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Protein

Protein capicua homolog

Gene

CIC

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

Functioni

Transcriptional repressor which may play a role in development of the central nervous system (CNS).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi200 – 26869HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiQ96RK0.
SIGNORiQ96RK0.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein capicua homolog
Gene namesi
Name:CIC
Synonyms:KIAA0306
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:14214. CIC.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26513.

Polymorphism and mutation databases

BioMutaiCIC.
DMDMi116241300.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16081608Protein capicua homologPRO_0000048598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei436 – 4361PhosphoserineBy similarity
Modified residuei496 – 4961PhosphoserineBy similarity
Modified residuei700 – 7001PhosphoserineCombined sources
Modified residuei721 – 7211PhosphoserineCombined sources
Modified residuei1268 – 12681N6-acetyllysineBy similarity
Modified residuei1291 – 12911PhosphothreonineBy similarity
Modified residuei1373 – 13731PhosphoserineCombined sources
Modified residuei1378 – 13781PhosphoserineCombined sources
Modified residuei1382 – 13821PhosphoserineCombined sources
Modified residuei1397 – 13971PhosphoserineCombined sources
Modified residuei1398 – 13981PhosphothreonineCombined sources
Modified residuei1402 – 14021PhosphoserineCombined sources
Modified residuei1409 – 14091PhosphoserineCombined sources
Modified residuei1595 – 15951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96RK0.
MaxQBiQ96RK0.
PaxDbiQ96RK0.
PRIDEiQ96RK0.

PTM databases

iPTMnetiQ96RK0.
PhosphoSiteiQ96RK0.

Expressioni

Tissue specificityi

Expressed in fetal brain.1 Publication

Gene expression databases

BgeeiQ96RK0.
CleanExiHS_CIC.
ExpressionAtlasiQ96RK0. baseline and differential.
GenevisibleiQ96RK0. HS.

Organism-specific databases

HPAiCAB026388.
HPA044341.

Interactioni

Subunit structurei

Interacts with ATXN1 and ATXN1L.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN1P542535EBI-945857,EBI-930964
CENPJQ9HC772EBI-945857,EBI-946194

Protein-protein interaction databases

BioGridi116767. 19 interactions.
DIPiDIP-49964N.
IntActiQ96RK0. 17 interactions.
MINTiMINT-2856152.
STRINGi9606.ENSP00000160740.

