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Protein

M-phase phosphoprotein 9

Gene

MPHOSPH9

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

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase phosphoprotein 9
Gene namesi
Name:MPHOSPH9
Synonyms:MPP9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7215. MPHOSPH9.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • centrosome Source: HPA
  • cytoplasm Source: HPA
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30921.

Polymorphism and mutation databases

DMDMi215274134.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11831183M-phase phosphoprotein 9PRO_0000096557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei994 – 9941PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated in M (mitotic) phase.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99550.
PaxDbiQ99550.
PeptideAtlasiQ99550.
PRIDEiQ99550.

PTM databases

iPTMnetiQ99550.
PhosphoSiteiQ99550.

Expressioni

Gene expression databases

BgeeiQ99550.
CleanExiHS_MPHOSPH9.
ExpressionAtlasiQ99550. baseline and differential.
GenevisibleiQ99550. HS.

Organism-specific databases

HPAiHPA037485.
HPA037486.

Interactioni

Protein-protein interaction databases

BioGridi115493. 30 interactions.
IntActiQ99550. 29 interactions.
STRINGi9606.ENSP00000445859.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili609 – 804196Sequence analysisAdd
BLAST
Coiled coili1109 – 117466Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IKA1. Eukaryota.
ENOG410XSEU. LUCA.
GeneTreeiENSGT00500000044984.
HOGENOMiHOG000113636.
HOVERGENiHBG108143.
InParanoidiQ99550.
KOiK16775.
OMAiRSPEKCA.
OrthoDBiEOG7P5T03.
TreeFamiTF336168.

Family and domain databases

InterProiIPR026636. MPHOSPH9.
[Graphical view]
PANTHERiPTHR14926. PTHR14926. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q99550-1) [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
MEEFDLVKTL HKTSSSVGSD ENSLHSLGLN LNTDRSSPHL STNGVSSFSG
60 70 80 90 100
KTRPSVIQGT VEVLTSLMQE LQNSGKTDSE LWKNCETRWL QLFNLVEKQC
110 120 130 140 150
QEQIVAQQEQ FHNQIQHIQE EIKNLVKLQT SSASLASCEG NSSNKQVSSE
160 170 180 190 200
SQMGFFSLSS ERNESVIHYP ESTEPEIQQE MSTSQPDCNV DSCSVSSGYG
210 220 230 240 250
TFCISELNLY KSKDPKEFME HIDVPKGQYV APAVPAESLV DGVKNENFYI
260 270 280 290 300
QTPEECHVSL KEDVSISPGE FEHNFLGENK VSEVYSGKTN SNAITSWAQK
310 320 330 340 350
LKQNQPKRAH VEDGGSRSKQ GNEQSKKTPI EKSDFAAATH PRAFYLSKPD
360 370 380 390 400
ETPNAWMSDS GTGLTYWKLE EKDMHHSLPE TLEKTFISLS STDVSPNQSN
410 420 430 440 450
TSNEMKLPSL KDIYYKKQRE NKQLPERNLT SASNPNHPPE VLTLDPTLHM
460 470 480 490 500
KPKQQISGIQ PHGLPNALDD RISFSPDSVL EPSMSSPSDI DSFSQASNVT
510 520 530 540 550
SQLPGFPKYP SHTKASPVDS WKNQTFQNES RTSSTFPSVY TITSNDISVN
560 570 580 590 600
TVDEENTVMV ASASVSQSQL PGTANSVPEC ISLTSLEDPV ILSKIRQNLK
610 620 630 640 650
EKHARHIADL RAYYESEINS LKQKLEAKEI SGVEDWKITN QILVDRCGQL
660 670 680 690 700
DSALHEATSR VRTLENKNNL LEIEVNDLRE RFSAASSASK ILQERIEEMR
710 720 730 740 750
TSSKEKDNTI IRLKSRLQDL EEAFENAYKL SDDKEAQLKQ ENKMFQDLLG
760 770 780 790 800
EYESLGKEHR RVKDALNTTE NKLLDAYTQI SDLKRMISKL EAQVKQVEHE
810 820 830 840 850
NMLSLRHNSR IHVRPSRANT LATSDVSRRK WLIPGAEYSI FTGQPLDTQD
860 870 880 890 900
SNVDNQLEET CSLGHRSPLE KDSSPGSSST SLLIKKQRET SDTPIMRALK
910 920 930 940 950
ELDEGKIFKN WGTQTEKEDT SNINPRQTET SVNASRSPEK CAQQRQKRLN
960 970 980 990 1000
SASQRSSSLP PSNRKSSTPT KREIMLTPVT VAYSPKRSPK ENLSPGFSHL
1010 1020 1030 1040 1050
LSKNESSPIR FDILLDDLDT VPVSTLQRTN PRKQLQFLPL DDSEEKTYSE
1060 1070 1080 1090 1100
KATDNHVNHS SCPEPVPNGV KKVSVRTAWE KNKSVSYEQC KPVSVTPQGN
1110 1120 1130 1140 1150
DFEYTAKIRT LAETERFFDE LTKEKDQIEA ALSRMPSPGG RITLQTRLNQ
1160 1170 1180
EALEDRLERI NRELGSVRMT LKKFHVLRTS ANL
Note: No experimental confirmation. Gene prediction based on EST data.
Length:1,183
Mass (Da):133,024
Last modified:July 9, 2014 - v4
Checksum:i035ABB95C20547E4
GO
Isoform 2 (identifier: Q99550-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1151-1183: EALEDRLERINRELGSVRMTLKKFHVLRTSANL → TPQICEESSHKCAFAGHYVPCHLYDYRFQG

