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Protein

HIRA-interacting protein 3

Gene

HIRIP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in chromatin function and histone metabolism via its interaction with HIRA and histones.1 Publication

GO - Biological processi

  • chromatin assembly or disassembly Source: ProtInc
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
HIRA-interacting protein 3
Gene namesi
Name:HIRIP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:4917. HIRIP3.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: Nuclear throughout the cell cycle and is excluded from condensed chromatin during mitosis.

GO - Cellular componenti

  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29294.

Polymorphism and mutation databases

BioMutaiHIRIP3.
DMDMi116242511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556HIRA-interacting protein 3PRO_0000083989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei84 – 841PhosphothreonineCombined sources
Modified residuei87 – 871PhosphoserineCombined sources
Modified residuei98 – 981PhosphoserineCombined sources
Modified residuei100 – 1001PhosphoserineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources
Modified residuei142 – 1421PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineCombined sources
Modified residuei159 – 1591PhosphoserineCombined sources
Modified residuei160 – 1601PhosphoserineCombined sources
Modified residuei196 – 1961PhosphoserineCombined sources
Modified residuei199 – 1991PhosphoserineCombined sources
Modified residuei223 – 2231PhosphoserineCombined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei289 – 2891PhosphoserineCombined sources
Modified residuei291 – 2911PhosphoserineCombined sources
Modified residuei330 – 3301PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineCombined sources
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei357 – 3571PhosphoserineCombined sources
Modified residuei358 – 3581PhosphothreonineCombined sources
Modified residuei359 – 3591PhosphoserineCombined sources
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei370 – 3701PhosphoserineCombined sources
Modified residuei372 – 3721PhosphoserineCombined sources
Modified residuei530 – 5301PhosphoserineBy similarity
Modified residuei550 – 5501PhosphoserineCombined sources
Modified residuei551 – 5511PhosphoserineCombined sources
Modified residuei555 – 5551PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by CK2.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9BW71.
MaxQBiQ9BW71.
PaxDbiQ9BW71.
PRIDEiQ9BW71.

PTM databases

iPTMnetiQ9BW71.
PhosphoSiteiQ9BW71.

Expressioni

Tissue specificityi

Widely expressed. Isoform 1 is predominant in skeletal muscle. Isoform 2 is predominant in liver and heart.1 Publication

Gene expression databases

BgeeiQ9BW71.
CleanExiHS_HIRIP3.
GenevisibleiQ9BW71. HS.

Organism-specific databases

HPAiHPA051897.
HPA063205.

Interactioni

Subunit structurei

Interacts with HIRA. Weak interaction with histones H2B and H3. Interacts with CK2.2 Publications

Protein-protein interaction databases

BioGridi114053. 33 interactions.
IntActiQ9BW71. 7 interactions.
MINTiMINT-1411245.
STRINGi9606.ENSP00000279392.

Structurei

3D structure databases

ProteinModelPortaliQ9BW71.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi129 – 253125Glu-richAdd
BLAST
Compositional biasi398 – 4036Poly-Ser

Phylogenomic databases

eggNOGiENOG410IZNK. Eukaryota.
ENOG4111SS6. LUCA.
GeneTreeiENSGT00390000014062.
HOGENOMiHOG000112903.
HOVERGENiHBG066199.
InParanoidiQ9BW71.
OMAiEENPRRA.
OrthoDBiEOG790G1V.
PhylomeDBiQ9BW71.
TreeFamiTF331753.

Family and domain databases

InterProiIPR019098. Histone_chaperone_domain_CHZ.
[Graphical view]
PfamiPF09649. CHZ. 1 hit.
[Graphical view]
SMARTiSM01082. CHZ. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BW71-1) [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
MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL
60 70 80 90 100
KRLVEEELLK MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES
110 120 130 140 150
ESGSEASSPD YFGPPAKNGV AAEVSPAKEE NPRRASKAVE ESSDEERQRD
160 170 180 190 200
LPAQRGEESS EEEEKGYKGK TRKKPVVKKQ APGKASVSRK QAREESEESE
210 220 230 240 250
AEPVQRTAKK VEGNKGTKSL KESEQESEEE ILAQKKEQRE EEVEEEEKEE
260 270 280 290 300
DEEKGDWKPR TRSNGRRKSA REERSCKQKS QAKRLLGDSD SEEEQKEAAS
310 320 330 340 350
SGDDSGRDRE PPVQRKSEDR TQLKGGKRLS GSSEDEEDSG KGEPTAKGSR
360 370 380 390 400
KMARLGSTSG EESDLEREVS DSEAGGGPQG ERKNRSSKKS SRKGRTRSSS
410 420 430 440 450
SSSDGSPEAK GGKAGSGRRG EDHPAVMRLK RYIRACGAHR NYKKLLGSCC
460 470 480 490 500
SHKERLSILR AELEALGMKG TPSLGKCRAL KEQREEAAEV ASLDVANIIS
510 520 530 540 550
GSGRPRRRTA WNPLGEAAPP GELYRRTLDS DEERPRPAPP DWSHMRGIIS

SDGESN
Length:556
Mass (Da):61,957
Last modified:October 17, 2006 - v3
Checksum:iACABE2E0032B8C13
GO
Isoform 2 (identifier: Q9BW71-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-413: Missing.

Show »
Length:243
Mass (Da):27,612
Checksum:i6DE219CC60F3BAB8
GO
Isoform 3 (identifier: Q9BW71-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-175: ESGSEASSPD...GYKGKTRKKP → GWLRSPWRGP...GPEGAEGGGS
     176-556: Missing.