Structurei

Secondary structure

1
1608
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Helixi37 – 393Combined sources
Beta strandi44 – 463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M41NMR-A34-48[»]
4J2JX-ray2.50D/E/F28-48[»]
4J2LX-ray3.15C/D21-48[»]
ProteinModelPortaliQ96RK0.
SMRiQ96RK0. Positions 201-268.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 4619Interaction with ATXN1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi42 – 13897Pro-richAdd
BLAST
Compositional biasi508 – 1303796Pro-richAdd
BLAST
Compositional biasi1524 – 160178Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410ITBG. Eukaryota.
ENOG4111S7E. LUCA.
GeneTreeiENSGT00530000063757.
HOVERGENiHBG081174.
InParanoidiQ96RK0.
PhylomeDBiQ96RK0.
TreeFamiTF323412.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96RK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYSAHRPLMP ASSAASRGLG MFVWTNVEPR SVAVFPWHSL VPFLAPSQPD
60 70 80 90 100
PSVQPSEAQQ PASHPVASNQ SKEPAESAAV AHERPPGGTG SADPERPPGA
110 120 130 140 150
TCPESPGPGP PHPLGVVESG KGPPPTTEEE ASGPPGEPRL DSETESDHDD
160 170 180 190 200
AFLSIMSPEI QLPLPPGKRR TQSLSALPKE RDSSSEKDGR SPNKREKDHI
210 220 230 240 250
RRPMNAFMIF SKRHRALVHQ RHPNQDNRTV SKILGEWWYA LGPKEKQKYH
260 270 280 290 300
DLAFQVKEAH FKAHPDWKWC NKDRKKSSSE AKPTSLGLAG GHKETRERSM
310 320 330 340 350
SETGTAAAPG VSSELLSVAA QTLLSSDTKA PGSSSCGAER LHTVGGPGSA
360 370 380 390 400
RPRAFSHSGV HSLDGGEVDS QALQELTQMV SGPASYSGPK PSTQYGAPGP
410 420 430 440 450
FAAPGEGGAL AATGRPPLLP TRASRSQRAA SEDMTSDEER MVICEEEGDD
460 470 480 490 500
DVIADDGFGT TDIDLKCKER VTDSESGDSS GEDPEGNKGF GRKVFSPVIR
510 520 530 540 550
SSFTHCRPPL DPEPPGPPDP PVAFGKGYGS APSSSASSPA SSSASAATSF
560 570 580 590 600
SLGSGTFKAQ ESGQGSTAGP LRPPPPGAGG PATPSKATRF LPMDPATFRR
610 620 630 640 650
KRPESVGGLE PPGPSVIAAP PSGGGNILQT LVLPPNKEEQ EGGGARVPSA
660 670 680 690 700
PAPSLAYGAP AAPLSRPAAT MVTNVVRPVS STPVPIASKP FPTSGRAEAS
710 720 730 740 750
PNDTAGARTE MGTGSRVPGG SPLGVSLVYS DKKSAAATSP APHLVAGPLL
760 770 780 790 800
GTVGKAPATV TNLLVGTPGY GAPAPPAVQF IAQGAPGGGT TAGSGAGAGS
810 820 830 840 850
GPNGPVPLGI LQPGALGKAG GITQVQYILP TLPQQLQVAP APAPAPGTKA
860 870 880 890 900
AAPSGPAPTT SIRFTLPPGT STNGKVLAAT APTPGIPILQ SVPSAPPPKA
910 920 930 940 950
QSVSPVQAPP PGGSAQLLPG KVLVPLAAPS MSVRGGGAGQ PLPLVSPPFS
960 970 980 990 1000
VPVQNGAQPP SKIIQLTPVP VSTPSGLVPP LSPATLPGPT SQPQKVLLPS
1010 1020 1030 1040 1050
STRITYVQSA GGHALPLGTS PASSQAGTVT SYGPTSSVAL GFTSLGPSGP
1060 1070 1080 1090 1100
AFVQPLLSAG QAPLLAPGQV GVSPVPSPQL PPACAAPGGP VITAFYSGSP
1110 1120 1130 1140 1150
APTSSAPLAQ PSQAPPSLVY TVATSTTPPA ATILPKGPPA PATATPAPTS
1160 1170 1180 1190 1200
PFPSATAGSM TYSLVAPKAQ RPSPKAPQKV KAAIASIPVG SFEAGASGRP
1210 1220 1230 1240 1250
GPAPRQPLEP GPVREPTAPE SELEGQPTPP APPPLPETWT PTARSSPPLP
1260 1270 1280 1290 1300
PPAEERTSAK GPETMASKFP SSSSDWRVPG QGLENRGEPP TPPSPAPAPA
1310 1320 1330 1340 1350
VAPGGSSESS SGRAAGDTPE RKEAAGTGKK VKVRPPPLKK TFDSVDNRVL
1360 1370 1380 1390 1400
SEVDFEERFA ELPEFRPEEV LPSPTLQSLA TSPRAILGSY RKKRKNSTDL
1410 1420 1430 1440 1450
DSAPEDPTSP KRKMRRRSSC SSEPNTPKSA KCEGDIFTFD RTGTEAEDVL
1460 1470 1480 1490 1500
GELEYDKVPY SSLRRTLDQR RALVMQLFQD HGFFPSAQAT AAFQARYADI
1510 1520 1530 1540 1550
FPSKVCLQLK IREVRQKIMQ AATPTEQPPG AEAPLPVPPP TGTAAAPAPT
1560 1570 1580 1590 1600
PSPAGGPDPT SPSSDSGTAQ AAPPLPPPPE SGPGQPGWEG APQPSPPPPG

PSTAATGR
Length:1,608
Mass (Da):163,820
Last modified:October 17, 2006 - v2
Checksum:i355603C8BD67244E
GO

Sequence cautioni

The sequence AAD11988.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041E → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_035936
Natural varianti492 – 4921R → W De novo variant found in a patient with mental retardation. 1 Publication
VAR_065090
Natural varianti652 – 6521A → T in a breast cancer sample; somatic mutation. 1 Publication
VAR_035937
Natural varianti982 – 9821S → G.2 Publications
Corresponds to variant rs17339472 [ dbSNP | Ensembl ].
VAR_028302

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF363689 mRNA. Translation: AAK73515.1.
AC006486 Genomic DNA. Translation: AAD11988.1. Sequence problems.
AB002304 mRNA. Translation: BAA20765.1.
CCDSiCCDS12601.1.
RefSeqiNP_001291744.1. NM_001304815.1.
NP_055940.3. NM_015125.4.
UniGeneiHs.388236.

