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Protein

Zinc finger protein 674

Gene

ZNF674

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

Functioni

May be involved in transcriptional regulation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri224 – 24623C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri252 – 27423C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri280 – 30223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri308 – 33023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri385 – 40723C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri413 – 43523C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri441 – 46323C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri469 – 49123C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri497 – 51923C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri525 – 54723C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri553 – 57523C2H2-type 11PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein 674
Gene namesi
Name:ZNF674
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17625. ZNF674.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

MalaCardsiZNF674.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA142670475.

Polymorphism and mutation databases

BioMutaiZNF674.
DMDMi94730686.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581Zinc finger protein 674PRO_0000233995Add
BLAST

Proteomic databases

MaxQBiQ2M3X9.
PaxDbiQ2M3X9.
PeptideAtlasiQ2M3X9.
PRIDEiQ2M3X9.

PTM databases

iPTMnetiQ2M3X9.
PhosphoSiteiQ2M3X9.

Expressioni

Tissue specificityi

Expressed in testis.1 Publication

Developmental stagei

Expressed in fetal brain.1 Publication

Gene expression databases

BgeeiQ2M3X9.
CleanExiHS_ZNF674.
ExpressionAtlasiQ2M3X9. baseline and differential.
GenevisibleiQ2M3X9. HS.

Organism-specific databases

HPAiHPA031026.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000429148.

Structurei

3D structure databases

ProteinModelPortaliQ2M3X9.
SMRiQ2M3X9. Positions 8-49, 202-579.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 7972KRABPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 11 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 KRAB domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri224 – 24623C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri252 – 27423C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri280 – 30223C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri308 – 33023C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri385 – 40723C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri413 – 43523C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri441 – 46323C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri469 – 49123C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri497 – 51923C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri525 – 54723C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri553 – 57523C2H2-type 11PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129694.
HOGENOMiHOG000234617.
HOVERGENiHBG018163.
InParanoidiQ2M3X9.
KOiK09228.
OMAiSSYHLIR.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ2M3X9.
TreeFamiTF337898.

Family and domain databases

Gene3Di3.30.160.60. 13 hits.
InterProiIPR001909. KRAB.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 8 hits.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 11 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 11 hits.
PS50157. ZINC_FINGER_C2H2_2. 11 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q2M3X9-1) [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
MAMSQESLTF KDVFVDFTLE EWQQLDSAQK NLYRDVMLEN YSHLVSVGHL
60 70 80 90 100
VGKPDVIFRL GPGDESWMAD GGTPVRTCAG EDRPEVWEVD EQIDHYKESQ
110 120 130 140 150
DKFLWQAAFI GKETLKDESG QECKICRKII YLNTDFVSVK QRLPKYYSWE
160 170 180 190 200
RCSKHHLNFL GQNRSYVRKK DDGCKAYWKV CLHYNLHKAQ PAERFFDPNQ
210 220 230 240 250
RGKALHQKQA LRKSQRSQTG EKLYKCTECG KVFIQKANLV VHQRTHTGEK
260 270 280 290 300
PYECCECAKA FSQKSTLIAH QRTHTGEKPY ECSECGKTFI QKSTLIKHQR
310 320 330 340 350
THTGEKPFVC DKCPKAFKSS YHLIRHEKTH IRQAFYKGIK CTTSSLIYQR
360 370 380 390 400
IHTSEKPQCS EHGKASDEKP SPTKHWRTHT KENIYECSKC GKSFRGKSHL
410 420 430 440 450
SVHQRIHTGE KPYECSICGK TFSGKSHLSV HHRTHTGEKP YECRRCGKAF
460 470 480 490 500
GEKSTLIVHQ RMHTGEKPYK CNECGKAFSE KSPLIKHQRI HTGERPYECT
510 520 530 540 550
DCKKAFSRKS TLIKHQRIHT GEKPYKCSEC GKAFSVKSTL IVHHRTHTGE
560 570 580
KPYECRDCGK AFSGKSTLIK HQRSHTGDKN L
Length:581
Mass (Da):67,199
Last modified:February 21, 2006 - v1
Checksum:i6DBD560342DE250D
GO
Isoform 2 (identifier: Q2M3X9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     80-85: Missing.

