        730        740        750
VRTISALAIA ALAEAATPYG IESFDSVLKP LWKGIRQHRG KGLAAFLKAI 
       760        770        780        790        800
GYLIPLMDAE YANYYTREVM LILIREFQSP DEEMKKIVLK VVKQCCGTDG 
       810        820        830        840        850
VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL ANKVGAAEII 
       860        870        880        890        900
SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF 
       910        920        930        940        950
QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ 
       960        970        980        990       1000
AADLISRTAV VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI 
      1010       1020       1030       1040       1050
VNVIGMHKMT PPIKDLLPRL TPILKNRHEK VQENCIDLVG RIADRGAEYV 
      1060       1070       1080       1090       1100
SAREWMRICF ELLELLKAHK KAIRRATVNT FGYIAKAIGP HDVLATLLNN 
      1110       1120       1130       1140       1150
LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE LNVQNGVLKS 
      1160       1170       1180       1190       1200
LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY 
      1210       1220       1230       1240       1250
GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC 
      1260       1270       1280       1290       1300
LQGLFHPARK VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL 

DYIL
Length:1,304
Mass (Da):145,830
Last modified:November 24, 2009 - v3
Checksum:i12F051757D2B9DEE
GO
Isoform 2 (identifier: O75533-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     140-144: GKTPD → FYSAA
     145-1304: Missing.

Note: No experimental confirmation available.
Show »
Length:144
Mass (Da):16,020
Checksum:i006D4294E06AB51E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti149A → V in AAC97189 (PubMed:9585501).Curated1
Sequence conflicti594R → L in AAC97189 (PubMed:9585501).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046182140 – 144GKTPD → FYSAA in isoform 2. 1 Publication5
Alternative sequenceiVSP_046183145 – 1304Missing in isoform 2. 1 PublicationAdd BLAST1160

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054284 mRNA Translation: AAC97189.1
AF086296 mRNA No translation available.
AC010746 Genomic DNA No translation available.
AF070540 mRNA Translation: AAC28633.1
CCDSiCCDS33356.1 [O75533-1]
CCDS46479.1 [O75533-2]
RefSeqiNP_036565.2, NM_012433.3 [O75533-1]
UniGeneiHs.632554

Genome annotation databases

EnsembliENST00000335508; ENSP00000335321; ENSG00000115524 [O75533-1]
ENST00000409915; ENSP00000428820; ENSG00000115524 [O75533-2]
ENST00000414963; ENSP00000402997; ENSG00000115524 [O75533-2]
GeneIDi23451
KEGGihsa:23451
UCSCiuc002uue.4 human [O75533-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiSF3B1_HUMAN
AccessioniPrimary (citable) accession number: O75533
Secondary accession number(s): E9PCH3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: November 24, 2009
Last modified: June 20, 2018
This is version 179 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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