Note: No experimental confirmation available.
Show »
Length:175
Mass (Da):19,709
Checksum:i8E6D1E89AC91F6BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581L → P in CAA11273 (PubMed:9710638).Curated
Sequence conflicti58 – 581L → P in CAA11274 (PubMed:9710638).Curated
Sequence conflicti58 – 581L → P in CAA11275 (PubMed:9710638).Curated
Sequence conflicti58 – 581L → P (PubMed:17391060).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti496 – 4961A → V.
Corresponds to variant rs35431046 [ dbSNP | Ensembl ].
VAR_051033
Natural varianti521 – 5211G → W.
Corresponds to variant rs11643314 [ dbSNP | Ensembl ].
VAR_028115

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 413313Missing in isoform 2. 1 PublicationVSP_003877Add
BLAST
Alternative sequencei101 – 17575ESGSE…TRKKP → GWLRSPWRGPPGCDEAEALH SGLWCPSKLQEAVGLLLLTQ GAPEYPPGRTGSARHEGYPF PREVSGPEGAEGGGS in isoform 3. 1 PublicationVSP_046024Add
BLAST
Alternative sequencei176 – 556381Missing in isoform 3. 1 PublicationVSP_046025Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223349 mRNA. Translation: CAA11273.1.
AJ223350 mRNA. Translation: CAA11274.1.
AJ223351 mRNA. Translation: CAA11275.2.
BX393533 mRNA. No translation available.
AC093512 Genomic DNA. No translation available.
BC000588 mRNA. Translation: AAH00588.1.
CCDSiCCDS10664.1. [Q9BW71-1]
CCDS58449.1. [Q9BW71-3]
RefSeqiNP_001184252.1. NM_001197323.1. [Q9BW71-3]
NP_003600.2. NM_003609.4. [Q9BW71-1]
UniGeneiHs.567370.

Genome annotation databases

EnsembliENST00000279392; ENSP00000279392; ENSG00000149929. [Q9BW71-1]
ENST00000564026; ENSP00000456824; ENSG00000149929. [Q9BW71-3]
GeneIDi8479.
KEGGihsa:8479.
UCSCiuc002dve.4. human. [Q9BW71-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223349 mRNA. Translation: CAA11273.1.
AJ223350 mRNA. Translation: CAA11274.1.
AJ223351 mRNA. Translation: CAA11275.2.
BX393533 mRNA. No translation available.
AC093512 Genomic DNA. No translation available.
BC000588 mRNA. Translation: AAH00588.1.
CCDSiCCDS10664.1. [Q9BW71-1]
CCDS58449.1. [Q9BW71-3]
RefSeqiNP_001184252.1. NM_001197323.1. [Q9BW71-3]
NP_003600.2. NM_003609.4. [Q9BW71-1]
UniGeneiHs.567370.

3D structure databases

ProteinModelPortaliQ9BW71.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114053. 33 interactions.
IntActiQ9BW71. 7 interactions.
MINTiMINT-1411245.
STRINGi9606.ENSP00000279392.

PTM databases

iPTMnetiQ9BW71.
PhosphoSiteiQ9BW71.

Polymorphism and mutation databases

BioMutaiHIRIP3.
DMDMi116242511.

Proteomic databases

EPDiQ9BW71.
MaxQBiQ9BW71.
PaxDbiQ9BW71.
PRIDEiQ9BW71.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279392; ENSP00000279392; ENSG00000149929. [Q9BW71-1]
ENST00000564026; ENSP00000456824; ENSG00000149929. [Q9BW71-3]
GeneIDi8479.
KEGGihsa:8479.
UCSCiuc002dve.4. human. [Q9BW71-1]

Organism-specific databases

CTDi8479.
GeneCardsiHIRIP3.
HGNCiHGNC:4917. HIRIP3.
HPAiHPA051897.
HPA063205.
MIMi603365. gene.
neXtProtiNX_Q9BW71.
PharmGKBiPA29294.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZNK. Eukaryota.
ENOG4111SS6. LUCA.
GeneTreeiENSGT00390000014062.
HOGENOMiHOG000112903.
HOVERGENiHBG066199.
InParanoidiQ9BW71.
OMAiEENPRRA.
OrthoDBiEOG790G1V.
PhylomeDBiQ9BW71.
TreeFamiTF331753.

Miscellaneous databases

GeneWikiiHIRIP3.
GenomeRNAii8479.
NextBioi31725.
PROiQ9BW71.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BW71.
CleanExiHS_HIRIP3.
GenevisibleiQ9BW71. HS.

Family and domain databases

InterProiIPR019098. Histone_chaperone_domain_CHZ.
[Graphical view]
PfamiPF09649. CHZ. 1 hit.
[Graphical view]
SMARTiSM01082. CHZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA."
    Lorain S., Quivy J.-P., Monier-Gavelle F., Scamps C., Lecluse Y., Almouzni G., Lipinski M.
    Mol. Cell. Biol. 18:5546-5556(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH HIRA, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2."
    Assrir N., Filhol O., Galisson F., Lipinski M.
    Biol. Chem. 388:391-398(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CK2, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  3. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Neuroblastoma.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-142; SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289 AND SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-87; SER-196; SER-227 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-100; SER-159; SER-160; SER-223; SER-227; SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-125; SER-196; SER-223 AND SER-227, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-159; SER-160; SER-196; SER-199; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333; SER-550; SER-551 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-142; SER-143; SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHIRP3_HUMAN
AccessioniPrimary (citable) accession number: Q9BW71
Secondary accession number(s): H3BSR3, O75707, O75708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 17, 2006
Last modified: April 13, 2016
This is version 125 of the entry and version 3 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.