Genome annotation databases

EnsembliENST00000575354; ENSP00000458663; ENSG00000079432.
GeneIDi23152.
KEGGihsa:23152.
UCSCiuc002otf.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF363689 mRNA. Translation: AAK73515.1.
AC006486 Genomic DNA. Translation: AAD11988.1. Sequence problems.
AB002304 mRNA. Translation: BAA20765.1.
CCDSiCCDS12601.1.
RefSeqiNP_001291744.1. NM_001304815.1.
NP_055940.3. NM_015125.4.
UniGeneiHs.388236.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M41NMR-A34-48[»]
4J2JX-ray2.50D/E/F28-48[»]
4J2LX-ray3.15C/D21-48[»]
ProteinModelPortaliQ96RK0.
SMRiQ96RK0. Positions 201-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116767. 19 interactions.
DIPiDIP-49964N.
IntActiQ96RK0. 17 interactions.
MINTiMINT-2856152.
STRINGi9606.ENSP00000160740.

PTM databases

iPTMnetiQ96RK0.
PhosphoSiteiQ96RK0.

Polymorphism and mutation databases

BioMutaiCIC.
DMDMi116241300.

Proteomic databases

EPDiQ96RK0.
MaxQBiQ96RK0.
PaxDbiQ96RK0.
PRIDEiQ96RK0.

Protocols and materials databases

DNASUi23152.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000575354; ENSP00000458663; ENSG00000079432.
GeneIDi23152.
KEGGihsa:23152.
UCSCiuc002otf.1. human.

Organism-specific databases

CTDi23152.
GeneCardsiCIC.
H-InvDBHIX0015175.
HIX0137483.
HGNCiHGNC:14214. CIC.
HPAiCAB026388.
HPA044341.
MIMi612082. gene.
neXtProtiNX_Q96RK0.
PharmGKBiPA26513.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITBG. Eukaryota.
ENOG4111S7E. LUCA.
GeneTreeiENSGT00530000063757.
HOVERGENiHBG081174.
InParanoidiQ96RK0.
PhylomeDBiQ96RK0.
TreeFamiTF323412.

Enzyme and pathway databases

SignaLinkiQ96RK0.
SIGNORiQ96RK0.

Miscellaneous databases

ChiTaRSiCIC. human.
GeneWikiiCIC_(gene).
GenomeRNAii23152.
PROiQ96RK0.
SOURCEiSearch...

Gene expression databases

BgeeiQ96RK0.
CleanExiHS_CIC.
ExpressionAtlasiQ96RK0. baseline and differential.
GenevisibleiQ96RK0. HS.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CIC, a member of a novel subfamily of the HMG-box superfamily, is transiently expressed in developing granule neurons."
    Lee C.-J., Chan W.-I., Cheung M., Cheng Y.-C., Appleby V.J., Orme A.T., Scotting P.J.
    Brain Res. Mol. Brain Res. 106:151-156(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, VARIANT GLY-982.
  2. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-1608, VARIANT GLY-982.
    Tissue: Brain.
  4. "CIC, a gene involved in cerebellar development and ErbB signaling, is significantly expressed in medulloblastomas."
    Lee C.-J., Chan W.-I., Scotting P.J.
    J. Neurooncol. 73:101-108(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, EXPRESSION IN MEDULLOBLASTOMA.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-721; SER-1373 AND SER-1382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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-721; SER-1373; SER-1382; SER-1397; SER-1402 AND SER-1409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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-721 AND SER-1373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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-1402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-173; SER-362; SER-700; SER-1397; THR-1398; SER-1409 AND SER-1595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-104 AND THR-652.
  13. Cited for: VARIANT TRP-492.

Entry informationi

Entry nameiCIC_HUMAN
AccessioniPrimary (citable) accession number: Q96RK0
Secondary accession number(s): Q7LGI1, Q9UEG5, Q9Y6T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: October 17, 2006
Last modified: June 8, 2016
This is version 134 of the entry and version 2 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

Miscellaneous

Expressed in medulloblastoma, a pediatric brain tumor which may arise from the granule cell lineage.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.