Note: No experimental confirmation available.
Show »
Length:575
Mass (Da):66,515
Checksum:iC3A93744B086D1AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221K → R in BAG58103 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821L → F.
Corresponds to variant rs1737367 [ dbSNP | Ensembl ].
VAR_046997
Natural varianti343 – 3431T → M.1 Publication
Corresponds to variant rs61730637 [ dbSNP | Ensembl ].
VAR_026152
Natural varianti412 – 4121P → L Rare variant found in patients with X-linked mental retardation; unknown pathological significance. 1 Publication
VAR_026153

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei80 – 856Missing in isoform 2. 1 PublicationVSP_044562

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY971607 mRNA. Translation: AAY40800.1.
AK295054 mRNA. Translation: BAG58103.1.
AL022165 Genomic DNA. No translation available.
AL031393 Genomic DNA. No translation available.
CCDSiCCDS48099.1. [Q2M3X9-1]
CCDS55406.1. [Q2M3X9-2]
RefSeqiNP_001034980.1. NM_001039891.2. [Q2M3X9-1]
NP_001139763.1. NM_001146291.1. [Q2M3X9-2]
NP_001177346.1. NM_001190417.1.
XP_011542243.1. XM_011543941.1. [Q2M3X9-1]
XP_011542244.1. XM_011543942.1. [Q2M3X9-1]
UniGeneiHs.636105.

Genome annotation databases

EnsembliENST00000414387; ENSP00000428248; ENSG00000251192. [Q2M3X9-2]
ENST00000523374; ENSP00000429148; ENSG00000251192. [Q2M3X9-1]
GeneIDi641339.
KEGGihsa:641339.
UCSCiuc004dgr.4. human. [Q2M3X9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY971607 mRNA. Translation: AAY40800.1.
AK295054 mRNA. Translation: BAG58103.1.
AL022165 Genomic DNA. No translation available.
AL031393 Genomic DNA. No translation available.
CCDSiCCDS48099.1. [Q2M3X9-1]
CCDS55406.1. [Q2M3X9-2]
RefSeqiNP_001034980.1. NM_001039891.2. [Q2M3X9-1]
NP_001139763.1. NM_001146291.1. [Q2M3X9-2]
NP_001177346.1. NM_001190417.1.
XP_011542243.1. XM_011543941.1. [Q2M3X9-1]
XP_011542244.1. XM_011543942.1. [Q2M3X9-1]
UniGeneiHs.636105.

3D structure databases

ProteinModelPortaliQ2M3X9.
SMRiQ2M3X9. Positions 8-49, 202-579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000429148.

PTM databases

iPTMnetiQ2M3X9.
PhosphoSiteiQ2M3X9.

Polymorphism and mutation databases

BioMutaiZNF674.
DMDMi94730686.

Proteomic databases

MaxQBiQ2M3X9.
PaxDbiQ2M3X9.
PeptideAtlasiQ2M3X9.
PRIDEiQ2M3X9.

Protocols and materials databases

DNASUi641339.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000414387; ENSP00000428248; ENSG00000251192. [Q2M3X9-2]
ENST00000523374; ENSP00000429148; ENSG00000251192. [Q2M3X9-1]
GeneIDi641339.
KEGGihsa:641339.
UCSCiuc004dgr.4. human. [Q2M3X9-1]

Organism-specific databases

CTDi641339.
GeneCardsiZNF674.
HGNCiHGNC:17625. ZNF674.
HPAiHPA031026.
MalaCardsiZNF674.
MIMi300573. gene.
neXtProtiNX_Q2M3X9.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA142670475.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00840000129694.
HOGENOMiHOG000234617.
HOVERGENiHBG018163.
InParanoidiQ2M3X9.
KOiK09228.
OMAiSSYHLIR.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ2M3X9.
TreeFamiTF337898.

Miscellaneous databases

GenomeRNAii641339.
PROiQ2M3X9.
SOURCEiSearch...

Gene expression databases

BgeeiQ2M3X9.
CleanExiHS_ZNF674.
ExpressionAtlasiQ2M3X9. baseline and differential.
GenevisibleiQ2M3X9. HS.

Family and domain databases

Gene3Di3.30.160.60. 13 hits.
InterProiIPR001909. KRAB.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF00096. zf-C2H2. 8 hits.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00355. ZnF_C2H2. 11 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
PROSITEiPS50805. KRAB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 11 hits.
PS50157. ZINC_FINGER_C2H2_2. 11 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS MET-343 AND LEU-412, POSSIBLE ASSOCIATION OF VARIANT LEU-412 WITH X-LINKED MENTAL RETARDATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "XLID-causing mutations and associated genes challenged in light of data from large-scale human exome sequencing."
    Piton A., Redin C., Mandel J.L.
    Am. J. Hum. Genet. 93:368-383(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ASSOCIATION OF VARIANT LEU-412 WITH X-LINKED MENTAL RETARDATION.

Entry informationi

Entry nameiZN674_HUMAN
AccessioniPrimary (citable) accession number: Q2M3X9
Secondary accession number(s): B4DHE2, E9PHQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: February 21, 2006
Last modified: July 6, 2016
This is version 101 of the entry and version 1 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

Caution

Although ZNF674 has been reported to be involved in X-linked mental retardation (PubMed:16385466), its pathological role is questionable (PubMed:23871722).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. 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.