Note: No experimental confirmation available.
Show »
Length:1,180
Mass (Da):132,615
Checksum:iE663949CB98D606B
GO

Sequence cautioni

The sequence BAB14359.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG52299.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW98394.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti947 – 9471K → E in BAB14359 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti277 – 2771G → S.1 Publication
Corresponds to variant rs36121382 [ dbSNP | Ensembl ].
VAR_047643
Natural varianti1078 – 10781A → D.
Corresponds to variant rs1260318 [ dbSNP | Ensembl ].
VAR_047644

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1151 – 118333EALED…TSANL → TPQICEESSHKCAFAGHYVP CHLYDYRFQG in isoform 2. 1 PublicationVSP_035838Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC068768 Genomic DNA. No translation available.
AC073857 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98392.1.
CH471054 Genomic DNA. Translation: EAW98394.1. Sequence problems.
AK023016 mRNA. Translation: BAB14359.1. Different initiation.
AK091181 mRNA. Translation: BAG52299.1. Different initiation.
BC130440 mRNA. Translation: AAI30441.1.
X98258 mRNA. Translation: CAA66911.1.
CCDSiCCDS9243.2. [Q99550-1]
RefSeqiNP_073619.3. NM_022782.3. [Q99550-1]
XP_006719252.1. XM_006719189.2.
XP_011536038.1. XM_011537736.1. [Q99550-1]
XP_011536039.1. XM_011537737.1. [Q99550-1]
XP_011536040.1. XM_011537738.1. [Q99550-1]
XP_011536041.1. XM_011537739.1. [Q99550-2]
XP_011536048.1. XM_011537746.1.
UniGeneiHs.577404.
Hs.735822.

Genome annotation databases

EnsembliENST00000606320; ENSP00000475489; ENSG00000051825. [Q99550-1]
GeneIDi10198.
KEGGihsa:10198.
UCSCiuc001uel.5. human. [Q99550-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC068768 Genomic DNA. No translation available.
AC073857 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98392.1.
CH471054 Genomic DNA. Translation: EAW98394.1. Sequence problems.
AK023016 mRNA. Translation: BAB14359.1. Different initiation.
AK091181 mRNA. Translation: BAG52299.1. Different initiation.
BC130440 mRNA. Translation: AAI30441.1.
X98258 mRNA. Translation: CAA66911.1.
CCDSiCCDS9243.2. [Q99550-1]
RefSeqiNP_073619.3. NM_022782.3. [Q99550-1]
XP_006719252.1. XM_006719189.2.
XP_011536038.1. XM_011537736.1. [Q99550-1]
XP_011536039.1. XM_011537737.1. [Q99550-1]
XP_011536040.1. XM_011537738.1. [Q99550-1]
XP_011536041.1. XM_011537739.1. [Q99550-2]
XP_011536048.1. XM_011537746.1.
UniGeneiHs.577404.
Hs.735822.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115493. 30 interactions.
IntActiQ99550. 29 interactions.
STRINGi9606.ENSP00000445859.

PTM databases

iPTMnetiQ99550.
PhosphoSiteiQ99550.

Polymorphism and mutation databases

DMDMi215274134.

Proteomic databases

EPDiQ99550.
PaxDbiQ99550.
PeptideAtlasiQ99550.
PRIDEiQ99550.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000606320; ENSP00000475489; ENSG00000051825. [Q99550-1]
GeneIDi10198.
KEGGihsa:10198.
UCSCiuc001uel.5. human. [Q99550-1]

Organism-specific databases

CTDi10198.
GeneCardsiMPHOSPH9.
HGNCiHGNC:7215. MPHOSPH9.
HPAiHPA037485.
HPA037486.
MIMi605501. gene.
neXtProtiNX_Q99550.
PharmGKBiPA30921.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKA1. Eukaryota.
ENOG410XSEU. LUCA.
GeneTreeiENSGT00500000044984.
HOGENOMiHOG000113636.
HOVERGENiHBG108143.
InParanoidiQ99550.
KOiK16775.
OMAiRSPEKCA.
OrthoDBiEOG7P5T03.
TreeFamiTF336168.

Miscellaneous databases

ChiTaRSiMPHOSPH9. human.
GenomeRNAii10198.
PROiQ99550.
SOURCEiSearch...

Gene expression databases

BgeeiQ99550.
CleanExiHS_MPHOSPH9.
ExpressionAtlasiQ99550. baseline and differential.
GenevisibleiQ99550. HS.

Family and domain databases

InterProiIPR026636. MPHOSPH9.
[Graphical view]
PANTHERiPTHR14926. PTHR14926. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 118-1183 (ISOFORM 1), VARIANT SER-277.
    Tissue: Tongue.
  4. "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] OF 133-1183 (ISOFORM 1).
  5. "Identification of novel M phase phosphoproteins by expression cloning."
    Matsumoto-Taniura N., Pirollet F., Monroe R., Gerace L., Westendorf J.M.
    Mol. Biol. Cell 7:1455-1469(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 967-1183 (ISOFORM 2), SUBCELLULAR LOCATION, PHOSPHORYLATION.
    Tissue: Lymphoblast.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods."
    Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I., Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M., Hyman A.A., Andersen J.S.
    EMBO J. 30:1520-1535(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-994, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiMPP9_HUMAN
AccessioniPrimary (citable) accession number: Q99550
Secondary accession number(s): A1L486
, A6NEE2, B3KR87, Q9H976, U3KQ28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 9, 2014
Last modified: July 6, 2016
This is version 132 of the entry and version 4 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 12
    Human chromosome 12: 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.